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Conserved domains on  [gi|223972653|ref|NP_001138868|]
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aldehyde dehydrogenase family 16 member A1 isoform 2 [Homo sapiens]

Protein Classification

aldehyde dehydrogenase family protein( domain architecture ID 34081)

aldehyde dehydrogenase family protein is an NAD(P)(+)-dependent enzyme that may oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and may play an important role in detoxification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ALDH-SF super family cl11961
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ...
19-441 0e+00

NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily (ALDH-SF) of NAD(P)+-dependent enzymes, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. Besides aldehyde detoxification, many ALDH isozymes possess multiple additional catalytic and non-catalytic functions such as participating in metabolic pathways, or as binding proteins, or osmoregulants, to mention a few. The enzyme has three domains, a NAD(P)+ cofactor-binding domain, a catalytic domain, and a bridging domain; and the active enzyme is generally either homodimeric or homotetrameric. The catalytic mechanism is proposed to involve cofactor binding, resulting in a conformational change and activation of an invariant catalytic cysteine nucleophile. The cysteine and aldehyde substrate form an oxyanion thiohemiacetal intermediate resulting in hydride transfer to the cofactor and formation of a thioacylenzyme intermediate. Hydrolysis of the thioacylenzyme and release of the carboxylic acid product occurs, and in most cases, the reduced cofactor dissociates from the enzyme. The evolutionary phylogenetic tree of ALDHs appears to have an initial bifurcation between what has been characterized as the classical aldehyde dehydrogenases, the ALDH family (ALDH) and extended family members or aldehyde dehydrogenase-like (ALDH-L) proteins. The ALDH proteins are represented by enzymes which share a number of highly conserved residues necessary for catalysis and cofactor binding and they include such proteins as retinal dehydrogenase, 10-formyltetrahydrofolate dehydrogenase, non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase, delta(1)-pyrroline-5-carboxylate dehydrogenases, alpha-ketoglutaric semialdehyde dehydrogenase, alpha-aminoadipic semialdehyde dehydrogenase, coniferyl aldehyde dehydrogenase and succinate-semialdehyde dehydrogenase. Included in this larger group are all human, Arabidopsis, Tortula, fungal, protozoan, and Drosophila ALDHs identified in families ALDH1 through ALDH22 with the exception of families ALDH18, ALDH19, and ALDH20 which are present in the ALDH-like group. The ALDH-like group is represented by such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.


The actual alignment was detected with superfamily member cd07111:

Pssm-ID: 448367 [Multi-domain]  Cd Length: 480  Bit Score: 664.09  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653  19 YGPVPESHACALAWLDTQDRCLGHYVNGKWLKPEHRNSVPCQDPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPG 98
Cdd:cd07111    1 YGPAPESAACALAWLDAHDRSFGHFINGKWVKPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFESWSALPG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653  99 VVRAQHLTRLAEVIQKHQRLLWTLESLVTGRAVREVRDGDVQLAQQLLHYHAIQASTQEEALAGWEPMGVIGLILPPTFS 178
Cdd:cd07111   81 HVRARHLYRIARHIQKHQRLFAVLESLDNGKPIRESRDCDIPLVARHFYHHAGWAQLLDTELAGWKPVGVVGQIVPWNFP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 179 FLEMMWRICPALAVGCTVVALVPPA-SPAPLLLAQLAGELGPFPGILNVLSGPASLVPILASQPGIRKVAFCGAPE---- 253
Cdd:cd07111  161 LLMLAWKICPALAMGNTVVLKPAEYtPLTALLFAEICAEAGLPPGVLNIVTGNGSFGSALANHPGVDKVAFTGSTEvgra 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 254 --------------------------------------------------GGLRLLIQESVWDEAMRRLQERMGRLRSGR 283
Cdd:cd07111  241 lrratagtgkklslelggkspfivfddadldsavegivdaiwfnqgqvccAGSRLLVQESVAEELIRKLKERMSHLRVGD 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 284 GLDGAVDMGARGAAACDLVQRFVREAQ-SQGAQVFQAGDV-PSERPFYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTA 361
Cdd:cd07111  321 PLDKAIDMGAIVDPAQLKRIRELVEEGrAEGADVFQPGADlPSKGPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTA 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 362 KEALLVANGTPRGGSASVWSERLGQALELGYGLQVGTVWINAHGLRDPSVPTGGCKESGCSWHGGPDGLYEYLRPSGTPA 441
Cdd:cd07111  401 KEAVALANNTPYGLAASVWSENLSLALEVALSLKAGVVWINGHNLFDAAAGFGGYRESGFGREGGKEGLYEYLRPSWEPA 480
AdhE super family cl43307
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ...
474-716 7.07e-32

Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and metabolism]; Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase is part of the Pathway/BioSystem: Proline degradation


The actual alignment was detected with superfamily member COG1012:

Pssm-ID: 440636 [Multi-domain]  Cd Length: 479  Bit Score: 129.86  E-value: 7.07e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 474 APPYGLFVGGRFQAPGARSSRPIRD-SSGNLHGYVAEGGAKDIRGAVEAAHQAFPGWAGQSPgaraallwalaaaLERRK 552
Cdd:COG1012    3 TPEYPLFIGGEWVAAASGETFDVINpATGEVLARVPAATAEDVDAAVAAARAAFPAWAATPP-------------AERAA 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 553 --STLASRLER------------QGAELKAAEAEVELSARRLR-AWGARVQAQGHTLQVAGLRGPVLRLREPLGVLAVVC 617
Cdd:COG1012   70 ilLRAADLLEErreelaalltleTGKPLAEARGEVDRAADFLRyYAGEARRLYGETIPSDAPGTRAYVRREPLGVVGAIT 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 618 PDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLALEVCQDMATV-FPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGS 696
Cdd:COG1012  150 PWNFPLALAAWKLAPALAAGNTVVLKPAEQTPLSALLLAELLEEAgLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGS 229
                        250       260
                 ....*....|....*....|.
gi 223972653 697 AQ-GSQFVEWAsAGNLKPVWA 716
Cdd:COG1012  230 TAvGRRIAAAA-AENLKRVTL 249
 
Name Accession Description Interval E-value
ALDH_F16 cd07111
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ...
19-441 0e+00

Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 member A1 (ALDH16A1) and other related sequences are present in this CD. The active site cysteine and glutamate residues are not conserved in the human ALDH16A1 protein sequence.


Pssm-ID: 143429 [Multi-domain]  Cd Length: 480  Bit Score: 664.09  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653  19 YGPVPESHACALAWLDTQDRCLGHYVNGKWLKPEHRNSVPCQDPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPG 98
Cdd:cd07111    1 YGPAPESAACALAWLDAHDRSFGHFINGKWVKPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFESWSALPG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653  99 VVRAQHLTRLAEVIQKHQRLLWTLESLVTGRAVREVRDGDVQLAQQLLHYHAIQASTQEEALAGWEPMGVIGLILPPTFS 178
Cdd:cd07111   81 HVRARHLYRIARHIQKHQRLFAVLESLDNGKPIRESRDCDIPLVARHFYHHAGWAQLLDTELAGWKPVGVVGQIVPWNFP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 179 FLEMMWRICPALAVGCTVVALVPPA-SPAPLLLAQLAGELGPFPGILNVLSGPASLVPILASQPGIRKVAFCGAPE---- 253
Cdd:cd07111  161 LLMLAWKICPALAMGNTVVLKPAEYtPLTALLFAEICAEAGLPPGVLNIVTGNGSFGSALANHPGVDKVAFTGSTEvgra 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 254 --------------------------------------------------GGLRLLIQESVWDEAMRRLQERMGRLRSGR 283
Cdd:cd07111  241 lrratagtgkklslelggkspfivfddadldsavegivdaiwfnqgqvccAGSRLLVQESVAEELIRKLKERMSHLRVGD 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 284 GLDGAVDMGARGAAACDLVQRFVREAQ-SQGAQVFQAGDV-PSERPFYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTA 361
Cdd:cd07111  321 PLDKAIDMGAIVDPAQLKRIRELVEEGrAEGADVFQPGADlPSKGPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTA 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 362 KEALLVANGTPRGGSASVWSERLGQALELGYGLQVGTVWINAHGLRDPSVPTGGCKESGCSWHGGPDGLYEYLRPSGTPA 441
Cdd:cd07111  401 KEAVALANNTPYGLAASVWSENLSLALEVALSLKAGVVWINGHNLFDAAAGFGGYRESGFGREGGKEGLYEYLRPSWEPA 480
AdhE COG1012
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ...
40-436 4.31e-71

Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and metabolism]; Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase is part of the Pathway/BioSystem: Proline degradation


Pssm-ID: 440636 [Multi-domain]  Cd Length: 479  Bit Score: 240.41  E-value: 4.31e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653  40 LGHYVNGKWLKPEHRNSVPCQDPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLL 119
Cdd:COG1012    6 YPLFIGGEWVAAASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERREEL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 120 WTLESLVTGRAVREVRdGDVQLAQQLLHYHA-----IQASTQEEALAG------WEPMGVIGLILPPTFSFLEMMWRICP 188
Cdd:COG1012   86 AALLTLETGKPLAEAR-GEVDRAADFLRYYAgearrLYGETIPSDAPGtrayvrREPLGVVGAITPWNFPLALAAWKLAP 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 189 ALAVGCTVValVPPASPAPL---LLAQLAGELGPFPGILNVLSGPAS-LVPILASQPGIRKVAFCGAPE----------- 253
Cdd:COG1012  165 ALAAGNTVV--LKPAEQTPLsalLLAELLEEAGLPAGVLNVVTGDGSeVGAALVAHPDVDKISFTGSTAvgrriaaaaae 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 254 ---------GGL----------------------------------RLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVD 290
Cdd:COG1012  243 nlkrvtlelGGKnpaivlddadldaaveaavrgafgnagqrctaasRLLVHESIYDEFVERLVAAAKALKVGDPLDPGTD 322
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 291 MGAR-GAAACDLVQRFVREAQSQGAQVFQAGDVPSERP--FYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLV 367
Cdd:COG1012  323 MGPLiSEAQLERVLAYIEDAVAEGAELLTGGRRPDGEGgyFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAIAL 402
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 368 ANGTPRGGSASVWSERLGQALELGYGLQVGTVWINAHGL-RDPSVPTGGCKESGCSWHGGPDGLYEYLRP 436
Cdd:COG1012  403 ANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTgAVPQAPFGGVKQSGIGREGGREGLEEYTET 472
Aldedh pfam00171
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ...
48-435 7.49e-67

Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. Members use NADP as a cofactor. The family includes the following members: The prototypical members are the aldehyde dehydrogenases EC:1.2.1.3. Succinate-semialdehyde dehydrogenase EC:1.2.1.16. Lactaldehyde dehydrogenase EC:1.2.1.22. Benzaldehyde dehydrogenase EC:1.2.1.28. Methylmalonate-semialdehyde dehydrogenase EC:1.2.1.27. Glyceraldehyde-3-phosphate dehydrogenase EC:1.2.1.9. Delta-1-pyrroline-5-carboxylate dehydrogenase EC: 1.5.1.12. Acetaldehyde dehydrogenase EC:1.2.1.10. Glutamate-5-semialdehyde dehydrogenase EC:1.2.1.41. This family also includes omega crystallin, an eye lens protein from squid and octopus that has little aldehyde dehydrogenase activity.


Pssm-ID: 425500 [Multi-domain]  Cd Length: 459  Bit Score: 228.18  E-value: 7.49e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653   48 WLKPEHRnSVPCQDPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTLESLVT 127
Cdd:pfam00171   1 WVDSESE-TIEVINPATGEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLEN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653  128 GRAVREVRdGDVQLAQQLLHYHA----------IQASTQEEALAGWEPMGVIGLILPPTFSFLEMMWRICPALAVGCTVV 197
Cdd:pfam00171  80 GKPLAEAR-GEVDRAIDVLRYYAglarrldgetLPSDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVV 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653  198 alVPPASPAPL---LLAQLAGELGPFPGILNVLSGPASLV-PILASQPGIRKVAFCGAPE-------------------- 253
Cdd:pfam00171 159 --LKPSELTPLtalLLAELFEEAGLPAGVLNVVTGSGAEVgEALVEHPDVRKVSFTGSTAvgrhiaeaaaqnlkrvtlel 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653  254 GGL----------------------------------RLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMGA-RGAAA 298
Cdd:pfam00171 237 GGKnplivledadldaaveaavfgafgnagqvctatsRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPlISKAQ 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653  299 CDLVQRFVREAQSQGAQVFQAGDVPSERP-FYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVANGTPRGGSA 377
Cdd:pfam00171 317 LERVLKYVEDAKEEGAKLLTGGEAGLDNGyFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAA 396
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 223972653  378 SVWSERLGQALELGYGLQVGTVWINAHGLRDP-SVPTGGCKESGCSWHGGPDGLYEYLR 435
Cdd:pfam00171 397 GVFTSDLERALRVARRLEAGMVWINDYTTGDAdGLPFGGFKQSGFGREGGPYGLEEYTE 455
PRK13473 PRK13473
aminobutyraldehyde dehydrogenase;
43-420 1.87e-47

aminobutyraldehyde dehydrogenase;


Pssm-ID: 237391  Cd Length: 475  Bit Score: 175.10  E-value: 1.87e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653  43 YVNGKWLKPEHRnSVPCQDPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTL 122
Cdd:PRK13473   6 LINGELVAGEGE-KQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEFARL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 123 ESLVTGRAVREVRDGDVQLAQQLLHYHA-----IQASTQEEALAGW------EPMGVIGLILPPTFSFLEMMWRICPALA 191
Cdd:PRK13473  85 ESLNCGKPLHLALNDEIPAIVDVFRFFAgaarcLEGKAAGEYLEGHtsmirrDPVGVVASIAPWNYPLMMAAWKLAPALA 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 192 VGCTVValVPPASPAP---LLLAQLAGELGPfPGILNVLSGPASLV-PILASQPGIRKVAFCG----------------- 250
Cdd:PRK13473 165 AGNTVV--LKPSEITPltaLKLAELAADILP-PGVLNVVTGRGATVgDALVGHPKVRMVSLTGsiatgkhvlsaaadsvk 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 251 ---------AP-----------------EGGL-----------RLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMGA 293
Cdd:PRK13473 242 rthlelggkAPvivfddadldavvegirTFGYynagqdctaacRIYAQRGIYDDLVAKLAAAVATLKVGDPDDEDTELGP 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 294 R-GAAACDLVQRFVREAQSQGAQVFQAGDVPSERP--FYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVANG 370
Cdd:PRK13473 322 LiSAAHRDRVAGFVERAKALGHIRVVTGGEAPDGKgyYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDEDQAVRWAND 401
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|
gi 223972653 371 TPRGGSASVWSERLGQALELGYGLQVGTVWINAHGLRDPSVPTGGCKESG 420
Cdd:PRK13473 402 SDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKQSG 451
AdhE COG1012
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ...
474-716 7.07e-32

Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and metabolism]; Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase is part of the Pathway/BioSystem: Proline degradation


Pssm-ID: 440636 [Multi-domain]  Cd Length: 479  Bit Score: 129.86  E-value: 7.07e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 474 APPYGLFVGGRFQAPGARSSRPIRD-SSGNLHGYVAEGGAKDIRGAVEAAHQAFPGWAGQSPgaraallwalaaaLERRK 552
Cdd:COG1012    3 TPEYPLFIGGEWVAAASGETFDVINpATGEVLARVPAATAEDVDAAVAAARAAFPAWAATPP-------------AERAA 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 553 --STLASRLER------------QGAELKAAEAEVELSARRLR-AWGARVQAQGHTLQVAGLRGPVLRLREPLGVLAVVC 617
Cdd:COG1012   70 ilLRAADLLEErreelaalltleTGKPLAEARGEVDRAADFLRyYAGEARRLYGETIPSDAPGTRAYVRREPLGVVGAIT 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 618 PDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLALEVCQDMATV-FPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGS 696
Cdd:COG1012  150 PWNFPLALAAWKLAPALAAGNTVVLKPAEQTPLSALLLAELLEEAgLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGS 229
                        250       260
                 ....*....|....*....|.
gi 223972653 697 AQ-GSQFVEWAsAGNLKPVWA 716
Cdd:COG1012  230 TAvGRRIAAAA-AENLKRVTL 249
ALDH_F1-2_Ald2-like cd07091
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ...
476-714 6.44e-25

ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD+-dependent retinal dehydrogenase 1 and related proteins; ALDH subfamily which includes the NAD+-dependent retinal dehydrogenase 1 (RALDH 1, ALDH1, EC=1.2.1.36), also known as aldehyde dehydrogenase family 1 member A1 (ALDH1A1), in humans, a homotetrameric, cytosolic enzyme that catalyzes the oxidation of retinaldehyde to retinoic acid. Human ALDH1B1 and ALDH2 are also in this cluster; both are mitochrondrial homotetramers which play important roles in acetaldehyde oxidation; ALDH1B1 in response to UV light exposure and ALDH2 during ethanol metabolism. 10-formyltetrahydrofolate dehydrogenase (FTHFDH, EC=1.5.1.6), also known as aldehyde dehydrogenase family 1 member L1 (ALDH1L1), in humans, a multi-domain homotetramer with an N-terminal formyl transferase domain and a C-terminal ALDH domain. FTHFDH catalyzes an NADP+-dependent dehydrogenase reaction resulting in the conversion of 10-formyltetrahydrofolate to tetrahydrofolate and CO2. Also included in this subfamily is the Arabidosis aldehyde dehydrogenase family 2 members B4 and B7 (EC=1.2.1.3), which are mitochondrial, homotetramers that oxidize acetaldehyde and glycolaldehyde, as well as, the Arabidosis cytosolic, homotetramer ALDH2C4 (EC=1.2.1.3), an enzyme involved in the oxidation of sinapalehyde and coniferaldehyde. Also included is the AldA aldehyde dehydrogenase of Aspergillus nidulans (locus AN0554), the aldehyde dehydrogenase 2 (YMR170c, ALD5, EC=1.2.1.5) of Saccharomyces cerevisiae, and other similar sequences.


Pssm-ID: 143410  Cd Length: 476  Bit Score: 108.84  E-value: 6.44e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 476 PYGLFVGGRF-QAPGARSSRPIRDSSGNLHGYVAEGGAKDIRGAVEAAHQAFPGWAGQSpgaraallwalAAALERRK-- 552
Cdd:cd07091    3 PTGLFINNEFvDSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFETGWWRK-----------MDPRERGRll 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 553 STLASRLERQGAELKAAEA-------------EVELSARRLR---AWGARVQaqGHTLQVAGlRGPVLRLREPLGVLAVV 616
Cdd:cd07091   72 NKLADLIERDRDELAALESldngkpleesakgDVALSIKCLRyyaGWADKIQ--GKTIPIDG-NFLAYTRREPIGVCGQI 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 617 CPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLALEVCQDMATV-FPAGLANVVTGDRDHLTRCLALHQDVQAMWYFG 695
Cdd:cd07091  149 IPWNFPLLMLAWKLAPALAAGNTVVLKPAEQTPLSALYLAELIKEAgFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTG 228
                        250       260
                 ....*....|....*....|
gi 223972653 696 S-AQGSQFVEWASAGNLKPV 714
Cdd:cd07091  229 StAVGRTIMEAAAKSNLKKV 248
Aldedh pfam00171
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ...
505-714 8.12e-24

Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. Members use NADP as a cofactor. The family includes the following members: The prototypical members are the aldehyde dehydrogenases EC:1.2.1.3. Succinate-semialdehyde dehydrogenase EC:1.2.1.16. Lactaldehyde dehydrogenase EC:1.2.1.22. Benzaldehyde dehydrogenase EC:1.2.1.28. Methylmalonate-semialdehyde dehydrogenase EC:1.2.1.27. Glyceraldehyde-3-phosphate dehydrogenase EC:1.2.1.9. Delta-1-pyrroline-5-carboxylate dehydrogenase EC: 1.5.1.12. Acetaldehyde dehydrogenase EC:1.2.1.10. Glutamate-5-semialdehyde dehydrogenase EC:1.2.1.41. This family also includes omega crystallin, an eye lens protein from squid and octopus that has little aldehyde dehydrogenase activity.


Pssm-ID: 425500 [Multi-domain]  Cd Length: 459  Bit Score: 105.31  E-value: 8.12e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653  505 GYVAEGGAKDIRGAVEAAHQAFPGWAGQSPGARAALLWALAAALERRKSTLAsRLER--QGAELKAAEAEVELSARRLRA 582
Cdd:pfam00171  21 ATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELA-ELETleNGKPLAEARGEVDRAIDVLRY 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653  583 W-GARVQAQGHTLQVAGLRGPVLRlREPLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLALEVCQDMAT 661
Cdd:pfam00171 100 YaGLARRLDGETLPSDPGRLAYTR-REPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPSELTPLTALLLAELFEE 178
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 223972653  662 V-FPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGSAQ-GSQFVEwASAGNLKPV 714
Cdd:pfam00171 179 AgLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAvGRHIAE-AAAQNLKRV 232
PRK13473 PRK13473
aminobutyraldehyde dehydrogenase;
476-712 1.16e-22

aminobutyraldehyde dehydrogenase;


Pssm-ID: 237391  Cd Length: 475  Bit Score: 101.91  E-value: 1.16e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 476 PYGLFVGGRFQAPGARSSRPIRDSSGNLHGYVAEGGAKDIRGAVEAAHQAFPGWAGQSPGaraallwalaaalERRKS-- 553
Cdd:PRK13473   2 QTKLLINGELVAGEGEKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPK-------------ERAEAll 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 554 TLASRLERQGAELKAAEA-------------EVELSARRLR--AWGARVQ--------AQGHTLQVaglrgpvlRlREPL 610
Cdd:PRK13473  69 KLADAIEENADEFARLESlncgkplhlalndEIPAIVDVFRffAGAARCLegkaageyLEGHTSMI--------R-RDPV 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 611 GVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLALEVCQDMATVFPAGLANVVTGDRDHLTRCLALHQDVQA 690
Cdd:PRK13473 140 GVVASIAPWNYPLMMAAWKLAPALAAGNTVVLKPSEITPLTALKLAELAADILPPGVLNVVTGRGATVGDALVGHPKVRM 219
                        250       260
                 ....*....|....*....|...
gi 223972653 691 MWYFGS-AQGSQFVEwASAGNLK 712
Cdd:PRK13473 220 VSLTGSiATGKHVLS-AAADSVK 241
D1pyr5carbox3 TIGR01238
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ...
505-713 1.02e-08

delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents one of several related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. Members of this branch are the C-terminal domain of the PutA bifunctional proline dehydrogenase / delta-1-pyrroline-5-carboxylate dehydrogenase. [Energy metabolism, Amino acids and amines]


Pssm-ID: 273518 [Multi-domain]  Cd Length: 500  Bit Score: 58.38  E-value: 1.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653  505 GYVAEGGAKDIRGAVEAAHQAFPGWAGQSPGARAALLWALAAALERRKSTLASRLERQ-GAELKAAEAEVELSARRLRAW 583
Cdd:TIGR01238  66 GQVFHANLAHVQAAIDSAQQAFPTWNATPAKERAAKLDRLADLLELHMPELMALCVREaGKTIHNAIAEVREAVDFCRYY 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653  584 GARVQaqgHTLQVAGLRgpvlrlrePLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLALEVCQDMATV- 662
Cdd:TIGR01238 146 AKQVR---DVLGEFSVE--------SRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQEAg 214
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 223972653  663 FPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGSAQGSQFVEWASAGNLKP 713
Cdd:TIGR01238 215 FPAGTIQLLPGRGADVGAALTSDPRIAGVAFTGSTEVAQLINQTLAQREDA 265
 
Name Accession Description Interval E-value
ALDH_F16 cd07111
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ...
19-441 0e+00

Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 member A1 (ALDH16A1) and other related sequences are present in this CD. The active site cysteine and glutamate residues are not conserved in the human ALDH16A1 protein sequence.


Pssm-ID: 143429 [Multi-domain]  Cd Length: 480  Bit Score: 664.09  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653  19 YGPVPESHACALAWLDTQDRCLGHYVNGKWLKPEHRNSVPCQDPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPG 98
Cdd:cd07111    1 YGPAPESAACALAWLDAHDRSFGHFINGKWVKPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFESWSALPG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653  99 VVRAQHLTRLAEVIQKHQRLLWTLESLVTGRAVREVRDGDVQLAQQLLHYHAIQASTQEEALAGWEPMGVIGLILPPTFS 178
Cdd:cd07111   81 HVRARHLYRIARHIQKHQRLFAVLESLDNGKPIRESRDCDIPLVARHFYHHAGWAQLLDTELAGWKPVGVVGQIVPWNFP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 179 FLEMMWRICPALAVGCTVVALVPPA-SPAPLLLAQLAGELGPFPGILNVLSGPASLVPILASQPGIRKVAFCGAPE---- 253
Cdd:cd07111  161 LLMLAWKICPALAMGNTVVLKPAEYtPLTALLFAEICAEAGLPPGVLNIVTGNGSFGSALANHPGVDKVAFTGSTEvgra 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 254 --------------------------------------------------GGLRLLIQESVWDEAMRRLQERMGRLRSGR 283
Cdd:cd07111  241 lrratagtgkklslelggkspfivfddadldsavegivdaiwfnqgqvccAGSRLLVQESVAEELIRKLKERMSHLRVGD 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 284 GLDGAVDMGARGAAACDLVQRFVREAQ-SQGAQVFQAGDV-PSERPFYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTA 361
Cdd:cd07111  321 PLDKAIDMGAIVDPAQLKRIRELVEEGrAEGADVFQPGADlPSKGPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTA 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 362 KEALLVANGTPRGGSASVWSERLGQALELGYGLQVGTVWINAHGLRDPSVPTGGCKESGCSWHGGPDGLYEYLRPSGTPA 441
Cdd:cd07111  401 KEAVALANNTPYGLAASVWSENLSLALEVALSLKAGVVWINGHNLFDAAAGFGGYRESGFGREGGKEGLYEYLRPSWEPA 480
ALDH cd07078
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ...
87-437 1.42e-104

NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of NAD(P)+ dependent enzymes, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. Besides aldehyde detoxification, many ALDH isozymes possess multiple additional catalytic and non-catalytic functions such as participating in metabolic pathways, or as binding proteins, or as osmoregulants, to mention a few. The enzyme has three domains, a NAD(P)+ cofactor-binding domain, a catalytic domain, and a bridging domain; and the active enzyme is generally either homodimeric or homotetrameric. The catalytic mechanism is proposed to involve cofactor binding, resulting in a conformational change and activation of an invariant catalytic cysteine nucleophile. The cysteine and aldehyde substrate form an oxyanion thiohemiacetal intermediate resulting in hydride transfer to the cofactor and formation of a thioacylenzyme intermediate. Hydrolysis of the thioacylenzyme and release of the carboxylic acid product occurs, and in most cases, the reduced cofactor dissociates from the enzyme. The evolutionary phylogenetic tree of ALDHs appears to have an initial bifurcation between what has been characterized as the classical aldehyde dehydrogenases, the ALDH family (ALDH) and extended family members or aldehyde dehydrogenase-like (ALDH-like) proteins. The ALDH proteins are represented by enzymes which share a number of highly conserved residues necessary for catalysis and cofactor binding and they include such proteins as retinal dehydrogenase, 10-formyltetrahydrofolate dehydrogenase, non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase, delta(1)-pyrroline-5-carboxylate dehydrogenases, alpha-ketoglutaric semialdehyde dehydrogenase, alpha-aminoadipic semialdehyde dehydrogenase, coniferyl aldehyde dehydrogenase and succinate-semialdehyde dehydrogenase. Included in this larger group are all human, Arabidopsis, Tortula, fungal, protozoan, and Drosophila ALDHs identified in families ALDH1 through ALDH22 with the exception of families ALDH18, ALDH19, and ALDH20 which are present in the ALDH-like group.


Pssm-ID: 143397 [Multi-domain]  Cd Length: 432  Bit Score: 327.24  E-value: 1.42e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653  87 RMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTLESLVTGRAVREVRdGDVQLAQQLLHYHAIQAST----------- 155
Cdd:cd07078    8 RAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEAL-GEVARAADTFRYYAGLARRlhgevipspdp 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 156 QEEALAGWEPMGVIGLILPPTFSFLEMMWRICPALAVGCTVVALVPPASP-APLLLAQLAGELGPFPGILNVLSGPASLV 234
Cdd:cd07078   87 GELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPlTALLLAELLAEAGLPPGVLNVVTGDGDEV 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 235 -PILASQPGIRKVAFCGAPEGG------------------------------------------------------LRLL 259
Cdd:cd07078  167 gAALASHPRVDKISFTGSTAVGkaimraaaenlkrvtlelggksplivfddadldaavkgavfgafgnagqvctaaSRLL 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 260 IQESVWDEAMRRLQERMGRLRSGRGLDGAVDMGAR-GAAACDLVQRFVREAQSQGAQVFQAGDVPSERP--FYPPTLVSN 336
Cdd:cd07078  247 VHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLiSAAQLDRVLAYIEDAKAEGAKLLCGGKRLEGGKgyFVPPTVLTD 326
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 337 LPPASPCAQVEVPWPVVVASPFRTAKEALLVANGTPRGGSASVWSERLGQALELGYGLQVGTVWINAHGL-RDPSVPTGG 415
Cdd:cd07078  327 VDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSVgAEPSAPFGG 406
                        410       420
                 ....*....|....*....|..
gi 223972653 416 CKESGCSWHGGPDGLYEYLRPS 437
Cdd:cd07078  407 VKQSGIGREGGPYGLEEYTEPK 428
ALDH-SF cd06534
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ...
87-437 5.39e-76

NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily (ALDH-SF) of NAD(P)+-dependent enzymes, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. Besides aldehyde detoxification, many ALDH isozymes possess multiple additional catalytic and non-catalytic functions such as participating in metabolic pathways, or as binding proteins, or osmoregulants, to mention a few. The enzyme has three domains, a NAD(P)+ cofactor-binding domain, a catalytic domain, and a bridging domain; and the active enzyme is generally either homodimeric or homotetrameric. The catalytic mechanism is proposed to involve cofactor binding, resulting in a conformational change and activation of an invariant catalytic cysteine nucleophile. The cysteine and aldehyde substrate form an oxyanion thiohemiacetal intermediate resulting in hydride transfer to the cofactor and formation of a thioacylenzyme intermediate. Hydrolysis of the thioacylenzyme and release of the carboxylic acid product occurs, and in most cases, the reduced cofactor dissociates from the enzyme. The evolutionary phylogenetic tree of ALDHs appears to have an initial bifurcation between what has been characterized as the classical aldehyde dehydrogenases, the ALDH family (ALDH) and extended family members or aldehyde dehydrogenase-like (ALDH-L) proteins. The ALDH proteins are represented by enzymes which share a number of highly conserved residues necessary for catalysis and cofactor binding and they include such proteins as retinal dehydrogenase, 10-formyltetrahydrofolate dehydrogenase, non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase, delta(1)-pyrroline-5-carboxylate dehydrogenases, alpha-ketoglutaric semialdehyde dehydrogenase, alpha-aminoadipic semialdehyde dehydrogenase, coniferyl aldehyde dehydrogenase and succinate-semialdehyde dehydrogenase. Included in this larger group are all human, Arabidopsis, Tortula, fungal, protozoan, and Drosophila ALDHs identified in families ALDH1 through ALDH22 with the exception of families ALDH18, ALDH19, and ALDH20 which are present in the ALDH-like group. The ALDH-like group is represented by such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.


Pssm-ID: 143395 [Multi-domain]  Cd Length: 367  Bit Score: 249.84  E-value: 5.39e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653  87 RMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTLESLVTGRAVREVRdGDVQLAQQLLHYHAIQA-----------ST 155
Cdd:cd06534    4 RAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEAL-GEVARAIDTFRYAAGLAdklggpelpspDP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 156 QEEALAGWEPMGVIGLILPPTFSFLEMMWRICPALAVGCTVVALVPPASPAP-LLLAQLAGELGPFPGILNVLSGPASLV 234
Cdd:cd06534   83 GGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTaLALAELLQEAGLPPGVVNVVPGGGDEV 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 235 -PILASQPGIRKVAFCGAPEGGLRLliqesvwdeaMRRLQERMGRLR------------SGRGLDGAVDMGARGA----- 296
Cdd:cd06534  163 gAALLSHPRVDKISFTGSTAVGKAI----------MKAAAENLKPVTlelggkspvivdEDADLDAAVEGAVFGAffnag 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 297 AACDLVQR-FVreaqsqgaqvfqagdvpsERPFYPP------TLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVAN 369
Cdd:cd06534  233 QICTAASRlLV------------------HESIYDEfveklvTVLVDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALAN 294
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 223972653 370 GTPRGGSASVWSERLGQALELGYGLQVGTVWINAHGL-RDPSVPTGGCKESGCSWHGGPDGLYEYLRPS 437
Cdd:cd06534  295 DTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIgVGPEAPFGGVKNSGIGREGGPYGLEEYTRTK 363
AdhE COG1012
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ...
40-436 4.31e-71

Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and metabolism]; Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase is part of the Pathway/BioSystem: Proline degradation


Pssm-ID: 440636 [Multi-domain]  Cd Length: 479  Bit Score: 240.41  E-value: 4.31e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653  40 LGHYVNGKWLKPEHRNSVPCQDPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLL 119
Cdd:COG1012    6 YPLFIGGEWVAAASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERREEL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 120 WTLESLVTGRAVREVRdGDVQLAQQLLHYHA-----IQASTQEEALAG------WEPMGVIGLILPPTFSFLEMMWRICP 188
Cdd:COG1012   86 AALLTLETGKPLAEAR-GEVDRAADFLRYYAgearrLYGETIPSDAPGtrayvrREPLGVVGAITPWNFPLALAAWKLAP 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 189 ALAVGCTVValVPPASPAPL---LLAQLAGELGPFPGILNVLSGPAS-LVPILASQPGIRKVAFCGAPE----------- 253
Cdd:COG1012  165 ALAAGNTVV--LKPAEQTPLsalLLAELLEEAGLPAGVLNVVTGDGSeVGAALVAHPDVDKISFTGSTAvgrriaaaaae 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 254 ---------GGL----------------------------------RLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVD 290
Cdd:COG1012  243 nlkrvtlelGGKnpaivlddadldaaveaavrgafgnagqrctaasRLLVHESIYDEFVERLVAAAKALKVGDPLDPGTD 322
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 291 MGAR-GAAACDLVQRFVREAQSQGAQVFQAGDVPSERP--FYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLV 367
Cdd:COG1012  323 MGPLiSEAQLERVLAYIEDAVAEGAELLTGGRRPDGEGgyFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAIAL 402
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 368 ANGTPRGGSASVWSERLGQALELGYGLQVGTVWINAHGL-RDPSVPTGGCKESGCSWHGGPDGLYEYLRP 436
Cdd:COG1012  403 ANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTgAVPQAPFGGVKQSGIGREGGREGLEEYTET 472
Aldedh pfam00171
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ...
48-435 7.49e-67

Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. Members use NADP as a cofactor. The family includes the following members: The prototypical members are the aldehyde dehydrogenases EC:1.2.1.3. Succinate-semialdehyde dehydrogenase EC:1.2.1.16. Lactaldehyde dehydrogenase EC:1.2.1.22. Benzaldehyde dehydrogenase EC:1.2.1.28. Methylmalonate-semialdehyde dehydrogenase EC:1.2.1.27. Glyceraldehyde-3-phosphate dehydrogenase EC:1.2.1.9. Delta-1-pyrroline-5-carboxylate dehydrogenase EC: 1.5.1.12. Acetaldehyde dehydrogenase EC:1.2.1.10. Glutamate-5-semialdehyde dehydrogenase EC:1.2.1.41. This family also includes omega crystallin, an eye lens protein from squid and octopus that has little aldehyde dehydrogenase activity.


Pssm-ID: 425500 [Multi-domain]  Cd Length: 459  Bit Score: 228.18  E-value: 7.49e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653   48 WLKPEHRnSVPCQDPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTLESLVT 127
Cdd:pfam00171   1 WVDSESE-TIEVINPATGEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLEN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653  128 GRAVREVRdGDVQLAQQLLHYHA----------IQASTQEEALAGWEPMGVIGLILPPTFSFLEMMWRICPALAVGCTVV 197
Cdd:pfam00171  80 GKPLAEAR-GEVDRAIDVLRYYAglarrldgetLPSDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVV 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653  198 alVPPASPAPL---LLAQLAGELGPFPGILNVLSGPASLV-PILASQPGIRKVAFCGAPE-------------------- 253
Cdd:pfam00171 159 --LKPSELTPLtalLLAELFEEAGLPAGVLNVVTGSGAEVgEALVEHPDVRKVSFTGSTAvgrhiaeaaaqnlkrvtlel 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653  254 GGL----------------------------------RLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMGA-RGAAA 298
Cdd:pfam00171 237 GGKnplivledadldaaveaavfgafgnagqvctatsRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPlISKAQ 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653  299 CDLVQRFVREAQSQGAQVFQAGDVPSERP-FYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVANGTPRGGSA 377
Cdd:pfam00171 317 LERVLKYVEDAKEEGAKLLTGGEAGLDNGyFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAA 396
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 223972653  378 SVWSERLGQALELGYGLQVGTVWINAHGLRDP-SVPTGGCKESGCSWHGGPDGLYEYLR 435
Cdd:pfam00171 397 GVFTSDLERALRVARRLEAGMVWINDYTTGDAdGLPFGGFKQSGFGREGGPYGLEEYTE 455
ALDH_HMSADH_HapE cd07115
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ...
61-436 1.17e-64

Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic semialdehyde dehydrogenase (HapE, EC=1.2.1.61) of Pseudomonas fluorescens ACB involved in 4-hydroxyacetophenone degradation, and putative hydroxycaproate semialdehyde dehydrogenase (ChnE) of Brachymonas petroleovorans involved in cyclohexane metabolism, and other similar sequences, are present in this CD.


Pssm-ID: 143433 [Multi-domain]  Cd Length: 453  Bit Score: 222.31  E-value: 1.17e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653  61 DPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTLESLVTGRAVREVRDGDVQ 140
Cdd:cd07115    3 NPATGELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARRLDVP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 141 LAQQLLHYHAIQASTQEEAL----AGW------EPMGVIGLILPPTFSFLEMMWRICPALAVGCTVValVPPASPAPL-- 208
Cdd:cd07115   83 RAADTFRYYAGWADKIEGEVipvrGPFlnytvrEPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVV--LKPAELTPLsa 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 209 -LLAQLAGELGPFPGILNVLSGPASLV-PILASQPGIRKVAFCGAPE--------------------------------- 253
Cdd:cd07115  161 lRIAELMAEAGFPAGVLNVVTGFGEVAgAALVEHPDVDKITFTGSTAvgrkimqgaagnlkrvslelggksanivfadad 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 254 ---------------------GGLRLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMGAR-GAAACDLVQRFVREAQS 311
Cdd:cd07115  241 ldaavraaatgifynqgqmctAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLvSQAQFDRVLDYVDVGRE 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 312 QGAQVFQAGDVPSERPFY-PPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVANGTPRGGSASVWSERLGQALEL 390
Cdd:cd07115  321 EGARLLTGGKRPGARGFFvEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGRAHRV 400
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*.
gi 223972653 391 GYGLQVGTVWINAHGLRDPSVPTGGCKESGCSWHGGPDGLYEYLRP 436
Cdd:cd07115  401 AAALKAGTVWINTYNRFDPGSPFGGYKQSGFGREMGREALDEYTEV 446
ALDH_DhaS cd07114
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ...
61-436 2.16e-61

Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized aldehyde dehydrogenase from Candidatus pelagibacter (DhaS) and other related sequences are present in this CD.


Pssm-ID: 143432 [Multi-domain]  Cd Length: 457  Bit Score: 213.57  E-value: 2.16e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653  61 DPITGENLASCLQAQAEDVAAAVEAARMAFKG--WSAHPGVVRAQHLTRLAEVIQKHQRLLWTLESLVTGRAVREVRdGD 138
Cdd:cd07114    3 NPATGEPWARVPEASAADVDRAVAAARAAFEGgaWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETR-AQ 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 139 VQLAQQLLHYHAIQASTQEEALAG-----------WEPMGVIGLILPPTFSFLEMMWRICPALAVGCTVVALVPPASPAP 207
Cdd:cd07114   82 VRYLAEWYRYYAGLADKIEGAVIPvdkgdylnftrREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPAS 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 208 LL-LAQLAGELGPFPGILNVLSGPASLVPI-LASQPGIRKVAFCGAPEG------------------------------- 254
Cdd:cd07114  162 TLeLAKLAEEAGFPPGVVNVVTGFGPETGEaLVEHPLVAKIAFTGGTETgrhiaraaaenlapvtlelggkspnivfdda 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 255 -----------------------GLRLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMG-ARGAAACDLVQRFVREAQ 310
Cdd:cd07114  242 dldaavngvvagifaaagqtcvaGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGpLATERQLEKVERYVARAR 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 311 SQGAQVFQAGDVPSERP-----FYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVANGTPRGGSASVWSERLG 385
Cdd:cd07114  322 EEGARVLTGGERPSGADlgagyFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWTRDLA 401
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|.
gi 223972653 386 QALELGYGLQVGTVWINAHGLRDPSVPTGGCKESGCSWHGGPDGLYEYLRP 436
Cdd:cd07114  402 RAHRVARAIEAGTVWVNTYRALSPSSPFGGFKDSGIGRENGIEAIREYTQT 452
ALDH_ACDHII_AcoD-like cd07559
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ...
41-420 2.14e-59

Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus AldA1 (SACOL0154)-like; Included in this CD is the NAD+-dependent, acetaldehyde dehydrogenase II (AcDHII, AcoD, EC=1.2.1.3) from Ralstonia (Alcaligenes) eutrophus H16 involved in the catabolism of acetoin and ethanol, and similar proteins, such as, the dimeric dihydrolipoamide dehydrogenase of the acetoin dehydrogenase enzyme system of Klebsiella pneumonia. Also included are sequences similar to the NAD+-dependent chloroacetaldehyde dehydrogenases (AldA and AldB) of Xanthobacter autotrophicus GJ10 which are involved in the degradation of 1,2-dichloroethane, as well as, the uncharacterized aldehyde dehydrogenase from Staphylococcus aureus (AldA1, locus SACOL0154) and other similar sequences.


Pssm-ID: 143471 [Multi-domain]  Cd Length: 480  Bit Score: 208.74  E-value: 2.14e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653  41 GHYVNGKWLKPEHRNSVPCQDPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLW 120
Cdd:cd07559    2 DNFINGEWVAPSKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 121 TLESLVTGRAVREVRDGDVQLAQQLLHYHAIQASTQEE----------ALAGWEPMGVIGLILPPTFSFLEMMWRICPAL 190
Cdd:cd07559   82 VAETLDNGKPIRETLAADIPLAIDHFRYFAGVIRAQEGslseidedtlSYHFHEPLGVVGQIIPWNFPLLMAAWKLAPAL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 191 AVGCTVValVPPASPAP---LLLAQLAGELGPfPGILNVLSGPASLV-PILASQPGIRKVAFCG---------------- 250
Cdd:cd07559  162 AAGNTVV--LKPASQTPlsiLVLMELIGDLLP-KGVVNVVTGFGSEAgKPLASHPRIAKLAFTGsttvgrlimqyaaenl 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 251 ----------------------------APEGGL---------------RLLIQESVWDEAMRRLQERMGRLRSGRGLDG 287
Cdd:cd07559  239 ipvtlelggkspniffddamdadddfddKAEEGQlgfafnqgevctcpsRALVQESIYDEFIERAVERFEAIKVGNPLDP 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 288 AVDMGAR-GAAACDLVQRFVREAQSQGAQVFQAGDVPSERP-----FYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTA 361
Cdd:cd07559  319 ETMMGAQvSKDQLEKILSYVDIGKEEGAEVLTGGERLTLGGldkgyFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFKDE 398
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 223972653 362 KEALLVANGTPRGGSASVWSERLGQALELGYGLQVGTVWINAHGLRDPSVPTGGCKESG 420
Cdd:cd07559  399 EEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQYPAHAPFGGYKKSG 457
ALDH_AldA-AAD23400 cd07106
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ...
61-436 2.47e-58

Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative aldehyde dehydrogenase, AldA, from Streptomyces aureofaciens (locus AAD23400) and other similar sequences are present in this CD.


Pssm-ID: 143424 [Multi-domain]  Cd Length: 446  Bit Score: 204.68  E-value: 2.47e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653  61 DPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTLESLVTGRAVREVRdGDVQ 140
Cdd:cd07106    3 NPATGEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQ-FEVG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 141 LAQQLLHYHA--------IQASTQEEALAGWEPMGVIGLILPPTFSFLEMMWRICPALAVGCTVVALVPPASP-APLLLA 211
Cdd:cd07106   82 GAVAWLRYTAsldlpdevIEDDDTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPlCTLKLG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 212 QLAGELGPfPGILNVLSGPASLVPILASQPGIRKVAFCGAPE--------------------GG---------------- 255
Cdd:cd07106  162 ELAQEVLP-PGVLNVVSGGDELGPALTSHPDIRKISFTGSTAtgkkvmasaaktlkrvtlelGGndaaivlpdvdidava 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 256 ------------------LRLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMG-ARGAAACDLVQRFVREAQSQGAQV 316
Cdd:cd07106  241 pklfwgafinsgqvcaaiKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGpVQNKMQYDKVKELVEDAKAKGAKV 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 317 FQAGDVPsERP--FYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVANGTPRGGSASVWSERLGQALELGYGL 394
Cdd:cd07106  321 LAGGEPL-DGPgyFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLERAEAVARRL 399
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|..
gi 223972653 395 QVGTVWINAHGLRDPSVPTGGCKESGCSWHGGPDGLYEYLRP 436
Cdd:cd07106  400 EAGTVWINTHGALDPDAPFGGHKQSGIGVEFGIEGLKEYTQT 441
ALDH_BADH-GbsA cd07119
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ...
43-434 2.00e-55

Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is the NAD+-dependent, betaine aldehyde dehydrogenase (BADH, GbsA, EC=1.2.1.8) of Bacillus subtilis involved in the synthesis of the osmoprotectant glycine betaine from choline or glycine betaine aldehyde.


Pssm-ID: 143437  Cd Length: 482  Bit Score: 197.53  E-value: 2.00e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653  43 YVNGKWLKPEHRNSVPCQDPITGENLASCLQAQAEDVAAAVEAARMAF--KGWSAHPGVVRAQHLTRLAEVIQKHQRLLW 120
Cdd:cd07119    1 YIDGEWVEAASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAFdsGEWPHLPAQERAALLFRIADKIREDAEELA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 121 TLESLVTGRAVREVRdGDVQLAQQLLHYHA----------IQASTQEEALAGWEPMGVIGLILPPTFSFLEMMWRICPAL 190
Cdd:cd07119   81 RLETLNTGKTLRESE-IDIDDVANCFRYYAglatketgevYDVPPHVISRTVREPVGVCGLITPWNYPLLQAAWKLAPAL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 191 AVGCTVValVPPASPAPLL---LAQLAGELGPFPGILNVLSGPASLV-PILASQPGIRKVAFCGAPE------------- 253
Cdd:cd07119  160 AAGNTVV--IKPSEVTPLTtiaLFELIEEAGLPAGVVNLVTGSGATVgAELAESPDVDLVSFTGGTAtgrsimraaagnv 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 254 -----------------------------------------GGLRLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMG 292
Cdd:cd07119  238 kkvalelggknpnivfadadfetavdqalngvffnagqvcsAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEMG 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 293 A-RGAAACDLVQRFVREAQSQGAQVFQAGDVPSERP-----FYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALL 366
Cdd:cd07119  318 PlVSAEHREKVLSYIQLGKEEGARLVCGGKRPTGDElakgyFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIR 397
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 223972653 367 VANGTPRGGSASVWSERLGQALELGYGLQVGTVWINAHGLRDPSVPTGGCKESGCSWHGGPDGLYEYL 434
Cdd:cd07119  398 LANDTPYGLAGAVWTKDIARANRVARRLRAGTVWINDYHPYFAEAPWGGYKQSGIGRELGPTGLEEYQ 465
ALDH_F1-2_Ald2-like cd07091
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ...
41-435 5.55e-55

ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD+-dependent retinal dehydrogenase 1 and related proteins; ALDH subfamily which includes the NAD+-dependent retinal dehydrogenase 1 (RALDH 1, ALDH1, EC=1.2.1.36), also known as aldehyde dehydrogenase family 1 member A1 (ALDH1A1), in humans, a homotetrameric, cytosolic enzyme that catalyzes the oxidation of retinaldehyde to retinoic acid. Human ALDH1B1 and ALDH2 are also in this cluster; both are mitochrondrial homotetramers which play important roles in acetaldehyde oxidation; ALDH1B1 in response to UV light exposure and ALDH2 during ethanol metabolism. 10-formyltetrahydrofolate dehydrogenase (FTHFDH, EC=1.5.1.6), also known as aldehyde dehydrogenase family 1 member L1 (ALDH1L1), in humans, a multi-domain homotetramer with an N-terminal formyl transferase domain and a C-terminal ALDH domain. FTHFDH catalyzes an NADP+-dependent dehydrogenase reaction resulting in the conversion of 10-formyltetrahydrofolate to tetrahydrofolate and CO2. Also included in this subfamily is the Arabidosis aldehyde dehydrogenase family 2 members B4 and B7 (EC=1.2.1.3), which are mitochondrial, homotetramers that oxidize acetaldehyde and glycolaldehyde, as well as, the Arabidosis cytosolic, homotetramer ALDH2C4 (EC=1.2.1.3), an enzyme involved in the oxidation of sinapalehyde and coniferaldehyde. Also included is the AldA aldehyde dehydrogenase of Aspergillus nidulans (locus AN0554), the aldehyde dehydrogenase 2 (YMR170c, ALD5, EC=1.2.1.5) of Saccharomyces cerevisiae, and other similar sequences.


Pssm-ID: 143410  Cd Length: 476  Bit Score: 196.28  E-value: 5.55e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653  41 GHYVNGKWLKPEHRNSVPCQDPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAH--PGVVRAQHLTRLAEVIQKHQRL 118
Cdd:cd07091    5 GLFINNEFVDSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFETGWWRkmDPRERGRLLNKLADLIERDRDE 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 119 LWTLESLVTGRAVREVRDGDVQLAQQLLHYHA----------IQASTQEEALAGWEPMGVIGLILPPTFSFLEMMWRICP 188
Cdd:cd07091   85 LAALESLDNGKPLEESAKGDVALSIKCLRYYAgwadkiqgktIPIDGNFLAYTRREPIGVCGQIIPWNFPLLMLAWKLAP 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 189 ALAVGCTVValVPPASPAPL---LLAQLAGELGPFPGILNVLSGPASLV-PILASQPGIRKVAFCGAPE----------- 253
Cdd:cd07091  165 ALAAGNTVV--LKPAEQTPLsalYLAELIKEAGFPPGVVNIVPGFGPTAgAAISSHMDVDKIAFTGSTAvgrtimeaaak 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 254 --------------------------------------------GGLRLLIQESVWDEAMRRLQERMGRLRSGRGLDGAV 289
Cdd:cd07091  243 snlkkvtlelggkspnivfddadldkavewaafgiffnqgqcccAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDPDT 322
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 290 DMGAR-GAAACDLVQRFVREAQSQGAQVFQAGDVPSERPFY-PPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLV 367
Cdd:cd07091  323 FQGPQvSKAQFDKILSYIESGKKEGATLLTGGERHGSKGYFiQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEVIER 402
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 223972653 368 ANGTPRGGSASVWSERLGQALELGYGLQVGTVWINAHGLRDPSVPTGGCKESGCSWHGGPDGLYEYLR 435
Cdd:cd07091  403 ANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTYNVFDAAVPFGGFKQSGFGRELGEEGLEEYTQ 470
ALDH_F8_HMSADH cd07093
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ...
61-420 1.43e-54

Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase family 8 member A1 (ALDH8A1) protein functions to convert 9-cis-retinal to 9-cis-retinoic acid and has a preference for NAD+. Also included in this CD is the 2-hydroxymuconic semialdehyde dehydrogenase (HMSADH) which catalyzes the conversion of 2-hydroxymuconic semialdehyde to 4-oxalocrotonate, a step in the meta cleavage pathway of aromatic hydrocarbons in bacteria. Such HMSADHs seen here are: XylG of the TOL plasmid pWW0 of Pseudomonas putida, TomC of Burkholderia cepacia G4, and AphC of Comamonas testosterone.


Pssm-ID: 143412 [Multi-domain]  Cd Length: 455  Bit Score: 194.71  E-value: 1.43e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653  61 DPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTLESLVTGRAVREVRDGDVQ 140
Cdd:cd07093    3 NPATGEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARTRDIP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 141 LAQQLLHYHAIQASTQE----EALAGW------EPMGVIGLILPPTFSFLEMMWRICPALAVGCTVValVPPASPAPL-- 208
Cdd:cd07093   83 RAAANFRFFADYILQLDgesyPQDGGAlnyvlrQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVV--LKPSEWTPLta 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 209 -LLAQLAGELGPFPGILNVLSGPASLV-PILASQPGIRKVAFCGAPE--------------------------------- 253
Cdd:cd07093  161 wLLAELANEAGLPPGVVNVVHGFGPEAgAALVAHPDVDLISFTGETAtgrtimraaapnlkpvslelggknpnivfadad 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 254 ---------------------GGLRLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMGARGAAA-CDLVQRFVREAQS 311
Cdd:cd07093  241 ldravdaavrssfsnngevclAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEhLEKVLGYVELARA 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 312 QGAQVFQAGDVPSERP-----FYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVANGTPRGGSASVWSERLGQ 386
Cdd:cd07093  321 EGATILTGGGRPELPDleggyFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTRDLGR 400
                        410       420       430
                 ....*....|....*....|....*....|....
gi 223972653 387 ALELGYGLQVGTVWINAHGLRDPSVPTGGCKESG 420
Cdd:cd07093  401 AHRVARRLEAGTVWVNCWLVRDLRTPFGGVKASG 434
ALDH_PADH_NahF cd07113
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ...
41-433 3.94e-54

Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, homodimeric, phenylacetaldehyde dehydrogenase (PADH, EC=1.2.1.39) PadA of Escherichia coli involved in the catabolism of 2-phenylethylamine, and other related sequences, are present in this CD. Also included is the Pseudomonas fluorescens ST StyD PADH involved in styrene catabolism, the Sphingomonas sp. LB126 FldD protein involved in fluorene degradation, and the Novosphingobium aromaticivorans NahF salicylaldehyde dehydrogenase involved in the NAD+-dependent conversion of salicylaldehyde to salicylate.


Pssm-ID: 143431  Cd Length: 477  Bit Score: 194.20  E-value: 3.94e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653  41 GHYVNGKWLKPEHRNSVPCQDPITGENLASCLQAQAEDVAAAVEAARMAFKG-WSAHPGVVRAQHLTRLAEVIQKHQRLL 119
Cdd:cd07113    1 GHFIDGRPVAGQSEKRLDITNPATEQVIASVASATEADVDAAVASAWRAFVSaWAKTTPAERGRILLRLADLIEQHGEEL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 120 WTLESLVTGRAVREVRDGDVQLAQQLLHYHAIQA-------------STQEEALAGW---EPMGVIGLILPPTFSFLEMM 183
Cdd:cd07113   81 AQLETLCSGKSIHLSRAFEVGQSANFLRYFAGWAtkingetlapsipSMQGERYTAFtrrEPVGVVAGIVPWNFSVMIAV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 184 WRICPALAVGCTVValVPPASPAPLLL---AQLAGELGPFPGILNVLSGPASLVPILASQPGIRKVAF------------ 248
Cdd:cd07113  161 WKIGAALATGCTIV--IKPSEFTPLTLlrvAELAKEAGIPDGVLNVVNGKGAVGAQLISHPDVAKVSFtgsvatgkkigr 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 249 ---------------------------------------------CGAPEgglRLLIQESVWDEAMRRLQERMGRLRSGR 283
Cdd:cd07113  239 qaasdltrvtlelggknaaaflkdadidwvveglltagflhqgqvCAAPE---RFYVHRSKFDELVTKLKQALSSFQVGS 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 284 GLDGAVDMGA-RGAAACDLVQRFVREAQSQGAQVFQAGDVPSERPFY-PPTLVSNLPPASPCAQVEVPWPVVVASPFRTA 361
Cdd:cd07113  316 PMDESVMFGPlANQPHFDKVCSYLDDARAEGDEIVRGGEALAGEGYFvQPTLVLARSADSRLMREETFGPVVSFVPYEDE 395
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 223972653 362 KEALLVANGTPRGGSASVWSERLGQALELGYGLQVGTVWINAHGLRDPSVPTGGCKESGCSWHGGPDGLYEY 433
Cdd:cd07113  396 EELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTFLDPAVPFGGMKQSGIGREFGSAFIDDY 467
ALDH_F5_SSADH_GabD cd07103
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ...
89-434 4.88e-53

Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; Succinate-semialdehyde dehydrogenase, mitochondrial (SSADH, GabD, EC=1.2.1.24) catalyzes the NAD+-dependent oxidation of succinate semialdehyde (SSA) to succinate. This group includes the human aldehyde dehydrogenase family 5 member A1 (ALDH5A1) which is a mitochondrial homotetramer that converts SSA to succinate in the last step of 4-aminobutyric acid (GABA) catabolism. This CD also includes the Arabidopsis SSADH gene product ALDH5F1. Mutations in this gene result in the accumulation of H2O2, suggesting a role in plant defense against the environmental stress of elevated reactive oxygen species.


Pssm-ID: 143421 [Multi-domain]  Cd Length: 451  Bit Score: 190.34  E-value: 4.88e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653  89 AFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTLESLVTGRAVREVRdGDVQLAQQLLHYHAiqastqEEA--LAG---- 162
Cdd:cd07103   31 AFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEAR-GEVDYAASFLEWFA------EEArrIYGrtip 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 163 -----------WEPMGVIGLILPPTFSFLeMMWR-ICPALAVGCTVValVPPASPAP---LLLAQLAGELGPFPGILNVL 227
Cdd:cd07103  104 spapgkrilviKQPVGVVAAITPWNFPAA-MITRkIAPALAAGCTVV--LKPAEETPlsaLALAELAEEAGLPAGVLNVV 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 228 SG-PASLVPILASQPGIRKVAFCG--------------------------AP-------------EGGL----------- 256
Cdd:cd07103  181 TGsPAEIGEALCASPRVRKISFTGstavgkllmaqaadtvkrvslelggnAPfivfddadldkavDGAIaskfrnagqtc 260
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 257 ----RLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMGAR-GAAACDLVQRFVREAQSQGAQVFQAGDVPSERP-FYP 330
Cdd:cd07103  261 vcanRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLiNERAVEKVEALVEDAVAKGAKVLTGGKRLGLGGyFYE 340
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 331 PTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVANGTPRGGSASVWSERLGQALELGYGLQVGTVWINAHGLRDPS 410
Cdd:cd07103  341 PTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDLARAWRVAEALEAGMVGINTGLISDAE 420
                        410       420
                 ....*....|....*....|....
gi 223972653 411 VPTGGCKESGCSWHGGPDGLYEYL 434
Cdd:cd07103  421 APFGGVKESGLGREGGKEGLEEYL 444
ALDH_ABALDH-YdcW cd07092
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ...
61-436 6.17e-53

Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD+-dependent, tetrameric, gamma-aminobutyraldehyde dehydrogenase (ABALDH), YdcW of Escherichia coli K12, catalyzes the oxidation of gamma-aminobutyraldehyde to gamma-aminobutyric acid. ABALDH can also oxidize n-alkyl medium-chain aldehydes, but with a lower catalytic efficiency.


Pssm-ID: 143411 [Multi-domain]  Cd Length: 450  Bit Score: 189.85  E-value: 6.17e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653  61 DPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTLESLVTGRAVREVRDGDVQ 140
Cdd:cd07092    3 DPATGEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRDDELP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 141 LAQQLLHYHAIQASTQEEALAG-----------WEPMGVIGLILPPTFSFLEMMWRICPALAVGCTVValVPPASPAP-- 207
Cdd:cd07092   83 GAVDNFRFFAGAARTLEGPAAGeylpghtsmirREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVV--LKPSETTPlt 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 208 -LLLAQLAGELGPfPGILNVLSGPASLV-PILASQPGIRKVAFCGAPEGGL----------------------------- 256
Cdd:cd07092  161 tLLLAELAAEVLP-PGVVNVVCGGGASAgDALVAHPRVRMVSLTGSVRTGKkvaraaadtlkrvhlelggkapvivfdda 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 257 -------------------------RLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMGARGAAA-CDLVQRFVREAq 310
Cdd:cd07092  240 dldaavagiatagyynagqdctaacRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAqRERVAGFVERA- 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 311 SQGAQVFQAGDVPSERP-FYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVANGTPRGGSASVWSERLGQALE 389
Cdd:cd07092  319 PAHARVLTGGRRAEGPGyFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDVGRAMR 398
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*..
gi 223972653 390 LGYGLQVGTVWINAHGLRDPSVPTGGCKESGCSWHGGPDGLYEYLRP 436
Cdd:cd07092  399 LSARLDFGTVWVNTHIPLAAEMPHGGFKQSGYGKDLSIYALEDYTRI 445
ALDH_GABALDH-PuuC cd07112
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ...
58-420 1.02e-51

Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase PuuC-like; NADP+-dependent, gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase (GABALDH) PuuC of Escherichia coli which catalyzes the conversion of putrescine to 4-aminobutanoate and other similar sequences are present in this CD.


Pssm-ID: 143430 [Multi-domain]  Cd Length: 462  Bit Score: 187.04  E-value: 1.02e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653  58 PCQDPITGENLASCLQAQAEDVAAAVEAARMAFKG--WSAHPGVVRAQHLTRLAEVIQKHQRLLWTLESLVTGRAVREVR 135
Cdd:cd07112    5 ATINPATGRVLAEVAACDAADVDRAVAAARRAFESgvWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPISDAL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 136 DGDVQLAQQLLHYHA--IQ------ASTQEEALA--GWEPMGVIGLILPPTFSFLEMMWRICPALAVGCTVValVPPASP 205
Cdd:cd07112   85 AVDVPSAANTFRWYAeaIDkvygevAPTGPDALAliTREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVV--LKPAEQ 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 206 APL---LLAQLAGELGPFPGILNVLSGPASLV-PILASQPGIRKVAFCGAPE---------------------------- 253
Cdd:cd07112  163 SPLtalRLAELALEAGLPAGVLNVVPGFGHTAgEALGLHMDVDALAFTGSTEvgrrfleysgqsnlkrvwlecggkspni 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 254 ----------------------------GGLRLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMGAR-GAAACDLVQR 304
Cdd:cd07112  243 vfadapdldaaaeaaaagifwnqgevcsAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALvSEAHFDKVLG 322
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 305 FVREAQSQGAQVFQAGDVPSERP---FYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVANGTPRGGSASVWS 381
Cdd:cd07112  323 YIESGKAEGARLVAGGKRVLTETggfFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAASVWT 402
                        410       420       430
                 ....*....|....*....|....*....|....*....
gi 223972653 382 ERLGQALELGYGLQVGTVWINAHGLRDPSVPTGGCKESG 420
Cdd:cd07112  403 SDLSRAHRVARRLRAGTVWVNCFDEGDITTPFGGFKQSG 441
ALDH_StaphAldA1 cd07117
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ...
41-420 2.86e-50

Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; Uncharacterized aldehyde dehydrogenase from Staphylococcus aureus (AldA1, locus SACOL0154) and other similar sequences are present in this CD.


Pssm-ID: 143435  Cd Length: 475  Bit Score: 183.04  E-value: 2.86e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653  41 GHYVNGKWLKPEHRNSVPCQDPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLW 120
Cdd:cd07117    2 GLFINGEWVKGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 121 TLESLVTGRAVREVRDGDVQLAQQLLHYHA--IQAST--------QEEALAGWEPMGVIGLILPPTFSFLEMMWRICPAL 190
Cdd:cd07117   82 MVETLDNGKPIRETRAVDIPLAADHFRYFAgvIRAEEgsanmideDTLSIVLREPIGVVGQIIPWNFPFLMAAWKLAPAL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 191 AVGCTVValVPPASPAP---LLLAQLAGELGPfPGILNVLSGPASLV-PILASQPGIRKVAFCG---------------- 250
Cdd:cd07117  162 AAGNTVV--IKPSSTTSlslLELAKIIQDVLP-KGVVNIVTGKGSKSgEYLLNHPGLDKLAFTGstevgrdvaiaaakkl 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 251 -----------------------APEG---------------GLRLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMG 292
Cdd:cd07117  239 ipatlelggksaniifddanwdkALEGaqlgilfnqgqvccaGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQMG 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 293 AR-GAAACDLVQRFVREAQSQGAQVFQAGDVPSERP-----FYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALL 366
Cdd:cd07117  319 AQvNKDQLDKILSYVDIAKEEGAKILTGGHRLTENGldkgfFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEVID 398
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....
gi 223972653 367 VANGTPRGGSASVWSERLGQALELGYGLQVGTVWINAHGLRDPSVPTGGCKESG 420
Cdd:cd07117  399 MANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTYNQIPAGAPFGGYKKSG 452
ALDH_AAS00426 cd07109
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ...
61-435 1.12e-49

Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; Uncharacterized aldehyde dehydrogenase of Saccharopolyspora spinosa (AAS00426) and other similar sequences, are present in this CD.


Pssm-ID: 143427 [Multi-domain]  Cd Length: 454  Bit Score: 180.89  E-value: 1.12e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653  61 DPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAH-PGVVRAQHLTRLAEVIQKHQRLLWTLESLVTGRAVREVRdGDV 139
Cdd:cd07109    3 DPSTGEVFARIARGGAADVDRAVQAARRAFESGWLRlSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQAR-ADV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 140 QLAQQLLHYHAIQAST-------QEEALAGW---EPMGVIGLILPPTFSfLEMMWR-ICPALAVGCTVValVPPASPAPL 208
Cdd:cd07109   82 EAAARYFEYYGGAADKlhgetipLGPGYFVYtvrEPHGVTGHIIPWNYP-LQITGRsVAPALAAGNAVV--VKPAEDAPL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 209 ---LLAQLAGELGPFPGILNVLSG-PASLVPILASQPGIRKVAFCGAPEGGL---------------------------- 256
Cdd:cd07109  159 talRLAELAEEAGLPAGALNVVTGlGAEAGAALVAHPGVDHISFTGSVETGIavmraaaenvvpvtlelggkspqivfad 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 257 --------------------------RLLIQESVWDEAMRRLQERMGRLRSGRGLDGaVDMGA-RGAAACDLVQRFVREA 309
Cdd:cd07109  239 adleaalpvvvnaiiqnagqtcsagsRLLVHRSIYDEVLERLVERFRALRVGPGLED-PDLGPlISAKQLDRVEGFVARA 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 310 QSQGAQVFQAGDVPSERP----FYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVANGTPRGGSASVWSERLG 385
Cdd:cd07109  318 RARGARIVAGGRIAEGAPaggyFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDGD 397
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....
gi 223972653 386 QALELGYGLQVGTVWINAHGLRDP-SVPTGGCKESGcswHG---GPDGLYEYLR 435
Cdd:cd07109  398 RALRVARRLRAGQVFVNNYGAGGGiELPFGGVKKSG---HGrekGLEALYNYTQ 448
ALDH_AldA_AN0554 cd07143
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ...
40-433 1.66e-48

Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde dehydrogenase (AldA) of Aspergillus nidulans (locus AN0554), and other similar sequences, are present in this CD.


Pssm-ID: 143461  Cd Length: 481  Bit Score: 178.49  E-value: 1.66e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653  40 LGHYVNGKWLKPEHRNSVPCQDPITGENLASCLQAQAEDVAAAVEAARMAFKG-WSAH-PGVVRAQHLTRLAEVIQKHQR 117
Cdd:cd07143    7 TGLFINGEFVDSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAFETdWGLKvSGSKRGRCLSKLADLMERNLD 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 118 LLWTLESLVTGRAVREVRDGDVQLAQQLLHYHA----------IQASTQEEALAGWEPMGVIGLILPPTFSFLEMMWRIC 187
Cdd:cd07143   87 YLASIEALDNGKTFGTAKRVDVQASADTFRYYGgwadkihgqvIETDIKKLTYTRHEPIGVCGQIIPWNFPLLMCAWKIA 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 188 PALAVGCTVValVPPASPAPL---LLAQLAGELGPFPGILNVLSGPASLV-PILASQPGIRKVAFCGAPE---------- 253
Cdd:cd07143  167 PALAAGNTIV--LKPSELTPLsalYMTKLIPEAGFPPGVINVVSGYGRTCgNAISSHMDIDKVAFTGSTLvgrkvmeaaa 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 254 ---------------------------------------------GGLRLLIQESVWDEAMRRLQERMGRLRSGRGLDGA 288
Cdd:cd07143  245 ksnlkkvtlelggkspnivfddadlesavvwtaygiffnhgqvccAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAED 324
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 289 VDMGAR-GAAACDLVQRFVREAQSQGAQVFQAGD-VPSERPFYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALL 366
Cdd:cd07143  325 TFQGPQvSQIQYERIMSYIESGKAEGATVETGGKrHGNEGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEEEAIK 404
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 223972653 367 VANGTPRGGSASVWSERLGQALELGYGLQVGTVWINAHGLRDPSVPTGGCKESGCSWHGGPDGLYEY 433
Cdd:cd07143  405 RANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNLLHHQVPFGGYKQSGIGRELGEYALENY 471
PRK13473 PRK13473
aminobutyraldehyde dehydrogenase;
43-420 1.87e-47

aminobutyraldehyde dehydrogenase;


Pssm-ID: 237391  Cd Length: 475  Bit Score: 175.10  E-value: 1.87e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653  43 YVNGKWLKPEHRnSVPCQDPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTL 122
Cdd:PRK13473   6 LINGELVAGEGE-KQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEFARL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 123 ESLVTGRAVREVRDGDVQLAQQLLHYHA-----IQASTQEEALAGW------EPMGVIGLILPPTFSFLEMMWRICPALA 191
Cdd:PRK13473  85 ESLNCGKPLHLALNDEIPAIVDVFRFFAgaarcLEGKAAGEYLEGHtsmirrDPVGVVASIAPWNYPLMMAAWKLAPALA 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 192 VGCTVValVPPASPAP---LLLAQLAGELGPfPGILNVLSGPASLV-PILASQPGIRKVAFCG----------------- 250
Cdd:PRK13473 165 AGNTVV--LKPSEITPltaLKLAELAADILP-PGVLNVVTGRGATVgDALVGHPKVRMVSLTGsiatgkhvlsaaadsvk 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 251 ---------AP-----------------EGGL-----------RLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMGA 293
Cdd:PRK13473 242 rthlelggkAPvivfddadldavvegirTFGYynagqdctaacRIYAQRGIYDDLVAKLAAAVATLKVGDPDDEDTELGP 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 294 R-GAAACDLVQRFVREAQSQGAQVFQAGDVPSERP--FYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVANG 370
Cdd:PRK13473 322 LiSAAHRDRVAGFVERAKALGHIRVVTGGEAPDGKgyYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDEDQAVRWAND 401
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|
gi 223972653 371 TPRGGSASVWSERLGQALELGYGLQVGTVWINAHGLRDPSVPTGGCKESG 420
Cdd:PRK13473 402 SDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKQSG 451
ALDH_SNDH cd07118
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ...
87-433 7.94e-46

Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone dehydrogenase (SNDH) from Gluconobacter oxydans UV10. In G. oxydans, D-sorbitol is converted to 2-keto-L-gulonate (a precursor of L-ascorbic acid) in sequential oxidation steps catalyzed by a FAD-dependent, L-sorbose dehydrogenase and an NAD(P)+-dependent, L-sorbosone dehydrogenase.


Pssm-ID: 143436 [Multi-domain]  Cd Length: 454  Bit Score: 170.21  E-value: 7.94e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653  87 RMAF-KG-WSAHPGVVRAQHLTRLAEVIQKHQRLLWTLESLVTGRAVREVRdGDVQLAQQLLHYHAIQAST--------- 155
Cdd:cd07118   29 RKAFdKGpWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQAR-GEIEGAADLWRYAASLARTlhgdsynnl 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 156 --QEEALAGWEPMGVIGLILPPTFSFLEMMWRICPALAVGCTVValVPPA---SPAPLLLAQLAGELGPFPGILNVLSGP 230
Cdd:cd07118  108 gdDMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVV--VKPSeftSGTTLMLAELLIEAGLPAGVVNIVTGY 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 231 ASLV-PILASQPGIRKVAFCG---------------------------------------APEGGL-------------- 256
Cdd:cd07118  186 GATVgQAMTEHPDVDMVSFTGstrvgkaiaaaaarnlkkvslelggknpqivfadadldaAADAVVfgvyfnageccnsg 265
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 257 -RLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMGAR-GAAACDLVQRFVREAQSQGAQVFQAGDVPSERP--FYPPT 332
Cdd:cd07118  266 sRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIiNEAQLAKITDYVDAGRAEGATLLLGGERLASAAglFYQPT 345
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 333 LVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVANGTPRGGSASVWSERLGQALELGYGLQVGTVWINAHGLRDPSVP 412
Cdd:cd07118  346 IFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDTALTVARRIRAGTVWVNTFLDGSPELP 425
                        410       420
                 ....*....|....*....|.
gi 223972653 413 TGGCKESGCSWHGGPDGLYEY 433
Cdd:cd07118  426 FGGFKQSGIGRELGRYGVEEY 446
ALDH_F10_BADH cd07110
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ...
61-434 2.13e-45

Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in this CD are the Arabidopsis betaine aldehyde dehydrogenase (BADH) 1 (chloroplast) and 2 (mitochondria), also known as, aldehyde dehydrogenase family 10 member A8 and aldehyde dehydrogenase family 10 member A9, respectively, and are putative dehydration- and salt-inducible BADHs (EC 1.2.1.8) that catalyze the oxidation of betaine aldehyde to the compatible solute glycine betaine.


Pssm-ID: 143428 [Multi-domain]  Cd Length: 456  Bit Score: 169.07  E-value: 2.13e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653  61 DPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTLESLVTGRAVREVR-D-GD 138
Cdd:cd07110    3 NPATEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAwDvDD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 139 V--------QLAQQLLHYHAIQASTQEEALAGW---EPMGVIGLILPPTFSFLEMMWRICPALAVGCTVVaLVPP--ASP 205
Cdd:cd07110   83 VagcfeyyaDLAEQLDAKAERAVPLPSEDFKARvrrEPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVV-LKPSelTSL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 206 APLLLAQLAGELGPFPGILNVLSGPASLVPI-LASQPGIRKVAFCGAPEGGL---------------------------- 256
Cdd:cd07110  162 TELELAEIAAEAGLPPGVLNVVTGTGDEAGApLAAHPGIDKISFTGSTATGSqvmqaaaqdikpvslelggkspiivfdd 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 257 --------------------------RLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMGA-RGAAACDLVQRFVREA 309
Cdd:cd07110  242 adlekavewamfgcfwnngqicsatsRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPlVSQAQYEKVLSFIARG 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 310 QSQGAQVFQAGDVPSERP---FYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVANGTPRGGSASVWSERLGQ 386
Cdd:cd07110  322 KEEGARLLCGGRRPAHLEkgyFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVISRDAER 401
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*...
gi 223972653 387 ALELGYGLQVGTVWINAHGLRDPSVPTGGCKESGCSWHGGPDGLYEYL 434
Cdd:cd07110  402 CDRVAEALEAGIVWINCSQPCFPQAPWGGYKRSGIGRELGEWGLDNYL 449
ALDH_MGR_2402 cd07108
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ...
61-420 4.76e-45

Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent aldehyde dehydrogenase of Magnetospirillum gryphiswaldense MSR-1 (MGR_2402) , and other similar sequences, are present in this CD.


Pssm-ID: 143426  Cd Length: 457  Bit Score: 167.92  E-value: 4.76e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653  61 DPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTLESLVTGRAVREVRDGDVQ 140
Cdd:cd07108    3 NPATGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALRTQARPEAA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 141 LAQQLLHYHAIQASTQE-EALAG---------WEPMGVIGLILPPTFSFLEMMWRICPALAVGCTVValVPPASPAP--- 207
Cdd:cd07108   83 VLADLFRYFGGLAGELKgETLPFgpdvltytvREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVV--LKAAEDAPlav 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 208 LLLAQLAGELGPfPGILNVLSGPASLV-PILASQPGIRKVAFCGAPE--------------------------------- 253
Cdd:cd07108  161 LLLAEILAQVLP-AGVLNVITGYGEECgAALVDHPDVDKVTFTGSTEvgkiiyraaadrlipvslelggkspmivfpdad 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 254 ----------------------GGLRLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMGA-RGAAACDLVQRFVREAQ 310
Cdd:cd07108  240 lddavdgaiagmrftrqgqsctAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAiISEKQFAKVCGYIDLGL 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 311 S-QGAQVFQAGDVPSERP-----FYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVANGTPRGGSASVWSERL 384
Cdd:cd07108  320 StSGATVLRGGPLPGEGPladgfFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWTRDL 399
                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 223972653 385 GQALELGYGLQVGTVWINAHGLRDPSVPTGGCKESG 420
Cdd:cd07108  400 GRALRAAHALEAGWVQVNQGGGQQPGQSYGGFKQSG 435
ALDH_ALD2-YMR170C cd07144
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ...
40-436 1.84e-44

Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c, ALD5, EC=1.2.1.5) and other similar sequences, are present in this CD.


Pssm-ID: 143462  Cd Length: 484  Bit Score: 166.81  E-value: 1.84e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653  40 LGHYVNGKWLKPEHRNSVPCQDPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAH-PGVVRAQHLTRLAEVIQKHQRL 118
Cdd:cd07144    8 TGLFINNEFVKSSDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFESWWSKvTGEERGELLDKLADLVEKNRDL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 119 LWTLESLVTGRAVREVRDGDVQLAQQLLHYHA----------IQASTQEEALAGWEPMGVIGLILPPTFSFLEMMWRICP 188
Cdd:cd07144   88 LAAIEALDSGKPYHSNALGDLDEIIAVIRYYAgwadkiqgktIPTSPNKLAYTLHEPYGVCGQIIPWNYPLAMAAWKLAP 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 189 ALAVGCTVValVPPASPAPLLL---AQLAGELGPFPGILNVLSGPASLV-PILASQPGIRKVAFCGAPEGGL-------- 256
Cdd:cd07144  168 ALAAGNTVV--IKPAENTPLSLlyfANLVKEAGFPPGVVNIIPGYGAVAgSALAEHPDVDKIAFTGSTATGRlvmkaaaq 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 257 ----------------------------------------------RLLIQESVWDEAMRRLQERMG-RLRSGRGLDGAV 289
Cdd:cd07144  246 nlkavtlecggkspalvfedadldqavkwaaagimynsgqnctatsRIYVQESIYDKFVEKFVEHVKqNYKVGSPFDDDT 325
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 290 DMGAR-GAAACDLVQRFVREAQSQGAQVFQAGDVPSERP----FYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEA 364
Cdd:cd07144  326 VVGPQvSKTQYDRVLSYIEKGKKEGAKLVYGGEKAPEGLgkgyFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYEEA 405
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 223972653 365 LLVANGTPRGGSASVWSERLGQALELGYGLQVGTVWINAHGLRDPSVPTGGCKESGCSWHGGPDGLYEYLRP 436
Cdd:cd07144  406 IKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSNDSDVGVPFGGFKMSGIGRELGEYGLETYTQT 477
ALDH_LactADH-AldA cd07088
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ...
43-435 1.69e-43

Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from Escherichia coli (AldA, LactADH, EC=1.2.1.22), an NAD(+)-dependent enzyme involved in the metabolism of L-fucose and L-rhamnose, and other similar sequences are present in this CD.


Pssm-ID: 143407 [Multi-domain]  Cd Length: 468  Bit Score: 163.98  E-value: 1.69e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653  43 YVNGKWLKPEHRNSVPCQDPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTL 122
Cdd:cd07088    1 YINGEFVPSSSGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 123 ESLVTGRAVREVRdGDVQLAQQLLHYHAIQA-----------STQEEALAGWEPMGVIGLILPPTFSFLEMMWRICPALA 191
Cdd:cd07088   81 IVEEQGKTLSLAR-VEVEFTADYIDYMAEWArriegeiipsdRPNENIFIFKVPIGVVAGILPWNFPFFLIARKLAPALV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 192 VGCTVValVPPASPAPLL---LAQLAGELGPFPGILNVLSGPASLV-PILASQPGIRKVAFCGAPEGGL----------- 256
Cdd:cd07088  160 TGNTIV--IKPSEETPLNaleFAELVDEAGLPAGVLNIVTGRGSVVgDALVAHPKVGMISLTGSTEAGQkimeaaaenit 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 257 -------------------------------------------RLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMGA 293
Cdd:cd07088  238 kvslelggkapaivmkdadldlavkaivdsriincgqvctcaeRVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDMGP 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 294 R-GAAACDLVQRFVREAQSQGAQVFQAGDVPSERP--FYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVANG 370
Cdd:cd07088  318 LvNEAALDKVEEMVERAVEAGATLLTGGKRPEGEKgyFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELAND 397
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 223972653 371 TPRGGSASVWSERLGQALELGYGLQVGTVWINAHGlrdPSVPTG---GCKESGCSWHGGPDGLYEYLR 435
Cdd:cd07088  398 SEYGLTSYIYTENLNTAMRATNELEFGETYINREN---FEAMQGfhaGWKKSGLGGADGKHGLEEYLQ 462
ALDH_PhdK-like cd07107
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ...
61-435 2.74e-43

Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain KP72-carboxybenzaldehyde dehydrogenase (PhdK), an enzyme involved in phenanthrene degradation, and other similar sequences, are present in this CD.


Pssm-ID: 143425 [Multi-domain]  Cd Length: 456  Bit Score: 162.93  E-value: 2.74e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653  61 DPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTLESLVTGRAVREVRdGDVQ 140
Cdd:cd07107    3 NPATGQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAML-GDVM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 141 LAQQLLHYHA----------IQASTQEEALAGWEPMGVIGLILPPTFSFLEMMWRICPALAVGCTVVALVPPASP-APLL 209
Cdd:cd07107   82 VAAALLDYFAglvtelkgetIPVGGRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPlSALR 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 210 LAQLAGELGPfPGILNVLSGPASLV-PILASQPGIRKVAFCGAPEGGL-------------------------------- 256
Cdd:cd07107  162 LAELAREVLP-PGVFNILPGDGATAgAALVRHPDVKRIALIGSVPTGRaimraaaegikhvtlelggknalivfpdadpe 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 257 -----------------------RLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMGA-RGAAACDLVQRFVREAQSQ 312
Cdd:cd07107  241 aaadaavagmnftwcgqscgstsRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPlVSRQQYDRVMHYIDSAKRE 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 313 GAQVFQAGDVPS----ERPFY-PPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVANGTPRGGSASVWSERLGQA 387
Cdd:cd07107  321 GARLVTGGGRPEgpalEGGFYvEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTNDISQA 400
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*...
gi 223972653 388 LELGYGLQVGTVWINAHGLRDPSVPTGGCKESGCSWHGGPDGLYEYLR 435
Cdd:cd07107  401 HRTARRVEAGYVWINGSSRHFLGAPFGGVKNSGIGREECLEELLSYTQ 448
PLN02278 PLN02278
succinic semialdehyde dehydrogenase
44-434 3.86e-43

succinic semialdehyde dehydrogenase


Pssm-ID: 215157 [Multi-domain]  Cd Length: 498  Bit Score: 163.32  E-value: 3.86e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653  44 VNGKWLKPEHRNSVPCQDPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTLE 123
Cdd:PLN02278  29 IGGKWTDAYDGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIANKEDLAQLM 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 124 SLVTGRAVREVRdGDVQLAQQLLHYHAIQA-----------STQEEALAGWEPMGVIGLILPPTFSfLEMMWR-ICPALA 191
Cdd:PLN02278 109 TLEQGKPLKEAI-GEVAYGASFLEYFAEEAkrvygdiipspFPDRRLLVLKQPVGVVGAITPWNFP-LAMITRkVGPALA 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 192 VGCTVValVPPASPAPLL---LAQLAGELGPFPGILNVLSGPASLV--PILASqPGIRKVAFCG---------------- 250
Cdd:PLN02278 187 AGCTVV--VKPSELTPLTalaAAELALQAGIPPGVLNVVMGDAPEIgdALLAS-PKVRKITFTGstavgkklmagaaatv 263
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 251 ----------AP-------------EGGL---------------RLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMG 292
Cdd:PLN02278 264 krvslelggnAPfivfddadldvavKGALaskfrnsgqtcvcanRILVQEGIYDKFAEAFSKAVQKLVVGDGFEEGVTQG 343
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 293 AR-GAAACDLVQRFVREAQSQGAQVFQAGDVPSERP-FYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVANG 370
Cdd:PLN02278 344 PLiNEAAVQKVESHVQDAVSKGAKVLLGGKRHSLGGtFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEEAIAIAND 423
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 223972653 371 TPRGGSASVWSERLGQALELGYGLQVGTVWINAHGLRDPSVPTGGCKESGCSWHGGPDGLYEYL 434
Cdd:PLN02278 424 TEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVAPFGGVKQSGLGREGSKYGIDEYL 487
ALDH_PsfA-ACA09737 cd07120
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ...
61-434 5.35e-43

Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the aldehyde dehydrogenase (PsfA, locus ACA09737) of Pseudomonas putida involved in furoic acid metabolism. Transcription of psfA was induced in response to 2-furoic acid, furfuryl alcohol, and furfural.


Pssm-ID: 143438 [Multi-domain]  Cd Length: 455  Bit Score: 162.13  E-value: 5.35e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653  61 DPITGENLASCLQAQAEDVAAAVEAARMAFKG--WSAHPGVvRAQHLTRLAEVIQKHQRLLWTLESLVTGRAVREVRdGD 138
Cdd:cd07120    3 DPATGEVIGTYADGGVAEAEAAIAAARRAFDEtdWAHDPRL-RARVLLELADAFEANAERLARLLALENGKILGEAR-FE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 139 VQLAQQLLHY----------HAIQASTQEEALAGWEPMGVIGLILPPTFSFLEMMWRICPALAVGCTVValVPPASPAPL 208
Cdd:cd07120   81 ISGAISELRYyaglarteagRMIEPEPGSFSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVV--VKPAGQTAQ 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 209 L---LAQLAGELGPFP-GILNVLSGPAS----------LVPIL--------------ASQPGIRKVA------------- 247
Cdd:cd07120  159 InaaIIRILAEIPSLPaGVVNLFTESGSegaahlvaspDVDVIsftgstatgraimaAAAPTLKRLGlelggktpcivfd 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 248 ---------------------FCGApegGLRLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMGAR-GAAACDLVQRF 305
Cdd:cd07120  239 dadldaalpkleraltifagqFCMA---GSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLiDRANVDRVDRM 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 306 VREAQSQGAQVFQAGDVPSERP----FYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVANGTPRGGSASVWS 381
Cdd:cd07120  316 VERAIAAGAEVVLRGGPVTEGLakgaFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWT 395
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|...
gi 223972653 382 ERLGQALELGYGLQVGTVWINAHGLRDPSVPTGGCKESGCSWHGGPDGLYEYL 434
Cdd:cd07120  396 RDLARAMRVARAIRAGTVWINDWNKLFAEAEEGGYRQSGLGRLHGVAALEDFI 448
ALDH_ACDHII-AcoD cd07116
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ...
41-420 6.24e-43

Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is the NAD+-dependent, acetaldehyde dehydrogenase II (AcDHII, AcoD, EC=1.2.1.3) from Ralstonia (Alcaligenes) eutrophus H16 involved in the catabolism of acetoin and ethanol, and similar proteins, such as, the dimeric dihydrolipoamide dehydrogenase of the acetoin dehydrogenase enzyme system of Klebsiella pneumonia. Also included are sequences similar to the NAD+-dependent chloroacetaldehyde dehydrogenases (AldA and AldB) of Xanthobacter autotrophicus GJ10 which are involved in the degradation of 1,2-dichloroethane. These proteins apparently require RpoN factors for expression.


Pssm-ID: 143434 [Multi-domain]  Cd Length: 479  Bit Score: 162.62  E-value: 6.24e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653  41 GHYVNGKWLKPEHRNSVPCQDPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLW 120
Cdd:cd07116    2 DNFIGGEWVAPVKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 121 TLESLVTGRAVREVRDGDVQLAQQLLHYHAIQASTQEEALAG----------WEPMGVIGLILPPTFSFLEMMWRICPAL 190
Cdd:cd07116   82 VAETWDNGKPVRETLAADIPLAIDHFRYFAGCIRAQEGSISEidentvayhfHEPLGVVGQIIPWNFPLLMATWKLAPAL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 191 AVGCTVValVPPASPAP---LLLAQLAGELGPfPGILNVLSGP-ASLVPILASQPGIRKVAFCGAPEGGL---------- 256
Cdd:cd07116  162 AAGNCVV--LKPAEQTPasiLVLMELIGDLLP-PGVVNVVNGFgLEAGKPLASSKRIAKVAFTGETTTGRlimqyaseni 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 257 -------------------------------------------------RLLIQESVWDEAMRRLQERMGRLRSGRGLDG 287
Cdd:cd07116  239 ipvtlelggkspniffadvmdaddaffdkalegfvmfalnqgevctcpsRALIQESIYDRFMERALERVKAIKQGNPLDT 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 288 AVDMGARGAAA-CDLVQRFVREAQSQGAQVFQAGD-----VPSERPFYPPTLVSNLPPASpCAQVEVPWPVVVASPFRTA 361
Cdd:cd07116  319 ETMIGAQASLEqLEKILSYIDIGKEEGAEVLTGGErnelgGLLGGGYYVPTTFKGGNKMR-IFQEEIFGPVLAVTTFKDE 397
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 223972653 362 KEALLVANGTPRGGSASVWSERLGQALELGYGLQVGTVWINAHGLRDPSVPTGGCKESG 420
Cdd:cd07116  398 EEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYPAHAAFGGYKQSG 456
ALDH_CddD-AldA-like cd07089
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ...
61-434 8.19e-43

Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric acid dehydrogenase (CddD) from Rhodococcus ruber SC1 which converts 6-oxolauric acid to dodecanedioic acid; and the aldehyde dehydrogenase (locus SSP0762) from Staphylococcus saprophyticus subsp. saprophyticus ATCC 15305 and also, the Mycobacterium tuberculosis H37Rv ALDH AldA (locus Rv0768) sequence; and other similar sequences, are included in this CD.


Pssm-ID: 143408 [Multi-domain]  Cd Length: 459  Bit Score: 161.64  E-value: 8.19e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653  61 DPITGENLASCLQAQAEDVAAAVEAARMAFKGWS-AHPGVVRAQHLTRLAEVIQKHQRLLWTLESLVTGRAVREVRDGDV 139
Cdd:cd07089    3 NPATEEVIGTAPDAGAADVDAAIAAARRAFDTGDwSTDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARAMQV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 140 QLAQQLLHYHAIQAS--TQEEALAGW-------------EPMGVIGLILPPTFSFLEMMWRICPALAVGCTVValVPPAS 204
Cdd:cd07089   83 DGPIGHLRYFADLADsfPWEFDLPVPalrggpgrrvvrrEPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVV--LKPAP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 205 PAPL---LLAQLAGELGPFPGILNVLSGPASLV-PILASQPGIRKVAFCGAPE--------------------GG----- 255
Cdd:cd07089  161 DTPLsalLLGEIIAETDLPAGVVNVVTGSDNAVgEALTTDPRVDMVSFTGSTAvgrrimaqaaatlkrvllelGGksani 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 256 -----------------------------LRLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMGAR-GAAACDLVQRF 305
Cdd:cd07089  241 vlddadlaaaapaavgvcmhnagqgcaltTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLiSAAQRDRVEGY 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 306 VREAQSQGAQVFQAGDVPSERP---FYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVANGTPRGGSASVWSE 382
Cdd:cd07089  321 IARGRDEGARLVTGGGRPAGLDkgfYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVWSA 400
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|..
gi 223972653 383 RLGQALELGYGLQVGTVWINAHGLRDPSVPTGGCKESGCSWHGGPDGLYEYL 434
Cdd:cd07089  401 DVDRAYRVARRIRTGSVGINGGGGYGPDAPFGGYKQSGLGRENGIEGLEEFL 452
ALDH_F1AB_F2_RALDH1 cd07141
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ...
43-434 2.48e-42

NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent retinal dehydrogenase 1 (RALDH 1, ALDH1, EC=1.2.1.36) also known as aldehyde dehydrogenase family 1 member A1 (ALDH1A1) in humans, is a homotetrameric, cytosolic enzyme that catalyzes the oxidation of retinaldehyde to retinoic acid. Human ALDH1B1 and ALDH2 are also in this cluster; both are mitochrondrial homotetramers which play important roles in acetaldehyde oxidation; ALDH1B1 in response to UV light exposure and ALDH2 during ethanol metabolism.


Pssm-ID: 143459  Cd Length: 481  Bit Score: 160.59  E-value: 2.48e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653  43 YVNGKWLKPEHRNSVPCQDPITGENLASCLQAQAEDVAAAVEAARMAFK---GWSAHPGVVRAQHLTRLAEVIQKHQRLL 119
Cdd:cd07141   10 FINNEWHDSVSGKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFKlgsPWRTMDASERGRLLNKLADLIERDRAYL 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 120 WTLESLVTGRAVREVRDGDVQLAQQLLHYHA----------IQASTQEEALAGWEPMGVIGLILPPTFSFLEMMWRICPA 189
Cdd:cd07141   90 ASLETLDNGKPFSKSYLVDLPGAIKVLRYYAgwadkihgktIPMDGDFFTYTRHEPVGVCGQIIPWNFPLLMAAWKLAPA 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 190 LAVGCTVValVPPASPAPL---LLAQLAGELGPFPGILNVLSG--PASLVPIlASQPGIRKVAFCGAPE----------- 253
Cdd:cd07141  170 LACGNTVV--LKPAEQTPLtalYLASLIKEAGFPPGVVNVVPGygPTAGAAI-SSHPDIDKVAFTGSTEvgkliqqaagk 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 254 --------------------------------------------GGLRLLIQESVWDEAMRRLQERMGRLRSGRGLDGAV 289
Cdd:cd07141  247 snlkrvtlelggkspnivfadadldyaveqahealffnmgqcccAGSRTFVQESIYDEFVKRSVERAKKRVVGNPFDPKT 326
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 290 DMGAR-GAAACDLVQRFVREAQSQGAQVFQAGDVPSERPFY-PPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLV 367
Cdd:cd07141  327 EQGPQiDEEQFKKILELIESGKKEGAKLECGGKRHGDKGYFiQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTIDEVIER 406
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 223972653 368 ANGTPRGGSASVWSERLGQALELGYGLQVGTVWINAHGLRDPSVPTGGCKESGCSWHGGPDGLYEYL 434
Cdd:cd07141  407 ANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVSPQAPFGGYKMSGNGRELGEYGLQEYT 473
ALDH_F2BC cd07142
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ...
43-435 2.90e-42

Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the Arabidosis aldehyde dehydrogenase family 2 members B4 and B7 (EC=1.2.1.3), which are mitochondrial homotetramers that oxidize acetaldehyde and glycolaldehyde, but not L-lactaldehyde. Also in this group, is the Arabidosis cytosolic, homotetramer ALDH2C4 (EC=1.2.1.3), an enzyme involved in the oxidation of sinapalehyde and coniferaldehyde.


Pssm-ID: 143460  Cd Length: 476  Bit Score: 160.35  E-value: 2.90e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653  43 YVNGKWLKPEHRNSVPCQDPITGENLASCLQAQAEDVAAAVEAARMAFK--GWSAHPGVVRAQHLTRLAEVIQKHQRLLW 120
Cdd:cd07142    7 FINGQFVDAASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDegPWPRMTGYERSRILLRFADLLEKHADELA 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 121 TLESLVTGRAVREVRDGDVQLAQQLLHYHA-----IQAST--QEEALAGW---EPMGVIGLILPPTFSFLEMMWRICPAL 190
Cdd:cd07142   87 ALETWDNGKPYEQARYAEVPLAARLFRYYAgwadkIHGMTlpADGPHHVYtlhEPIGVVGQIIPWNFPLLMFAWKVGPAL 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 191 AVGCTVValVPPASPAPL---LLAQLAGELGPFPGILNVLS--GPASLVPIlASQPGIRKVAFCGAPE------------ 253
Cdd:cd07142  167 ACGNTIV--LKPAEQTPLsalLAAKLAAEAGLPDGVLNIVTgfGPTAGAAI-ASHMDVDKVAFTGSTEvgkiimqlaaks 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 254 -------------------------------------------GGLRLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVD 290
Cdd:cd07142  244 nlkpvtlelggkspfivcedadvdkavelahfalffnqgqcccAGSRTFVHESIYDEFVEKAKARALKRVVGDPFRKGVE 323
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 291 MGARGA-AACDLVQRFVREAQSQGAQVFQAGDVPSERPFY-PPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVA 368
Cdd:cd07142  324 QGPQVDkEQFEKILSYIEHGKEEGATLITGGDRIGSKGYYiQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEVIKRA 403
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 223972653 369 NGTPRGGSASVWSERLGQALELGYGLQVGTVWINAHGLRDPSVPTGGCKESGCSWHGGPDGLYEYLR 435
Cdd:cd07142  404 NNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNCYDVFDASIPFGGYKMSGIGREKGIYALNNYLQ 470
ALDH_AldA-Rv0768 cd07139
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ...
43-434 1.53e-40

Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis NAD+-dependent, aldehyde dehydrogenase PDB structure, 3B4W, and the Mycobacterium tuberculosis H37Rv aldehyde dehydrogenase AldA (locus Rv0768) sequence, as well as the Rhodococcus rhodochrous ALDH involved in haloalkane catabolism, and other similar sequences, are included in this CD.


Pssm-ID: 143457 [Multi-domain]  Cd Length: 471  Bit Score: 155.43  E-value: 1.53e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653  43 YVNGKWLKPEHRNSVPCQDPITGENLASCLQAQAEDVAAAVEAARMAFKG--WSAHPGVVRAQHLTRLAEVIQKHQRLLW 120
Cdd:cd07139    2 FIGGRWVAPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAFDNgpWPRLSPAERAAVLRRLADALEARADELA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 121 TLESLVTGRAVREVRDGDVQLAQQLLHYHA-----------IQASTQEEALAGWEPMGVIGLILPPTFSFLEMMWRICPA 189
Cdd:cd07139   82 RLWTAENGMPISWSRRAQGPGPAALLRYYAalardfpfeerRPGSGGGHVLVRREPVGVVAAIVPWNAPLFLAALKIAPA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 190 LAVGCTVVALVPPASP-APLLLAQLAGELGPFPGILNVLSGPASLVPILASQPGIRKVAFCGAPEGGL------------ 256
Cdd:cd07139  162 LAAGCTVVLKPSPETPlDAYLLAEAAEEAGLPPGVVNVVPADREVGEYLVRHPGVDKVSFTGSTAAGRriaavcgerlar 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 257 ------------------------------------------RLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMGAR 294
Cdd:cd07139  242 vtlelggksaaivlddadldaavpglvpaslmnngqvcvaltRILVPRSRYDEVVEALAAAVAALKVGDPLDPATQIGPL 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 295 GAAA-CDLVQRFVREAQSQGAQVFQAGDVPSERP---FYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVANG 370
Cdd:cd07139  322 ASARqRERVEGYIAKGRAEGARLVTGGGRPAGLDrgwFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDAVRIAND 401
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 223972653 371 TPRGGSASVWSERLGQALELGYGLQVGTVWINAHGLrDPSVPTGGCKESGCSWHGGPDGLYEYL 434
Cdd:cd07139  402 SDYGLSGSVWTADVERGLAVARRIRTGTVGVNGFRL-DFGAPFGGFKQSGIGREGGPEGLDAYL 464
ALDH_F9_TMBADH cd07090
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ...
61-433 7.50e-40

NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, 4-trimethylaminobutyraldehyde dehydrogenase (TMABADH, EC=1.2.1.47), also known as aldehyde dehydrogenase family 9 member A1 (ALDH9A1) in humans, is a cytosolic tetramer which catalyzes the oxidation of gamma-aminobutyraldehyde involved in 4-aminobutyric acid (GABA) biosynthesis and also oxidizes betaine aldehyde (gamma-trimethylaminobutyraldehyde) which is involved in carnitine biosynthesis.


Pssm-ID: 143409 [Multi-domain]  Cd Length: 457  Bit Score: 153.23  E-value: 7.50e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653  61 DPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTLESLVTGRAVREVRdGDVQ 140
Cdd:cd07090    3 EPATGEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEAR-VDID 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 141 LAQQLLHYHAIQAST---QEEALAG-------WEPMGVIGLILPPTFSFLEMMWRICPALAVGCTVVALVPPASPA-PLL 209
Cdd:cd07090   82 SSADCLEYYAGLAPTlsgEHVPLPGgsfaytrREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLtALL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 210 LAQLAGELGPFPGILNVLSGPASLVPILASQPGIRKVAFCGA-PEG---------------------------------- 254
Cdd:cd07090  162 LAEILTEAGLPDGVFNVVQGGGETGQLLCEHPDVAKVSFTGSvPTGkkvmsaaakgikhvtlelggkspliifddadlen 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 255 -------------------GLRLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMGAR-GAAACDLVQRFVREAQSQGA 314
Cdd:cd07090  242 avngammanflsqgqvcsnGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALiSEEHLEKVLGYIESAKQEGA 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 315 QVFQAGDVPS-----ERPFY-PPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVANGTPRGGSASVWSERLGQAL 388
Cdd:cd07090  322 KVLCGGERVVpedglENGFYvSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTRDLQRAH 401
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*
gi 223972653 389 ELGYGLQVGTVWINAHGLRDPSVPTGGCKESGCSWHGGPDGLYEY 433
Cdd:cd07090  402 RVIAQLQAGTCWINTYNISPVEVPFGGYKQSGFGRENGTAALEHY 446
ALDH_CddD_SSP0762 cd07138
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ...
42-434 8.65e-40

Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase (CddD) from Rhodococcus ruber SC1 which converts 6-oxolauric acid to dodecanedioic acid, and the aldehyde dehydrogenase (locus SSP0762) from Staphylococcus saprophyticus subsp. saprophyticus ATCC 15305 and other similar sequences, are included in this CD.


Pssm-ID: 143456 [Multi-domain]  Cd Length: 466  Bit Score: 153.04  E-value: 8.65e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653  42 HYVNGKWLKPEHRNSVPCQDPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWT 121
Cdd:cd07138    1 FYIDGAWVAPAGTETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 122 LESLVTGRAVREVRDGDVQLAQQLLHyHAIQA-------STQEEALAGWEPMGVIGLILPPTFSFLEMMWRICPALAVGC 194
Cdd:cd07138   81 AITLEMGAPITLARAAQVGLGIGHLR-AAADAlkdfefeERRGNSLVVREPIGVCGLITPWNWPLNQIVLKVAPALAAGC 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 195 TVValVPPASPAPL---LLAQLAGELGPFPGILNVLSGPASLV-PILASQPGIRKVAF---------------------- 248
Cdd:cd07138  160 TVV--LKPSEVAPLsaiILAEILDEAGLPAGVFNLVNGDGPVVgEALSAHPDVDMVSFtgstragkrvaeaaadtvkrva 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 249 -----------------------------------CGAPEgglRLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMGA 293
Cdd:cd07138  238 lelggksaniilddadlekavprgvaacfansgqsCNAPT---RMLVPRSRYAEAEEIAAAAAEAYVVGDPRDPATTLGP 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 294 -RGAAACDLVQRFVREAQSQGAQVFQAGdvpSERP-------FYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEAL 365
Cdd:cd07138  315 lASAAQFDRVQGYIQKGIEEGARLVAGG---PGRPeglergyFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDEAI 391
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 223972653 366 LVANGTPRGGSASVWSERLGQALELGYGLQVGTVWINaHGLRDPSVPTGGCKESGCSWHGGPDGLYEYL 434
Cdd:cd07138  392 AIANDTPYGLAGYVWSADPERARAVARRLRAGQVHIN-GAAFNPGAPFGGYKQSGNGREWGRYGLEEFL 459
PLN02467 PLN02467
betaine aldehyde dehydrogenase
43-434 1.01e-39

betaine aldehyde dehydrogenase


Pssm-ID: 215260 [Multi-domain]  Cd Length: 503  Bit Score: 153.73  E-value: 1.01e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653  43 YVNGKWLKPEHRNSVPCQDPITGENLASCLQAQAEDVAAAVEAARMAF-----KGWSAHPGVVRAQHLTRLAEVIQKHQR 117
Cdd:PLN02467  11 FIGGEWREPVLGKRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAFkrnkgKDWARTTGAVRAKYLRAIAAKITERKS 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 118 LLWTLESLVTGRAVREVrDGDVQLAQQLLHYHAIQAstqeEALAG------------------WEPMGVIGLILPPTFSF 179
Cdd:PLN02467  91 ELAKLETLDCGKPLDEA-AWDMDDVAGCFEYYADLA----EALDAkqkapvslpmetfkgyvlKEPLGVVGLITPWNYPL 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 180 LEMMWRICPALAVGCTVVaLVPP--ASPAPLLLAQLAGELGPFPGILNVLS--GPASLVPiLASQPGIRKVAFCGAPEGG 255
Cdd:PLN02467 166 LMATWKVAPALAAGCTAV-LKPSelASVTCLELADICREVGLPPGVLNVVTglGTEAGAP-LASHPGVDKIAFTGSTATG 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 256 L------------------------------------------------------RLLIQESVWDEAMRRLQERMGRLRS 281
Cdd:PLN02467 244 RkimtaaaqmvkpvslelggkspiivfddvdldkavewamfgcfwtngqicsatsRLLVHERIASEFLEKLVKWAKNIKI 323
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 282 GRGLDGAVDMGAR-GAAACDLVQRFVREAQSQGAQVFQAGDVPS--ERPFY-PPTLVSNLPPASPCAQVEVPWPVVVASP 357
Cdd:PLN02467 324 SDPLEEGCRLGPVvSEGQYEKVLKFISTAKSEGATILCGGKRPEhlKKGFFiEPTIITDVTTSMQIWREEVFGPVLCVKT 403
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 223972653 358 FRTAKEALLVANGTPRGGSASVWSERLGQALELGYGLQVGTVWINAHGLRDPSVPTGGCKESGCSWHGGPDGLYEYL 434
Cdd:PLN02467 404 FSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQPCFCQAPWGGIKRSGFGRELGEWGLENYL 480
PRK09847 PRK09847
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
43-420 2.31e-38

gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional


Pssm-ID: 182108 [Multi-domain]  Cd Length: 494  Bit Score: 149.66  E-value: 2.31e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653  43 YVNGKWLKPEHRNSVPCQDPITGENLASCLQAQAEDVAAAVEAARMAFKG--WSAHPGVVRAQHLTRLAEVIQKHQRLLW 120
Cdd:PRK09847  23 FINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFERgdWSLSSPAKRKAVLNKLADLMEAHAEELA 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 121 TLESLVTGRAVREVRDGDVQLAQQLLHYHA----------IQASTQEEALAGWEPMGVIGLILPPTFSFLEMMWRICPAL 190
Cdd:PRK09847 103 LLETLDTGKPIRHSLRDDIPGAARAIRWYAeaidkvygevATTSSHELAMIVREPVGVIAAIVPWNFPLLLTCWKLGPAL 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 191 AVGCTVValVPPASPAPLL---LAQLAGELGPFPGILNVLSGPASLV-PILASQPGIRKVAFCGAPE------------- 253
Cdd:PRK09847 183 AAGNSVI--LKPSEKSPLSairLAGLAKEAGLPDGVLNVVTGFGHEAgQALSRHNDIDAIAFTGSTRtgkqllkdagdsn 260
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 254 -------------------------------------------GGLRLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVD 290
Cdd:PRK09847 261 mkrvwleaggksanivfadcpdlqqaasataagifynqgqvciAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATT 340
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 291 MGAR-GAAACDLVQRFVREAQSQGaQVFQAGDVPSERPFYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVAN 369
Cdd:PRK09847 341 MGTLiDCAHADSVHSFIREGESKG-QLLLDGRNAGLAAAIGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQLAN 419
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|.
gi 223972653 370 GTPRGGSASVWSERLGQALELGYGLQVGTVWINAHGLRDPSVPTGGCKESG 420
Cdd:PRK09847 420 DSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSG 470
ALDH_BenzADH-like cd07104
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ...
89-427 3.67e-38

ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, p-hydroxybenzaldehyde dehydrogenase and related proteins; ALDH subfamily which includes the NAD(P)+-dependent, benzaldehyde dehydrogenase II (XylC, BenzADH, EC=1.2.1.28) involved in the oxidation of benzyl alcohol to benzoate; p-hydroxybenzaldehyde dehydrogenase (PchA, HBenzADH) which catalyzes the oxidation of p-hydroxybenzaldehyde to p-hydroxybenzoic acid; vanillin dehydrogenase (Vdh, VaniDH) involved in the metabolism of ferulic acid as seen in Pseudomonas putida KT2440; and other related sequences.


Pssm-ID: 143422 [Multi-domain]  Cd Length: 431  Bit Score: 147.68  E-value: 3.67e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653  89 AFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLwtLESLV--TGrAVREVRDGDVQLAQQLLHYHA---------IQASTQE 157
Cdd:cd07104   12 AQKAWAATPPQERAAILRKAAEILEERRDEI--ADWLIreSG-STRPKAAFEVGAAIAILREAAglprrpegeILPSDVP 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 158 --EALAGWEPMGVIGLILPPTFSFLEMMWRICPALAVGCTVValVPPASPAP----LLLAQLAGELGPFPGILNVLSGPA 231
Cdd:cd07104   89 gkESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVV--LKPDSRTPvtggLLIAEIFEEAGLPKGVLNVVPGGG 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 232 SLV-PILASQPGIRKVAFCGAPE--------------------GG------L---------------------------- 256
Cdd:cd07104  167 SEIgDALVEHPRVRMISFTGSTAvgrhigelagrhlkkvalelGGnnplivLddadldlavsaaafgaflhqgqicmaag 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 257 RLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMG-ARGAAACDLVQRFVREAQSQGAQVFQAGDVpsERPFYPPTLVS 335
Cdd:cd07104  247 RILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGpLINERQVDRVHAIVEDAVAAGARLLTGGTY--EGLFYQPTVLS 324
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 336 NLPPASPCAQVEVPWPVVVASPFRTAKEALLVANGTPRGGSASVWSERLGQALELGYGLQVGTVWINAHGLRD-PSVPTG 414
Cdd:cd07104  325 DVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHINDQTVNDePHVPFG 404
                        410
                 ....*....|...
gi 223972653 415 GCKESGCSWHGGP 427
Cdd:cd07104  405 GVKASGGGRFGGP 417
ALDH_AldH-CAJ73105 cd07131
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ...
42-434 4.76e-38

Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; Uncharacterized aldehyde dehydrogenase of Candidatus kuenenia AldH (locus CAJ73105) and similar sequences with similarity to alpha-aminoadipic semialdehyde dehydrogenase (AASADH, human ALDH7A1, EC=1.2.1.31), Arabidopsis ALDH7B4, and Streptomyces clavuligerus delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH) are included in this CD.


Pssm-ID: 143449 [Multi-domain]  Cd Length: 478  Bit Score: 148.26  E-value: 4.76e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653  42 HYVNGKWLKPEHRNSVPCQDPITGENLASCLQA-QAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLW 120
Cdd:cd07131    1 NYIGGEWVDSASGETFDSRNPADLEEVVGTFPLsTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 121 TLESLVTGRAVREVRdGDVQLAQQLLHYHAIQAST-----------QEEALAGWEPMGVIGLILPPTFSFLEMMWRICPA 189
Cdd:cd07131   81 RLVTREMGKPLAEGR-GDVQEAIDMAQYAAGEGRRlfgetvpselpNKDAMTRRQPIGVVALITPWNFPVAIPSWKIFPA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 190 LAVGCTVValVPPASPAPLL---LAQLAGELGPFPGILNVLSGPASLV-PILASQPGIRKVAFCG--------------- 250
Cdd:cd07131  160 LVCGNTVV--FKPAEDTPACalkLVELFAEAGLPPGVVNVVHGRGEEVgEALVEHPDVDVVSFTGstevgerigetcarp 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 251 ------------------------APEGGL---------------RLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDM 291
Cdd:cd07131  238 nkrvalemggknpiivmddadldlALEGALwsafgttgqrctatsRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETDM 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 292 G-ARGAAACDLVQRFVREAQSQGAQVFQAGDVPSERP-----FYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEAL 365
Cdd:cd07131  318 GpLINEAQLEKVLNYNEIGKEEGATLLLGGERLTGGGyekgyFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAI 397
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 223972653 366 LVANGTPRGGSASVWSERLGQALELGYGLQVGTVWINAhglrdPSV------PTGGCKESGcswHGGPDGLYEYL 434
Cdd:cd07131  398 EIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNA-----PTIgaevhlPFGGVKKSG---NGHREAGTTAL 464
ALDH_F7_AASADH-like cd07086
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ...
42-441 3.35e-36

NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH subfamily which includes the NAD+-dependent, alpha-aminoadipic semialdehyde dehydrogenase (AASADH, EC=1.2.1.31), also known as Antiquitin-1, ALDH7A1, ALDH7B or delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH), and other similar sequences, such as the uncharacterized aldehyde dehydrogenase of Candidatus kuenenia AldH (locus CAJ73105).


Pssm-ID: 143405 [Multi-domain]  Cd Length: 478  Bit Score: 142.70  E-value: 3.35e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653  42 HYVNGKWLKPEhRNSVPCQDPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWT 121
Cdd:cd07086    1 GVIGGEWVGSG-GETFTSRNPANGEPIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 122 LESLVTGRAVREVRdGDVQ-----------LAQQLlhYHAIQASTQEE--ALAGWEPMGVIGLILPPTFSFLEMMWRICP 188
Cdd:cd07086   80 LVSLEMGKILPEGL-GEVQemidicdyavgLSRML--YGLTIPSERPGhrLMEQWNPLGVVGVITAFNFPVAVPGWNAAI 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 189 ALAVGCTVValVPPASPAPL-------LLAQLAGELGPFPGILNVLSGPASLVPILASQPGIRKVAFCG----------- 250
Cdd:cd07086  157 ALVCGNTVV--WKPSETTPLtaiavtkILAEVLEKNGLPPGVVNLVTGGGDGGELLVHDPRVPLVSFTGstevgrrvget 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 251 ----------------------------APEGGL---------------RLLIQESVWDEAMRRLQERMGRLRSGRGLDG 287
Cdd:cd07086  235 varrfgrvllelggnnaiivmddadldlAVRAVLfaavgtagqrctttrRLIVHESVYDEFLERLVKAYKQVRIGDPLDE 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 288 AVDMG-ARGAAACDLVQRFVREAQSQGAQVFQAGDVPSERP---FYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKE 363
Cdd:cd07086  315 GTLVGpLINQAAVEKYLNAIEIAKSQGGTVLTGGKRIDGGEpgnYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEE 394
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 364 ALLVANGTPRGGSASVWSERLGQALE-LG-YGLQVGTVWINA-------HGlrdpsvPTGGCKESGcswhGGpdglyeyl 434
Cdd:cd07086  395 AIAINNDVPQGLSSSIFTEDLREAFRwLGpKGSDCGIVNVNIptsgaeiGG------AFGGEKETG----GG-------- 456

                 ....*..
gi 223972653 435 RPSGTPA 441
Cdd:cd07086  457 RESGSDA 463
ALDH_F1L_FTFDH cd07140
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ...
43-435 1.55e-35

10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate dehydrogenase (FTHFDH, EC=1.5.1.6), also known as aldehyde dehydrogenase family 1 member L1 (ALDH1L1) in humans, is a multi-domain homotetramer with an N-terminal formyl transferase domain and a C-terminal ALDH domain. FTHFDH catalyzes an NADP+-dependent dehydrogenase reaction resulting in the conversion of 10-formyltetrahydrofolate to tetrahydrofolate and CO2. The ALDH domain is also capable of the oxidation of short chain aldehydes to their corresponding acids.


Pssm-ID: 143458 [Multi-domain]  Cd Length: 486  Bit Score: 141.09  E-value: 1.55e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653  43 YVNGKWLKPEHRNSVPCQDPITGENLASCLQAQAEDVAAAVEAARMAFKG--WSAHPGVVRAQHLTRLAEVIQKHQRLLW 120
Cdd:cd07140    9 FINGEFVDAEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFENgeWGKMNARDRGRLMYRLADLMEEHQEELA 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 121 TLESLVTGRAVREVRDGDVQLAQQLLHYHA-----IQAST---------QEEALAGWEPMGVIGLILPPTFSFLEMMWRI 186
Cdd:cd07140   89 TIESLDSGAVYTLALKTHVGMSIQTFRYFAgwcdkIQGKTipinqarpnRNLTLTKREPIGVCGIVIPWNYPLMMLAWKM 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 187 CPALAVGCTVValVPPASPAPLL---LAQLAGELGPFPGILNVLSGPASLV-PILASQPGIRKVAFCGAPEGGL------ 256
Cdd:cd07140  169 AACLAAGNTVV--LKPAQVTPLTalkFAELTVKAGFPKGVINILPGSGSLVgQRLSDHPDVRKLGFTGSTPIGKhimksc 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 257 -------------------------------------------------RLLIQESVWDEAMRRLQERMGRLRSGRGLDG 287
Cdd:cd07140  247 avsnlkkvslelggkspliifadcdmdkavrmgmssvffnkgenciaagRLFVEESIHDEFVRRVVEEVKKMKIGDPLDR 326
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 288 AVDMGARGAAA-CDLVQRFVREAQSQGAQVFQAG-DVPSERPFYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAK-EA 364
Cdd:cd07140  327 STDHGPQNHKAhLDKLVEYCERGVKEGATLVYGGkQVDRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKFDDGDvDG 406
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 223972653 365 LLV-ANGTPRGGSASVWSERLGQALELGYGLQVGTVWINAHGLRDPSVPTGGCKESGCSWHGGPDGLYEYLR 435
Cdd:cd07140  407 VLQrANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEEALNEYLK 478
ALDH_DDALDH cd07099
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ...
61-436 2.24e-35

Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4'-diapolycopene-dialdehyde dehydrogenase (DDALDH) involved in C30 carotenoid synthesis in Methylomonas sp. strain 16a and other similar sequences are present in this CD. DDALDH converts 4,4'-diapolycopene-dialdehyde into 4,4'-diapolycopene-diacid.


Pssm-ID: 143417 [Multi-domain]  Cd Length: 453  Bit Score: 140.05  E-value: 2.24e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653  61 DPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTLESLVTGRAVREVRdGDVQ 140
Cdd:cd07099    2 NPATGEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAG-LEVL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 141 LAQQLLHYHAIQAstqEEALA-----------------GWEPMGVIGLILPPTFSFLEMMWRICPALAVGCTVValVPPA 203
Cdd:cd07099   81 LALEAIDWAARNA---PRVLAprkvptgllmpnkkatvEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVV--LKPS 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 204 SPAPL---LLAQLAGELGPFPGILNVLSGPASLVPILASQpGIRKVAFCGAPEGGL------------------------ 256
Cdd:cd07099  156 EVTPLvgeLLAEAWAAAGPPQGVLQVVTGDGATGAALIDA-GVDKVAFTGSVATGRkvmaaaaerlipvvlelggkdpmi 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 257 ------------------------------RLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMGARGAAA-CDLVQRF 305
Cdd:cd07099  235 vladadleraaaaavwgamvnagqtcisveRVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARqLDIVRRH 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 306 VREAQSQGAQVFQAGDVPSER-PFYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVANGTPRGGSASVWSERL 384
Cdd:cd07099  315 VDDAVAKGAKALTGGARSNGGgPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRDL 394
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....
gi 223972653 385 GQALELGYGLQVGTVWINAHGLRD--PSVPTGGCKESGCSWHGGPDGLYEYLRP 436
Cdd:cd07099  395 ARAEAIARRLEAGAVSINDVLLTAgiPALPFGGVKDSGGGRRHGAEGLREFCRP 448
ALDH_LactADH_F420-Bios cd07145
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ...
57-420 2.88e-35

Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, lactaldehyde dehydrogenase (EC=1.2.1.22) involved the biosynthesis of coenzyme F(420) in Methanocaldococcus jannaschii through the oxidation of lactaldehyde to lactate and generation of NAPH, and similar sequences are included in this CD.


Pssm-ID: 143463 [Multi-domain]  Cd Length: 456  Bit Score: 139.79  E-value: 2.88e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653  57 VPCQDPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTLESLVTGRAVREVRd 136
Cdd:cd07145    1 IEVRNPANGEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSR- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 137 GDVQLAQQLLHYHAIQASTQEE---------------ALAGWEPMGVIGLILPPTFSFLEMMWRICPALAVGCTVValVP 201
Cdd:cd07145   80 VEVERTIRLFKLAAEEAKVLRGetipvdayeynerriAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVV--VK 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 202 PASPAPL---LLAQLAGELGPFPGILNVLSGPASLV-PILASQPGIRKVAFCGAPEGGL--------------------- 256
Cdd:cd07145  158 PSSNTPLtaiELAKILEEAGLPPGVINVVTGYGSEVgDEIVTNPKVNMISFTGSTAVGLliaskaggtgkkvalelggsd 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 257 ---------------------------------RLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMGAR-GAAACDLV 302
Cdd:cd07145  238 pmivlkdadleravsiavrgrfenagqvcnavkRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLiSPEAVERM 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 303 QRFVREAQSQGAQVFQAGDVPsERPFYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVANGTPRGGSASVWSE 382
Cdd:cd07145  318 ENLVNDAVEKGGKILYGGKRD-EGSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVFTN 396
                        410       420       430
                 ....*....|....*....|....*....|....*....
gi 223972653 383 RLGQALELGYGLQVGTVWINAHG-LRDPSVPTGGCKESG 420
Cdd:cd07145  397 DINRALKVARELEAGGVVINDSTrFRWDNLPFGGFKKSG 435
ALDH_KGSADH-YcbD cd07097
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ...
42-420 3.61e-35

Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; Kinetic studies of the Bacillus subtilis ALDH-like ycbD protein, which is involved in d-glucarate/d-galactarate utilization, reveal that it is a NADP+-dependent, alpha-ketoglutaric semialdehyde dehydrogenase (KGSADH). KGSADHs (EC 1.2.1.26) catalyze the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. Interestingly, the NADP+-dependent, tetrameric, 2,5-dioxopentanoate dehydrogenase (EC=1.2.1.26), an enzyme involved in the catabolic pathway for D-arabinose in Sulfolobus solfataricus, also clusters in this group. This CD shows a distant phylogenetic relationship to the Azospirillum brasilense KGSADH-II (-III) group.


Pssm-ID: 143415 [Multi-domain]  Cd Length: 473  Bit Score: 139.69  E-value: 3.61e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653  42 HYVNGKWLKP----EHRNsvPCQdpiTGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQR 117
Cdd:cd07097    3 NYIDGEWVAGgdgeENRN--PSD---TSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 118 LLWTLESLVTGRAVREVRdGDVQLAQQLLHYHA---------IQASTQE--EALAGWEPMGVIGLILPPTFSFLEMMWRI 186
Cdd:cd07097   78 ELARLLTREEGKTLPEAR-GEVTRAGQIFRYYAgealrlsgeTLPSTRPgvEVETTREPLGVVGLITPWNFPIAIPAWKI 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 187 CPALAVGCTVValVPPASPAPLLLAQLA---GELGPFPGILNVLSGPASLV-PILASQPGIRKVAFCGAPEGGL------ 256
Cdd:cd07097  157 APALAYGNTVV--FKPAELTPASAWALVeilEEAGLPAGVFNLVMGSGSEVgQALVEHPDVDAVSFTGSTAVGRriaaaa 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 257 ------------------------------------------------RLLIQESVWDEAMRRLQERMGRLRSGRGLDGA 288
Cdd:cd07097  235 aargarvqlemggknplvvlddadldlavecavqgaffstgqrctassRLIVTEGIHDRFVEALVERTKALKVGDALDEG 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 289 VDMG-ARGAAACDLVQRFVREAQSQGAQVFQAGD-VPSERP--FYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEA 364
Cdd:cd07097  315 VDIGpVVSERQLEKDLRYIEIARSEGAKLVYGGErLKRPDEgyYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEA 394
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 223972653 365 LLVANGTPRGGSASVWSERLGQALELGYGLQVGTVWINA--HGLrDPSVPTGGCKESG 420
Cdd:cd07097  395 LAIANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLptAGV-DYHVPFGGRKGSS 451
PLN02766 PLN02766
coniferyl-aldehyde dehydrogenase
43-435 1.55e-34

coniferyl-aldehyde dehydrogenase


Pssm-ID: 215410 [Multi-domain]  Cd Length: 501  Bit Score: 138.42  E-value: 1.55e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653  43 YVNGKWLKPEHRNSVPCQDPITGENLASCLQAQAEDVAAAVEAARMAFKG--WSAHPGVVRAQHLTRLAEVIQKHQRLLW 120
Cdd:PLN02766  24 FINGEFVDAASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDHgpWPRMSGFERGRIMMKFADLIEEHIEELA 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 121 TLESLVTGRAVREVRDGDVQLAQQLLHYHA-----IQAST--QEEALAGW---EPMGVIGLILPPTFSFLEMMWRICPAL 190
Cdd:PLN02766 104 ALDTIDAGKLFALGKAVDIPAAAGLLRYYAgaadkIHGETlkMSRQLQGYtlkEPIGVVGHIIPWNFPSTMFFMKVAPAL 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 191 AVGCTVValVPPASPAP---LLLAQLAGELGPFPGILNVLSGPASLV-PILASQPGIRKVAFCGAPE------------- 253
Cdd:PLN02766 184 AAGCTMV--VKPAEQTPlsaLFYAHLAKLAGVPDGVINVVTGFGPTAgAAIASHMDVDKVSFTGSTEvgrkimqaaatsn 261
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 254 ------------------------------------------GGLRLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDM 291
Cdd:PLN02766 262 lkqvslelggkspllifddadvdmavdlallgifynkgeicvASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPFDPRARQ 341
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 292 GAR-GAAACDLVQRFVREAQSQGAQVFQAGDVPSERPFY-PPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVAN 369
Cdd:PLN02766 342 GPQvDKQQFEKILSYIEHGKREGATLLTGGKPCGDKGYYiEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEEAIKKAN 421
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 223972653 370 GTPRGGSASVWSERLGQALELGYGLQVGTVWINAHGLRDPSVPTGGCKESGCSWHGGPDGLYEYLR 435
Cdd:PLN02766 422 NTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFAFDPDCPFGGYKMSGFGRDQGMDALDKYLQ 487
ALDH_SSADH1_GabD1 cd07100
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ...
89-432 3.71e-34

Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde dehydrogenase 1 (SSADH1, GabD1, EC=1.2.1.16) catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde (SSA) to succinate. SSADH activity in Mycobacterium tuberculosis (Mtb) is encoded by both gabD1 (Rv0234c) and gabD2 (Rv1731). The Mtb GabD1 SSADH1 reportedly is an enzyme of the gamma-aminobutyrate shunt, which forms a functional link between two TCA half-cycles by converting alpha-ketoglutarate to succinate.


Pssm-ID: 143418 [Multi-domain]  Cd Length: 429  Bit Score: 135.67  E-value: 3.71e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653  89 AFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTLESLVTGRAVREVRdGDVQLAQQLLHYHAIQAstqEEALAG------ 162
Cdd:cd07100   11 AFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEAR-AEVEKCAWICRYYAENA---EAFLADepietd 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 163 -------WEPMGVIGLILPPTFSFLEMMwRIC-PALAVGCTVvaLVPPASPAP---LLLAQLAGELGPFPGILNVLSGPA 231
Cdd:cd07100   87 agkayvrYEPLGVVLGIMPWNFPFWQVF-RFAaPNLMAGNTV--LLKHASNVPgcaLAIEELFREAGFPEGVFQNLLIDS 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 232 SLVPILASQPGIRKVAFCGAPEGG-----------------L-------------------------------------R 257
Cdd:cd07100  164 DQVEAIIADPRVRGVTLTGSERAGravaaeagknlkksvleLggsdpfivlddadldkavktavkgrlqnagqsciaakR 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 258 LLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMG--ARgAAACDLVQRFVREAQSQGAQVFQAGDVPsERP--FYPPTL 333
Cdd:cd07100  244 FIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGplAR-KDLRDELHEQVEEAVAAGATLLLGGKRP-DGPgaFYPPTV 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 334 VSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVANGTPRGGSASVWSERLGQALELGYGLQVGTVWINAHGLRDPSVPT 413
Cdd:cd07100  322 LTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMVFINGMVKSDPRLPF 401
                        410       420
                 ....*....|....*....|..
gi 223972653 414 GGCKESGcswHG---GPDGLYE 432
Cdd:cd07100  402 GGVKRSG---YGrelGRFGIRE 420
PLN02466 PLN02466
aldehyde dehydrogenase family 2 member
42-435 2.49e-33

aldehyde dehydrogenase family 2 member


Pssm-ID: 215259 [Multi-domain]  Cd Length: 538  Bit Score: 135.32  E-value: 2.49e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653  42 HYVNGKWLKPEHRNSVPCQDPITGENLASCLQAQAEDVAAAVEAARMAFKG--WSAHPGVVRAQHLTRLAEVIQKHQRLL 119
Cdd:PLN02466  60 LLINGQFVDAASGKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFDEgpWPKMTAYERSRILLRFADLLEKHNDEL 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 120 WTLESLVTGRAVREVRDGDVQLAQQLLHYHA----------IQASTQEEALAGWEPMGVIGLILPPTFSFLEMMWRICPA 189
Cdd:PLN02466 140 AALETWDNGKPYEQSAKAELPMFARLFRYYAgwadkihgltVPADGPHHVQTLHEPIGVAGQIIPWNFPLLMFAWKVGPA 219
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 190 LAVGCTVVALVPPASP-APLLLAQLAGELGPFPGILNVLSG-PASLVPILASQPGIRKVAFCGAPE-------------- 253
Cdd:PLN02466 220 LACGNTIVLKTAEQTPlSALYAAKLLHEAGLPPGVLNVVSGfGPTAGAALASHMDVDKLAFTGSTDtgkivlelaaksnl 299
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 254 -----------------------------------------GGLRLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMG 292
Cdd:PLN02466 300 kpvtlelggkspfivcedadvdkavelahfalffnqgqcccAGSRTFVHERVYDEFVEKAKARALKRVVGDPFKKGVEQG 379
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 293 AR-GAAACDLVQRFVREAQSQGAQVFQAGDVPSERPFY-PPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVANG 370
Cdd:PLN02466 380 PQiDSEQFEKILRYIKSGVESGATLECGGDRFGSKGYYiQPTVFSNVQDDMLIAQDEIFGPVQSILKFKDLDEVIRRANN 459
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 223972653 371 TPRGGSASVWSERLGQALELGYGLQVGTVWINAHGLRDPSVPTGGCKESGCSWHGGPDGLYEYLR 435
Cdd:PLN02466 460 TRYGLAAGVFTQNLDTANTLSRALRVGTVWVNCFDVFDAAIPFGGYKMSGIGREKGIYSLNNYLQ 524
ALDH_y4uC cd07149
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ...
61-420 5.74e-33

Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; Uncharacterized aldehyde dehydrogenase (ORF name y4uC) with sequence similarity to the moss Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123) believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and similar sequences are included in this CD.


Pssm-ID: 143467 [Multi-domain]  Cd Length: 453  Bit Score: 132.72  E-value: 5.74e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653  61 DPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTLESLVTGRAVREVRdGDVQ 140
Cdd:cd07149    5 SPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDAR-KEVD 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 141 LAQQLLHYHA------------IQASTQEEALAGW---EPMGVIGLILPPTFSFLEMMWRICPALAVGCTVValVPPASP 205
Cdd:cd07149   84 RAIETLRLSAeeakrlagetipFDASPGGEGRIGFtirEPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVV--LKPASQ 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 206 APL---LLAQLAGELGPFPGILNVLSGPASLV-PILASQPGIRKVAFCGAPEGGL------------------------- 256
Cdd:cd07149  162 TPLsalKLAELLLEAGLPKGALNVVTGSGETVgDALVTDPRVRMISFTGSPAVGEaiarkaglkkvtlelgsnaavivda 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 257 ---------------------------RLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMGAR-GAAACDLVQRFVRE 308
Cdd:cd07149  242 dadlekavercvsgafanagqvcisvqRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMiSEAEAERIEEWVEE 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 309 AQSQGAQVFQAGDVpsERPFYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVANGTPRGGSASVWSERLGQAL 388
Cdd:cd07149  322 AVEGGARLLTGGKR--DGAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVFTNDLQKAL 399
                        410       420       430
                 ....*....|....*....|....*....|...
gi 223972653 389 ELGYGLQVGTVWIN-AHGLRDPSVPTGGCKESG 420
Cdd:cd07149  400 KAARELEVGGVMINdSSTFRVDHMPYGGVKESG 432
ALDH_VaniDH_like cd07150
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ...
61-433 1.21e-32

Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved in the metabolism of ferulic acid and other related sequences are included in this CD. The E. coli vanillin dehydrogenase (LigV) preferred NAD+ to NADP+ and exhibited a broad substrate preference, including vanillin, benzaldehyde, protocatechualdehyde, m-anisaldehyde, and p-hydroxybenzaldehyde.


Pssm-ID: 143468 [Multi-domain]  Cd Length: 451  Bit Score: 131.68  E-value: 1.21e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653  61 DPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTLESLVTGRAVREVrDGDVQ 140
Cdd:cd07150    5 NPADGSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKA-WFETT 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 141 LAQQLLHY-----HAIQASTQEEALAGW------EPMGVIGLILPPTFSFLEMMWRICPALAVGCTVValVPPASPAP-- 207
Cdd:cd07150   84 FTPELLRAaagecRRVRGETLPSDSPGTvsmsvrRPLGVVAGITPFNYPLILATKKVAFALAAGNTVV--LKPSEETPvi 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 208 -LLLAQLAGELGPFPGILNVLSGPASLV-PILASQPGIRKVAFCGAPEGGL----------------------------- 256
Cdd:cd07150  162 gLKIAEIMEEAGLPKGVFNVVTGGGAEVgDELVDDPRVRMVTFTGSTAVGReiaekagrhlkkitlelggknplivlada 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 257 -------------------------RLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMG-ARGAAACDLVQRFVREAQ 310
Cdd:cd07150  242 dldyavraaafgafmhqgqicmsasRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGpLISPRQVERIKRQVEDAV 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 311 SQGAQVFQAGDVpsERPFYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVANGTPRGGSASVWSERLGQALEL 390
Cdd:cd07150  322 AKGAKLLTGGKY--DGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTNDLQRAFKL 399
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....
gi 223972653 391 GYGLQVGTVWINAHGLRD-PSVPTGGCKESGCSWHGGPDGLYEY 433
Cdd:cd07150  400 AERLESGMVHINDPTILDeAHVPFGGVKASGFGREGGEWSMEEF 443
gabD PRK11241
NADP-dependent succinate-semialdehyde dehydrogenase I;
43-434 5.87e-32

NADP-dependent succinate-semialdehyde dehydrogenase I;


Pssm-ID: 183050 [Multi-domain]  Cd Length: 482  Bit Score: 130.41  E-value: 5.87e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653  43 YVNGKWLKPEHRNSVPCQDPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTL 122
Cdd:PRK11241  14 LINGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMMEHQDDLARL 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 123 ESLVTGRAVREVRdGDVQLAQQLLHYHAIQA-----------STQEEALAGWEPMGVIGLILPPTFSFLEMMWRICPALA 191
Cdd:PRK11241  94 MTLEQGKPLAEAK-GEISYAASFIEWFAEEGkriygdtipghQADKRLIVIKQPIGVTAAITPWNFPAAMITRKAGPALA 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 192 VGCTVValVPPASPAP---LLLAQLAGELGPFPGILNVLSGPASLV-PILASQPGIRKVAFCG----------------- 250
Cdd:PRK11241 173 AGCTMV--LKPASQTPfsaLALAELAIRAGIPAGVFNVVTGSAGAVgGELTSNPLVRKLSFTGsteigrqlmeqcakdik 250
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 251 ----------------------APEGGL---------------RLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMGA 293
Cdd:PRK11241 251 kvslelggnapfivfddadldkAVEGALaskfrnagqtcvcanRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEKGVTIGP 330
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 294 R-GAAACDLVQRFVREAQSQGAQVFQAGDVPS-ERPFYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVANGT 371
Cdd:PRK11241 331 LiDEKAVAKVEEHIADALEKGARVVCGGKAHElGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEADVIAQANDT 410
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 223972653 372 PRGGSASVWSERLGQALELGYGLQVGTVWINAHGLRDPSVPTGGCKESGCSWHGGPDGLYEYL 434
Cdd:PRK11241 411 EFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYL 473
AdhE COG1012
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ...
474-716 7.07e-32

Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and metabolism]; Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase is part of the Pathway/BioSystem: Proline degradation


Pssm-ID: 440636 [Multi-domain]  Cd Length: 479  Bit Score: 129.86  E-value: 7.07e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 474 APPYGLFVGGRFQAPGARSSRPIRD-SSGNLHGYVAEGGAKDIRGAVEAAHQAFPGWAGQSPgaraallwalaaaLERRK 552
Cdd:COG1012    3 TPEYPLFIGGEWVAAASGETFDVINpATGEVLARVPAATAEDVDAAVAAARAAFPAWAATPP-------------AERAA 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 553 --STLASRLER------------QGAELKAAEAEVELSARRLR-AWGARVQAQGHTLQVAGLRGPVLRLREPLGVLAVVC 617
Cdd:COG1012   70 ilLRAADLLEErreelaalltleTGKPLAEARGEVDRAADFLRyYAGEARRLYGETIPSDAPGTRAYVRREPLGVVGAIT 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 618 PDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLALEVCQDMATV-FPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGS 696
Cdd:COG1012  150 PWNFPLALAAWKLAPALAAGNTVVLKPAEQTPLSALLLAELLEEAgLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGS 229
                        250       260
                 ....*....|....*....|.
gi 223972653 697 AQ-GSQFVEWAsAGNLKPVWA 716
Cdd:COG1012  230 TAvGRRIAAAA-AENLKRVTL 249
ALDH_PhpJ cd07146
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ...
101-435 8.43e-32

Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative phosphonoformaldehyde dehydrogenase (PhpJ), an aldehyde dehydrogenase homolog reportedly involved in the biosynthesis of phosphinothricin tripeptides in Streptomyces viridochromogenes DSM 40736, and similar sequences are included in this CD.


Pssm-ID: 143464 [Multi-domain]  Cd Length: 451  Bit Score: 129.40  E-value: 8.43e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 101 RAQHLTRLAEVIQKHQRLLWTLESLVTGRAVREVRDgDVQLAQQLLHYHAIQA-STQEEALAG--------------WEP 165
Cdd:cd07146   42 RSAILNKAAALLEARREEFARLITLESGLCLKDTRY-EVGRAADVLRFAAAEAlRDDGESFSCdltangkarkiftlREP 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 166 MGVIGLILPPTFSFLEMMWRICPALAVGCTVValVPPASPAPL---LLAQLAGELGPFPGILNVLSG-PASLVPILASQP 241
Cdd:cd07146  121 LGVVLAITPFNHPLNQVAHKIAPAIAANNRIV--LKPSEKTPLsaiYLADLLYEAGLPPDMLSVVTGePGEIGDELITHP 198
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 242 GIRKVAFCGA-----------------------------PEGGL-----------------------RLLIQESVWDEAM 269
Cdd:cd07146  199 DVDLVTFTGGvavgkaiaatagykrqllelggndplivmDDADLeraatlavagsyansgqrctavkRILVHESVADEFV 278
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 270 RRLQERMGRLRSGRGLDGAVDMGA---RGAAacDLVQRFVREAQSQGAQVFQAGdvpsER--PFYPPTLVSNLPPASPCA 344
Cdd:cd07146  279 DLLVEKSAALVVGDPMDPATDMGTvidEEAA--IQIENRVEEAIAQGARVLLGN----QRqgALYAPTVLDHVPPDAELV 352
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 345 QVEVPWPVVVASPFRTAKEALLVANGTPRGGSASVWSERLGQALELGYGLQVGTVWIN-AHGLRDPSVPTGGCKESGCsw 423
Cdd:cd07146  353 TEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTNDLDTIKRLVERLDVGTVNVNeVPGFRSELSPFGGVKDSGL-- 430
                        410
                 ....*....|..
gi 223972653 424 hGGPDGLYEYLR 435
Cdd:cd07146  431 -GGKEGVREAMK 441
ALDH_HBenzADH cd07151
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ...
46-420 7.32e-30

NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, p-hydroxybenzaldehyde dehydrogenase (PchA, HBenzADH) which catalyzes oxidation of p-hydroxybenzaldehyde to p-hydroxybenzoic acid and other related sequences are included in this CD.


Pssm-ID: 143469 [Multi-domain]  Cd Length: 465  Bit Score: 123.57  E-value: 7.32e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653  46 GKWLKPEHRNSVPCQDPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHqrllwtlESL 125
Cdd:cd07151    1 GEWRDGTSERTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEER-------RDE 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 126 VTGRAVREvrDGDVQLAQQLlHYHAIQASTQEEA--------------LAGWE------PMGVIGLILPPTFSFLEMMWR 185
Cdd:cd07151   74 IVEWLIRE--SGSTRIKANI-EWGAAMAITREAAtfplrmegrilpsdVPGKEnrvyrePLGVVGVISPWNFPLHLSMRS 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 186 ICPALAVGCTVValVPPASPAP----LLLAQLAGELGPFPGILNVLSGPAS---------LVPILASQPGIRKV-----A 247
Cdd:cd07151  151 VAPALALGNAVV--LKPASDTPitggLLLAKIFEEAGLPKGVLNVVVGAGSeigdafvehPVPRLISFTGSTPVgrhigE 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 248 FCG--------------------------APEGGL---------------RLLIQESVWDEAMRRLQERMGRLRSGRGLD 286
Cdd:cd07151  229 LAGrhlkkvalelggnnpfvvledadidaAVNAAVfgkflhqgqicmainRIIVHEDVYDEFVEKFVERVKALPYGDPSD 308
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 287 GAVDMGAR-GAAACDLVQRFVREAQSQGAQVFQAGDVpsERPFYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEAL 365
Cdd:cd07151  309 PDTVVGPLiNESQVDGLLDKIEQAVEEGATLLVGGEA--EGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEAL 386
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 223972653 366 LVANGTPRGGSASVWSERLGQALELGYGLQVGTVWINAHGLRD-PSVPTGGCKESG 420
Cdd:cd07151  387 ELANDTEYGLSGAVFTSDLERGVQFARRIDAGMTHINDQPVNDePHVPFGGEKNSG 442
ALDH_F21_LactADH-like cd07094
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ...
61-436 1.96e-29

ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related proteins; ALDH subfamily which includes Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123), and NAD+-dependent, lactaldehyde dehydrogenase (EC=1.2.1.22) and like sequences.


Pssm-ID: 143413 [Multi-domain]  Cd Length: 453  Bit Score: 122.16  E-value: 1.96e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653  61 DPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTLESLVTGRAVREVRD---- 136
Cdd:cd07094    5 NPYDGEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARVevdr 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 137 --GDVQLAQQLLHYH--------AIQASTQEEALAGWEPMGVIGLILPPTFSFLEMMWRICPALAVGCTVValVPPASPA 206
Cdd:cd07094   85 aiDTLRLAAEEAERIrgeeipldATQGSDNRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVV--LKPASKT 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 207 PL---LLAQLAGELGPFPGILNVLSG-PASLVPILASQPGIRKVAFCGAPE------------------GGL-------- 256
Cdd:cd07094  163 PLsalELAKILVEAGVPEGVLQVVTGeREVLGDAFAADERVAMLSFTGSAAvgealranaggkrialelGGNapvivdrd 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 257 --------------------------RLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMGAR-GAAACDLVQRFVREA 309
Cdd:cd07094  243 adldaaiealakggfyhagqvcisvqRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLiSEEAAERVERWVEEA 322
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 310 QSQGAQVFQAGDvpSERPFYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVANGTPRGGSASVWSERLGQALE 389
Cdd:cd07094  323 VEAGARLLCGGE--RDGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRDLNVAFK 400
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*...
gi 223972653 390 LGYGLQVGTVWINAHG-LRDPSVPTGGCKESGCSWHGGPDGLYEYLRP 436
Cdd:cd07094  401 AAEKLEVGGVMVNDSSaFRTDWMPFGGVKESGVGREGVPYAMEEMTEE 448
ALDH_SSADH2_GabD2 cd07101
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ...
61-433 4.54e-29

Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde dehydrogenase 2 (SSADH2) and similar proteins are in this CD. SSADH1 (GabD1, EC=1.2.1.16) catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde to succinate. SSADH activity in Mycobacterium tuberculosis is encoded by both gabD1 (Rv0234c) and gabD2 (Rv1731), however ,the Vmax of GabD1 was shown to be much higher than that of GabD2, and GabD2 (SSADH2) is likely to serve physiologically as a dehydrogenase for a different aldehyde(s).


Pssm-ID: 143419 [Multi-domain]  Cd Length: 454  Bit Score: 121.26  E-value: 4.54e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653  61 DPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTLESLVTGRAVREVRDGDVQ 140
Cdd:cd07101    2 APFTGEPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEVLD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 141 LAQQLLHYhaiqASTQEEALA----------------GWEPMGVIGLILPPTFSFLEMMWRICPALAVGCTVVALVPPAS 204
Cdd:cd07101   82 VAIVARYY----ARRAERLLKprrrrgaipvltrttvNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQT 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 205 P-APLLLAQLAGELGPFPGILNVLSGPASLV--------------------PILASQPGIRKVAFC-------------- 249
Cdd:cd07101  158 AlTALWAVELLIEAGLPRDLWQVVTGPGSEVggaivdnadyvmftgstatgRVVAERAGRRLIGCSlelggknpmivled 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 250 --------GAPEGGL-----------RLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMGA-RGAAACDLVQRFVREA 309
Cdd:cd07101  238 adldkaaaGAVRACFsnagqlcvsieRIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSlISQAQLDRVTAHVDDA 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 310 QSQGAQVFQAGdvpSERP-----FYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVANGTPRGGSASVWSERL 384
Cdd:cd07101  318 VAKGATVLAGG---RARPdlgpyFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTRDG 394
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....
gi 223972653 385 GQALELGYGLQVGTVWIN-----AHGLRDpsVPTGGCKESGCSWHGGPDGLYEY 433
Cdd:cd07101  395 ARGRRIAARLRAGTVNVNegyaaAWASID--APMGGMKDSGLGRRHGAEGLLKY 446
PRK13252 PRK13252
betaine aldehyde dehydrogenase; Provisional
42-420 5.88e-28

betaine aldehyde dehydrogenase; Provisional


Pssm-ID: 183918  Cd Length: 488  Bit Score: 118.44  E-value: 5.88e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653  42 HYVNGKWLKPEHRNSVPCQDPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWT 121
Cdd:PRK13252   9 LYIDGAYVEATSGETFEVINPATGEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRERNDELAA 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 122 LESLVTGRAVREVRDGDVQLAQQLLHYHAIQASTQE---EALAG-------WEPMGVIGLILPPTFSFLEMMWRICPALA 191
Cdd:PRK13252  89 LETLDTGKPIQETSVVDIVTGADVLEYYAGLAPALEgeqIPLRGgsfvytrREPLGVCAGIGAWNYPIQIACWKSAPALA 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 192 VGCTVValVPPASPAPLL---LAQLAGELGPFPGILNVLSGPASLVPILASQPGIRKVAFCG-APEG------------- 254
Cdd:PRK13252 169 AGNAMI--FKPSEVTPLTalkLAEIYTEAGLPDGVFNVVQGDGRVGAWLTEHPDIAKVSFTGgVPTGkkvmaaaaaslke 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 255 ----------------------------------------GLRLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMGAR 294
Cdd:PRK13252 247 vtmelggksplivfddadldraadiamlanfyssgqvctnGTRVFVQKSIKAAFEARLLERVERIRIGDPMDPATNFGPL 326
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 295 -GAAACDLVQRFVREAQSQGAQVFQAGDVPSER-----PFYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVA 368
Cdd:PRK13252 327 vSFAHRDKVLGYIEKGKAEGARLLCGGERLTEGgfangAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDEDEVIARA 406
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|..
gi 223972653 369 NGTPRGGSASVWSERLGQALELGYGLQVGTVWINAHGLRDPSVPTGGCKESG 420
Cdd:PRK13252 407 NDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTWGESPAEMPVGGYKQSG 458
ALDH_SaliADH cd07105
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ...
89-435 1.97e-27

Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2.1.65) involved in the upper naphthalene catabolic pathway of Pseudomonas strain C18 and other similar sequences are present in this CD.


Pssm-ID: 143423 [Multi-domain]  Cd Length: 432  Bit Score: 115.75  E-value: 1.97e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653  89 AFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTLESLVTGrAVREVRDGDVQLAQQLLHYHAIQASTQEE---------- 158
Cdd:cd07105   12 AFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETG-ATAAWAGFNVDLAAGMLREAASLITQIIGgsipsdkpgt 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 159 -ALAGWEPMGVIGLILPPTFSFLEMMWRICPALAVGCTVVALVPPASPAP-LLLAQLAGELGPFPGILNVLS-GP---AS 232
Cdd:cd07105   91 lAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRThWLIGRVFHEAGLPKGVLNVVThSPedaPE 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 233 LVPILASQPGIRKVAFCG---------------------------------------APEGGL---------------RL 258
Cdd:cd07105  171 VVEALIAHPAVRKVNFTGstrvgriiaetaakhlkpvllelggkapaivledadldaAANAALfgaflnsgqicmsteRI 250
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 259 LIQESVWDEAMRRLQERMGRLRSGrgldGAVDMGARGAAACDLVQRFVREAQSQGAQVFqAGDVPSERP---FYPPTLVS 335
Cdd:cd07105  251 IVHESIADEFVEKLKAAAEKLFAG----PVVLGSLVSAAAADRVKELVDDALSKGAKLV-VGGLADESPsgtSMPPTILD 325
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 336 NLPPASPCAQVEVPWPVVVASPFRTAKEALLVANGTPRGGSASVWSERLGQALELGYGLQVGTVWINAHGLRD-PSVPTG 414
Cdd:cd07105  326 NVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVHINGMTVHDePTLPHG 405
                        410       420
                 ....*....|....*....|.
gi 223972653 415 GCKESGCSWHGGPDGLYEYLR 435
Cdd:cd07105  406 GVKSSGYGRFNGKWGIDEFTE 426
ALDH_BenzADH cd07152
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ...
89-433 5.05e-27

NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II (XylC, BenzADH, EC=1.2.1.28) is involved in the oxidation of benzyl alcohol to benzoate. In Acinetobacter calcoaceticus, this process is carried out by the chromosomally encoded, benzyl alcohol dehydrogenase (xylB) and benzaldehyde dehydrogenase II (xylC) enzymes; whereas in Pseudomonas putida they are encoded by TOL plasmids.


Pssm-ID: 143470 [Multi-domain]  Cd Length: 443  Bit Score: 114.70  E-value: 5.05e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653  89 AFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTLESLVTGrAVREVRDGDVQLAQQLLHyHAIQASTQEE---------- 158
Cdd:cd07152   25 AQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESG-SIRPKAGFEVGAAIGELH-EAAGLPTQPQgeilpsapgr 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 159 -ALAGWEPMGVIGLILPPTFSFLEMMWRICPALAVGCTVVALVPPASPAP--LLLAQLAGELGPFPGILNVLSGPASLVP 235
Cdd:cd07152  103 lSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSggVVIARLFEEAGLPAGVLHVLPGGADAGE 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 236 ILASQPGIRKVAFCGAPEGGL------------------------------------------------------RLLIQ 261
Cdd:cd07152  183 ALVEDPNVAMISFTGSTAVGRkvgeaagrhlkkvslelggknalivlddadldlaasngawgaflhqgqicmaagRHLVH 262
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 262 ESVWDEAMRRLQERMGRLRSGRGLDGAVDMGAR-GAAACDLVQRFVREAQSQGAQVFQAGDvpSERPFYPPTLVSNLPPA 340
Cdd:cd07152  263 ESVADAYTAKLAAKAKHLPVGDPATGQVALGPLiNARQLDRVHAIVDDSVAAGARLEAGGT--YDGLFYRPTVLSGVKPG 340
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 341 SPCAQVEVPWPVVVASPFRTAKEALLVANGTPRGGSASVWSERLGQALELGYGLQVGTVWINAHGLRD-PSVPTGGCKES 419
Cdd:cd07152  341 MPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALADRLRTGMLHINDQTVNDePHNPFGGMGAS 420
                        410
                 ....*....|....*
gi 223972653 420 GC-SWHGGPDGLYEY 433
Cdd:cd07152  421 GNgSRFGGPANWEEF 435
ALDH_PutA-P5CDH-RocA cd07124
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ...
22-436 2.89e-26

Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate dehydrogenase (EC=1.5.1.12 ), RocA: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. The proline catabolic enzymes, proline dehydrogenase and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH), catalyze the two-step oxidation of proline to glutamate; P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA). In this CD, monofunctional enzyme sequences such as seen in the Bacillus subtilis RocA P5CDH are also present. These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis.


Pssm-ID: 143442  Cd Length: 512  Bit Score: 113.47  E-value: 2.89e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653  22 VPESHACALAWLDTQDRCLG-HY---VNGKWLKPEHR-NSV-PCQdpiTGENLASCLQAQAEDVAAAVEAARMAFKGWSA 95
Cdd:cd07124   11 DEENRAAFRAALARVREELGrEYplvIGGKEVRTEEKiESRnPAD---PSEVLGTVQKATKEEAEAAVQAARAAFPTWRR 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653  96 HPGVVRAQHLTRLAEVIQKHQRLLWTLESLVTGRAVREVrDGDVQLAQQLLHYHAIQAstqeEALAG------------- 162
Cdd:cd07124   88 TPPEERARLLLRAAALLRRRRFELAAWMVLEVGKNWAEA-DADVAEAIDFLEYYAREM----LRLRGfpvemvpgednry 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 163 -WEPMGVIGLILPPTFSFLEMMWRICPALAVGCTVValVPPASPAPL---LLAQLAGELGPFPGILNVLSGPASLV-PIL 237
Cdd:cd07124  163 vYRPLGVGAVISPWNFPLAILAGMTTAALVTGNTVV--LKPAEDTPViaaKLVEILEEAGLPPGVVNFLPGPGEEVgDYL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 238 ASQPGIRKVAFCGAPEGGL------------------------------------------------------------R 257
Cdd:cd07124  241 VEHPDVRFIAFTGSREVGLriyeraakvqpgqkwlkrviaemggknaiivdedadldeaaegivrsafgfqgqkcsacsR 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 258 LLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMGAR-GAAACDLVQRFVREAQSQGaQVFQAGDVPSERP---FYPPTL 333
Cdd:cd07124  321 VIVHESVYDEFLERLVERTKALKVGDPEDPEVYMGPViDKGARDRIRRYIEIGKSEG-RLLLGGEVLELAAegyFVQPTI 399
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 334 VSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVANGTPRGGSASVWS---ERLGQALElgyGLQVGTVWINahglRD-- 408
Cdd:cd07124  400 FADVPPDHRLAQEEIFGPVLAVIKAKDFDEALEIANDTEYGLTGGVFSrspEHLERARR---EFEVGNLYAN----RKit 472
                        490       500       510
                 ....*....|....*....|....*....|...
gi 223972653 409 ---PSV-PTGGCKESGC-SWHGGPDGLYEYLRP 436
Cdd:cd07124  473 galVGRqPFGGFKMSGTgSKAGGPDYLLQFMQP 505
gabD2 PRK09407
succinic semialdehyde dehydrogenase; Reviewed
51-433 2.97e-25

succinic semialdehyde dehydrogenase; Reviewed


Pssm-ID: 236501 [Multi-domain]  Cd Length: 524  Bit Score: 110.35  E-value: 2.97e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653  51 PEHRNSVPCQDPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTLESLVTGRA 130
Cdd:PRK09407  28 GAAGPTREVTAPFTGEPLATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLETGKA 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 131 VREVRDGDVQLAQQLLHYhaiqASTQEEALA----------------GWEPMGVIGLILPPTFSFLEMMWRICPALAVGC 194
Cdd:PRK09407 108 RRHAFEEVLDVALTARYY----ARRAPKLLAprrragalpvltktteLRQPKGVVGVISPWNYPLTLAVSDAIPALLAGN 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 195 TVVAlvPPASPAP---LLLAQLAGELGPFPGILNVLSGPASLV--------------------PILASQPGIRKVAFC-- 249
Cdd:PRK09407 184 AVVL--KPDSQTPltaLAAVELLYEAGLPRDLWQVVTGPGPVVgtalvdnadylmftgstatgRVLAEQAGRRLIGFSle 261
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 250 --------------------GAPEGGL-----------RLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMGA-RGAA 297
Cdd:PRK09407 262 lggknpmivlddadldkaaaGAVRACFsnagqlcisieRIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSADMGSlISEA 341
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 298 ACDLVQRFVREAQSQGAQVFqAGDVPseRP-----FYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVANGTP 372
Cdd:PRK09407 342 QLETVSAHVDDAVAKGATVL-AGGKA--RPdlgplFYEPTVLTGVTPDMELAREETFGPVVSVYPVADVDEAVERANDTP 418
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 223972653 373 RGGSASVWSERLGQALELGYGLQVGTVWIN-----AHGLRDpsVPTGGCKESGCSWHGGPDGLYEY 433
Cdd:PRK09407 419 YGLNASVWTGDTARGRAIAARIRAGTVNVNegyaaAWGSVD--APMGGMKDSGLGRRHGAEGLLKY 482
ALDH_F1-2_Ald2-like cd07091
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ...
476-714 6.44e-25

ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD+-dependent retinal dehydrogenase 1 and related proteins; ALDH subfamily which includes the NAD+-dependent retinal dehydrogenase 1 (RALDH 1, ALDH1, EC=1.2.1.36), also known as aldehyde dehydrogenase family 1 member A1 (ALDH1A1), in humans, a homotetrameric, cytosolic enzyme that catalyzes the oxidation of retinaldehyde to retinoic acid. Human ALDH1B1 and ALDH2 are also in this cluster; both are mitochrondrial homotetramers which play important roles in acetaldehyde oxidation; ALDH1B1 in response to UV light exposure and ALDH2 during ethanol metabolism. 10-formyltetrahydrofolate dehydrogenase (FTHFDH, EC=1.5.1.6), also known as aldehyde dehydrogenase family 1 member L1 (ALDH1L1), in humans, a multi-domain homotetramer with an N-terminal formyl transferase domain and a C-terminal ALDH domain. FTHFDH catalyzes an NADP+-dependent dehydrogenase reaction resulting in the conversion of 10-formyltetrahydrofolate to tetrahydrofolate and CO2. Also included in this subfamily is the Arabidosis aldehyde dehydrogenase family 2 members B4 and B7 (EC=1.2.1.3), which are mitochondrial, homotetramers that oxidize acetaldehyde and glycolaldehyde, as well as, the Arabidosis cytosolic, homotetramer ALDH2C4 (EC=1.2.1.3), an enzyme involved in the oxidation of sinapalehyde and coniferaldehyde. Also included is the AldA aldehyde dehydrogenase of Aspergillus nidulans (locus AN0554), the aldehyde dehydrogenase 2 (YMR170c, ALD5, EC=1.2.1.5) of Saccharomyces cerevisiae, and other similar sequences.


Pssm-ID: 143410  Cd Length: 476  Bit Score: 108.84  E-value: 6.44e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 476 PYGLFVGGRF-QAPGARSSRPIRDSSGNLHGYVAEGGAKDIRGAVEAAHQAFPGWAGQSpgaraallwalAAALERRK-- 552
Cdd:cd07091    3 PTGLFINNEFvDSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFETGWWRK-----------MDPRERGRll 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 553 STLASRLERQGAELKAAEA-------------EVELSARRLR---AWGARVQaqGHTLQVAGlRGPVLRLREPLGVLAVV 616
Cdd:cd07091   72 NKLADLIERDRDELAALESldngkpleesakgDVALSIKCLRyyaGWADKIQ--GKTIPIDG-NFLAYTRREPIGVCGQI 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 617 CPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLALEVCQDMATV-FPAGLANVVTGDRDHLTRCLALHQDVQAMWYFG 695
Cdd:cd07091  149 IPWNFPLLMLAWKLAPALAAGNTVVLKPAEQTPLSALYLAELIKEAgFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTG 228
                        250       260
                 ....*....|....*....|
gi 223972653 696 S-AQGSQFVEWASAGNLKPV 714
Cdd:cd07091  229 StAVGRTIMEAAAKSNLKKV 248
ALDH_F11_NP-GAPDH cd07082
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ...
43-420 1.29e-24

NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family 11; NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase (NP-GAPDH, EC=1.2.1.9) catalyzes the irreversible oxidation of glyceraldehyde 3-phosphate to 3-phosphoglycerate generating NADPH for biosynthetic reactions. This CD also includes the Arabidopsis thaliana osmotic-stress-inducible ALDH family 11, ALDH11A3 and similar sequences. In autotrophic eukaryotes, NP-GAPDH generates NADPH for biosynthetic processes from photosynthetic glyceraldehyde-3-phosphate exported from the chloroplast and catalyzes one of the classic glycolytic bypass reactions unique to plants.


Pssm-ID: 143401 [Multi-domain]  Cd Length: 473  Bit Score: 108.04  E-value: 1.29e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653  43 YVNGKWLKPEHrNSVPCQDPITGENLASCLQAQAEDVAAAVEAARMAFKGWSA-HPGVVRAQHLTRLAEVIQKHQRLLWT 121
Cdd:cd07082    5 LINGEWKESSG-KTIEVYSPIDGEVIGSVPALSALEILEAAETAYDAGRGWWPtMPLEERIDCLHKFADLLKENKEEVAN 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 122 LESLVTGR----AVREV-RDGD--VQLAQQLLHYHA------IQASTQE-EALAGWEPMGVIgLILPP-------TFSfl 180
Cdd:cd07082   84 LLMWEIGKtlkdALKEVdRTIDyiRDTIEELKRLDGdslpgdWFPGTKGkIAQVRREPLGVV-LAIGPfnyplnlTVS-- 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 181 emmwRICPALAVGCTVValVPPASPAPLL---LAQLAGELGPFPGILNVLSGPASLV--PILASqPGIRKVAFCGAPEGG 255
Cdd:cd07082  161 ----KLIPALIMGNTVV--FKPATQGVLLgipLAEAFHDAGFPKGVVNVVTGRGREIgdPLVTH-GRIDVISFTGSTEVG 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 256 LRL----------------------------------------------------LIQESVWDEAMRRLQERMGRLRSGR 283
Cdd:cd07082  234 NRLkkqhpmkrlvlelggkdpaivlpdadlelaakeivkgalsysgqrctaikrvLVHESVADELVELLKEEVAKLKVGM 313
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 284 GLDGAVDMGA---RGAAacDLVQRFVREAQSQGAQVFQAGDVPSERPFYPpTLVSNLPPASPCAQVEVPWPVVVASPFRT 360
Cdd:cd07082  314 PWDNGVDITPlidPKSA--DFVEGLIDDAVAKGATVLNGGGREGGNLIYP-TLLDPVTPDMRLAWEEPFGPVLPIIRVND 390
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 223972653 361 AKEALLVANGTPRGGSASVWSERLGQALELGYGLQVGTVWINAHGLRDPSV-PTGGCKESG 420
Cdd:cd07082  391 IEEAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINSKCQRGPDHfPFLGRKDSG 451
ALDH_ACDHII_AcoD-like cd07559
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ...
477-714 2.71e-24

Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus AldA1 (SACOL0154)-like; Included in this CD is the NAD+-dependent, acetaldehyde dehydrogenase II (AcDHII, AcoD, EC=1.2.1.3) from Ralstonia (Alcaligenes) eutrophus H16 involved in the catabolism of acetoin and ethanol, and similar proteins, such as, the dimeric dihydrolipoamide dehydrogenase of the acetoin dehydrogenase enzyme system of Klebsiella pneumonia. Also included are sequences similar to the NAD+-dependent chloroacetaldehyde dehydrogenases (AldA and AldB) of Xanthobacter autotrophicus GJ10 which are involved in the degradation of 1,2-dichloroethane, as well as, the uncharacterized aldehyde dehydrogenase from Staphylococcus aureus (AldA1, locus SACOL0154) and other similar sequences.


Pssm-ID: 143471 [Multi-domain]  Cd Length: 480  Bit Score: 107.04  E-value: 2.71e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 477 YGLFVGGRFQAP-GARSSRPIRDSSGNLHGYVAEGGAKDIRGAVEAAHQAFPGWAGQSPgaraallwalaaaLERRK--S 553
Cdd:cd07559    1 YDNFINGEWVAPsKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSV-------------AERANilN 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 554 TLASRLERQGAELKAAE-------------AEVELSARRLRAWGARVQAQGHTLQVAGLRGPVLRLREPLGVLAVVCPDE 620
Cdd:cd07559   68 KIADRIEENLELLAVAEtldngkpiretlaADIPLAIDHFRYFAGVIRAQEGSLSEIDEDTLSYHFHEPLGVVGQIIPWN 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 621 WPLLAFVSLLAPALAYGNTVVMVPSAACPLLALEVCQDMATVFPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGSAQGS 700
Cdd:cd07559  148 FPLLMAAWKLAPALAAGNTVVLKPASQTPLSILVLMELIGDLLPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVG 227
                        250
                 ....*....|....
gi 223972653 701 QFVEWASAGNLKPV 714
Cdd:cd07559  228 RLIMQYAAENLIPV 241
ALDH_F21_RNP123 cd07147
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ...
165-421 2.95e-24

Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) was first described in the moss Tortula ruralis and is believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and ALDH21A1 expression represents a unique stress tolerance mechanism. So far, of plants, only the bryophyte sequence has been observed, but similar protein sequences from bacteria and archaea are also present in this CD.


Pssm-ID: 143465 [Multi-domain]  Cd Length: 452  Bit Score: 106.56  E-value: 2.95e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 165 PMGVIGLILPPTFSFLEMMWRICPALAVGCTVValVPPASPAP---LLLAQLAGELGPFPGILNVLSGPASLVPILASQP 241
Cdd:cd07147  123 PIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFV--LKPASRTPlsaLILGEVLAETGLPKGAFSVLPCSRDDADLLVTDE 200
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 242 GIRKVAFCGAPEGGL----------------------------------------------------RLLIQESVWDEAM 269
Cdd:cd07147  201 RIKLLSFTGSPAVGWdlkaragkkkvvlelggnaavivdsdadldfaaqriifgafyqagqscisvqRVLVHRSVYDEFK 280
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 270 RRLQERMGRLRSGRGLDGAVDMGAR-GAAACDLVQRFVREAQSQGAQVFQAGDVpsERPFYPPTLVSNLPPASPCAQVEV 348
Cdd:cd07147  281 SRLVARVKALKTGDPKDDATDVGPMiSESEAERVEGWVNEAVDAGAKLLTGGKR--DGALLEPTILEDVPPDMEVNCEEV 358
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 223972653 349 PWPVVVASPFRTAKEALLVANGTPRGGSASVWSERLGQALELGYGLQVGTVWIN-AHGLRDPSVPTGGCKESGC 421
Cdd:cd07147  359 FGPVVTVEPYDDFDEALAAVNDSKFGLQAGVFTRDLEKALRAWDELEVGGVVINdVPTFRVDHMPYGGVKDSGI 432
ALDH_ABALDH-YdcW cd07092
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ...
499-714 2.97e-24

Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD+-dependent, tetrameric, gamma-aminobutyraldehyde dehydrogenase (ABALDH), YdcW of Escherichia coli K12, catalyzes the oxidation of gamma-aminobutyraldehyde to gamma-aminobutyric acid. ABALDH can also oxidize n-alkyl medium-chain aldehydes, but with a lower catalytic efficiency.


Pssm-ID: 143411 [Multi-domain]  Cd Length: 450  Bit Score: 106.64  E-value: 2.97e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 499 SSGNLHGYVAEGGAKDIRGAVEAAHQAFPGWAGQSPGaraallwalaaalERRKS--TLASRLERQGAELKAAEA----- 571
Cdd:cd07092    5 ATGEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPA-------------ERSKAllKLADAIEENAEELAALESrntgk 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 572 --------EVELSARRLR--AWGARVQ--------AQGHTLQVaglrgpvlrLREPLGVLAVVCPDEWPLLAFVSLLAPA 633
Cdd:cd07092   72 plhlvrddELPGAVDNFRffAGAARTLegpaageyLPGHTSMI---------RREPIGVVAQIAPWNYPLMMAAWKIAPA 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 634 LAYGNTVVMVPSAACPLLALEVCQDMATVFPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGSAQGSQFVEWASAGNLKP 713
Cdd:cd07092  143 LAAGNTVVLKPSETTPLTTLLLAELAAEVLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAADTLKR 222

                 .
gi 223972653 714 V 714
Cdd:cd07092  223 V 223
PRK10090 PRK10090
aldehyde dehydrogenase A; Provisional
165-434 3.97e-24

aldehyde dehydrogenase A; Provisional


Pssm-ID: 182233 [Multi-domain]  Cd Length: 409  Bit Score: 105.59  E-value: 3.97e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 165 PMGVIGLILPPTFSFLEMMWRICPALAVGCTVValVPPASPAP---LLLAQLAGELGPFPGILNVLSGPASLV-PILASQ 240
Cdd:PRK10090  71 ALGVTTGILPWNFPFFLIARKMAPALLTGNTIV--IKPSEFTPnnaIAFAKIVDEIGLPKGVFNLVLGRGETVgQELAGN 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 241 PGIRKVAFCGAPEGGL------------------------------------------------------RLLIQESVWD 266
Cdd:PRK10090 149 PKVAMVSMTGSVSAGEkimaaaaknitkvclelggkapaivmddadldlavkaivdsrvinsgqvcncaeRVYVQKGIYD 228
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 267 EAMRRLQERMGRLRSGRGLDG-AVDMGAR-GAAACDLVQRFVREAQSQGAQVFQAGDVPSERP-FYPPTLVSNLPPASPC 343
Cdd:PRK10090 229 QFVNRLGEAMQAVQFGNPAERnDIAMGPLiNAAALERVEQKVARAVEEGARVALGGKAVEGKGyYYPPTLLLDVRQEMSI 308
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 344 AQVEVPWPVVVASPFRTAKEALLVANGTPRGGSASVWSERLGQALELGYGLQVGTVWINAHGLRDPSVPTGGCKESGCSW 423
Cdd:PRK10090 309 MHEETFGPVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENFEAMQGFHAGWRKSGIGG 388
                        330
                 ....*....|.
gi 223972653 424 HGGPDGLYEYL 434
Cdd:PRK10090 389 ADGKHGLHEYL 399
ALDH_F15-22 cd07098
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ...
254-430 5.99e-24

Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ALDH15A1 (Saccharomyces cerevisiae YHR039C) and ALDH22A1 (Arabidopsis thaliana, EC=1.2.1.3), and similar sequences, are in this CD. Significant improvement of stress tolerance in tobacco plants was observed by overexpressing the ALDH22A1 gene from maize (Zea mays) and was accompanied by a reduction of malondialdehyde derived from cellular lipid peroxidation.


Pssm-ID: 143416 [Multi-domain]  Cd Length: 465  Bit Score: 105.84  E-value: 5.99e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 254 GGLRLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMGAR-GAAACDLVQRFVREAQSQGAQVFqAGDVPSERP----- 327
Cdd:cd07098  268 GIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMiSPARFDRLEELVADAVEKGARLL-AGGKRYPHPeypqg 346
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 328 -FYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVANGTPRGGSASVWSERLGQALELGYGLQVGTVWINAHGL 406
Cdd:cd07098  347 hYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYGLGASVFGKDIKRARRIASQLETGMVAINDFGV 426
                        170       180
                 ....*....|....*....|....*.
gi 223972653 407 R--DPSVPTGGCKESGCSWHGGPDGL 430
Cdd:cd07098  427 NyyVQQLPFGGVKGSGFGRFAGEEGL 452
Aldedh pfam00171
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ...
505-714 8.12e-24

Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. Members use NADP as a cofactor. The family includes the following members: The prototypical members are the aldehyde dehydrogenases EC:1.2.1.3. Succinate-semialdehyde dehydrogenase EC:1.2.1.16. Lactaldehyde dehydrogenase EC:1.2.1.22. Benzaldehyde dehydrogenase EC:1.2.1.28. Methylmalonate-semialdehyde dehydrogenase EC:1.2.1.27. Glyceraldehyde-3-phosphate dehydrogenase EC:1.2.1.9. Delta-1-pyrroline-5-carboxylate dehydrogenase EC: 1.5.1.12. Acetaldehyde dehydrogenase EC:1.2.1.10. Glutamate-5-semialdehyde dehydrogenase EC:1.2.1.41. This family also includes omega crystallin, an eye lens protein from squid and octopus that has little aldehyde dehydrogenase activity.


Pssm-ID: 425500 [Multi-domain]  Cd Length: 459  Bit Score: 105.31  E-value: 8.12e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653  505 GYVAEGGAKDIRGAVEAAHQAFPGWAGQSPGARAALLWALAAALERRKSTLAsRLER--QGAELKAAEAEVELSARRLRA 582
Cdd:pfam00171  21 ATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELA-ELETleNGKPLAEARGEVDRAIDVLRY 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653  583 W-GARVQAQGHTLQVAGLRGPVLRlREPLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLALEVCQDMAT 661
Cdd:pfam00171 100 YaGLARRLDGETLPSDPGRLAYTR-REPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPSELTPLTALLLAELFEE 178
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 223972653  662 V-FPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGSAQ-GSQFVEwASAGNLKPV 714
Cdd:pfam00171 179 AgLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAvGRHIAE-AAAQNLKRV 232
ALDH_BADH-GbsA cd07119
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ...
480-714 3.24e-23

Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is the NAD+-dependent, betaine aldehyde dehydrogenase (BADH, GbsA, EC=1.2.1.8) of Bacillus subtilis involved in the synthesis of the osmoprotectant glycine betaine from choline or glycine betaine aldehyde.


Pssm-ID: 143437  Cd Length: 482  Bit Score: 103.93  E-value: 3.24e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 480 FVGGRFQAPGARSSRPIRD-SSGNLHGYVAEGGAKDIRGAVEAAHQAF--PGWAGQSPGARAALLWALAAALERRKSTLA 556
Cdd:cd07119    1 YIDGEWVEAASGKTRDIINpANGEVIATVPEGTAEDAKRAIAAARRAFdsGEWPHLPAQERAALLFRIADKIREDAEELA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 557 sRLE--RQGAELKAAEAEVELSARRLRAW--------GARVQAQGHTLQVAglrgpvlrLREPLGVLAVVCPDEWPLLAF 626
Cdd:cd07119   81 -RLEtlNTGKTLRESEIDIDDVANCFRYYaglatketGEVYDVPPHVISRT--------VREPVGVCGLITPWNYPLLQA 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 627 VSLLAPALAYGNTVVMVPSAACPLLALEVCQDMATV-FPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGSAQGSQFVEW 705
Cdd:cd07119  152 AWKLAPALAAGNTVVIKPSEVTPLTTIALFELIEEAgLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMR 231

                 ....*....
gi 223972653 706 ASAGNLKPV 714
Cdd:cd07119  232 AAAGNVKKV 240
ALDH_F2BC cd07142
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ...
479-714 4.80e-23

Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the Arabidosis aldehyde dehydrogenase family 2 members B4 and B7 (EC=1.2.1.3), which are mitochondrial homotetramers that oxidize acetaldehyde and glycolaldehyde, but not L-lactaldehyde. Also in this group, is the Arabidosis cytosolic, homotetramer ALDH2C4 (EC=1.2.1.3), an enzyme involved in the oxidation of sinapalehyde and coniferaldehyde.


Pssm-ID: 143460  Cd Length: 476  Bit Score: 103.34  E-value: 4.80e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 479 LFVGGRFQAPGARSSRPIRD-SSGNLHGYVAEGGAKDIRGAVEAAHQAFP--GWAGQSPgaraallwalaaaLERRK--S 553
Cdd:cd07142    6 LFINGQFVDAASGKTFPTIDpRNGEVIAHVAEGDAEDVDRAVKAARKAFDegPWPRMTG-------------YERSRilL 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 554 TLASRLERQGAELKAAE-------------AEVELSARRLRAW-GARVQAQGHTLQVAGLRGpVLRLREPLGVLAVVCPD 619
Cdd:cd07142   73 RFADLLEKHADELAALEtwdngkpyeqaryAEVPLAARLFRYYaGWADKIHGMTLPADGPHH-VYTLHEPIGVVGQIIPW 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 620 EWPLLAFVSLLAPALAYGNTVVMVPSAACPLLALEVCQDMATV-FPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGSAQ 698
Cdd:cd07142  152 NFPLLMFAWKVGPALACGNTIVLKPAEQTPLSALLAAKLAAEAgLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTE 231
                        250
                 ....*....|....*..
gi 223972653 699 -GSQFVEWASAGNLKPV 714
Cdd:cd07142  232 vGKIIMQLAAKSNLKPV 248
ALDH_KGSADH-YcbD cd07097
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ...
480-698 6.19e-23

Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; Kinetic studies of the Bacillus subtilis ALDH-like ycbD protein, which is involved in d-glucarate/d-galactarate utilization, reveal that it is a NADP+-dependent, alpha-ketoglutaric semialdehyde dehydrogenase (KGSADH). KGSADHs (EC 1.2.1.26) catalyze the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. Interestingly, the NADP+-dependent, tetrameric, 2,5-dioxopentanoate dehydrogenase (EC=1.2.1.26), an enzyme involved in the catabolic pathway for D-arabinose in Sulfolobus solfataricus, also clusters in this group. This CD shows a distant phylogenetic relationship to the Azospirillum brasilense KGSADH-II (-III) group.


Pssm-ID: 143415 [Multi-domain]  Cd Length: 473  Bit Score: 102.71  E-value: 6.19e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 480 FVGGRFQAPGARssRPIRDSS--GNLHGYVAEGGAKDIRGAVEAAHQAFPGWAGQSPGARAALLWALAAALERRKSTLAS 557
Cdd:cd07097    4 YIDGEWVAGGDG--EENRNPSdtSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELAR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 558 RLER-QGAELKAAEAEVELSARRLRAWGARVQAQ-GHTLQVAGLRGPVLRLREPLGVLAVVCPDEWPLLAFVSLLAPALA 635
Cdd:cd07097   82 LLTReEGKTLPEARGEVTRAGQIFRYYAGEALRLsGETLPSTRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIAPALA 161
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 223972653 636 YGNTVVMVPSAACPLLALEVCQDMATV-FPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGSAQ 698
Cdd:cd07097  162 YGNTVVFKPAELTPASAWALVEILEEAgLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTA 225
ALDH cd07078
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ...
518-714 6.28e-23

NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of NAD(P)+ dependent enzymes, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. Besides aldehyde detoxification, many ALDH isozymes possess multiple additional catalytic and non-catalytic functions such as participating in metabolic pathways, or as binding proteins, or as osmoregulants, to mention a few. The enzyme has three domains, a NAD(P)+ cofactor-binding domain, a catalytic domain, and a bridging domain; and the active enzyme is generally either homodimeric or homotetrameric. The catalytic mechanism is proposed to involve cofactor binding, resulting in a conformational change and activation of an invariant catalytic cysteine nucleophile. The cysteine and aldehyde substrate form an oxyanion thiohemiacetal intermediate resulting in hydride transfer to the cofactor and formation of a thioacylenzyme intermediate. Hydrolysis of the thioacylenzyme and release of the carboxylic acid product occurs, and in most cases, the reduced cofactor dissociates from the enzyme. The evolutionary phylogenetic tree of ALDHs appears to have an initial bifurcation between what has been characterized as the classical aldehyde dehydrogenases, the ALDH family (ALDH) and extended family members or aldehyde dehydrogenase-like (ALDH-like) proteins. The ALDH proteins are represented by enzymes which share a number of highly conserved residues necessary for catalysis and cofactor binding and they include such proteins as retinal dehydrogenase, 10-formyltetrahydrofolate dehydrogenase, non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase, delta(1)-pyrroline-5-carboxylate dehydrogenases, alpha-ketoglutaric semialdehyde dehydrogenase, alpha-aminoadipic semialdehyde dehydrogenase, coniferyl aldehyde dehydrogenase and succinate-semialdehyde dehydrogenase. Included in this larger group are all human, Arabidopsis, Tortula, fungal, protozoan, and Drosophila ALDHs identified in families ALDH1 through ALDH22 with the exception of families ALDH18, ALDH19, and ALDH20 which are present in the ALDH-like group.


Pssm-ID: 143397 [Multi-domain]  Cd Length: 432  Bit Score: 102.29  E-value: 6.28e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 518 AVEAAHQAFPGWAGQSPGARAALLWALAAALERRKSTLASRLER-QGAELKAAEAEVELSARRLR---AWGARVQAQGHT 593
Cdd:cd07078    3 AVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLeTGKPIEEALGEVARAADTFRyyaGLARRLHGEVIP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 594 LQVAGLRGpvLRLREPLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLALEVCQDMATV-FPAGLANVVT 672
Cdd:cd07078   83 SPDPGELA--IVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAgLPPGVLNVVT 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 223972653 673 GDRDHLTRCLALHQDVQAMWYFGSAQGSQFVEWASAGNLKPV 714
Cdd:cd07078  161 GDGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAENLKRV 202
ALDH_HMSADH_HapE cd07115
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ...
499-714 8.04e-23

Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic semialdehyde dehydrogenase (HapE, EC=1.2.1.61) of Pseudomonas fluorescens ACB involved in 4-hydroxyacetophenone degradation, and putative hydroxycaproate semialdehyde dehydrogenase (ChnE) of Brachymonas petroleovorans involved in cyclohexane metabolism, and other similar sequences, are present in this CD.


Pssm-ID: 143433 [Multi-domain]  Cd Length: 453  Bit Score: 102.13  E-value: 8.04e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 499 SSGNLHGYVAEGGAKDIRGAVEAAHQAFPGWAGQSPGARAALLWALAAALERRKSTLAsRLERQ--GAELKAAE-AEVEL 575
Cdd:cd07115    5 ATGELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELA-RLESLdtGKPIRAARrLDVPR 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 576 SARRLRAWGARVQAQGHtlQVAGLRGPVLR--LREPLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLAL 653
Cdd:cd07115   84 AADTFRYYAGWADKIEG--EVIPVRGPFLNytVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSAL 161
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 223972653 654 EVCQDMATV-FPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGSAQGSQFVEWASAGNLKPV 714
Cdd:cd07115  162 RIAELMAEAgFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLKRV 223
PRK13473 PRK13473
aminobutyraldehyde dehydrogenase;
476-712 1.16e-22

aminobutyraldehyde dehydrogenase;


Pssm-ID: 237391  Cd Length: 475  Bit Score: 101.91  E-value: 1.16e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 476 PYGLFVGGRFQAPGARSSRPIRDSSGNLHGYVAEGGAKDIRGAVEAAHQAFPGWAGQSPGaraallwalaaalERRKS-- 553
Cdd:PRK13473   2 QTKLLINGELVAGEGEKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPK-------------ERAEAll 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 554 TLASRLERQGAELKAAEA-------------EVELSARRLR--AWGARVQ--------AQGHTLQVaglrgpvlRlREPL 610
Cdd:PRK13473  69 KLADAIEENADEFARLESlncgkplhlalndEIPAIVDVFRffAGAARCLegkaageyLEGHTSMI--------R-RDPV 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 611 GVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLALEVCQDMATVFPAGLANVVTGDRDHLTRCLALHQDVQA 690
Cdd:PRK13473 140 GVVASIAPWNYPLMMAAWKLAPALAAGNTVVLKPSEITPLTALKLAELAADILPPGVLNVVTGRGATVGDALVGHPKVRM 219
                        250       260
                 ....*....|....*....|...
gi 223972653 691 MWYFGS-AQGSQFVEwASAGNLK 712
Cdd:PRK13473 220 VSLTGSiATGKHVLS-AAADSVK 241
ALDH_VaniDH_like cd07150
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ...
500-714 2.23e-22

Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved in the metabolism of ferulic acid and other related sequences are included in this CD. The E. coli vanillin dehydrogenase (LigV) preferred NAD+ to NADP+ and exhibited a broad substrate preference, including vanillin, benzaldehyde, protocatechualdehyde, m-anisaldehyde, and p-hydroxybenzaldehyde.


Pssm-ID: 143468 [Multi-domain]  Cd Length: 451  Bit Score: 100.87  E-value: 2.23e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 500 SGNLHGYVAEGGAKDIRGAVEAAHQAFPGWAGQSPGARAALLWALAAALERRKSTLASRLERQ-GAELKAAEAEVELSAR 578
Cdd:cd07150    8 DGSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEgGSTYGKAWFETTFTPE 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 579 RLRAWGARVQA-QGHTLQ--VAGLRGPVlrLREPLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLALEV 655
Cdd:cd07150   88 LLRAAAGECRRvRGETLPsdSPGTVSMS--VRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVIGLKI 165
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 656 CQDMATV-FPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGSAQGSQFVEWASAGNLKPV 714
Cdd:cd07150  166 AEIMEEAgLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAGRHLKKI 225
ALDH_AldA-AAD23400 cd07106
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ...
507-714 7.12e-22

Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative aldehyde dehydrogenase, AldA, from Streptomyces aureofaciens (locus AAD23400) and other similar sequences are present in this CD.


Pssm-ID: 143424 [Multi-domain]  Cd Length: 446  Bit Score: 99.14  E-value: 7.12e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 507 VAEGGAKDIRGAVEAAHQAFPGWAGQSPGARAALLWALAAALERRKSTLASRLER-QGAELKAAEAEVELSARRLRAwga 585
Cdd:cd07106   13 APVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLeQGKPLAEAQFEVGGAVAWLRY--- 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 586 rvqaqghtlqVAGLRGPVLRLRE-----------PLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLALE 654
Cdd:cd07106   90 ----------TASLDLPDEVIEDddtrrvelrrkPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCTLK 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 655 VCQDMATVFPAGLANVVTGDRDhLTRCLALHQDVQAMWYFGSAQGSQFVEWASAGNLKPV 714
Cdd:cd07106  160 LGELAQEVLPPGVLNVVSGGDE-LGPALTSHPDIRKISFTGSTATGKKVMASAAKTLKRV 218
ALDH_MGR_2402 cd07108
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ...
505-741 9.18e-22

Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent aldehyde dehydrogenase of Magnetospirillum gryphiswaldense MSR-1 (MGR_2402) , and other similar sequences, are present in this CD.


Pssm-ID: 143426  Cd Length: 457  Bit Score: 98.97  E-value: 9.18e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 505 GYVAEGGAKDIRGAVEAAHQAFPGWAGQSPGARAALLWALAAALERRKSTLASRLERQ-GAELK-AAEAEVELSARRLRA 582
Cdd:cd07108   11 GEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALEtGNALRtQARPEAAVLADLFRY 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 583 WGarvqaqghtlQVAG-LRGPVLRL---------REPLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLA 652
Cdd:cd07108   91 FG----------GLAGeLKGETLPFgpdvltytvREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLAV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 653 LEVCQDMATVFPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGSAQGSQFVEWASAGNLKPVWASRG-------CPRAwD 725
Cdd:cd07108  161 LLLAEILAQVLPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGgkspmivFPDA-D 239
                        250
                 ....*....|....*.
gi 223972653 726 QEAEGAGPELGLRVAR 741
Cdd:cd07108  240 LDDAVDGAIAGMRFTR 255
ALDH_GABALDH-PuuC cd07112
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ...
507-715 1.01e-21

Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase PuuC-like; NADP+-dependent, gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase (GABALDH) PuuC of Escherichia coli which catalyzes the conversion of putrescine to 4-aminobutanoate and other similar sequences are present in this CD.


Pssm-ID: 143430 [Multi-domain]  Cd Length: 462  Bit Score: 98.83  E-value: 1.01e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 507 VAEGGAKDIRGAVEAAHQAFPG--WAGQSPgaraallwalaaalERRKSTL---ASRLERQGAEL-------------KA 568
Cdd:cd07112   18 VAACDAADVDRAVAAARRAFESgvWSRLSP--------------AERKAVLlrlADLIEAHRDELalletldmgkpisDA 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 569 AEAEVELSARRLRaWGARVQAQghtlqVAGLRGPV------LRLREPLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVM 642
Cdd:cd07112   84 LAVDVPSAANTFR-WYAEAIDK-----VYGEVAPTgpdalaLITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVL 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 223972653 643 VPSAACPLLALEVCQDMATV-FPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGS-AQGSQFVEWASAGNLKPVW 715
Cdd:cd07112  158 KPAEQSPLTALRLAELALEAgLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGStEVGRRFLEYSGQSNLKRVW 232
ALDH_AAS00426 cd07109
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ...
499-714 1.45e-21

Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; Uncharacterized aldehyde dehydrogenase of Saccharopolyspora spinosa (AAS00426) and other similar sequences, are present in this CD.


Pssm-ID: 143427 [Multi-domain]  Cd Length: 454  Bit Score: 98.46  E-value: 1.45e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 499 SSGNLHGYVAEGGAKDIRGAVEAAHQAFPGWAGQSPGARAALLWALAAALERRKSTLASRLERQ--GAELKAAEAEVELS 576
Cdd:cd07109    5 STGEVFARIARGGAADVDRAVQAARRAFESGWLRLSPAERGRLLLRIARLIREHADELARLESLdtGKPLTQARADVEAA 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 577 ARRLRAWGARVQA-QGHTLQVaglrGP---VLRLREPLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLA 652
Cdd:cd07109   85 ARYFEYYGGAADKlHGETIPL----GPgyfVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLTA 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 223972653 653 LEVCQDMATV-FPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGSAQGSQFVEWASAGNLKPV 714
Cdd:cd07109  161 LRLAELAEEAgLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAENVVPV 223
ALDH_AldA_AN0554 cd07143
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ...
476-714 1.65e-21

Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde dehydrogenase (AldA) of Aspergillus nidulans (locus AN0554), and other similar sequences, are present in this CD.


Pssm-ID: 143461  Cd Length: 481  Bit Score: 98.37  E-value: 1.65e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 476 PYGLFVGGRFqAPGARSSRP--IRDSSGNLHGYVAEGGAKDIRGAVEAAHQAFPG-WAGQSPGARA-ALLWALAAALERR 551
Cdd:cd07143    6 PTGLFINGEF-VDSVHGGTVkvYNPSTGKLITKIAEATEADVDIAVEVAHAAFETdWGLKVSGSKRgRCLSKLADLMERN 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 552 KSTLAS--RLERQGAELKAAEAEVELSARRLRAWGARV-QAQGHTLQVAGLRGPVLRlREPLGVLAVVCPDEWPLLAFVS 628
Cdd:cd07143   85 LDYLASieALDNGKTFGTAKRVDVQASADTFRYYGGWAdKIHGQVIETDIKKLTYTR-HEPIGVCGQIIPWNFPLLMCAW 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 629 LLAPALAYGNTVVMVPSAACPLLALEVCQDMATV-FPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGS-AQGSQFVEWA 706
Cdd:cd07143  164 KIAPALAAGNTIVLKPSELTPLSALYMTKLIPEAgFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGStLVGRKVMEAA 243

                 ....*...
gi 223972653 707 SAGNLKPV 714
Cdd:cd07143  244 AKSNLKKV 251
ALDH_F6_MMSDH cd07085
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ...
40-402 2.45e-21

Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate semialdehyde dehydrogenase (MMSDH, EC=1.2.1.27) [acylating] from Bacillus subtilis is involved in valine metabolism and catalyses the NAD+- and CoA-dependent oxidation of methylmalonate semialdehyde into propionyl-CoA. Mitochondrial human MMSDH ALDH6A1 and Arabidopsis MMSDH ALDH6B2 are also present in this CD.


Pssm-ID: 143404 [Multi-domain]  Cd Length: 478  Bit Score: 97.97  E-value: 2.45e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653  40 LGHYVNGKWLKPEHRNSVPCQDPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLL 119
Cdd:cd07085    1 LKLFINGEWVESKTTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDEL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 120 WTLESLVTGRAVREVRdGDVQLAQQLLHY-----HAIQASTQEEALAG------WEPMGVIGLILPptFSFLEM--MWRI 186
Cdd:cd07085   81 ARLITLEHGKTLADAR-GDVLRGLEVVEFacsipHLLKGEYLENVARGidtysyRQPLGVVAGITP--FNFPAMipLWMF 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 187 CPALAVGCTVValVPPASPAPL---LLAQLAGELGPFPGILNVLSGPASLVPILASQPGIRKVAFCG-----------AP 252
Cdd:cd07085  158 PMAIACGNTFV--LKPSERVPGaamRLAELLQEAGLPDGVLNVVHGGKEAVNALLDHPDIKAVSFVGstpvgeyiyerAA 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 253 EGGLR-------------------------------------------LLIQESVWDEAMRRLQERMGRLRSGRGLDGAV 289
Cdd:cd07085  236 ANGKRvqalggaknhavvmpdadleqtanalvgaafgaagqrcmalsvAVAVGDEADEWIPKLVERAKKLKVGAGDDPGA 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 290 DMGAR-GAAACDLVQRFVREAQSQGAQVFQAG-DVPSerPFYP------PTLVSNLPPASPCAQVEVPWPVVVASPFRTA 361
Cdd:cd07085  316 DMGPViSPAAKERIEGLIESGVEEGAKLVLDGrGVKV--PGYEngnfvgPTILDNVTPDMKIYKEEIFGPVLSIVRVDTL 393
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|.
gi 223972653 362 KEALLVANGTPRGGSASVWSERLGQALELGYGLQVGTVWIN 402
Cdd:cd07085  394 DEAIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGIN 434
ALDH_PhdK-like cd07107
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ...
499-714 4.34e-21

Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain KP72-carboxybenzaldehyde dehydrogenase (PhdK), an enzyme involved in phenanthrene degradation, and other similar sequences, are present in this CD.


Pssm-ID: 143425 [Multi-domain]  Cd Length: 456  Bit Score: 97.06  E-value: 4.34e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 499 SSGNLHGYVAEGGAKDIRGAVEAAHQAFPGWAGQSPgaraallwalaaaLERRK--STLASRLERQGAELKAAEA----- 571
Cdd:cd07107    5 ATGQVLARVPAASAADVDRAVAAARAAFPEWRATTP-------------LERARmlRELATRLREHAEELALIDAldcgn 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 572 -------EVELSARRLRAWGARV-QAQGHTLQVAGlRGPVLRLREPLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMV 643
Cdd:cd07107   72 pvsamlgDVMVAAALLDYFAGLVtELKGETIPVGG-RNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVK 150
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 223972653 644 PSAACPLLALEVCQDMATVFPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGSAQGSQFVEWASAGNLKPV 714
Cdd:cd07107  151 PPEQAPLSALRLAELAREVLPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIKHV 221
ALDH_LactADH-AldA cd07088
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ...
480-714 1.05e-20

Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from Escherichia coli (AldA, LactADH, EC=1.2.1.22), an NAD(+)-dependent enzyme involved in the metabolism of L-fucose and L-rhamnose, and other similar sequences are present in this CD.


Pssm-ID: 143407 [Multi-domain]  Cd Length: 468  Bit Score: 95.80  E-value: 1.05e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 480 FVGGRFQAPGARSSRPIRD-SSGNLHGYVAEGGAKDIRGAVEAAHQAFPGWAGQSPGARAALLWALAAALERRKSTLASR 558
Cdd:cd07088    1 YINGEFVPSSSGETIDVLNpATGEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 559 L-ERQGAELKAAEAEVELSARRLR--AWGARvQAQGHTLQVAGLRGPVLRLREPLGVLAVVCPDEWPLLAFVSLLAPALA 635
Cdd:cd07088   81 IvEEQGKTLSLARVEVEFTADYIDymAEWAR-RIEGEIIPSDRPNENIFIFKVPIGVVAGILPWNFPFFLIARKLAPALV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 636 YGNTVVMVPSAACPLLALEVCQDMATV-FPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGSAQGSQFVEWASAGNLKPV 714
Cdd:cd07088  160 TGNTIVIKPSEETPLNALEFAELVDEAgLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAENITKV 239
ALDH_P5CDH cd07083
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ...
43-436 3.10e-20

ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH subfamily of the NAD+-dependent, delta(1)-pyrroline-5-carboxylate dehydrogenases (P5CDH, EC=1.5.1.12). The proline catabolic enzymes, proline dehydrogenase and P5CDH catalyze the two-step oxidation of proline to glutamate. P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA). These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes. Monofunctional enzyme sequences such as those seen in the Bacillus RocA P5CDH are also present in this subfamily as well as the human ALDH4A1 P5CDH and the Drosophila Aldh17 P5CDH.


Pssm-ID: 143402 [Multi-domain]  Cd Length: 500  Bit Score: 94.95  E-value: 3.10e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653  43 YVNGKWLKP-EHRNSVPCQDPitGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWT 121
Cdd:cd07083   22 VIGGEWVDTkERMVSVSPFAP--SEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRRRELIA 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 122 LESLVTGRAVREVRDgDVQLAQQLLHYHAIQA---STQEEALAG---------WEPMGVIGLILPPTFSFLEMMWRICPA 189
Cdd:cd07083  100 TLTYEVGKNWVEAID-DVAEAIDFIRYYARAAlrlRYPAVEVVPypgednesfYVGLGAGVVISPWNFPVAIFTGMIVAP 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 190 LAVGCTVVAlvPPASPAPLLLA---QLAGELGPFPGILNVLSGPASLV-PILASQPGIRKVAFCGAPEGGL--------- 256
Cdd:cd07083  179 VAVGNTVIA--KPAEDAVVVGYkvfEIFHEAGFPPGVVQFLPGVGEEVgAYLTEHERIRGINFTGSLETGKkiyeaaarl 256
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 257 ---------------------------------------------------RLLIQESVWDEAMRRLQERMGRLRSGRGL 285
Cdd:cd07083  257 apgqtwfkrlyvetggknaiivdetadfelvvegvvvsafgfqgqkcsaasRLILTQGAYEPVLERLLKRAERLSVGPPE 336
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 286 DGAVDMGAR-GAAACDLVQRFVREAQSQGAQVFQAGDVPSERPFYPPTLVSNLPPASPCAQVEVPWPV--VVASPFRTAK 362
Cdd:cd07083  337 ENGTDLGPViDAEQEAKVLSYIEHGKNEGQLVLGGKRLEGEGYFVAPTVVEEVPPKARIAQEEIFGPVlsVIRYKDDDFA 416
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 223972653 363 EALLVANGTPRGGSASVWSERLGQALELGYGLQVGTVWINAH--GLRDPSVPTGGCKESGCSWH-GGPDGLYEYLRP 436
Cdd:cd07083  417 EALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINRKitGALVGVQPFGGFKLSGTNAKtGGPHYLRRFLEM 493
ALDH_LactADH_F420-Bios cd07145
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ...
499-698 1.58e-19

Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, lactaldehyde dehydrogenase (EC=1.2.1.22) involved the biosynthesis of coenzyme F(420) in Methanocaldococcus jannaschii through the oxidation of lactaldehyde to lactate and generation of NAPH, and similar sequences are included in this CD.


Pssm-ID: 143463 [Multi-domain]  Cd Length: 456  Bit Score: 92.03  E-value: 1.58e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 499 SSGNLHGYVAEGGAKDIRGAVEAAHQAFPGWAGQSPGARAALLWALAAALERRKSTLASRLERQ-GAELKAAEAEVELSA 577
Cdd:cd07145    7 ANGEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEvGKPIKQSRVEVERTI 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 578 R--RLRAWGARVqAQGHTLQVAGL----RGPVLRLREPLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLL 651
Cdd:cd07145   87 RlfKLAAEEAKV-LRGETIPVDAYeyneRRIAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSSNTPLT 165
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 223972653 652 ALEVCQDMATV-FPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGSAQ 698
Cdd:cd07145  166 AIELAKILEEAgLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTA 213
ALDH_StaphAldA1 cd07117
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ...
477-731 1.67e-19

Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; Uncharacterized aldehyde dehydrogenase from Staphylococcus aureus (AldA1, locus SACOL0154) and other similar sequences are present in this CD.


Pssm-ID: 143435  Cd Length: 475  Bit Score: 92.13  E-value: 1.67e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 477 YGLFVGGRF-QAPGARSSRPIRDSSGNLHGYVAEGGAKDIRGAVEAAHQAFPGWAGQSPGARAALLWALAAALERRKSTL 555
Cdd:cd07117    1 YGLFINGEWvKGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 556 ASrLER--QGAELKAAEA-EVELSARRLRAWGARVQAQGHTLQVAGLRGPVLRLREPLGVLAVVCPDEWPLLAFVSLLAP 632
Cdd:cd07117   81 AM-VETldNGKPIRETRAvDIPLAADHFRYFAGVIRAEEGSANMIDEDTLSIVLREPIGVVGQIIPWNFPFLMAAWKLAP 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 633 ALAYGNTVVMVPSAACPLLALEVCQDMATVFPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGSAQGSQFVEWASAGNLK 712
Cdd:cd07117  160 ALAAGNTVVIKPSSTTSLSLLELAKIIQDVLPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAKKLI 239
                        250       260
                 ....*....|....*....|....*..
gi 223972653 713 PVWASRGCPRA--------WDQEAEGA 731
Cdd:cd07117  240 PATLELGGKSAniifddanWDKALEGA 266
ALDH_ACDHII-AcoD cd07116
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ...
477-714 2.28e-19

Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is the NAD+-dependent, acetaldehyde dehydrogenase II (AcDHII, AcoD, EC=1.2.1.3) from Ralstonia (Alcaligenes) eutrophus H16 involved in the catabolism of acetoin and ethanol, and similar proteins, such as, the dimeric dihydrolipoamide dehydrogenase of the acetoin dehydrogenase enzyme system of Klebsiella pneumonia. Also included are sequences similar to the NAD+-dependent chloroacetaldehyde dehydrogenases (AldA and AldB) of Xanthobacter autotrophicus GJ10 which are involved in the degradation of 1,2-dichloroethane. These proteins apparently require RpoN factors for expression.


Pssm-ID: 143434 [Multi-domain]  Cd Length: 479  Bit Score: 91.74  E-value: 2.28e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 477 YGLFVGGRFQAP-GARSSRPIRDSSGNLHGYVAEGGAKDIRGAVEAAHQAFPGWAGQSPgaraallwalaaaLERRK--S 553
Cdd:cd07116    1 YDNFIGGEWVAPvKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKEAWGKTSV-------------AERANilN 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 554 TLASRLERQGAELKAAE-------------AEVELSARRLRAWGARVQAQGHTLQVAGLRGPVLRLREPLGVLAVVCPDE 620
Cdd:cd07116   68 KIADRMEANLEMLAVAEtwdngkpvretlaADIPLAIDHFRYFAGCIRAQEGSISEIDENTVAYHFHEPLGVVGQIIPWN 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 621 WPLLAFVSLLAPALAYGNTVVMVPSAACP---LLALEVCQDMatvFPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGS- 696
Cdd:cd07116  148 FPLLMATWKLAPALAAGNCVVLKPAEQTPasiLVLMELIGDL---LPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGEt 224
                        250
                 ....*....|....*...
gi 223972653 697 AQGSQFVEWASAgNLKPV 714
Cdd:cd07116  225 TTGRLIMQYASE-NIIPV 241
ALDH_F16 cd07111
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ...
477-712 2.40e-19

Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 member A1 (ALDH16A1) and other related sequences are present in this CD. The active site cysteine and glutamate residues are not conserved in the human ALDH16A1 protein sequence.


Pssm-ID: 143429 [Multi-domain]  Cd Length: 480  Bit Score: 91.69  E-value: 2.40e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 477 YGLFVGGRFQAPGARSSRPIRD-SSGNLHGYVAEGGAKDIRGAVEAAHQAFPGWAgQSPGARAALLWALAAALERRKSTL 555
Cdd:cd07111   22 FGHFINGKWVKPENRKSFPTINpATGEVLASVLQAEEEDVDAAVAAARTAFESWS-ALPGHVRARHLYRIARHIQKHQRL 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 556 ASRLER--QGAELKAA-EAEVELSARRLRAWGarVQAQghtLQVAGLRGPvlrlrEPLGVLAVVCPDEWPLLAFVSLLAP 632
Cdd:cd07111  101 FAVLESldNGKPIRESrDCDIPLVARHFYHHA--GWAQ---LLDTELAGW-----KPVGVVGQIVPWNFPLLMLAWKICP 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 633 ALAYGNTVVMVPSAACPLLAL---EVCQDMAtvFPAGLANVVTGDrDHLTRCLALHQDVQAMWYFGSAQGSQFVEWASAG 709
Cdd:cd07111  171 ALAMGNTVVLKPAEYTPLTALlfaEICAEAG--LPPGVLNIVTGN-GSFGSALANHPGVDKVAFTGSTEVGRALRRATAG 247

                 ...
gi 223972653 710 NLK 712
Cdd:cd07111  248 TGK 250
ALDH-SF cd06534
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ...
520-714 2.53e-19

NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily (ALDH-SF) of NAD(P)+-dependent enzymes, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. Besides aldehyde detoxification, many ALDH isozymes possess multiple additional catalytic and non-catalytic functions such as participating in metabolic pathways, or as binding proteins, or osmoregulants, to mention a few. The enzyme has three domains, a NAD(P)+ cofactor-binding domain, a catalytic domain, and a bridging domain; and the active enzyme is generally either homodimeric or homotetrameric. The catalytic mechanism is proposed to involve cofactor binding, resulting in a conformational change and activation of an invariant catalytic cysteine nucleophile. The cysteine and aldehyde substrate form an oxyanion thiohemiacetal intermediate resulting in hydride transfer to the cofactor and formation of a thioacylenzyme intermediate. Hydrolysis of the thioacylenzyme and release of the carboxylic acid product occurs, and in most cases, the reduced cofactor dissociates from the enzyme. The evolutionary phylogenetic tree of ALDHs appears to have an initial bifurcation between what has been characterized as the classical aldehyde dehydrogenases, the ALDH family (ALDH) and extended family members or aldehyde dehydrogenase-like (ALDH-L) proteins. The ALDH proteins are represented by enzymes which share a number of highly conserved residues necessary for catalysis and cofactor binding and they include such proteins as retinal dehydrogenase, 10-formyltetrahydrofolate dehydrogenase, non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase, delta(1)-pyrroline-5-carboxylate dehydrogenases, alpha-ketoglutaric semialdehyde dehydrogenase, alpha-aminoadipic semialdehyde dehydrogenase, coniferyl aldehyde dehydrogenase and succinate-semialdehyde dehydrogenase. Included in this larger group are all human, Arabidopsis, Tortula, fungal, protozoan, and Drosophila ALDHs identified in families ALDH1 through ALDH22 with the exception of families ALDH18, ALDH19, and ALDH20 which are present in the ALDH-like group. The ALDH-like group is represented by such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.


Pssm-ID: 143395 [Multi-domain]  Cd Length: 367  Bit Score: 90.37  E-value: 2.53e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 520 EAAHQAFPGWAGQSPGARAALLWALAAALERRKSTLASRLER-QGAELKAAEAEVELSARRLR---AWGARVQAQGHTLQ 595
Cdd:cd06534    1 AAARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLeTGKPIEEALGEVARAIDTFRyaaGLADKLGGPELPSP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 596 VAGLRGpvLRLREPLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLALEVCQDMATV-FPAGLANVVTGD 674
Cdd:cd06534   81 DPGGEA--YVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAgLPPGVVNVVPGG 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 223972653 675 RDHLTRCLALHQDVQAMWYFGSAQGSQFVEWASAGNLKPV 714
Cdd:cd06534  159 GDEVGAALLSHPRVDKISFTGSTAVGKAIMKAAAENLKPV 198
PRK09847 PRK09847
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
479-719 4.61e-19

gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional


Pssm-ID: 182108 [Multi-domain]  Cd Length: 494  Bit Score: 91.11  E-value: 4.61e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 479 LFVGGRFQAPGARSSRPIRDSSGNLH-GYVAEGGAKDIRGAVEAAHQAFPG--WAGQSPGaraallwalaaaleRRKSTL 555
Cdd:PRK09847  22 LFINGEYTAAAENETFETVDPVTQAPlAKIARGKSVDIDRAVSAARGVFERgdWSLSSPA--------------KRKAVL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 556 ---ASRLERQGAELKAAEA-------------EVELSARRLRAWGARVQAQGHTLQVAGLRGPVLRLREPLGVLAVVCPD 619
Cdd:PRK09847  88 nklADLMEAHAEELALLETldtgkpirhslrdDIPGAARAIRWYAEAIDKVYGEVATTSSHELAMIVREPVGVIAAIVPW 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 620 EWPLLAFVSLLAPALAYGNTVVMVPSAACPLLALEVCQDMATV-FPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGSAQ 698
Cdd:PRK09847 168 NFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAgLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTR 247
                        250       260
                 ....*....|....*....|..
gi 223972653 699 -GSQFVEWASAGNLKPVWASRG 719
Cdd:PRK09847 248 tGKQLLKDAGDSNMKRVWLEAG 269
ALDH_PADH_NahF cd07113
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ...
478-714 4.63e-19

Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, homodimeric, phenylacetaldehyde dehydrogenase (PADH, EC=1.2.1.39) PadA of Escherichia coli involved in the catabolism of 2-phenylethylamine, and other related sequences, are present in this CD. Also included is the Pseudomonas fluorescens ST StyD PADH involved in styrene catabolism, the Sphingomonas sp. LB126 FldD protein involved in fluorene degradation, and the Novosphingobium aromaticivorans NahF salicylaldehyde dehydrogenase involved in the NAD+-dependent conversion of salicylaldehyde to salicylate.


Pssm-ID: 143431  Cd Length: 477  Bit Score: 90.96  E-value: 4.63e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 478 GLFVGGRFQAPGARSSRPIRD-SSGNLHGYVAEGGAKDIRGAVEAAHQAFPG-WAGQSPGARaallwalaaalERRKSTL 555
Cdd:cd07113    1 GHFIDGRPVAGQSEKRLDITNpATEQVIASVASATEADVDAAVASAWRAFVSaWAKTTPAER-----------GRILLRL 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 556 ASRLERQGAELKAAEA-------------EVELSARRLR---AWGARVQaqGHTLQV-----AGLRGPVLRLREPLGVLA 614
Cdd:cd07113   70 ADLIEQHGEELAQLETlcsgksihlsrafEVGQSANFLRyfaGWATKIN--GETLAPsipsmQGERYTAFTRREPVGVVA 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 615 VVCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLALEVCQdMATV--FPAGLANVVTGDRDhLTRCLALHQDVQAMW 692
Cdd:cd07113  148 GIVPWNFSVMIAVWKIGAALATGCTIVIKPSEFTPLTLLRVAE-LAKEagIPDGVLNVVNGKGA-VGAQLISHPDVAKVS 225
                        250       260
                 ....*....|....*....|..
gi 223972653 693 YFGSAQGSQFVEWASAGNLKPV 714
Cdd:cd07113  226 FTGSVATGKKIGRQAASDLTRV 247
ALDH_F1L_FTFDH cd07140
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ...
476-714 5.83e-19

10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate dehydrogenase (FTHFDH, EC=1.5.1.6), also known as aldehyde dehydrogenase family 1 member L1 (ALDH1L1) in humans, is a multi-domain homotetramer with an N-terminal formyl transferase domain and a C-terminal ALDH domain. FTHFDH catalyzes an NADP+-dependent dehydrogenase reaction resulting in the conversion of 10-formyltetrahydrofolate to tetrahydrofolate and CO2. The ALDH domain is also capable of the oxidation of short chain aldehydes to their corresponding acids.


Pssm-ID: 143458 [Multi-domain]  Cd Length: 486  Bit Score: 90.63  E-value: 5.83e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 476 PYGLFVGGRF-QAPGARSSRPIRDSSGNLHGYVAEGGAKDIRGAVEAAHQAFPG--WAGQSPGARAALLWALAAALERRK 552
Cdd:cd07140    5 PHQLFINGEFvDAEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFENgeWGKMNARDRGRLMYRLADLMEEHQ 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 553 STLAS--RLERQGAELKAAEAEVELSARRLR---AWGARVQaqGHTLQVAGLRgP----VLRLREPLGVLAVVCPDEWPL 623
Cdd:cd07140   85 EELATieSLDSGAVYTLALKTHVGMSIQTFRyfaGWCDKIQ--GKTIPINQAR-PnrnlTLTKREPIGVCGIVIPWNYPL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 624 LAFVSLLAPALAYGNTVVMVPSAACPLLALEVCQDMATV-FPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGSAQ-GSQ 701
Cdd:cd07140  162 MMLAWKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAgFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPiGKH 241
                        250
                 ....*....|...
gi 223972653 702 FVEWASAGNLKPV 714
Cdd:cd07140  242 IMKSCAVSNLKKV 254
PLN02466 PLN02466
aldehyde dehydrogenase family 2 member
479-714 7.33e-19

aldehyde dehydrogenase family 2 member


Pssm-ID: 215259 [Multi-domain]  Cd Length: 538  Bit Score: 90.64  E-value: 7.33e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 479 LFVGGRFQAPGARSSRPIRD-SSGNLHGYVAEGGAKDIRGAVEAAHQAF---PgWAGQSPgaraallwalaaaLERRKST 554
Cdd:PLN02466  60 LLINGQFVDAASGKTFPTLDpRTGEVIAHVAEGDAEDVNRAVAAARKAFdegP-WPKMTA-------------YERSRIL 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 555 L--ASRLERQGAEL-------------KAAEAEVELSARRLR---AW-----GARVQAQG-HTLQVaglrgpvlrLREPL 610
Cdd:PLN02466 126 LrfADLLEKHNDELaaletwdngkpyeQSAKAELPMFARLFRyyaGWadkihGLTVPADGpHHVQT---------LHEPI 196
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 611 GVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLALEVCQDMATV-FPAGLANVVTGDRDHLTRCLALHQDVQ 689
Cdd:PLN02466 197 GVAGQIIPWNFPLLMFAWKVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAgLPPGVLNVVSGFGPTAGAALASHMDVD 276
                        250       260
                 ....*....|....*....|....*.
gi 223972653 690 AMWYFGSAQGSQFV-EWASAGNLKPV 714
Cdd:PLN02466 277 KLAFTGSTDTGKIVlELAAKSNLKPV 302
ALDH_PsfA-ACA09737 cd07120
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ...
499-712 8.56e-19

Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the aldehyde dehydrogenase (PsfA, locus ACA09737) of Pseudomonas putida involved in furoic acid metabolism. Transcription of psfA was induced in response to 2-furoic acid, furfuryl alcohol, and furfural.


Pssm-ID: 143438 [Multi-domain]  Cd Length: 455  Bit Score: 90.10  E-value: 8.56e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 499 SSGNLHGYVAEGGAKDIRGAVEAAHQAF--PGWAgQSPGARAALLWALAAALERRKSTLASRLER-QGAELKAAEAEVEL 575
Cdd:cd07120    5 ATGEVIGTYADGGVAEAEAAIAAARRAFdeTDWA-HDPRLRARVLLELADAFEANAERLARLLALeNGKILGEARFEISG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 576 SARRLRAWG--ARVQAqGHTLQVAGLRGPVLrLREPLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLAL 653
Cdd:cd07120   84 AISELRYYAglARTEA-GRMIEPEPGSFSLV-LREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQINA 161
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 223972653 654 EV--CQDMATVFPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGSAQGSQFVEWASAGNLK 712
Cdd:cd07120  162 AIirILAEIPSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPTLK 222
PLN02766 PLN02766
coniferyl-aldehyde dehydrogenase
479-714 1.29e-18

coniferyl-aldehyde dehydrogenase


Pssm-ID: 215410 [Multi-domain]  Cd Length: 501  Bit Score: 89.88  E-value: 1.29e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 479 LFVGGRF-QAPGARSSRPIRDSSGNLHGYVAEGGAKDIRGAVEAAHQAF-----PGWAGQSPGaraallwalaaaleRRK 552
Cdd:PLN02766  23 LFINGEFvDAASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFdhgpwPRMSGFERG--------------RIM 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 553 STLASRLERQGAELKAAEA-------------EVELSARRLRAW-GARVQAQGHTLQVAG-LRGpvLRLREPLGVLAVVC 617
Cdd:PLN02766  89 MKFADLIEEHIEELAALDTidagklfalgkavDIPAAAGLLRYYaGAADKIHGETLKMSRqLQG--YTLKEPIGVVGHII 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 618 PDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLALEVCQ--DMATVfPAGLANVVTGDRDHLTRCLALHQDVQAMWYFG 695
Cdd:PLN02766 167 PWNFPSTMFFMKVAPALAAGCTMVVKPAEQTPLSALFYAHlaKLAGV-PDGVINVVTGFGPTAGAAIASHMDVDKVSFTG 245
                        250       260
                 ....*....|....*....|
gi 223972653 696 SAQ-GSQFVEWASAGNLKPV 714
Cdd:PLN02766 246 STEvGRKIMQAAATSNLKQV 265
ALDH_ALD2-YMR170C cd07144
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ...
476-714 1.64e-18

Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c, ALD5, EC=1.2.1.5) and other similar sequences, are present in this CD.


Pssm-ID: 143462  Cd Length: 484  Bit Score: 89.39  E-value: 1.64e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 476 PYGLFVGGRFQAPGARSSRP-IRDSSGNLHGYVAEGGAKDIRGAVEAAHQAFPGWAGQSPGAraallwalaaalERRK-- 552
Cdd:cd07144    7 PTGLFINNEFVKSSDGETIKtVNPSTGEVIASVYAAGEEDVDKAVKAARKAFESWWSKVTGE------------ERGEll 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 553 STLASRLERQGAELKAAEA----------------EVELSARRLRAWGARVQAQGHTLQVAGLRgpvLRLREPLGVLAVV 616
Cdd:cd07144   75 DKLADLVEKNRDLLAAIEAldsgkpyhsnalgdldEIIAVIRYYAGWADKIQGKTIPTSPNKLA---YTLHEPYGVCGQI 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 617 CPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLALEVCQDMATV-FPAGLANVVTGDRDHLTRCLALHQDVQAMWYFG 695
Cdd:cd07144  152 IPWNYPLAMAAWKLAPALAAGNTVVIKPAENTPLSLLYFANLVKEAgFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTG 231
                        250
                 ....*....|....*....
gi 223972653 696 SAQGSQFVEWASAGNLKPV 714
Cdd:cd07144  232 STATGRLVMKAAAQNLKAV 250
PLN02467 PLN02467
betaine aldehyde dehydrogenase
471-714 4.71e-18

betaine aldehyde dehydrogenase


Pssm-ID: 215260 [Multi-domain]  Cd Length: 503  Bit Score: 87.87  E-value: 4.71e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 471 PSPAPPYGLFVGGRFQAPGARSSRP-IRDSSGNLHGYVAEGGAKDIRGAVEAAHQAFPG-----WAGQSPGARAALLWAL 544
Cdd:PLN02467   2 AIPVPRRQLFIGGEWREPVLGKRIPvVNPATEETIGDIPAATAEDVDAAVEAARKAFKRnkgkdWARTTGAVRAKYLRAI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 545 AAALERRKSTLAsRLERQ--GAELKAAEAEV-------ELSARRLRAWGARvQAQGHTLQVAGLRGPVlrLREPLGVLAV 615
Cdd:PLN02467  82 AAKITERKSELA-KLETLdcGKPLDEAAWDMddvagcfEYYADLAEALDAK-QKAPVSLPMETFKGYV--LKEPLGVVGL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 616 VCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLALE---VCQDMAtvFPAGLANVVTGDRDHLTRCLALHQDVQAMW 692
Cdd:PLN02467 158 ITPWNYPLLMATWKVAPALAAGCTAVLKPSELASVTCLEladICREVG--LPPGVLNVVTGLGTEAGAPLASHPGVDKIA 235
                        250       260
                 ....*....|....*....|..
gi 223972653 693 YFGSAQGSQFVEWASAGNLKPV 714
Cdd:PLN02467 236 FTGSTATGRKIMTAAAQMVKPV 257
ALDH_CddD_SSP0762 cd07138
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ...
479-696 6.14e-18

Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase (CddD) from Rhodococcus ruber SC1 which converts 6-oxolauric acid to dodecanedioic acid, and the aldehyde dehydrogenase (locus SSP0762) from Staphylococcus saprophyticus subsp. saprophyticus ATCC 15305 and other similar sequences, are included in this CD.


Pssm-ID: 143456 [Multi-domain]  Cd Length: 466  Bit Score: 87.17  E-value: 6.14e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 479 LFVGGRFQAPGARSSRPIRD-SSGNLHGYVAEGGAKDIRGAVEAAHQAFPGWAGQSPgaraallwalaaaLERRK--STL 555
Cdd:cd07138    1 FYIDGAWVAPAGTETIDVINpATEEVIGTVPLGTAADVDRAVAAARRAFPAWSATSV-------------EERAAllERI 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 556 ASRLERQGAELKAAEAEvELSARRlrAWGARVQAQG------HTLQVAGL------RGPVLRLREPLGVLAVVCPDEWPL 623
Cdd:cd07138   68 AEAYEARADELAQAITL-EMGAPI--TLARAAQVGLgighlrAAADALKDfefeerRGNSLVVREPIGVCGLITPWNWPL 144
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 223972653 624 LAFVSLLAPALAYGNTVVMVPSAACPLLAL---EVCQDMAtvFPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGS 696
Cdd:cd07138  145 NQIVLKVAPALAAGCTVVLKPSEVAPLSAIilaEILDEAG--LPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGS 218
ALDH_DhaS cd07114
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ...
507-714 6.78e-18

Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized aldehyde dehydrogenase from Candidatus pelagibacter (DhaS) and other related sequences are present in this CD.


Pssm-ID: 143432 [Multi-domain]  Cd Length: 457  Bit Score: 87.22  E-value: 6.78e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 507 VAEGGAKDIRGAVEAAHQAF--PGWAGQSPgaraallwalaaaLERRK--STLASRLERQGAELKAAE--------AEVE 574
Cdd:cd07114   13 VPEASAADVDRAVAAARAAFegGAWRKLTP-------------TERGKllRRLADLIEANAEELAELEtrdngkliRETR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 575 LSARRLRAW-----GARVQAQGHTLQVAglRGPVLR--LREPLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVPSAA 647
Cdd:cd07114   80 AQVRYLAEWyryyaGLADKIEGAVIPVD--KGDYLNftRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEH 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 223972653 648 CPLLALEVCQDMATV-FPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGSAQGSQFVEWASAGNLKPV 714
Cdd:cd07114  158 TPASTLELAKLAEEAgFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAENLAPV 225
ALDH_F6_MMSDH cd07085
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ...
479-716 7.92e-18

Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate semialdehyde dehydrogenase (MMSDH, EC=1.2.1.27) [acylating] from Bacillus subtilis is involved in valine metabolism and catalyses the NAD+- and CoA-dependent oxidation of methylmalonate semialdehyde into propionyl-CoA. Mitochondrial human MMSDH ALDH6A1 and Arabidopsis MMSDH ALDH6B2 are also present in this CD.


Pssm-ID: 143404 [Multi-domain]  Cd Length: 478  Bit Score: 87.19  E-value: 7.92e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 479 LFVGGRFQAPGARSSRPIRD-SSGNLHGYVAEGGAKDIRGAVEAAHQAFPGWAGQSPGARAALLWALAAALERRKSTLAS 557
Cdd:cd07085    3 LFINGEWVESKTTEWLDVYNpATGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDELAR 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 558 RLER-QGAELKAAEAEVelsARRLR----AWGARVQAQGHTLQVAGLRGPVLRLREPLGVLAVVCPDEWPLLAFVSLLAP 632
Cdd:cd07085   83 LITLeHGKTLADARGDV---LRGLEvvefACSIPHLLKGEYLENVARGIDTYSYRQPLGVVAGITPFNFPAMIPLWMFPM 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 633 ALAYGNTVVMVPSAACPLLAL---EVCQDMAtvFPAGLANVVTGDRDHLTRCLAlHQDVQAMWYFGSAQGSQFVEWASAG 709
Cdd:cd07085  160 AIACGNTFVLKPSERVPGAAMrlaELLQEAG--LPDGVLNVVHGGKEAVNALLD-HPDIKAVSFVGSTPVGEYIYERAAA 236

                 ....*..
gi 223972653 710 NLKPVWA 716
Cdd:cd07085  237 NGKRVQA 243
ALDH_F8_HMSADH cd07093
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ...
499-714 9.99e-18

Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase family 8 member A1 (ALDH8A1) protein functions to convert 9-cis-retinal to 9-cis-retinoic acid and has a preference for NAD+. Also included in this CD is the 2-hydroxymuconic semialdehyde dehydrogenase (HMSADH) which catalyzes the conversion of 2-hydroxymuconic semialdehyde to 4-oxalocrotonate, a step in the meta cleavage pathway of aromatic hydrocarbons in bacteria. Such HMSADHs seen here are: XylG of the TOL plasmid pWW0 of Pseudomonas putida, TomC of Burkholderia cepacia G4, and AphC of Comamonas testosterone.


Pssm-ID: 143412 [Multi-domain]  Cd Length: 455  Bit Score: 86.47  E-value: 9.99e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 499 SSGNLHGYVAEGGAKDIRGAVEAAHQAFPGWAGQSPgaraallwalaaaLERRK--STLASRLERQGAELKAAE------ 570
Cdd:cd07093    5 ATGEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSP-------------AERARilHKVADLIEARADELALLEsldtgk 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 571 -------AEVELSARRLRAWGARVQAQGHTL--QVAGLRGPVlrLREPLGVLAVVCPdeW--PLLAFVSLLAPALAYGNT 639
Cdd:cd07093   72 pitlartRDIPRAAANFRFFADYILQLDGESypQDGGALNYV--LRQPVGVAGLITP--WnlPLMLLTWKIAPALAFGNT 147
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 223972653 640 VVMVPSAACPLLALEVCQDMATV-FPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGS-AQGSQFVEwASAGNLKPV 714
Cdd:cd07093  148 VVLKPSEWTPLTAWLLAELANEAgLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGEtATGRTIMR-AAAPNLKPV 223
ALDH_AldA-Rv0768 cd07139
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ...
479-714 1.11e-17

Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis NAD+-dependent, aldehyde dehydrogenase PDB structure, 3B4W, and the Mycobacterium tuberculosis H37Rv aldehyde dehydrogenase AldA (locus Rv0768) sequence, as well as the Rhodococcus rhodochrous ALDH involved in haloalkane catabolism, and other similar sequences, are included in this CD.


Pssm-ID: 143457 [Multi-domain]  Cd Length: 471  Bit Score: 86.47  E-value: 1.11e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 479 LFVGGRFQAPGARSSRPIRD-SSGNLHGYVAEGGAKDIRGAVEAAHQAFPG--WAGQSPGARAALLWALAAALERRKSTL 555
Cdd:cd07139    1 LFIGGRWVAPSGSETIDVVSpATEEVVGRVPEATPADVDAAVAAARRAFDNgpWPRLSPAERAAVLRRLADALEARADEL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 556 ASRLERQ-GAELKAAE-AEVELSARRLRAWGArvQAQGHTL---QVAGLRGPVLRLREPLGVLAVVCPDEWPLLAFVSLL 630
Cdd:cd07139   81 ARLWTAEnGMPISWSRrAQGPGPAALLRYYAA--LARDFPFeerRPGSGGGHVLVRREPVGVVAAIVPWNAPLFLAALKI 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 631 APALAYGNTVVMVPSAACPLLAL---EVCQDMAtvFPAGLANVVTGDRD---HLTRclalHQDVQAMWYFGSAQGSQFVE 704
Cdd:cd07139  159 APALAAGCTVVLKPSPETPLDAYllaEAAEEAG--LPPGVVNVVPADREvgeYLVR----HPGVDKVSFTGSTAAGRRIA 232
                        250
                 ....*....|
gi 223972653 705 WASAGNLKPV 714
Cdd:cd07139  233 AVCGERLARV 242
PRK03137 PRK03137
1-pyrroline-5-carboxylate dehydrogenase; Provisional
89-434 1.22e-17

1-pyrroline-5-carboxylate dehydrogenase; Provisional


Pssm-ID: 179543  Cd Length: 514  Bit Score: 86.91  E-value: 1.22e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653  89 AFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTLESLVTGRAVREVrDGDVQLAQQLLHYHAIQA-----STQEEALAG- 162
Cdd:PRK03137  85 AFETWKKWSPEDRARILLRAAAIIRRRKHEFSAWLVKEAGKPWAEA-DADTAEAIDFLEYYARQMlkladGKPVESRPGe 163
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 163 -----WEPMGViGLILPP-TFSFLEMMWRICPALAVGCTVVAlvPPASPAPLLLAQLAG---ELGPFPGILNVLSG-PAS 232
Cdd:PRK03137 164 hnryfYIPLGV-GVVISPwNFPFAIMAGMTLAAIVAGNTVLL--KPASDTPVIAAKFVEvleEAGLPAGVVNFVPGsGSE 240
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 233 LVPILASQPGIRKVAFCGAPEGGL-------------------------------------------------------- 256
Cdd:PRK03137 241 VGDYLVDHPKTRFITFTGSREVGLriyeraakvqpgqiwlkrviaemggkdaivvdedadldlaaesivasafgfsgqkc 320
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 257 ----RLLIQESVWDEAMRRLQERMGRLRSGRGLDGAvDMGAR-GAAACDLVQRFVREAQSQGAQVFQAGDVPSERPFYPP 331
Cdd:PRK03137 321 sacsRAIVHEDVYDEVLEKVVELTKELTVGNPEDNA-YMGPViNQASFDKIMSYIEIGKEEGRLVLGGEGDDSKGYFIQP 399
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 332 TLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVANGTPRGGSASVWS---ERLGQALELgygLQVGTVWIN------ 402
Cdd:PRK03137 400 TIFADVDPKARIMQEEIFGPVVAFIKAKDFDHALEIANNTEYGLTGAVISnnrEHLEKARRE---FHVGNLYFNrgctga 476
                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 223972653 403 ---AHglrdpsvPTGGCKESGC-SWHGGPDGLYEYL 434
Cdd:PRK03137 477 ivgYH-------PFGGFNMSGTdSKAGGPDYLLLFL 505
ALDH_F10_BADH cd07110
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ...
499-714 2.05e-17

Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in this CD are the Arabidopsis betaine aldehyde dehydrogenase (BADH) 1 (chloroplast) and 2 (mitochondria), also known as, aldehyde dehydrogenase family 10 member A8 and aldehyde dehydrogenase family 10 member A9, respectively, and are putative dehydration- and salt-inducible BADHs (EC 1.2.1.8) that catalyze the oxidation of betaine aldehyde to the compatible solute glycine betaine.


Pssm-ID: 143428 [Multi-domain]  Cd Length: 456  Bit Score: 85.48  E-value: 2.05e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 499 SSGNLHGYVAEGGAKDIRGAVEAAHQAFPGWAGQSPGARAALLWALAAALERRKSTLAsRLERQGAELKAAEAEVELS-- 576
Cdd:cd07110    5 ATEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELA-ELEARDNGKPLDEAAWDVDdv 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 577 ----------ARRLRAWGARvqaqghTLQVAGLRGPVLRLREPLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVPSA 646
Cdd:cd07110   84 agcfeyyadlAEQLDAKAER------AVPLPSEDFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSE 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 223972653 647 ACPLLALEVCQDMATV-FPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGSAQGSQFVEWASAGNLKPV 714
Cdd:cd07110  158 LTSLTELELAEIAAEAgLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQDIKPV 226
gabD1 PRK09406
succinic semialdehyde dehydrogenase; Reviewed
257-420 2.91e-17

succinic semialdehyde dehydrogenase; Reviewed


Pssm-ID: 181826 [Multi-domain]  Cd Length: 457  Bit Score: 85.17  E-value: 2.91e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 257 RLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMGARGA-AACDLVQRFVREAQSQGAQVFQAGDVPsERP--FYPPTL 333
Cdd:PRK09406 270 RFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATeQGRDEVEKQVDDAVAAGATILCGGKRP-DGPgwFYPPTV 348
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 334 VSNLPPASPCAQVEVPWPVvvASPFRTAK--EALLVANGTPRGGSASVWSERLGQALELGYGLQVGTVWINAHGLRDPSV 411
Cdd:PRK09406 349 ITDITPDMRLYTEEVFGPV--ASLYRVADidEAIEIANATTFGLGSNAWTRDEAEQERFIDDLEAGQVFINGMTVSYPEL 426

                 ....*....
gi 223972653 412 PTGGCKESG 420
Cdd:PRK09406 427 PFGGVKRSG 435
ALDH_F5_SSADH_GabD cd07103
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ...
505-714 4.30e-17

Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; Succinate-semialdehyde dehydrogenase, mitochondrial (SSADH, GabD, EC=1.2.1.24) catalyzes the NAD+-dependent oxidation of succinate semialdehyde (SSA) to succinate. This group includes the human aldehyde dehydrogenase family 5 member A1 (ALDH5A1) which is a mitochondrial homotetramer that converts SSA to succinate in the last step of 4-aminobutyric acid (GABA) catabolism. This CD also includes the Arabidopsis SSADH gene product ALDH5F1. Mutations in this gene result in the accumulation of H2O2, suggesting a role in plant defense against the environmental stress of elevated reactive oxygen species.


Pssm-ID: 143421 [Multi-domain]  Cd Length: 451  Bit Score: 84.41  E-value: 4.30e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 505 GYVAEGGAKDIRGAVEAAHQAFPGWAGQSPgaraallwalaaaLER-------------RKSTLAS--RLErQGAELKAA 569
Cdd:cd07103   11 GEVPDAGAADADAAIDAAAAAFKTWRKTTA-------------RERaailrrwadlireRAEDLARllTLE-QGKPLAEA 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 570 EAEVELSARRLRaW----GARVQAQGHTLQVAGLRgpVLRLREPLGVLAVVCPdeW--PLLAFVSLLAPALAYGNTVVMV 643
Cdd:cd07103   77 RGEVDYAASFLE-WfaeeARRIYGRTIPSPAPGKR--ILVIKQPVGVVAAITP--WnfPAAMITRKIAPALAAGCTVVLK 151
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 223972653 644 PSAACPLLALEVCQDMATV-FPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGS-AQGSQFVEwASAGNLKPV 714
Cdd:cd07103  152 PAEETPLSALALAELAEEAgLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGStAVGKLLMA-QAADTVKRV 223
ALDH_F7_AASADH cd07130
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ...
43-387 9.58e-17

NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; Alpha-aminoadipic semialdehyde dehydrogenase (AASADH, EC=1.2.1.31), also known as ALDH7A1, Antiquitin-1, ALDH7B, or delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH), is a NAD+-dependent ALDH. Human ALDH7A1 is involved in the pipecolic acid pathway of lysine catabolism, catalyzing the oxidation of alpha-aminoadipic semialdehyde to alpha-aminoadipate. Arabidopsis thaliana ALDH7B4 appears to be an osmotic-stress-inducible ALDH gene encoding a turgor-responsive or stress-inducible ALDH. The Streptomyces clavuligerus P6CDH appears to be involved in cephamycin biosynthesis, catalyzing the second stage of the two-step conversion of lysine to alpha-aminoadipic acid. The ALDH7A1 enzyme and others in this group have been observed as tetramers, yet the bacterial P6CDH enzyme has been reported as a monomer.


Pssm-ID: 143448  Cd Length: 474  Bit Score: 83.80  E-value: 9.58e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653  43 YVNGKWLKPEHrnSVPCQDPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTL 122
Cdd:cd07130    2 VYDGEWGGGGG--VVTSISPANGEPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 123 ESLVTGRAVREVRdGDVQ-----------LAQQLlhYHAIQAStqEEA----LAGWEPMGVIGLIlpPTFSFLEMMWRIC 187
Cdd:cd07130   80 VSLEMGKILPEGL-GEVQemidicdfavgLSRQL--YGLTIPS--ERPghrmMEQWNPLGVVGVI--TAFNFPVAVWGWN 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 188 PALAVGCTVVALVPPASPAPL-------LLAQLAGELGPFPGILNVLSGPASLVPILASQPGIRKVAFCGAPE------- 253
Cdd:cd07130  153 AAIALVCGNVVVWKPSPTTPLtaiavtkIVARVLEKNGLPGAIASLVCGGADVGEALVKDPRVPLVSFTGSTAvgrqvgq 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 254 -------------GG----------------------------------LRLLIQESVWDEAMRRLQERMGRLRSGRGLD 286
Cdd:cd07130  233 avaarfgrsllelGGnnaiivmedadldlavravlfaavgtagqrctttRRLIVHESIYDEVLERLKKAYKQVRIGDPLD 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 287 GAVDMGA-RGAAACDLVQRFVREAQSQGAQVFQAGDVpSERP--FYPPTLVSNLPPAsPCAQVEVPWPVVVASPFRTAKE 363
Cdd:cd07130  313 DGTLVGPlHTKAAVDNYLAAIEEAKSQGGTVLFGGKV-IDGPgnYVEPTIVEGLSDA-PIVKEETFAPILYVLKFDTLEE 390
                        410       420
                 ....*....|....*....|....
gi 223972653 364 ALLVANGTPRGGSASVWSERLGQA 387
Cdd:cd07130  391 AIAWNNEVPQGLSSSIFTTDLRNA 414
ALDH_EDX86601 cd07102
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ...
62-436 1.61e-16

Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (locus EDX86601) and other similar sequences, are present in this CD.


Pssm-ID: 143420 [Multi-domain]  Cd Length: 452  Bit Score: 82.68  E-value: 1.61e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653  62 PITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTLESLVTGRAVR----EVRDG 137
Cdd:cd07102    3 PIDGSVIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAqaggEIRGM 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 138 D------VQLAQQLLHYHAIQASTQEEALAGWEPMGVIGLILPPTFSFLEMMWRICPALAVGCTVvaLVPPASPAPLL-- 209
Cdd:cd07102   83 LerarymISIAEEALADIRVPEKDGFERYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAV--ILKHSPQTPLCge 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 210 -LAQLAGELGPFPGILNVLSGPASLVPILASQPGIRKVAFCGAPEGGL-------------------------------- 256
Cdd:cd07102  161 rFAAAFAEAGLPEGVFQVLHLSHETSAALIADPRIDHVSFTGSVAGGRaiqraaagrfikvglelggkdpayvrpdadld 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 257 ----------------------RLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMG--ARGAAAcDLVQRFVREAQSQ 312
Cdd:cd07102  241 aaaeslvdgaffnsgqsccsieRIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGpvVSARAA-DFVRAQIADAIAK 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 313 GA------QVFQAGDVPSerPFYPPTLVSNLPPASPCAQVEVPWPVV----VASPfrtaKEALLVANGTPRGGSASVWSE 382
Cdd:cd07102  320 GAralidgALFPEDKAGG--AYLAPTVLTNVDHSMRVMREETFGPVVgimkVKSD----AEAIALMNDSEYGLTASVWTK 393
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....
gi 223972653 383 RLGQALELGYGLQVGTVWINAHGLRDPSVPTGGCKESGCSWHGGPDGLYEYLRP 436
Cdd:cd07102  394 DIARAEALGEQLETGTVFMNRCDYLDPALAWTGVKDSGRGVTLSRLGYDQLTRP 447
ALDH_BenzADH-like cd07104
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ...
514-714 3.62e-16

ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, p-hydroxybenzaldehyde dehydrogenase and related proteins; ALDH subfamily which includes the NAD(P)+-dependent, benzaldehyde dehydrogenase II (XylC, BenzADH, EC=1.2.1.28) involved in the oxidation of benzyl alcohol to benzoate; p-hydroxybenzaldehyde dehydrogenase (PchA, HBenzADH) which catalyzes the oxidation of p-hydroxybenzaldehyde to p-hydroxybenzoic acid; vanillin dehydrogenase (Vdh, VaniDH) involved in the metabolism of ferulic acid as seen in Pseudomonas putida KT2440; and other related sequences.


Pssm-ID: 143422 [Multi-domain]  Cd Length: 431  Bit Score: 81.42  E-value: 3.62e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 514 DIRGAVEAAHQAFPGWAGQSPGARAALLWALAAALERRKSTLASRLERQ-GAELKAAEAEVELSARRLR-AWGARVQAQG 591
Cdd:cd07104    1 DVDRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIREsGSTRPKAAFEVGAAIAILReAAGLPRRPEG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 592 HTLQvAGLRGPVLRL-REPLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACP-----LLAlEVCQDMAtvFPA 665
Cdd:cd07104   81 EILP-SDVPGKESMVrRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPvtgglLIA-EIFEEAG--LPK 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 223972653 666 GLANVVTGDRDHLTRCLALHQDVQAMWYFGSAQGSQFVEWASAGNLKPV 714
Cdd:cd07104  157 GVLNVVPGGGSEIGDALVEHPRVRMISFTGSTAVGRHIGELAGRHLKKV 205
ALDH_SNDH cd07118
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ...
504-714 5.09e-16

Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone dehydrogenase (SNDH) from Gluconobacter oxydans UV10. In G. oxydans, D-sorbitol is converted to 2-keto-L-gulonate (a precursor of L-ascorbic acid) in sequential oxidation steps catalyzed by a FAD-dependent, L-sorbose dehydrogenase and an NAD(P)+-dependent, L-sorbosone dehydrogenase.


Pssm-ID: 143436 [Multi-domain]  Cd Length: 454  Bit Score: 81.23  E-value: 5.09e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 504 HGYV----AEGGAKDIRGAVEAAHQAFP-GWAGQSPGARAALLWALAAALERRKSTLASRLE--RQGAELKAAEAEVELS 576
Cdd:cd07118    6 HGVVvaryAEGTVEDVDAAVAAARKAFDkGPWPRMSGAERAAVLLKVADLIRARRERLALIEtlESGKPISQARGEIEGA 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 577 ARRLR-AWGARVQAQGHTLQVAGLRGPVLRLREPLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLALEV 655
Cdd:cd07118   86 ADLWRyAASLARTLHGDSYNNLGDDMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTTLML 165
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 223972653 656 CQDMATV-FPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGSAQ-GSQFVEwASAGNLKPV 714
Cdd:cd07118  166 AELLIEAgLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRvGKAIAA-AAARNLKKV 225
ALDH_AldH-CAJ73105 cd07131
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ...
480-714 7.09e-16

Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; Uncharacterized aldehyde dehydrogenase of Candidatus kuenenia AldH (locus CAJ73105) and similar sequences with similarity to alpha-aminoadipic semialdehyde dehydrogenase (AASADH, human ALDH7A1, EC=1.2.1.31), Arabidopsis ALDH7B4, and Streptomyces clavuligerus delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH) are included in this CD.


Pssm-ID: 143449 [Multi-domain]  Cd Length: 478  Bit Score: 80.85  E-value: 7.09e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 480 FVGGRF--QAPGAR--SSRPIRDSsgNLHGYVAEGGAKDIRGAVEAAHQAFPGWAGQSPGARAALLWALAAALERRKSTL 555
Cdd:cd07131    2 YIGGEWvdSASGETfdSRNPADLE--EVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEEL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 556 ASRLERQ-GAELKAAEAEVElsarrlRAWGARVQAQGHTLQVAGLRGP-------VLRLREPLGVLAVVCPDEWPLLAFV 627
Cdd:cd07131   80 ARLVTREmGKPLAEGRGDVQ------EAIDMAQYAAGEGRRLFGETVPselpnkdAMTRRQPIGVVALITPWNFPVAIPS 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 628 SLLAPALAYGNTVVMVPSAACPLLALEVCQD-MATVFPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGSAQGSQFVEWA 706
Cdd:cd07131  154 WKIFPALVCGNTVVFKPAEDTPACALKLVELfAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGET 233

                 ....*...
gi 223972653 707 SAGNLKPV 714
Cdd:cd07131  234 CARPNKRV 241
ALDH_PutA-P5CDH-RocA cd07124
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ...
477-688 4.15e-15

Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate dehydrogenase (EC=1.5.1.12 ), RocA: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. The proline catabolic enzymes, proline dehydrogenase and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH), catalyze the two-step oxidation of proline to glutamate; P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA). In this CD, monofunctional enzyme sequences such as seen in the Bacillus subtilis RocA P5CDH are also present. These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis.


Pssm-ID: 143442  Cd Length: 512  Bit Score: 78.80  E-value: 4.15e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 477 YGLFVGGR-FQAPGARSSRPIRDSSGNLhGYVAEGGAKDIRGAVEAAHQAFPGWAGQSPGARAALLWALAAALERRKSTL 555
Cdd:cd07124   33 YPLVIGGKeVRTEEKIESRNPADPSEVL-GTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRRFEL 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 556 ASRLERQ-GAELKAAEAEV-------ELSARRLRAWGARVqaqghtlqVAGLRGPVLRLR-EPLGVLAVVCPDEWPLLAF 626
Cdd:cd07124  112 AAWMVLEvGKNWAEADADVaeaidflEYYAREMLRLRGFP--------VEMVPGEDNRYVyRPLGVGAVISPWNFPLAIL 183
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 223972653 627 VSLLAPALAYGNTVVMVPSAACPLLA---LEVCQDMAtvFPAGLANVVTGDRDHLTRCLALHQDV 688
Cdd:cd07124  184 AGMTTAALVTGNTVVLKPAEDTPVIAaklVEILEEAG--LPPGVVNFLPGPGEEVGDYLVEHPDV 246
PRK13968 PRK13968
putative succinate semialdehyde dehydrogenase; Provisional
61-433 1.72e-14

putative succinate semialdehyde dehydrogenase; Provisional


Pssm-ID: 184426 [Multi-domain]  Cd Length: 462  Bit Score: 76.44  E-value: 1.72e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653  61 DPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTLESLVTGRAVREVRdGDVQ 140
Cdd:PRK13968  13 NPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQAR-AEVA 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 141 LAQQLLHYHAIQAST----------QEEALAGWEPMGVIGLILPPTFSFLEMMWRICPALAVGCT-VVALVPPASPAPLL 209
Cdd:PRK13968  92 KSANLCDWYAEHGPAmlkaeptlveNQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGyLLKHAPNVMGCAQL 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 210 LAQLAGELGPFPGILNVLSGPASLVPILASQPGIRKVAFCGAPEGGL--------------------------------- 256
Cdd:PRK13968 172 IAQVFKDAGIPQGVYGWLNADNDGVSQMINDSRIAAVTVTGSVRAGAaigaqagaalkkcvlelggsdpfivlndadlel 251
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 257 ---------------------RLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMG--ARGAAACDLVQRfVREAQSQG 313
Cdd:PRK13968 252 avkaavagryqntgqvcaaakRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGpmARFDLRDELHHQ-VEATLAEG 330
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 314 AQVFQAGD-VPSERPFYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVANGTPRGGSASVWSERLGQALELGY 392
Cdd:PRK13968 331 ARLLLGGEkIAGAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTTDETQARQMAA 410
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|.
gi 223972653 393 GLQVGTVWINAHGLRDPSVPTGGCKESGCSWHGGPDGLYEY 433
Cdd:PRK13968 411 RLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEF 451
ALDH_F11_NP-GAPDH cd07082
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ...
499-674 6.45e-14

NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family 11; NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase (NP-GAPDH, EC=1.2.1.9) catalyzes the irreversible oxidation of glyceraldehyde 3-phosphate to 3-phosphoglycerate generating NADPH for biosynthetic reactions. This CD also includes the Arabidopsis thaliana osmotic-stress-inducible ALDH family 11, ALDH11A3 and similar sequences. In autotrophic eukaryotes, NP-GAPDH generates NADPH for biosynthetic processes from photosynthetic glyceraldehyde-3-phosphate exported from the chloroplast and catalyzes one of the classic glycolytic bypass reactions unique to plants.


Pssm-ID: 143401 [Multi-domain]  Cd Length: 473  Bit Score: 74.92  E-value: 6.45e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 499 SSGNLHGYVAEGGAKDIRGAVEAAHQAFPGWAGQSPGaraallwalaaalERRKSTL---ASRLERQGAE---------- 565
Cdd:cd07082   24 IDGEVIGSVPALSALEILEAAETAYDAGRGWWPTMPL-------------EERIDCLhkfADLLKENKEEvanllmweig 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 566 --LKAAEAEVELSARRLRawgarvqaqgHTLQVAG-LRGPVLRL--------------REPLGVLAVVCPDEWPLLAFVS 628
Cdd:cd07082   91 ktLKDALKEVDRTIDYIR----------DTIEELKrLDGDSLPGdwfpgtkgkiaqvrREPLGVVLAIGPFNYPLNLTVS 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 223972653 629 LLAPALAYGNTVVMVPSAACPLLA---LEVCQDMAtvFPAGLANVVTGD 674
Cdd:cd07082  161 KLIPALIMGNTVVFKPATQGVLLGiplAEAFHDAG--FPKGVVNVVTGR 207
ALDH_F1AB_F2_RALDH1 cd07141
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ...
507-714 1.31e-13

NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent retinal dehydrogenase 1 (RALDH 1, ALDH1, EC=1.2.1.36) also known as aldehyde dehydrogenase family 1 member A1 (ALDH1A1) in humans, is a homotetrameric, cytosolic enzyme that catalyzes the oxidation of retinaldehyde to retinoic acid. Human ALDH1B1 and ALDH2 are also in this cluster; both are mitochrondrial homotetramers which play important roles in acetaldehyde oxidation; ALDH1B1 in response to UV light exposure and ALDH2 during ethanol metabolism.


Pssm-ID: 143459  Cd Length: 481  Bit Score: 73.92  E-value: 1.31e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 507 VAEGGAKDIRGAVEAAHQAF-PGwagqSPgaraallWALAAALERRK--STLASRLERQGAELKAAEA------------ 571
Cdd:cd07141   38 VQEGDKADVDKAVKAARAAFkLG----SP-------WRTMDASERGRllNKLADLIERDRAYLASLETldngkpfsksyl 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 572 -EVELSARRLR---AWGARVQaqGHTLQVaglRGPVLRL--REPLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVPS 645
Cdd:cd07141  107 vDLPGAIKVLRyyaGWADKIH--GKTIPM---DGDFFTYtrHEPVGVCGQIIPWNFPLLMAAWKLAPALACGNTVVLKPA 181
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 223972653 646 AACPLLALEVCQDMATV-FPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGSAQ-GSQFVEWASAGNLKPV 714
Cdd:cd07141  182 EQTPLTALYLASLIKEAgFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEvGKLIQQAAGKSNLKRV 252
ALDH_CddD-AldA-like cd07089
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ...
505-714 1.75e-13

Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric acid dehydrogenase (CddD) from Rhodococcus ruber SC1 which converts 6-oxolauric acid to dodecanedioic acid; and the aldehyde dehydrogenase (locus SSP0762) from Staphylococcus saprophyticus subsp. saprophyticus ATCC 15305 and also, the Mycobacterium tuberculosis H37Rv ALDH AldA (locus Rv0768) sequence; and other similar sequences, are included in this CD.


Pssm-ID: 143408 [Multi-domain]  Cd Length: 459  Bit Score: 73.43  E-value: 1.75e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 505 GYVAEGGAKDIRGAVEAAHQAFPGWAGQSPGAraallwalaaalERRK--STLASRLERQGAELKA---AEA-------- 571
Cdd:cd07089   11 GTAPDAGAADVDAAIAAARRAFDTGDWSTDAE------------ERARclRQLHEALEARKEELRAllvAEVgapvmtar 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 572 --EVELSARRLRAWG------ARVQAQGHTLQVAGLRGPVLRlREPLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMV 643
Cdd:cd07089   79 amQVDGPIGHLRYFAdladsfPWEFDLPVPALRGGPGRRVVR-REPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLK 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 223972653 644 PSAACPLLALEVCQDMA-TVFPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGS-AQGSQFVEwASAGNLKPV 714
Cdd:cd07089  158 PAPDTPLSALLLGEIIAeTDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGStAVGRRIMA-QAAATLKRV 229
ALDH_y4uC cd07149
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ...
500-698 1.81e-13

Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; Uncharacterized aldehyde dehydrogenase (ORF name y4uC) with sequence similarity to the moss Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123) believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and similar sequences are included in this CD.


Pssm-ID: 143467 [Multi-domain]  Cd Length: 453  Bit Score: 73.40  E-value: 1.81e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 500 SGNLHGYVAEGGAKDIRGAVEAAHQAFPGWAGQSPGARAALLWALAAALERRKSTLASRLERQGAE-LKAAEAEVELSAR 578
Cdd:cd07149    8 DGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKpIKDARKEVDRAIE 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 579 --RLRAWGARvQAQGHTLQVAGLRGPVLR----LREPLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLA 652
Cdd:cd07149   88 tlRLSAEEAK-RLAGETIPFDASPGGEGRigftIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPASQTPLSA 166
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 223972653 653 LEVCQDMATV-FPAGLANVVTGDRDHLTRCLALHQDVqAMWYF-GSAQ 698
Cdd:cd07149  167 LKLAELLLEAgLPKGALNVVTGSGETVGDALVTDPRV-RMISFtGSPA 213
ALDH_F9_TMBADH cd07090
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ...
496-714 2.56e-13

NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, 4-trimethylaminobutyraldehyde dehydrogenase (TMABADH, EC=1.2.1.47), also known as aldehyde dehydrogenase family 9 member A1 (ALDH9A1) in humans, is a cytosolic tetramer which catalyzes the oxidation of gamma-aminobutyraldehyde involved in 4-aminobutyric acid (GABA) biosynthesis and also oxidizes betaine aldehyde (gamma-trimethylaminobutyraldehyde) which is involved in carnitine biosynthesis.


Pssm-ID: 143409 [Multi-domain]  Cd Length: 457  Bit Score: 72.72  E-value: 2.56e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 496 IRDSSGNLHGYVAEGGAKDIRGAVEAAHQAFPGWAGQSPgaraallwalaaaLERRKSTL-ASRLERQ------------ 562
Cdd:cd07090    2 IEPATGEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSG-------------MERGRILRkAADLLRErndeiarletid 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 563 -GAELKAAEAEVELSARRLRAWGARVQA-QGHTLQVAGLRGPVLRlREPLGVlaVVCPDEW--PLLAFVSLLAPALAYGN 638
Cdd:cd07090   69 nGKPIEEARVDIDSSADCLEYYAGLAPTlSGEHVPLPGGSFAYTR-REPLGV--CAGIGAWnyPIQIASWKSAPALACGN 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 639 TVVMVPSAACPLLALEvcqdMATVF-----PAGLANVVTGDRDhLTRCLALHQDVQAMWYFGSAQGSQFVEWASAGNLKP 713
Cdd:cd07090  146 AMVYKPSPFTPLTALL----LAEILteaglPDGVFNVVQGGGE-TGQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGIKH 220

                 .
gi 223972653 714 V 714
Cdd:cd07090  221 V 221
ALDH_F21_LactADH-like cd07094
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ...
500-697 1.07e-12

ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related proteins; ALDH subfamily which includes Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123), and NAD+-dependent, lactaldehyde dehydrogenase (EC=1.2.1.22) and like sequences.


Pssm-ID: 143413 [Multi-domain]  Cd Length: 453  Bit Score: 70.92  E-value: 1.07e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 500 SGNLHGYVAEGGAKDIRGAVEAAHQAFPGWAGQSPGARAALLWALAAALERRKSTLASRLERQ-GAELKAAEAEVELSAR 578
Cdd:cd07094    8 DGEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEgGKPIKDARVEVDRAID 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 579 RLRAWGARVQA-QGHTLQVAGLRGPVLRL----REPLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLAL 653
Cdd:cd07094   88 TLRLAAEEAERiRGEEIPLDATQGSDNRLawtiREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASKTPLSAL 167
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 223972653 654 EVCQdmaTVFPAGLA----NVVTGDRDHLTRCLALHQDVQAMWYFGSA 697
Cdd:cd07094  168 ELAK---ILVEAGVPegvlQVVTGEREVLGDAFAADERVAMLSFTGSA 212
ALDH_SaliADH cd07105
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ...
514-714 4.59e-12

Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2.1.65) involved in the upper naphthalene catabolic pathway of Pseudomonas strain C18 and other similar sequences are present in this CD.


Pssm-ID: 143423 [Multi-domain]  Cd Length: 432  Bit Score: 68.76  E-value: 4.59e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 514 DIRGAVEAAHQAFPGWAGQSPGaraallwalaaalERRK--STLASRLERQGAELKAAEAE------------VELSARR 579
Cdd:cd07105    1 DADQAVEAAAAAFPAWSKTPPS-------------ERRDilLKAADLLESRRDEFIEAMMEetgataawagfnVDLAAGM 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 580 LRAWGARV-QAQGHTLQVAGLRGPVLRLREPLGVLAVVCPdeW--PL-LAFVSLLAPaLAYGNTVVMVPSAACPLLALEV 655
Cdd:cd07105   68 LREAASLItQIIGGSIPSDKPGTLAMVVKEPVGVVLGIAP--WnaPViLGTRAIAYP-LAAGNTVVLKASELSPRTHWLI 144
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 223972653 656 CQDM-ATVFPAGLANVVTGDRDH---LTRCLALHQDVQAMWYFGSAQ-GSQFVEWAsAGNLKPV 714
Cdd:cd07105  145 GRVFhEAGLPKGVLNVVTHSPEDapeVVEALIAHPAVRKVNFTGSTRvGRIIAETA-AKHLKPV 207
PLN02419 PLN02419
methylmalonate-semialdehyde dehydrogenase [acylating]
44-402 4.47e-11

methylmalonate-semialdehyde dehydrogenase [acylating]


Pssm-ID: 166060 [Multi-domain]  Cd Length: 604  Bit Score: 66.31  E-value: 4.47e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653  44 VNGKWLKPEHRNSVPCQDPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTLE 123
Cdd:PLN02419 118 IGGSFVESQSSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDKLAMNI 197
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 124 SLVTGRAVREvRDGDVQLAQQLLHYHAIQASTQE-----------EALAGWEPMGVIGLILPPTFSFLEMMWRICPALAV 192
Cdd:PLN02419 198 TTEQGKTLKD-SHGDIFRGLEVVEHACGMATLQMgeylpnvsngvDTYSIREPLGVCAGICPFNFPAMIPLWMFPVAVTC 276
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 193 GCTVVALVPPASP-APLLLAQLAGELGPFPGILNVLSGPASLVPILASQPGIRKVAFCGAPEGGLRLLIQESVwdeAMRR 271
Cdd:PLN02419 277 GNTFILKPSEKDPgASVILAELAMEAGLPDGVLNIVHGTNDTVNAICDDEDIRAVSFVGSNTAGMHIYARAAA---KGKR 353
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 272 LQERMGRLRSGRGL-DGAVD----------MGARG--------------------------------------------- 295
Cdd:PLN02419 354 IQSNMGAKNHGLVLpDANIDatlnallaagFGAAGqrcmalstvvfvgdakswedklverakalkvtcgsepdadlgpvi 433
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 296 -AAACDLVQRFVREAQSQGAQVFQAGD---VPSERP--FYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVAN 369
Cdd:PLN02419 434 sKQAKERICRLIQSGVDDGAKLLLDGRdivVPGYEKgnFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEAISIIN 513
                        410       420       430
                 ....*....|....*....|....*....|...
gi 223972653 370 GTPRGGSASVWSERLGQALELGYGLQVGTVWIN 402
Cdd:PLN02419 514 KNKYGNGAAIFTSSGAAARKFQMDIEAGQIGIN 546
PLN02278 PLN02278
succinic semialdehyde dehydrogenase
507-674 4.56e-11

succinic semialdehyde dehydrogenase


Pssm-ID: 215157 [Multi-domain]  Cd Length: 498  Bit Score: 65.87  E-value: 4.56e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 507 VAEGGAKDIRGAVEAAHQAFPGWAGQSPGARAALLWALAAALERRKSTLAS--RLErQGAELKAAEAEVELSARRLRaWG 584
Cdd:PLN02278  56 VPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIANKEDLAQlmTLE-QGKPLKEAIGEVAYGASFLE-YF 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 585 AR--VQAQGHTLQVAGLRGPVLRLREPLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPL--LALEVCQDMA 660
Cdd:PLN02278 134 AEeaKRVYGDIIPSPFPDRRLLVLKQPVGVVGAITPWNFPLAMITRKVGPALAAGCTVVVKPSELTPLtaLAAAELALQA 213
                        170
                 ....*....|....
gi 223972653 661 TVfPAGLANVVTGD 674
Cdd:PLN02278 214 GI-PPGVLNVVMGD 226
ALDH_EDX86601 cd07102
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ...
515-714 6.80e-11

Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (locus EDX86601) and other similar sequences, are present in this CD.


Pssm-ID: 143420 [Multi-domain]  Cd Length: 452  Bit Score: 65.34  E-value: 6.80e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 515 IRGAVEAAHQAFPGWAGQSPGARAALLWALAAALERRKSTLASRLERQ-GAELKAAEAEVELSARRLR---AWGARVQAQ 590
Cdd:cd07102   20 VRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQmGRPIAQAGGEIRGMLERARymiSIAEEALAD 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 591 GHTLQVAGLRGPVLRlrEPLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLALEVCQ--DMATVfPAGLA 668
Cdd:cd07102  100 IRVPEKDGFERYIRR--EPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCGERFAAafAEAGL-PEGVF 176
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 223972653 669 NVVTGDRDHLTRCLALHqDVQAMWYFGSAQGSQFVEWASAGNLKPV 714
Cdd:cd07102  177 QVLHLSHETSAALIADP-RIDHVSFTGSVAGGRAIQRAAAGRFIKV 221
PLN02315 PLN02315
aldehyde dehydrogenase family 7 member
30-437 1.39e-10

aldehyde dehydrogenase family 7 member


Pssm-ID: 177949  Cd Length: 508  Bit Score: 64.47  E-value: 1.39e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653  30 LAWLDTQDRCLGHYVNGKWlkPEHRNSVPCQDPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLA 109
Cdd:PLN02315  11 LSEIGLSSRNLGCYVGGEW--RANGPLVSSVNPANNQPIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQIG 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 110 EVIQKHQRLLWTLESLVTGR----AVREVR------DGDVQLAQQLLHYHAIQASTQEEALAGWEPMGVIGLILPPTFSF 179
Cdd:PLN02315  89 DALRAKLDYLGRLVSLEMGKilaeGIGEVQeiidmcDFAVGLSRQLNGSIIPSERPNHMMMEVWNPLGIVGVITAFNFPC 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 180 LEMMWRICPALAVGCTVVALVPPASP-----APLLLAQLAGELGPFPGILNVLSGPASLVPILASQPGIRKVAFCGAPEG 254
Cdd:PLN02315 169 AVLGWNACIALVCGNCVVWKGAPTTPlitiaMTKLVAEVLEKNNLPGAIFTSFCGGAEIGEAIAKDTRIPLVSFTGSSKV 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 255 GL------------------------------------------------------RLLIQESVWDEAMRRLQERMGRLR 280
Cdd:PLN02315 249 GLmvqqtvnarfgkcllelsgnnaiivmddadiqlavrsvlfaavgtagqrcttcrRLLLHESIYDDVLEQLLTVYKQVK 328
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 281 SGRGLDGAVDMGA-RGAAACDLVQRFVREAQSQGAQVFQAGD-VPSERPFYPPTLVSnLPPASPCAQVEVPWPVVVASPF 358
Cdd:PLN02315 329 IGDPLEKGTLLGPlHTPESKKNFEKGIEIIKSQGGKILTGGSaIESEGNFVQPTIVE-ISPDADVVKEELFGPVLYVMKF 407
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 359 RTAKEALLVANGTPRGGSASVWSERLGQALElgyglqvgtvWINAH----GLRDPSVPT---------GGCKESGCSWHG 425
Cdd:PLN02315 408 KTLEEAIEINNSVPQGLSSSIFTRNPETIFK----------WIGPLgsdcGIVNVNIPTngaeiggafGGEKATGGGREA 477
                        490
                 ....*....|..
gi 223972653 426 GPDGLYEYLRPS 437
Cdd:PLN02315 478 GSDSWKQYMRRS 489
ALDH_DDALDH cd07099
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ...
501-676 1.65e-10

Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4'-diapolycopene-dialdehyde dehydrogenase (DDALDH) involved in C30 carotenoid synthesis in Methylomonas sp. strain 16a and other similar sequences are present in this CD. DDALDH converts 4,4'-diapolycopene-dialdehyde into 4,4'-diapolycopene-diacid.


Pssm-ID: 143417 [Multi-domain]  Cd Length: 453  Bit Score: 63.78  E-value: 1.65e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 501 GNLHGYVAEGGAKDIRGAVEAAHQAFPGWAGQSPGARAALLWALAAALERRKSTLASRLER-QGAELKAAEAEVELSARR 579
Cdd:cd07099    6 GEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAeTGKPRADAGLEVLLALEA 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 580 LRAW---GARVQAQGHTLQVAGLRGPVLRL-REPLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLALEV 655
Cdd:cd07099   86 IDWAarnAPRVLAPRKVPTGLLMPNKKATVeYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPLVGELL 165
                        170       180
                 ....*....|....*....|..
gi 223972653 656 CQDMATV-FPAGLANVVTGDRD 676
Cdd:cd07099  166 AEAWAAAgPPQGVLQVVTGDGA 187
ALDH_BenzADH cd07152
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ...
501-714 1.69e-10

NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II (XylC, BenzADH, EC=1.2.1.28) is involved in the oxidation of benzyl alcohol to benzoate. In Acinetobacter calcoaceticus, this process is carried out by the chromosomally encoded, benzyl alcohol dehydrogenase (xylB) and benzaldehyde dehydrogenase II (xylC) enzymes; whereas in Pseudomonas putida they are encoded by TOL plasmids.


Pssm-ID: 143470 [Multi-domain]  Cd Length: 443  Bit Score: 63.85  E-value: 1.69e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 501 GNLHGYVAEGGAKDIRGAVEAAHQAFPGWAGQSPGARAALLWALAAALERRKSTLASRLERQ-GAELKAAEAEVELSARR 579
Cdd:cd07152    1 GAVLGEVGVADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVREsGSIRPKAGFEVGAAIGE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 580 LR-AWGARVQAQGHTLQVAGLRGPVLRlREPLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPllaleVCQD 658
Cdd:cd07152   81 LHeAAGLPTQPQGEILPSAPGRLSLAR-RVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTP-----VSGG 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 223972653 659 M--ATVF-----PAGLANVVTGDRDhLTRCLALHQDVQAMWYFGSAQGSQFVEWASAGNLKPV 714
Cdd:cd07152  155 VviARLFeeaglPAGVLHVLPGGAD-AGEALVEDPNVAMISFTGSTAVGRKVGEAAGRHLKKV 216
PLN00412 PLN00412
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
42-420 5.54e-10

NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional


Pssm-ID: 215110 [Multi-domain]  Cd Length: 496  Bit Score: 62.47  E-value: 5.54e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653  42 HYVNGKWLKPEHRNSVPCQDPITGE---NLASCLQAQAEDVAAAVeaaRMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRL 118
Cdd:PLN00412  18 YYADGEWRTSSSGKSVAITNPSTRKtqyKVQACTQEEVNKAMESA---KAAQKAWAKTPLWKRAELLHKAAAILKEHKAP 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 119 LwtLESLV------TGRAVREV-RDGDV----------QLAQ-QLLHYHAIQASTQEE-ALAGWEPMGVIGLILPPTFSF 179
Cdd:PLN00412  95 I--AECLVkeiakpAKDAVTEVvRSGDLisytaeegvrILGEgKFLVSDSFPGNERNKyCLTSKIPLGVVLAIPPFNYPV 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 180 LEMMWRICPALAVGCTVVaLVPP--ASPAPLLLAQ---LAGelgpFP-GILNVLSGPASLV-PILASQPGIRKVAFCGAP 252
Cdd:PLN00412 173 NLAVSKIAPALIAGNAVV-LKPPtqGAVAALHMVHcfhLAG----FPkGLISCVTGKGSEIgDFLTMHPGVNCISFTGGD 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 253 EG---------------------------------------------GLR------LLIQESVWDEAMRRLQERMGRLRS 281
Cdd:PLN00412 248 TGiaiskkagmvplqmelggkdacivledadldlaaaniikggfsysGQRctavkvVLVMESVADALVEKVNAKVAKLTV 327
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 282 GRGLDGAVDMGARGAAACDLVQRFVREAQSQGAQVFQagDVPSERPFYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTA 361
Cdd:PLN00412 328 GPPEDDCDITPVVSESSANFIEGLVMDAKEKGATFCQ--EWKREGNLIWPLLLDNVRPDMRIAWEEPFGPVLPVIRINSV 405
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 362 KEALLVANGTPRGGSASVWSERLGQALELGYGLQVGTVWINAHGLRDPS-VPTGGCKESG 420
Cdd:PLN00412 406 EEGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQINSAPARGPDhFPFQGLKDSG 465
ALDH_RL0313 cd07148
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ...
257-432 1.03e-09

Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; Uncharacterized aldehyde dehydrogenase (locus RL0313) with sequence similarity to the moss Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123) believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and similar sequences are included in this CD.


Pssm-ID: 143466 [Multi-domain]  Cd Length: 455  Bit Score: 61.28  E-value: 1.03e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 257 RLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMGAR-GAAACDLVQRFVREAQSQGAQVFqAGDVPSERPFYPPTLVS 335
Cdd:cd07148  270 RVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLiRPREVDRVEEWVNEAVAAGARLL-CGGKRLSDTTYAPTVLL 348
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 336 NLPPASPCAQVEVPWPVVVASPFRTAKEALLVANGTPRGGSASVWSERLGQALELGYGLQVGTVWINAH-GLRDPSVPTG 414
Cdd:cd07148  349 DPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAVFTKDLDVALKAVRRLDATAVMVNDHtAFRVDWMPFA 428
                        170
                 ....*....|....*...
gi 223972653 415 GCKESGCSWHGGPDGLYE 432
Cdd:cd07148  429 GRRQSGYGTGGIPYTMHD 446
ALDH_HBenzADH cd07151
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ...
513-674 1.87e-09

NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, p-hydroxybenzaldehyde dehydrogenase (PchA, HBenzADH) which catalyzes oxidation of p-hydroxybenzaldehyde to p-hydroxybenzoic acid and other related sequences are included in this CD.


Pssm-ID: 143469 [Multi-domain]  Cd Length: 465  Bit Score: 60.78  E-value: 1.87e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 513 KDIRGAVEAAHQAFPGWAGQSPGARAALLWALAAALERRKSTLASRLERQ--GAELKAAeAEVELSARRLRawgarvQAQ 590
Cdd:cd07151   32 EDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIREsgSTRIKAN-IEWGAAMAITR------EAA 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 591 GHTLQVAGLRGPVL------RL-REPLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACP----LLalevcqdM 659
Cdd:cd07151  105 TFPLRMEGRILPSDvpgkenRVyREPLGVVGVISPWNFPLHLSMRSVAPALALGNAVVLKPASDTPitggLL-------L 177
                        170       180
                 ....*....|....*....|
gi 223972653 660 ATVF-----PAGLANVVTGD 674
Cdd:cd07151  178 AKIFeeaglPKGVLNVVVGA 197
ALDH_SGSD_AstD cd07095
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ...
514-698 1.87e-09

N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate 5-semialdehyde dehydrogenase or succinylglutamic semialdehyde dehydrogenase (SGSD, E. coli AstD, EC=1.2.1.71) involved in L-arginine degradation via the arginine succinyltransferase (AST) pathway and catalyzes the NAD+-dependent reduction of succinylglutamate semialdehyde into succinylglutamate.


Pssm-ID: 143414 [Multi-domain]  Cd Length: 431  Bit Score: 60.36  E-value: 1.87e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 514 DIRGAVEAAHQAFPGWAGQSPGARAALLWALAAALERRKSTLASRLERQ--------GAELKAAEAEVELS--ARRLRAW 583
Cdd:cd07095    1 QVDAAVAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISREtgkplweaQTEVAAMAGKIDISikAYHERTG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 584 GARVQAQGHTLqvaglrgpVLRLRePLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLALEVCQDMATV- 662
Cdd:cd07095   81 ERATPMAQGRA--------VLRHR-PHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAg 151
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 223972653 663 FPAGLANVVTGDRDhLTRCLALHQDVQAMWYFGSAQ 698
Cdd:cd07095  152 LPPGVLNLVQGGRE-TGEALAAHEGIDGLLFTGSAA 186
ALDH_PutA-P5CDH cd07125
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ...
480-676 2.36e-09

Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the aldehyde dehydrogenase (ALDH) protein superfamily, proline dehydrogenase and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, (EC=1.5.1.12 )), catalyze the two-step oxidation of proline to glutamate; P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA) These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes.


Pssm-ID: 143443 [Multi-domain]  Cd Length: 518  Bit Score: 60.29  E-value: 2.36e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 480 FVGGRFQAPGARssRPIRDSSGN--LHGYVAEGGAKDIRGAVEAAHQAFPGWAGQSPgaraallwalaaalERRKSTL-- 555
Cdd:cd07125   36 IINGEETETGEG--APVIDPADHerTIGEVSLADAEDVDAALAIAAAAFAGWSATPV--------------EERAEILek 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 556 -ASRLERQGAELKA----------AEAEVELS---------ARRLRAWGARVQAQGHTLQVAGLRgpvlrlREPLGVLAV 615
Cdd:cd07125  100 aADLLEANRGELIAlaaaeagktlADADAEVReaidfcryyAAQARELFSDPELPGPTGELNGLE------LHGRGVFVC 173
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 223972653 616 VCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLALEVCQDM--ATVfPAGLANVVTGDRD 676
Cdd:cd07125  174 ISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQTPLIAARAVELLheAGV-PRDVLQLVPGDGE 235
gabD PRK11241
NADP-dependent succinate-semialdehyde dehydrogenase I;
480-704 4.65e-09

NADP-dependent succinate-semialdehyde dehydrogenase I;


Pssm-ID: 183050 [Multi-domain]  Cd Length: 482  Bit Score: 59.54  E-value: 4.65e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 480 FVGGRF-QAPGARSSRPIRDSSGNLHGYVAEGGAKDIRGAVEAAHQAFPGWAGQSPGARAALLWALAAALERRKSTLASR 558
Cdd:PRK11241  14 LINGEWlDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMMEHQDDLARL 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 559 LE-RQGAELKAAEAEVELSARRLRaWGARVQAQ--GHTLQVAGLRGPVLRLREPLGVLAVVCPDEWPLLAFVSLLAPALA 635
Cdd:PRK11241  94 MTlEQGKPLAEAKGEISYAASFIE-WFAEEGKRiyGDTIPGHQADKRLIVIKQPIGVTAAITPWNFPAAMITRKAGPALA 172
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 223972653 636 YGNTVVMVPSAACPL--LALEVCQDMATVfPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGSAQ-GSQFVE 704
Cdd:PRK11241 173 AGCTMVLKPASQTPFsaLALAELAIRAGI-PAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEiGRQLME 243
D1pyr5carbox3 TIGR01238
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ...
505-713 1.02e-08

delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents one of several related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. Members of this branch are the C-terminal domain of the PutA bifunctional proline dehydrogenase / delta-1-pyrroline-5-carboxylate dehydrogenase. [Energy metabolism, Amino acids and amines]


Pssm-ID: 273518 [Multi-domain]  Cd Length: 500  Bit Score: 58.38  E-value: 1.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653  505 GYVAEGGAKDIRGAVEAAHQAFPGWAGQSPGARAALLWALAAALERRKSTLASRLERQ-GAELKAAEAEVELSARRLRAW 583
Cdd:TIGR01238  66 GQVFHANLAHVQAAIDSAQQAFPTWNATPAKERAAKLDRLADLLELHMPELMALCVREaGKTIHNAIAEVREAVDFCRYY 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653  584 GARVQaqgHTLQVAGLRgpvlrlrePLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLALEVCQDMATV- 662
Cdd:TIGR01238 146 AKQVR---DVLGEFSVE--------SRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQEAg 214
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 223972653  663 FPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGSAQGSQFVEWASAGNLKP 713
Cdd:TIGR01238 215 FPAGTIQLLPGRGADVGAALTSDPRIAGVAFTGSTEVAQLINQTLAQREDA 265
astD PRK09457
succinylglutamic semialdehyde dehydrogenase; Reviewed
512-698 1.54e-08

succinylglutamic semialdehyde dehydrogenase; Reviewed


Pssm-ID: 181873  Cd Length: 487  Bit Score: 57.66  E-value: 1.54e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 512 AKDIRGAVEAAHQAFPGWAGQSPGARAALLWALAAALERRKSTLASRLERQ--------GAELKAAEAEVELSarrLRAW 583
Cdd:PRK09457  36 AAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAEVIAREtgkplweaATEVTAMINKIAIS---IQAY 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 584 GARVqaqGHTLQVAGLRGPVLRLRePLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLALEV--CQDMAT 661
Cdd:PRK09457 113 HERT---GEKRSEMADGAAVLRHR-PHGVVAVFGPYNFPGHLPNGHIVPALLAGNTVVFKPSELTPWVAELTvkLWQQAG 188
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 223972653 662 VfPAGLANVVTGDRDhLTRCLALHQDVQAMWYFGSAQ 698
Cdd:PRK09457 189 L-PAGVLNLVQGGRE-TGKALAAHPDIDGLLFTGSAN 223
PLN02419 PLN02419
methylmalonate-semialdehyde dehydrogenase [acylating]
461-719 1.68e-08

methylmalonate-semialdehyde dehydrogenase [acylating]


Pssm-ID: 166060 [Multi-domain]  Cd Length: 604  Bit Score: 57.83  E-value: 1.68e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 461 STLPAGPEIGPSPAPPYGL--FVGGRF-QAPGARSSRPIRDSSGNLHGYVAEGGAKDIRGAVEAAHQAFPGWAGQSPGAR 537
Cdd:PLN02419  96 SWLSTSPEQSTQPQMPPRVpnLIGGSFvESQSSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTR 175
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 538 AALLWALAAALERRKSTLASRLE-RQGAELKAAEAEVELSARRLR-AWGARVQAQGHTLQVAGLRGPVLRLREPLGVLAV 615
Cdd:PLN02419 176 QRVMLKFQELIRKNMDKLAMNITtEQGKTLKDSHGDIFRGLEVVEhACGMATLQMGEYLPNVSNGVDTYSIREPLGVCAG 255
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 616 VCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLALEVCQ-DMATVFPAGLANVVTGDRDHLTrCLALHQDVQAMWYF 694
Cdd:PLN02419 256 ICPFNFPAMIPLWMFPVAVTCGNTFILKPSEKDPGASVILAElAMEAGLPDGVLNIVHGTNDTVN-AICDDEDIRAVSFV 334
                        250       260
                 ....*....|....*....|....*
gi 223972653 695 GSAQGSQFVEWASAGNLKPVWASRG 719
Cdd:PLN02419 335 GSNTAGMHIYARAAAKGKRIQSNMG 359
PRK10090 PRK10090
aldehyde dehydrogenase A; Provisional
560-708 2.20e-08

aldehyde dehydrogenase A; Provisional


Pssm-ID: 182233 [Multi-domain]  Cd Length: 409  Bit Score: 57.05  E-value: 2.20e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 560 ERQGAELKAAEAEVELSARRLR---AWGARVQaqGHTLQVAGLRGPVLRLREPLGVLAVVCPDEWPLLAFVSLLAPALAY 636
Cdd:PRK10090  21 EEGGKIQQLAEVEVAFTADYIDymaEWARRYE--GEIIQSDRPGENILLFKRALGVTTGILPWNFPFFLIARKMAPALLT 98
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 223972653 637 GNTVVMVPSAACPLLALEVCQDMATV-FPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGS-AQGSQFVEWASA 708
Cdd:PRK10090  99 GNTIVIKPSEFTPNNAIAFAKIVDEIgLPKGVFNLVLGRGETVGQELAGNPKVAMVSMTGSvSAGEKIMAAAAK 172
ALDH_PhpJ cd07146
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ...
549-697 4.30e-08

Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative phosphonoformaldehyde dehydrogenase (PhpJ), an aldehyde dehydrogenase homolog reportedly involved in the biosynthesis of phosphinothricin tripeptides in Streptomyces viridochromogenes DSM 40736, and similar sequences are included in this CD.


Pssm-ID: 143464 [Multi-domain]  Cd Length: 451  Bit Score: 56.21  E-value: 4.30e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 549 ERRKSTLASRLERQ-GAELKAAEAEVELSARRLRAWGA---RVQAQGHTLQVAGLRGP--VLRLREPLGVLAVVCPDEWP 622
Cdd:cd07146   54 EARREEFARLITLEsGLCLKDTRYEVGRAADVLRFAAAealRDDGESFSCDLTANGKArkIFTLREPLGVVLAITPFNHP 133
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 223972653 623 LLAFVSLLAPALAYGNTVVMVPSAACPLLAL---EVCQDMAtvFPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGSA 697
Cdd:cd07146  134 LNQVAHKIAPAIAANNRIVLKPSEKTPLSAIylaDLLYEAG--LPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGV 209
PRK03137 PRK03137
1-pyrroline-5-carboxylate dehydrogenase; Provisional
505-674 5.49e-08

1-pyrroline-5-carboxylate dehydrogenase; Provisional


Pssm-ID: 179543  Cd Length: 514  Bit Score: 56.10  E-value: 5.49e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 505 GYVAEGGAKDIRGAVEAAHQAFPGWAGQSPGARAALLWALAAALERRKSTLASRLERQ-GAELKAAEAEV-------ELS 576
Cdd:PRK03137  65 GRVSKATKELAEKAMQAALEAFETWKKWSPEDRARILLRAAAIIRRRKHEFSAWLVKEaGKPWAEADADTaeaidflEYY 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 577 ARRLRAWgarvqAQGHTlqVAGLRGPVLRLR-EPLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLALEV 655
Cdd:PRK03137 145 ARQMLKL-----ADGKP--VESRPGEHNRYFyIPLGVGVVISPWNFPFAIMAGMTLAAIVAGNTVLLKPASDTPVIAAKF 217
                        170       180
                 ....*....|....*....|
gi 223972653 656 CQDMATV-FPAGLANVVTGD 674
Cdd:PRK03137 218 VEVLEEAgLPAGVVNFVPGS 237
ALDH_PutA-P5CDH cd07125
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ...
58-420 8.13e-08

Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the aldehyde dehydrogenase (ALDH) protein superfamily, proline dehydrogenase and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, (EC=1.5.1.12 )), catalyze the two-step oxidation of proline to glutamate; P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA) These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes.


Pssm-ID: 143443 [Multi-domain]  Cd Length: 518  Bit Score: 55.66  E-value: 8.13e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653  58 PCQDPITGE-NLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTLESLVTGRAVREVrD 136
Cdd:cd07125   49 PVIDPADHErTIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEILEKAADLLEANRGELIALAAAEAGKTLADA-D 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 137 GDVQLAQQLLHYHAIQA-----------STQEEALAGWEPMGVIGLILPPTFSFLEMMWRICPALAVGCTVVAlvPPASP 205
Cdd:cd07125  128 AEVREAIDFCRYYAAQArelfsdpelpgPTGELNGLELHGRGVFVCISPWNFPLAIFTGQIAAALAAGNTVIA--KPAEQ 205
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 206 APL---LLAQLAGELGPFPGILNVLSGPASLV-PILASQPGIRKVAFCGAPE-----------------------GG--- 255
Cdd:cd07125  206 TPLiaaRAVELLHEAGVPRDVLQLVPGDGEEIgEALVAHPRIDGVIFTGSTEtaklinralaerdgpilpliaetGGkna 285
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 256 ------------------------------LRLLI-QESVWDEAMRRLQERMGRLRSGRGLDGAVDMG--ARGAAAcDLV 302
Cdd:cd07125  286 mivdstalpeqavkdvvqsafgsagqrcsaLRLLYlQEEIAERFIEMLKGAMASLKVGDPWDLSTDVGplIDKPAG-KLL 364
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 303 QRFVREAQSQGAQVFQAgDVPSERP-FYPPTLVSNlpPASPCAQVEVPWPV--VVASPFRTAKEALLVANGTPRGGSASV 379
Cdd:cd07125  365 RAHTELMRGEAWLIAPA-PLDDGNGyFVAPGIIEI--VGIFDLTTEVFGPIlhVIRFKAEDLDEAIEDINATGYGLTLGI 441
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*..
gi 223972653 380 WSERLGQALELGYGLQVGTVWINahglRD------PSVPTGGCKESG 420
Cdd:cd07125  442 HSRDEREIEYWRERVEAGNLYIN----RNitgaivGRQPFGGWGLSG 484
ALDH_SSADH1_GabD1 cd07100
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ...
515-714 9.64e-08

Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde dehydrogenase 1 (SSADH1, GabD1, EC=1.2.1.16) catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde (SSA) to succinate. SSADH activity in Mycobacterium tuberculosis (Mtb) is encoded by both gabD1 (Rv0234c) and gabD2 (Rv1731). The Mtb GabD1 SSADH1 reportedly is an enzyme of the gamma-aminobutyrate shunt, which forms a functional link between two TCA half-cycles by converting alpha-ketoglutarate to succinate.


Pssm-ID: 143418 [Multi-domain]  Cd Length: 429  Bit Score: 55.16  E-value: 9.64e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 515 IRGAVEAAHQAFPGWAGQSPgaraallwalaaaLERRK--STLASRLERQGAEL------------KAAEAEVELSARRL 580
Cdd:cd07100    1 IEAALDRAHAAFLAWRKTSF-------------AERAAllRKLADLLRERKDELarlitlemgkpiAEARAEVEKCAWIC 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 581 R--AWGARVQAQGHTLQVAGLRGPVlrLREPLGVLAVVCPdeW--PLLAFVSLLAPALAYGNTVVMVPSAACPLLAL--- 653
Cdd:cd07100   68 RyyAENAEAFLADEPIETDAGKAYV--RYEPLGVVLGIMP--WnfPFWQVFRFAAPNLMAGNTVLLKHASNVPGCALaie 143
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 223972653 654 EVCQDMAtvFPAGLANVVTGDRDHLTRCLAlHQDVQAMWYFGSAQGSQFVEWASAGNLKPV 714
Cdd:cd07100  144 ELFREAG--FPEGVFQNLLIDSDQVEAIIA-DPRVRGVTLTGSERAGRAVAAEAGKNLKKS 201
PRK11905 PRK11905
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
505-654 1.32e-07

bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed


Pssm-ID: 237018 [Multi-domain]  Cd Length: 1208  Bit Score: 55.26  E-value: 1.32e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653  505 GYVAEGGAKDIRGAVEAAHQAFPGWAGQSPgaraallwalaaalERRKSTL---ASRLERQGAELKA------------A 569
Cdd:PRK11905  582 GTVTEASAEDVERALAAAQAAFPEWSATPA--------------AERAAILeraADLMEAHMPELFAlavreagktlanA 647
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653  570 EAEVELSARRLRAWGARVQaqgHTLQVAGlrgpvlrlREPLGVlaVVCPDEW--PLLAFVSLLAPALAYGNTVVMVPSAA 647
Cdd:PRK11905  648 IAEVREAVDFLRYYAAQAR---RLLNGPG--------HKPLGP--VVCISPWnfPLAIFTGQIAAALVAGNTVLAKPAEQ 714

                  ....*..
gi 223972653  648 CPLLALE 654
Cdd:PRK11905  715 TPLIAAR 721
ALDH_F3-13-14_CALDH-like cd07087
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ...
557-714 2.19e-07

ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other related proteins; ALDH subfamily which includes NAD(P)+-dependent, aldehyde dehydrogenase, family 3 member A1 and B1 (ALDH3A1, ALDH3B1, EC=1.2.1.5) and fatty aldehyde dehydrogenase, family 3 member A2 (ALDH3A2, EC=1.2.1.3), and also plant ALDH family members ALDH3F1, ALDH3H1, and ALDH3I1, fungal ALDH14 (YMR110C) and the protozoan family 13 member (ALDH13), as well as coniferyl aldehyde dehydrogenases (CALDH, EC=1.2.1.68), and other similar sequences, such as the Pseudomonas putida benzaldehyde dehydrogenase I that is involved in the metabolism of mandelate.


Pssm-ID: 143406 [Multi-domain]  Cd Length: 426  Bit Score: 54.07  E-value: 2.19e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 557 SRLERQGAELKAAEAEVELSARRLRAWGARVQAQgHTLQVAGLRGPVLRlrEPLGVLAVVCPDEWPLLAFVSLLAPALAY 636
Cdd:cd07087   51 PPAEAYLTEIAVVLGEIDHALKHLKKWMKPRRVS-VPLLLQPAKAYVIP--EPLGVVLIIGPWNYPLQLALAPLIGAIAA 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 637 GNTVVMVPSAACP----LLALEVcqdmATVFPAGLANVVTGDRDHLTRCLALHQDVqaMWYFGSAQGSQFVEWASAGNLK 712
Cdd:cd07087  128 GNTVVLKPSELAPatsaLLAKLI----PKYFDPEAVAVVEGGVEVATALLAEPFDH--IFFTGSPAVGKIVMEAAAKHLT 201

                 ..
gi 223972653 713 PV 714
Cdd:cd07087  202 PV 203
PRK13252 PRK13252
betaine aldehyde dehydrogenase; Provisional
475-714 3.46e-07

betaine aldehyde dehydrogenase; Provisional


Pssm-ID: 183918  Cd Length: 488  Bit Score: 53.35  E-value: 3.46e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 475 PPYGLFVGGRFQAPGARSSRP-IRDSSGNLHGYVAEGGAKDIRGAVEAAHQAFPGWAGQSPgaraallwalaaaLER--- 550
Cdd:PRK13252   5 PLQSLYIDGAYVEATSGETFEvINPATGEVLATVQAATPADVEAAVASAKQGQKIWAAMTA-------------MERsri 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 551 -RKStlASRLERQGAELKAAE-------------AEVELSARRLRAWGARVQA-QGHTLQvagLRGP--VLRLREPLGVL 613
Cdd:PRK13252  72 lRRA--VDILRERNDELAALEtldtgkpiqetsvVDIVTGADVLEYYAGLAPAlEGEQIP---LRGGsfVYTRREPLGVC 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 614 AVVCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLALEVcqdmATVF-----PAGLANVVTGDRDhLTRCLALHQDV 688
Cdd:PRK13252 147 AGIGAWNYPIQIACWKSAPALAAGNAMIFKPSEVTPLTALKL----AEIYteaglPDGVFNVVQGDGR-VGAWLTEHPDI 221
                        250       260
                 ....*....|....*....|....*.
gi 223972653 689 QAMWYFGSAQGSQFVEWASAGNLKPV 714
Cdd:PRK13252 222 AKVSFTGGVPTGKKVMAAAAASLKEV 247
ALDH_F21_RNP123 cd07147
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ...
500-676 5.74e-07

Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) was first described in the moss Tortula ruralis and is believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and ALDH21A1 expression represents a unique stress tolerance mechanism. So far, of plants, only the bryophyte sequence has been observed, but similar protein sequences from bacteria and archaea are also present in this CD.


Pssm-ID: 143465 [Multi-domain]  Cd Length: 452  Bit Score: 52.63  E-value: 5.74e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 500 SGNLHGYVAEGGAKDIRGAVEAAHQAFPGWAGQSPGARAALLWALAAALERRKSTLASRLERQ-GAELKAAEAEV----- 573
Cdd:cd07147    8 TGEVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEaGKPIKDARGEVaraid 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 574 --ELSARRLRAWGARVQAQGHTLQVAGLRGPVLRLrePLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLL 651
Cdd:cd07147   88 tfRIAAEEATRIYGEVLPLDISARGEGRQGLVRRF--PIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPASRTPLS 165
                        170       180
                 ....*....|....*....|....*.
gi 223972653 652 ALEVCQDMA-TVFPAGLANVVTGDRD 676
Cdd:cd07147  166 ALILGEVLAeTGLPKGAFSVLPCSRD 191
ALDH_AlkH-like cd07134
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ...
549-684 7.66e-07

Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name P12693, EC=1.2.1.3) of the alkBFGHJKL operon that allows Pseudomonas putida to metabolize alkanes and the aldehyde dehydrogenase AldX of Bacillus subtilis (locus P46329, EC=1.2.1.3), and similar sequences, are present in this CD.


Pssm-ID: 143452 [Multi-domain]  Cd Length: 433  Bit Score: 52.23  E-value: 7.66e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 549 ERRKSTLASRLER----------QGAELKAA--------EAEVELS------------ARRLRAWgARVQAQGHTLQVAG 598
Cdd:cd07134   13 ALRASTAAERIAKlkrlkkailaRREEIIAAlaadfrkpAAEVDLTeilpvlseinhaIKHLKKW-MKPKRVRTPLLLFG 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 599 LRGPVLRlrEPLGVLAVVCPDEWPL-LAFvSLLAPALAYGNTVVMVPSAACPLLALEVCQDMATVFPAGLANVVTGDRDH 677
Cdd:cd07134   92 TKSKIRY--EPKGVCLIISPWNYPFnLAF-GPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREAFDEDEVAVFEGDAEV 168

                 ....*..
gi 223972653 678 LTRCLAL 684
Cdd:cd07134  169 AQALLEL 175
PTZ00381 PTZ00381
aldehyde dehydrogenase family protein; Provisional
557-714 1.18e-06

aldehyde dehydrogenase family protein; Provisional


Pssm-ID: 240392  Cd Length: 493  Bit Score: 51.95  E-value: 1.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 557 SRLERQGAELKAAEAEVELSARRLRAWGARVQAQGHTLQvagLRGPVLRLREPLGVLAVVCPDEWPLLAFVSLLAPALAY 636
Cdd:PTZ00381  60 HPFETKMTEVLLTVAEIEHLLKHLDEYLKPEKVDTVGVF---GPGKSYIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAA 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 637 GNTVVMVPSAacplLALEVCQDMATVFPAGLAN----VVTGDRDHLTRCLALHQDVqaMWYFGSAQGSQFVEWASAGNLK 712
Cdd:PTZ00381 137 GNTVVLKPSE----LSPHTSKLMAKLLTKYLDPsyvrVIEGGVEVTTELLKEPFDH--IFFTGSPRVGKLVMQAAAENLT 210

                 ..
gi 223972653 713 PV 714
Cdd:PTZ00381 211 PC 212
ALDH_F7_AASADH-like cd07086
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ...
480-698 1.34e-06

NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH subfamily which includes the NAD+-dependent, alpha-aminoadipic semialdehyde dehydrogenase (AASADH, EC=1.2.1.31), also known as Antiquitin-1, ALDH7A1, ALDH7B or delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH), and other similar sequences, such as the uncharacterized aldehyde dehydrogenase of Candidatus kuenenia AldH (locus CAJ73105).


Pssm-ID: 143405 [Multi-domain]  Cd Length: 478  Bit Score: 51.41  E-value: 1.34e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 480 FVGGRFQAPGAR---SSRPIRDSSgnlHGYVAEGGAKDIRGAVEAAHQAFPGWAGQSPGARAALLWALAAALERRKSTLA 556
Cdd:cd07086    2 VIGGEWVGSGGEtftSRNPANGEP---IARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 557 SRLERQ-GAELKAAEAEVE-----------LSaRRLrawgarvqaQGHTlqVAGLRgPVLRLRE---PLGVLAVVCPDEW 621
Cdd:cd07086   79 RLVSLEmGKILPEGLGEVQemidicdyavgLS-RML---------YGLT--IPSER-PGHRLMEqwnPLGVVGVITAFNF 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 622 PLLAFVSLLAPALAYGNTVVMVPSAACPLLALEVCQDMATV-----FPAGLANVVTGDRDhLTRCLALHQDVQAMWYFGS 696
Cdd:cd07086  146 PVAVPGWNAAIALVCGNTVVWKPSETTPLTAIAVTKILAEVlekngLPPGVVNLVTGGGD-GGELLVHDPRVPLVSFTGS 224

                 ..
gi 223972653 697 AQ 698
Cdd:cd07086  225 TE 226
PLN00412 PLN00412
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
609-699 4.69e-06

NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional


Pssm-ID: 215110 [Multi-domain]  Cd Length: 496  Bit Score: 49.75  E-value: 4.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 609 PLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVP---SAACPLLALEvCQDMATvFPAGLANVVTGDRDHLTRCLALH 685
Cdd:PLN00412 158 PLGVVLAIPPFNYPVNLAVSKIAPALIAGNAVVLKPptqGAVAALHMVH-CFHLAG-FPKGLISCVTGKGSEIGDFLTMH 235
                         90
                 ....*....|....
gi 223972653 686 QDVQAMWYFGSAQG 699
Cdd:PLN00412 236 PGVNCISFTGGDTG 249
ALDH_SGSD_AstD cd07095
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ...
87-258 1.05e-05

N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate 5-semialdehyde dehydrogenase or succinylglutamic semialdehyde dehydrogenase (SGSD, E. coli AstD, EC=1.2.1.71) involved in L-arginine degradation via the arginine succinyltransferase (AST) pathway and catalyzes the NAD+-dependent reduction of succinylglutamate semialdehyde into succinylglutamate.


Pssm-ID: 143414 [Multi-domain]  Cd Length: 431  Bit Score: 48.42  E-value: 1.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653  87 RMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTLESLVTGRAVREVRdGDVQ-----LAQQLLHYHAiQASTQEEALA 161
Cdd:cd07095   10 RAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQ-TEVAamagkIDISIKAYHE-RTGERATPMA 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 162 GWE------PMGVIGLILPPTFSFLEMMWRICPALAVGCTVValVPPASPAPL---LLAQLAGELGPFPGILNVLSGPAS 232
Cdd:cd07095   88 QGRavlrhrPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVV--FKPSELTPAvaeLMVELWEEAGLPPGVLNLVQGGRE 165
                        170       180
                 ....*....|....*....|....*.
gi 223972653 233 LVPILASQPGIRKVAFCGAPEGGLRL 258
Cdd:cd07095  166 TGEALAAHEGIDGLLFTGSAATGLLL 191
PRK11904 PRK11904
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
490-657 1.27e-05

bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;


Pssm-ID: 237017 [Multi-domain]  Cd Length: 1038  Bit Score: 48.66  E-value: 1.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653  490 ARSSRPIRDSSGNLH------------GYVAEGGAKDIRGAVEAAHQAFPGWAgQSPGaraallwalaaalERRKSTL-- 555
Cdd:PRK11904  550 QWQAGPIINGEGEARpvvspadrrrvvGEVAFADAEQVEQALAAARAAFPAWS-RTPV-------------EERAAILer 615
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653  556 -ASRLERQGAELKA------------AEAEVELSARRLRAWGArvQAQGHTLQVAGLRGPV-----LRLrEPLGVLAVVC 617
Cdd:PRK11904  616 aADLLEANRAELIAlcvreagktlqdAIAEVREAVDFCRYYAA--QARRLFGAPEKLPGPTgesneLRL-HGRGVFVCIS 692
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 223972653  618 PDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLALEVCQ 657
Cdd:PRK11904  693 PWNFPLAIFLGQVAAALAAGNTVIAKPAEQTPLIAAEAVK 732
ALDH_KGSADH-like cd07084
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ...
605-701 2.15e-05

ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12-like; ALDH subfamily which includes the NAD(P)+-dependent, alpha-ketoglutaric semialdehyde dehydrogenases (KGSADH, EC 1.2.1.26); plant delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12 ), ALDH family 12; the N-terminal domain of the MaoC (monoamine oxidase C) dehydratase regulatory protein; and orthologs of MaoC, PaaZ and PaaN, which are putative ring-opening enzymes of the aerobic phenylacetic acid catabolic pathway.


Pssm-ID: 143403 [Multi-domain]  Cd Length: 442  Bit Score: 47.62  E-value: 2.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 605 RLREPLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLALEVCQDM--ATVFPAGLANVVTGDRdHLTRCL 682
Cdd:cd07084   96 GYRWPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLhyAGLLPPEDVTLINGDG-KTMQAL 174
                         90
                 ....*....|....*....
gi 223972653 683 ALHQDVQAMWYFGSAQGSQ 701
Cdd:cd07084  175 LLHPNPKMVLFTGSSRVAE 193
gabD2 PRK09407
succinic semialdehyde dehydrogenase; Reviewed
487-674 5.14e-05

succinic semialdehyde dehydrogenase; Reviewed


Pssm-ID: 236501 [Multi-domain]  Cd Length: 524  Bit Score: 46.41  E-value: 5.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 487 APGARSSRPIRDS-SGNLHGYVAEGGAKDIRGAVEAAHQAFPGWAGQSPGaraallwalaaalERRKSTLASR---LERQ 562
Cdd:PRK09407  27 DGAAGPTREVTAPfTGEPLATVPVSTAADVEAAFARARAAQRAWAATPVR-------------ERAAVLLRFHdlvLENR 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 563 GAELKAAEAEvelsarrlrAWGARVQAQGHTLQVAGL-----------------RG--PVL----RLREPLGVLAVVCPD 619
Cdd:PRK09407  94 EELLDLVQLE---------TGKARRHAFEEVLDVALTaryyarrapkllaprrrAGalPVLtkttELRQPKGVVGVISPW 164
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 223972653 620 EWPLLAFVSLLAPALAYGNTVVMVPSAACPLLALeVCQDMATV--FPAGLANVVTGD 674
Cdd:PRK09407 165 NYPLTLAVSDAIPALLAGNAVVLKPDSQTPLTAL-AAVELLYEagLPRDLWQVVTGP 220
ALDH_AlkH-like cd07134
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ...
249-425 5.54e-05

Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name P12693, EC=1.2.1.3) of the alkBFGHJKL operon that allows Pseudomonas putida to metabolize alkanes and the aldehyde dehydrogenase AldX of Bacillus subtilis (locus P46329, EC=1.2.1.3), and similar sequences, are present in this CD.


Pssm-ID: 143452 [Multi-domain]  Cd Length: 433  Bit Score: 46.45  E-value: 5.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 249 CGAPEgglRLLIQESVWDEAMRRLQERMGRLRSGRGLDGAVDMGAR--GAAACDLVQRFVREAQSQGAQVFQAGDVPSER 326
Cdd:cd07134  240 CIAPD---YVFVHESVKDAFVEHLKAEIEKFYGKDAARKASPDLARivNDRHFDRLKGLLDDAVAKGAKVEFGGQFDAAQ 316
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 327 PFYPPTLVSNLPPASPCAQVEVPWPVVVASPFRTAKEALLVANGTPRGGSASVWSERLGQALELGYGLQVGTVWIN---A 403
Cdd:cd07134  317 RYIAPTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVNdvvL 396
                        170       180
                 ....*....|....*....|...
gi 223972653 404 HGLrDPSVPTGGCKESGC-SWHG 425
Cdd:cd07134  397 HFL-NPNLPFGGVNNSGIgSYHG 418
astD PRK09457
succinylglutamic semialdehyde dehydrogenase; Reviewed
41-258 9.32e-05

succinylglutamic semialdehyde dehydrogenase; Reviewed


Pssm-ID: 181873  Cd Length: 487  Bit Score: 45.72  E-value: 9.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653  41 GHYVNGKWL--KPEHRNSVpcqDPITGENLASCLQAQAEDVAAAVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRL 118
Cdd:PRK09457   2 TLWINGDWIagQGEAFESR---NPVSGEVLWQGNDATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 119 LWTLESLVTGRAVREVRD------GDVQLAQQllHYHAIQASTQEEALAG-----WEPMGVIGLILPPTFSFLEMMWRIC 187
Cdd:PRK09457  79 LAEVIARETGKPLWEAATevtamiNKIAISIQ--AYHERTGEKRSEMADGaavlrHRPHGVVAVFGPYNFPGHLPNGHIV 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 223972653 188 PALAVGCTVValVPPASPAPL---LLAQLAGELGPFPGILNVLSGPASLVPILASQPGIRKVAFCGAPEGGLRL 258
Cdd:PRK09457 157 PALLAGNTVV--FKPSELTPWvaeLTVKLWQQAGLPAGVLNLVQGGRETGKALAAHPDIDGLLFTGSANTGYLL 228
ALDH_YwdH-P39616 cd07136
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ...
607-714 1.70e-04

Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH aldehyde dehydrogenase (locus P39616) most closely related to the ALDHs and fatty ALDHs of families 3 and 14, and similar sequences, are included in this CD.


Pssm-ID: 143454 [Multi-domain]  Cd Length: 449  Bit Score: 44.80  E-value: 1.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 607 REPLGVLAVVCPDEWPL-LAFVSLLApALAYGNTVVMVPSAACPLLAlEVCQDM-ATVFPAGLANVVTGDRD---HLtrc 681
Cdd:cd07136   98 YEPYGVVLIIAPWNYPFqLALAPLIG-AIAAGNTAVLKPSELTPNTS-KVIAKIiEETFDEEYVAVVEGGVEenqEL--- 172
                         90       100       110
                 ....*....|....*....|....*....|...
gi 223972653 682 laLHQDVQAMWYFGSAQGSQFVEWASAGNLKPV 714
Cdd:cd07136  173 --LDQKFDYIFFTGSVRVGKIVMEAAAKHLTPV 203
ALDH_CALDH_CalB cd07133
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ...
557-676 2.26e-04

Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) of Pseudomonas sp. strain HR199 (CalB) which catalyzes the NAD+-dependent oxidation of coniferyl aldehyde to ferulic acid, and similar sequences, are present in this CD.


Pssm-ID: 143451 [Multi-domain]  Cd Length: 434  Bit Score: 44.40  E-value: 2.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 557 SRLERQGAELKAAEAEVELSARRLRAWgARVQAQGHTLQVAGLRGPVLRlrEPLGVLAVVCPDEWPL-LAFVSLLApALA 635
Cdd:cd07133   52 SRHETLLAEILPSIAGIKHARKHLKKW-MKPSRRHVGLLFLPAKAEVEY--QPLGVVGIIVPWNYPLyLALGPLIA-ALA 127
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 223972653 636 YGNTVVMVPSAACPLLAlEVCQDM-ATVFPAGLANVVTGDRD 676
Cdd:cd07133  128 AGNRVMIKPSEFTPRTS-ALLAELlAEYFDEDEVAVVTGGAD 168
putA PRK11809
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ...
93-253 2.58e-04

trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed


Pssm-ID: 236989 [Multi-domain]  Cd Length: 1318  Bit Score: 44.58  E-value: 2.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653   93 WSAHPGVVRAQHLTRLAEVIQKH-QRLLWTL--ESLVT-GRAVREVRDgdvqlAQQLLHYHAIQAStQEEALAGWEPMGV 168
Cdd:PRK11809  698 WFATPPAERAAILERAADLMEAQmQTLMGLLvrEAGKTfSNAIAEVRE-----AVDFLRYYAGQVR-DDFDNDTHRPLGP 771
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653  169 IGLILPPTFSFLEMMWRICPALAVGCTVVAlvPPASPAPLLLAQ---LAGELGPFPGILNVLSGPASLV-PILASQPGIR 244
Cdd:PRK11809  772 VVCISPWNFPLAIFTGQVAAALAAGNSVLA--KPAEQTPLIAAQavrILLEAGVPAGVVQLLPGRGETVgAALVADARVR 849

                  ....*....
gi 223972653  245 KVAFCGAPE 253
Cdd:PRK11809  850 GVMFTGSTE 858
PutA2 COG4230
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
505-652 2.85e-04

Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];


Pssm-ID: 443374 [Multi-domain]  Cd Length: 1156  Bit Score: 44.54  E-value: 2.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653  505 GYVAEGGAKDIRGAVEAAHQAFPGWAGQSPgaraallwalaaalERRKSTL---ASRLERQGAELKA------------A 569
Cdd:COG4230   585 GTVVEATAADVEAALAAAQAAFPAWSATPV--------------EERAAILeraADLLEAHRAELMAllvreagktlpdA 650
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653  570 EAEVelsarR-----LRAWGARVQAQGHTLQVaglrgpvlrlREPLGVlaVVCPDEW--PLLAFVSLLAPALAYGNTVVM 642
Cdd:COG4230   651 IAEV-----ReavdfCRYYAAQARRLFAAPTV----------LRGRGV--FVCISPWnfPLAIFTGQVAAALAAGNTVLA 713
                         170
                  ....*....|
gi 223972653  643 VPSAACPLLA 652
Cdd:COG4230   714 KPAEQTPLIA 723
PRK11904 PRK11904
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
89-250 2.99e-04

bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;


Pssm-ID: 237017 [Multi-domain]  Cd Length: 1038  Bit Score: 44.42  E-value: 2.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653   89 AFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTLESLVTGR----AVREVRDgdvqlAQQLLHYHAIQAS---TQEEALA 161
Cdd:PRK11904  597 AFPAWSRTPVEERAAILERAADLLEANRAELIALCVREAGKtlqdAIAEVRE-----AVDFCRYYAAQARrlfGAPEKLP 671
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653  162 G---------WEPMGVIGLILPPTFS---FLEmmwRICPALAVGCTVVAlvPPASPAPL---LLAQLAGELGPFPGILNV 226
Cdd:PRK11904  672 GptgesnelrLHGRGVFVCISPWNFPlaiFLG---QVAAALAAGNTVIA--KPAEQTPLiaaEAVKLLHEAGIPKDVLQL 746
                         170       180
                  ....*....|....*....|....*
gi 223972653  227 LSGP-ASLVPILASQPGIRKVAFCG 250
Cdd:PRK11904  747 LPGDgATVGAALTADPRIAGVAFTG 771
ALDH_F14-YMR110C cd07135
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ...
607-714 3.60e-04

Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde dehydrogenase family 14 (ALDH14), isolated mainly from the mitochondrial outer membrane of Saccharomyces cerevisiae (YMR110C) and most closely related to the plant and animal ALDHs and fatty ALDHs family 3 members, and similar fungal sequences, are present in this CD.


Pssm-ID: 143453 [Multi-domain]  Cd Length: 436  Bit Score: 43.75  E-value: 3.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 607 REPLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLALEVCQDMATVFPAGLANVVTGDRDHLTRCLALHQ 686
Cdd:cd07135  106 KEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAELVPKYLDPDAFQVVQGGVPETTALLEQKF 185
                         90       100
                 ....*....|....*....|....*...
gi 223972653 687 DvqAMWYFGSAQGSQFVEWASAGNLKPV 714
Cdd:cd07135  186 D--KIFYTGSGRVGRIIAEAAAKHLTPV 211
ALDH_P5CDH cd07083
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ...
505-713 3.91e-04

ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH subfamily of the NAD+-dependent, delta(1)-pyrroline-5-carboxylate dehydrogenases (P5CDH, EC=1.5.1.12). The proline catabolic enzymes, proline dehydrogenase and P5CDH catalyze the two-step oxidation of proline to glutamate. P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA). These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes. Monofunctional enzyme sequences such as those seen in the Bacillus RocA P5CDH are also present in this subfamily as well as the human ALDH4A1 P5CDH and the Drosophila Aldh17 P5CDH.


Pssm-ID: 143402 [Multi-domain]  Cd Length: 500  Bit Score: 43.72  E-value: 3.91e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 505 GYVAEGGAKDIRGAVEAAHQAFPGWAGQSPGARAALLWALAAALERRKSTLASRLERQ-GAELKAAEAEVELSARRLRAW 583
Cdd:cd07083   47 GTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRRRELIATLTYEvGKNWVEAIDDVAEAIDFIRYY 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 584 GarVQAQGHTLQVAGLRGPVLRLRE----PLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLALEVCQDM 659
Cdd:cd07083  127 A--RAALRLRYPAVEVVPYPGEDNEsfyvGLGAGVVISPWNFPVAIFTGMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIF 204
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 223972653 660 ATV-FPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGSAQGSQFVeWASAGNLKP 713
Cdd:cd07083  205 HEAgFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSLETGKKI-YEAAARLAP 258
ALDH_SSADH2_GabD2 cd07101
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ...
606-674 7.73e-04

Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde dehydrogenase 2 (SSADH2) and similar proteins are in this CD. SSADH1 (GabD1, EC=1.2.1.16) catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde to succinate. SSADH activity in Mycobacterium tuberculosis is encoded by both gabD1 (Rv0234c) and gabD2 (Rv1731), however ,the Vmax of GabD1 was shown to be much higher than that of GabD2, and GabD2 (SSADH2) is likely to serve physiologically as a dehydrogenase for a different aldehyde(s).


Pssm-ID: 143419 [Multi-domain]  Cd Length: 454  Bit Score: 42.68  E-value: 7.73e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 606 LREPLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLALEVCQDM-ATVFPAGLANVVTGD 674
Cdd:cd07101  115 NRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTALTALWAVELLiEAGLPRDLWQVVTGP 184
putA PRK11809
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ...
505-652 7.80e-04

trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed


Pssm-ID: 236989 [Multi-domain]  Cd Length: 1318  Bit Score: 43.04  E-value: 7.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653  505 GYVAEGGAKDIRGAVEAAHQAFPGWAGQSPGARAALLWALAAALERRKSTLASRLERQ-GAELKAAEAEVELSARRLRAW 583
Cdd:PRK11809  674 GYVREATPAEVEQALESAVNAAPIWFATPPAERAAILERAADLMEAQMQTLMGLLVREaGKTFSNAIAEVREAVDFLRYY 753
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 223972653  584 GARVQAQ----GHtlqvaglrgpvlrlrEPLGVlaVVCPDEW--PLLAFVSLLAPALAYGNTVVMVPSAACPLLA 652
Cdd:PRK11809  754 AGQVRDDfdndTH---------------RPLGP--VVCISPWnfPLAIFTGQVAAALAAGNSVLAKPAEQTPLIA 811
ALDH_F3FHI cd07137
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ...
608-721 8.33e-04

Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde dehydrogenase family members 3F1, 3H1, and 3I1 (ALDH3F1, ALDH3H1, and ALDH3I1), and similar plant sequences, are in this CD. In Arabidopsis thaliana, stress-regulated expression of ALDH3I1 was observed in leaves and osmotic stress expression of ALDH3H1 was observed in root tissue, whereas, ALDH3F1 expression was not stress responsive. Functional analysis of ALDH3I1 suggest it may be involved in a detoxification pathway in plants that limits aldehyde accumulation and oxidative stress.


Pssm-ID: 143455 [Multi-domain]  Cd Length: 432  Bit Score: 42.40  E-value: 8.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 608 EPLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLAlevcQDMATVFPAGLAN----VVTGDRDHLTrcLA 683
Cdd:cd07137  100 EPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATS----ALLAKLIPEYLDTkaikVIEGGVPETT--AL 173
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 223972653 684 LHQDVQAMWYFGSAQGSQFVEWASAGNLKPVWASRG--CP 721
Cdd:cd07137  174 LEQKWDKIFFTGSPRVGRIIMAAAAKHLTPVTLELGgkCP 213
ALDH_F3AB cd07132
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ...
607-714 8.84e-04

Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, aldehyde dehydrogenase, family 3 members A1 and B1 (ALDH3A1, ALDH3B1, EC=1.2.1.5) and fatty aldehyde dehydrogenase, family 3 member A2 (ALDH3A2, EC=1.2.1.3), and similar sequences are included in this CD. Human ALDH3A1 is a homodimer with a critical role in cellular defense against oxidative stress; it catalyzes the oxidation of various cellular membrane lipid-derived aldehydes. Corneal crystalline ALDH3A1 protects the cornea and underlying lens against UV-induced oxidative stress. Human ALDH3A2, a microsomal homodimer, catalyzes the oxidation of long-chain aliphatic aldehydes to fatty acids. Human ALDH3B1 is highly expressed in the kidney and liver and catalyzes the oxidation of various medium- and long-chain saturated and unsaturated aliphatic aldehydes.


Pssm-ID: 143450 [Multi-domain]  Cd Length: 443  Bit Score: 42.59  E-value: 8.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 607 REPLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLAlevcQDMATVFPAGLAN----VVTGDRDHLTRCL 682
Cdd:cd07132   98 KEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATA----KLLAELIPKYLDKecypVVLGGVEETTELL 173
                         90       100       110
                 ....*....|....*....|....*....|..
gi 223972653 683 ALHQDVqaMWYFGSAQGSQFVEWASAGNLKPV 714
Cdd:cd07132  174 KQRFDY--IFYTGSTSVGKIVMQAAAKHLTPV 203
ALDH_KGSADH-like cd07084
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ...
87-258 3.03e-03

ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12-like; ALDH subfamily which includes the NAD(P)+-dependent, alpha-ketoglutaric semialdehyde dehydrogenases (KGSADH, EC 1.2.1.26); plant delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12 ), ALDH family 12; the N-terminal domain of the MaoC (monoamine oxidase C) dehydratase regulatory protein; and orthologs of MaoC, PaaZ and PaaN, which are putative ring-opening enzymes of the aerobic phenylacetic acid catabolic pathway.


Pssm-ID: 143403 [Multi-domain]  Cd Length: 442  Bit Score: 40.68  E-value: 3.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653  87 RMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTLESLVTGRAVREVRDGDVQLAQqLLHYHAIQASTQEEALAGWE-- 164
Cdd:cd07084    9 DISTKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFAENICGDQVQ-LRARAFVIYSYRIPHEPGNHlg 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 165 ------------PMGVIGLILPPTFSFLEMMWRICPALAVGCTVvaLVPPASPAPLLLAQ---LAGELGPFP-GILNVLS 228
Cdd:cd07084   88 qglkqqshgyrwPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPV--IVKPHTAVSIVMQImvrLLHYAGLLPpEDVTLIN 165
                        170       180       190
                 ....*....|....*....|....*....|
gi 223972653 229 GPASLVPILASQPGIRKVAFCGAPEGGLRL 258
Cdd:cd07084  166 GDGKTMQALLLHPNPKMVLFTGSSRVAEKL 195
ALDH_KGSADH cd07129
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ...
515-699 3.60e-03

Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) Dehydrogenase (KGSADH, EC 1.2.1.26) catalyzes the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. This CD contains such sequences as those seen in Azospirillum brasilense, KGSADH-II (D-glucarate/D-galactarate-inducible) and KGSADH-III (hydroxy-L-proline-inducible). Both show similar high substrate specificity for KGSA and different coenzyme specificity; KGSADH-II is NAD+-dependent and KGSADH-III is NADP+-dependent. Also included in this CD is the NADP(+)-dependent aldehyde dehydrogenase from Vibrio harveyi which catalyzes the oxidation of long-chain aliphatic aldehydes to acids.


Pssm-ID: 143447 [Multi-domain]  Cd Length: 454  Bit Score: 40.60  E-value: 3.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 515 IRGAVEAAHQAFPGWAGQSPgaraallwalaaalERRKS---TLASRLERQGAELKA-AEAEVELSARRL-----RAWG- 584
Cdd:cd07129    1 VDAAAAAAAAAFESYRALSP--------------ARRAAfleAIADEIEALGDELVArAHAETGLPEARLqgelgRTTGq 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 585 ----ARVQAQGHTLQV---------AGLRGPVLRLRE-PLGVLAVVCPDEWPlLAFvSLL----APALAYGNTVVMVPSA 646
Cdd:cd07129   67 lrlfADLVREGSWLDAridpadpdrQPLPRPDLRRMLvPLGPVAVFGASNFP-LAF-SVAggdtASALAAGCPVVVKAHP 144
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 223972653 647 ACP----LLALEVCQDM-ATVFPAGLANVVTGDRDHLTRCLALHQDVQAMWYFGSAQG 699
Cdd:cd07129  145 AHPgtseLVARAIRAALrATGLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRG 202
ALDH_RL0313 cd07148
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ...
573-667 3.64e-03

Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; Uncharacterized aldehyde dehydrogenase (locus RL0313) with sequence similarity to the moss Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123) believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and similar sequences are included in this CD.


Pssm-ID: 143466 [Multi-domain]  Cd Length: 455  Bit Score: 40.48  E-value: 3.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653 573 VELSARRLRAWGARVQAQGHTLQVAGLRGpvLRLREPLGVLAVVCPDEWPLLAFVSLLAPALAYGNTVVMVPSAACPLLA 652
Cdd:cd07148   90 VELAADELGQLGGREIPMGLTPASAGRIA--FTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPALATPLSC 167
                         90
                 ....*....|....*
gi 223972653 653 LEVcqdMATVFPAGL 667
Cdd:cd07148  168 LAF---VDLLHEAGL 179
PRK11905 PRK11905
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
82-278 4.03e-03

bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed


Pssm-ID: 237018 [Multi-domain]  Cd Length: 1208  Bit Score: 40.62  E-value: 4.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653   82 AVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTLESLVTGR----AVREVRDgdvqlAQQLLHYHAIQAsTQE 157
Cdd:PRK11905  595 ALAAAQAAFPEWSATPAAERAAILERAADLMEAHMPELFALAVREAGKtlanAIAEVRE-----AVDFLRYYAAQA-RRL 668
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653  158 EALAGWEPMGVIGLILPPTFSFLEMMWRICPALAVGCTVVAlvPPASPAPlLLAQLAGEL----GPFPGILNVLSGPASL 233
Cdd:PRK11905  669 LNGPGHKPLGPVVCISPWNFPLAIFTGQIAAALVAGNTVLA--KPAEQTP-LIAARAVRLlheaGVPKDALQLLPGDGRT 745
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 223972653  234 V-PILASQPGIRKVAFCGAPEGGlrLLIQesvwdeamRRLQERMGR 278
Cdd:PRK11905  746 VgAALVADPRIAGVMFTGSTEVA--RLIQ--------RTLAKRSGP 781
PutA2 COG4230
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
82-250 5.35e-03

Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];


Pssm-ID: 443374 [Multi-domain]  Cd Length: 1156  Bit Score: 40.31  E-value: 5.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653   82 AVEAARMAFKGWSAHPGVVRAQHLTRLAEVIQKHQRLLWTLESLVTGR----AVREVRDgdvqlAQQLLHYHAIQASTQE 157
Cdd:COG4230   598 ALAAAQAAFPAWSATPVEERAAILERAADLLEAHRAELMALLVREAGKtlpdAIAEVRE-----AVDFCRYYAAQARRLF 672
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972653  158 EALAGWEPMGVIGLILPptfsflemmW---------RICPALAVGCTVVAlvPPASPAPlLLAQLAGEL----GPFPGIL 224
Cdd:COG4230   673 AAPTVLRGRGVFVCISP---------WnfplaiftgQVAAALAAGNTVLA--KPAEQTP-LIAARAVRLlheaGVPADVL 740
                         170       180
                  ....*....|....*....|....*..
gi 223972653  225 NVLSGPASLV-PILASQPGIRKVAFCG 250
Cdd:COG4230   741 QLLPGDGETVgAALVADPRIAGVAFTG 767
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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