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Conserved domains on  [gi|2219515474|dbj|BDH76614|]
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1-pyrroline-5-carboxylate dehydrogenase [Actinomyces naeslundii]

Protein Classification

bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase( domain architecture ID 10483053)

bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase catalyzes the two-step oxidation of proline to glutamate

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 ...
482-965 8.57e-164

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 cd07125:

Pssm-ID: 448367 [Multi-domain]  Cd Length: 518  Bit Score: 496.33  E-value: 8.57e-164
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  482 DAGVPEETgtLEERSRRLFVSEPDSDPALAANRQwARDIAAAIPDSTRGlaEVEAGAARLATNAEVDTLVTATAEAAGVW 561
Cdd:cd07125     11 DLEVPLEA--LADALKAFDEKEWEAIPIINGEET-ETGEGAPVIDPADH--ERTIGEVSLADAEDVDAALAIAAAAFAGW 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  562 QSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDPEVSEAIDFCHHYAESSLLLHDGGHMVG-------ARF 634
Cdd:cd07125     86 SATPVEERAEILEKAADLLEANRGELIALAAAEAGKTLADADAEVREAIDFCRYYAAQARELFSDPELPGptgelngLEL 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  635 IPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELVRAFHDAGIPEDLVVLAPLEDGDVSRHLVTHK 714
Cdd:cd07125    166 HGRGVFVCISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHP 245
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  715 DVDRVVLTGSYDTARLFRSWK-----PDMHLLGETSGKNAIIVTPSADPDIAVRDAVYSAFAHAGQKCSASSLLVLVSSA 789
Cdd:cd07125    246 RIDGVIFTGSTETAKLINRALaerdgPILPLIAETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEI 325
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  790 gtSERIARQLVDATASLRVRLPLSLDSQMGPVVVPDDEKAVRGLTTLGSGEHWVLKPRYLGDG---LWTPGIRAGVvpGS 866
Cdd:cd07125    326 --AERFIEMLKGAMASLKVGDPWDLSTDVGPLIDKPAGKLLRAHTELMRGEAWLIAPAPLDDGngyFVAPGIIEIV--GI 401
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  867 EFHLTEYFAPVIGVMR--VDTLQEAIEAVNAVDYGLTSGIQTLDATELAIWLEGVQAGNLYVNRGITGAIVRRQPFGGWK 944
Cdd:cd07125    402 FDLTTEVFGPILHVIRfkAEDLDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYINRNITGAIVGRQPFGGWG 481
                          490       500
                   ....*....|....*....|.
gi 2219515474  945 RSAIGSttKAGGPSYLLGLGE 965
Cdd:cd07125    482 LSGTGP--KAGGPNYLLRFGN 500
Pro_dh pfam01619
Proline dehydrogenase;
148-436 4.44e-79

Proline dehydrogenase;


:

Pssm-ID: 426348 [Multi-domain]  Cd Length: 296  Bit Score: 261.66  E-value: 4.44e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  148 ALARLRKGGNRLNVNLLGEAVLGEKEAARRLAEVSRLVT----------REDVDYVSVKVSAVTGPHNPWGFDEVVAHGV 217
Cdd:pfam01619    4 TIEKLRKQGYRFSLDMLGEAALTEADADRYLDAYLRAIDalgkaagpwpLGPRPGISVKLSALHPRYEPLERERVMAELL 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  218 QALLPLYRLARDNGTFLNLDMEDYKDLDLTIAVFTAILDQEDMYGYE-AGIVLQAYLPDSLGAMQRLQEWASRRvaagGS 296
Cdd:pfam01619   84 ERLRPLCRLAKELGVRLNIDAEEADRLDLTLDLFERLLAEPELRGWNgVGITLQAYLKDALAVLDWLLELARRR----GR 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  297 RIKVRVVKGANLSMEKVDAEIHGWELTTWPSKQATDTNYKRMLSWAMtpERTRAIRLGVAGQNLFDIAFAYELRAARGVE 376
Cdd:pfam01619  160 PLGVRLVKGAYWDSEIKRAQQGGWPYPVFTRKEATDANYEACARFLL--ENHDRIYPQFATHNARSVAAALALAEELGIP 237
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2219515474  377 -DGVEFEMLSGMATGLQEVVRRDTGHLLLYVPVVDPHEFdvaISYLVRRLEENAAPENFMS 436
Cdd:pfam01619  238 pRRFEFQQLYGMGDNLSFALVAAGYRVRKYAPVGPHEEL---LAYLVRRLLENTANSSFVR 295
 
Name Accession Description Interval E-value
ALDH_PutA-P5CDH cd07125
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ...
482-965 8.57e-164

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: 496.33  E-value: 8.57e-164
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  482 DAGVPEETgtLEERSRRLFVSEPDSDPALAANRQwARDIAAAIPDSTRGlaEVEAGAARLATNAEVDTLVTATAEAAGVW 561
Cdd:cd07125     11 DLEVPLEA--LADALKAFDEKEWEAIPIINGEET-ETGEGAPVIDPADH--ERTIGEVSLADAEDVDAALAIAAAAFAGW 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  562 QSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDPEVSEAIDFCHHYAESSLLLHDGGHMVG-------ARF 634
Cdd:cd07125     86 SATPVEERAEILEKAADLLEANRGELIALAAAEAGKTLADADAEVREAIDFCRYYAAQARELFSDPELPGptgelngLEL 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  635 IPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELVRAFHDAGIPEDLVVLAPLEDGDVSRHLVTHK 714
Cdd:cd07125    166 HGRGVFVCISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHP 245
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  715 DVDRVVLTGSYDTARLFRSWK-----PDMHLLGETSGKNAIIVTPSADPDIAVRDAVYSAFAHAGQKCSASSLLVLVSSA 789
Cdd:cd07125    246 RIDGVIFTGSTETAKLINRALaerdgPILPLIAETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEI 325
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  790 gtSERIARQLVDATASLRVRLPLSLDSQMGPVVVPDDEKAVRGLTTLGSGEHWVLKPRYLGDG---LWTPGIRAGVvpGS 866
Cdd:cd07125    326 --AERFIEMLKGAMASLKVGDPWDLSTDVGPLIDKPAGKLLRAHTELMRGEAWLIAPAPLDDGngyFVAPGIIEIV--GI 401
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  867 EFHLTEYFAPVIGVMR--VDTLQEAIEAVNAVDYGLTSGIQTLDATELAIWLEGVQAGNLYVNRGITGAIVRRQPFGGWK 944
Cdd:cd07125    402 FDLTTEVFGPILHVIRfkAEDLDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYINRNITGAIVGRQPFGGWG 481
                          490       500
                   ....*....|....*....|.
gi 2219515474  945 RSAIGSttKAGGPSYLLGLGE 965
Cdd:cd07125    482 LSGTGP--KAGGPNYLLRFGN 500
PutA COG0506
Proline dehydrogenase [Amino acid transport and metabolism]; Proline dehydrogenase is part of ...
27-982 9.83e-129

Proline dehydrogenase [Amino acid transport and metabolism]; Proline dehydrogenase is part of the Pathway/BioSystem: Proline degradation


Pssm-ID: 440272 [Multi-domain]  Cd Length: 975  Bit Score: 419.07  E-value: 9.83e-129
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474   27 ALGEKAVARARRWADESASEPVPRSAKLLSRILADPDGLTFTTRFVDDVVRPTDLDVAGDALKRLSSGRTDFLPPALAGA 106
Cdd:COG0506      8 ALRARAVALARRLVEAIRAAPEGGVEALLREYLLSPQEGVALMCLAEALLRLPDNATADRLIRDKLAKSPSFLVNASTWG 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  107 MGLGSAAsRLAPRTVTAVARRVFREIVGDLVVDATDKSLGPALARLRKGGNRLNVNLLGEAVLGEKEAARRLAEVSRLVT 186
Cdd:COG0506     88 LMLTLVG-RLGEPVIRPAVRRAMRRMARRFVAGETIEEALKAARKLRAKGYRVSLDLLGEAVLTEAEAERYLDAYLEALE 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  187 R-----EDVDYVSVKVSAVTGPHNPWGFDEVVAHGVQALLPLYRLARDNGTFLNLDMEDYKDLDLTIAVFTAILDQEDMY 261
Cdd:COG0506    167 AigaagVDRPGVSVKLSALGPRYSPAQRERVVEELLERLRPLARAAREAGIFVTIDMEEYDRLDLTLDVFERLLADPELA 246
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  262 GY-EAGIVLQAYLPDSLGAMQRLQEWASRrvaaGGSRIKVRVVKGANLSMEKVDAEIHGWELTTWPSKQATDTNYKRMLS 340
Cdd:COG0506    247 GWpGVGIVLQAYLKRAEADLDRLAALARR----GGRRIRVRLVKGAYWDPEIVRAQVHGWPYPVFTRKADTDANYLRCAR 322
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  341 WAMtpERTRAIRLGVAGQNLFDIAFAYELRAARGV-EDGVEFEMLSGMATGLQE-VVRRDTGHLLLYVPVVDPHEFDVAI 418
Cdd:COG0506    323 KLL--EAGDAIYPQFATHNARTIAAALALAGERGRpPDRFEFQMLYGMGEDLQRaLAAVDGGRLLLYCPVVAPVGGDAAL 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  419 SYLVRRLEENAAPENFMSGVFDLAADEVVFGRERDRFLAALSDLDPDAPVPEPNRRQDRLAERDAGVPEETGTLEERSRR 498
Cdd:COG0506    401 AYLLRRLLENNSFLNFFVADFDDDEDLLEFPREPPRFLAALAAPTPPPPPPLRRQRRRRRRARGGALAAALAAAAAAAAL 480
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  499 LFVSEPdSDPALAANRQWARDIAAAIPDSTRGLAEVEAGAARLATNAEVDTLVTATAEAAGVWQSLDPAERAAALHRVGD 578
Cdd:COG0506    481 AAAAAA-AAALAAAAAGAAAAAAAAAVAVVPAAAAAVVAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 559
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  579 VLAARRAELIEVAGSEAGKTIDQSDPEVSEAIDFCHHYAEsslllhDGGHMVGARFIPVDVTVVASPWNFPLAIPTGGVA 658
Cdd:COG0506    560 AEAAEAALLLAAAAAEAAAAAALAAAAAEAAAAAAAAAAA------AAAARAAAPPPPPPGGLVALLPLGPLAAAAAAAA 633
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  659 AALAAGSAVILKPAPPARRCAAELVRAFHDAGIPEDLVVLAPLEDGDVSRHLVTHKDVDRVVLTGSYDTARLFRswkpdm 738
Cdd:COG0506    634 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAALAALLLLLGGAGGGVLVLGAGGGAGGAAALTLAAAAAA------ 707
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  739 hllgeTSGKNAIIVTPSADPDIAVRDAVYSAFAHAGQKCSASSLLVLVSSAGTSERIARQLVDATASLRVRLPLSLDSQM 818
Cdd:COG0506    708 -----ATAATAAAAAAAAALAAAAAAAAAAAAAAAGGAAAAAAAAAAAAAVAAVAASAAASASASASLLSLLALLLLDAD 782
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  819 GPVVVPDDEKAVRGLTTLGSGEHWVLKPR--YLGDGLWTPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAV 896
Cdd:COG0506    783 LVILLLALAAAAAALLVGGPGAAALALGIveDAAAAALLLALAALELGEEELLLPGGGPLVPGLLTAPLLVALILGLIVL 862
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  897 DYGLTSGIQTLDATELAIWLEGVQAGNLYVNRGITGAIVRRQPFGGWKRSAIGSTTKAGGPSYLLGLGEVEPARGQGGKV 976
Cdd:COG0506    863 VLLEIVLVLALVLALALDLAALIGLGLTGGLLGGGGGIVGRRGGGGGAGGRVGGGGGGGGGGGGGGGGGGGGGGGGGGGG 942

                   ....*.
gi 2219515474  977 EQGTAA 982
Cdd:COG0506    943 GGGGGG 948
Aldedh pfam00171
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ...
540-960 5.56e-85

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: 284.04  E-value: 5.56e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  540 RLATNAEVDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDPEVSEAIDFCHHYAES 619
Cdd:pfam00171   24 PAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKPLAEARGEVDRAIDVLRYYAGL 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  620 SLLLH------DGGHMVGARFIPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELVRAFHDAGIPE 693
Cdd:pfam00171  104 ARRLDgetlpsDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPSELTPLTALLLAELFEEAGLPA 183
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  694 DLVVLAPLEDGDVSRHLVTHKDVDRVVLTGSYDTARLF-----RSWKPdmhLLGETSGKNAIIVTPSADPDIAVRDAVYS 768
Cdd:pfam00171  184 GVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIaeaaaQNLKR---VTLELGGKNPLIVLEDADLDAAVEAAVFG 260
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  769 AFAHAGQKCSASSLLVLVSSAgtSERIARQLVDATASLRVRLPLSLDSQMGPVVVPDDEKAVRGLTTLGSGEHWVLK--- 845
Cdd:pfam00171  261 AFGNAGQVCTATSRLLVHESI--YDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQLERVLKYVEDAKEEGAKLLtgg 338
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  846 PRYLGDGLW-TPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLDATELAIWLEGVQAGNL 924
Cdd:pfam00171  339 EAGLDNGYFvEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGVFTSDLERALRVARRLEAGMV 418
                          410       420       430
                   ....*....|....*....|....*....|....*.
gi 2219515474  925 YVNRGITGAIVRRqPFGGWKRSAIGsttKAGGPSYL 960
Cdd:pfam00171  419 WINDYTTGDADGL-PFGGFKQSGFG---REGGPYGL 450
Pro_dh pfam01619
Proline dehydrogenase;
148-436 4.44e-79

Proline dehydrogenase;


Pssm-ID: 426348 [Multi-domain]  Cd Length: 296  Bit Score: 261.66  E-value: 4.44e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  148 ALARLRKGGNRLNVNLLGEAVLGEKEAARRLAEVSRLVT----------REDVDYVSVKVSAVTGPHNPWGFDEVVAHGV 217
Cdd:pfam01619    4 TIEKLRKQGYRFSLDMLGEAALTEADADRYLDAYLRAIDalgkaagpwpLGPRPGISVKLSALHPRYEPLERERVMAELL 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  218 QALLPLYRLARDNGTFLNLDMEDYKDLDLTIAVFTAILDQEDMYGYE-AGIVLQAYLPDSLGAMQRLQEWASRRvaagGS 296
Cdd:pfam01619   84 ERLRPLCRLAKELGVRLNIDAEEADRLDLTLDLFERLLAEPELRGWNgVGITLQAYLKDALAVLDWLLELARRR----GR 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  297 RIKVRVVKGANLSMEKVDAEIHGWELTTWPSKQATDTNYKRMLSWAMtpERTRAIRLGVAGQNLFDIAFAYELRAARGVE 376
Cdd:pfam01619  160 PLGVRLVKGAYWDSEIKRAQQGGWPYPVFTRKEATDANYEACARFLL--ENHDRIYPQFATHNARSVAAALALAEELGIP 237
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2219515474  377 -DGVEFEMLSGMATGLQEVVRRDTGHLLLYVPVVDPHEFdvaISYLVRRLEENAAPENFMS 436
Cdd:pfam01619  238 pRRFEFQQLYGMGDNLSFALVAAGYRVRKYAPVGPHEEL---LAYLVRRLLENTANSSFVR 295
PRK11904 PRK11904
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
148-961 9.18e-77

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


Pssm-ID: 237017 [Multi-domain]  Cd Length: 1038  Bit Score: 275.15  E-value: 9.18e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  148 ALAR---LRKGGNRLNVNLLGEAVLGEKEAARRLAEVSRL---VTREDVDY-------VSVKVSAVTGPHNPWGFDEVVA 214
Cdd:PRK11904   189 ALKRarsARNKGYRYSFDMLGEAALTAADAERYFKAYARAieaIGRAAGGAdlparpgISIKLSALHPRYEAAQRERVLA 268
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  215 HGVQALLPLYRLARDNGTFLNLDMEDYKDLDLTIAVFTAILDQEDMYGYEA-GIVLQAYLPDSLGAMQRLQEWASRRvaa 293
Cdd:PRK11904   269 ELVPRVLELARLAKEANIGLTIDAEEADRLELSLDLFEALFRDPSLKGWGGfGLAVQAYQKRALPVLDWLADLARRQ--- 345
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  294 gGSRIKVRVVKGANLSMEKVDAEIHGweLTTWP---SKQATDTNY----KRMLSwamtpERTrAIRLGVAGQNLFDIAFA 366
Cdd:PRK11904   346 -GRRIPVRLVKGAYWDSEIKRAQELG--LPGYPvftRKAATDVSYlacaRKLLS-----ARG-AIYPQFATHNAHTVAAI 416
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  367 YELRAargvEDGVEFEMLSGMATGLQEVVRRDTG-HLLLYVPVvDPHEfDVaISYLVRRLEENAAPENFMSGVFD----- 440
Cdd:PRK11904   417 LEMAG----HRGFEFQRLHGMGEALYDALLDAPGiPCRIYAPV-GSHK-DL-LPYLVRRLLENGANSSFVHRLVDpdvpi 489
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  441 --LAADEVvfgrerdRFLAALSDL-DPDAPVPE----PNRRQDRlaerdaGVpeETGtlEERSRRLFVSEPDSdpalAAN 513
Cdd:PRK11904   490 eeLVADPV-------EKLRSFETLpNPKIPLPRdifgPERKNSK------GL--NLN--DRSELEPLAAAIAA----FLE 548
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  514 RQWArdiAAAIPDSTRGLAEV--------EAGAARLATNAEVDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRA 585
Cdd:PRK11904   549 KQWQ---AGPIINGEGEARPVvspadrrrVVGEVAFADAEQVEQALAAARAAFPAWSRTPVEERAAILERAADLLEANRA 625
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  586 ELIEVAGSEAGKTIDQSDPEVSEAIDFCHHYA-ESSLLLHDGGHMVG-------ARFIPVDVTVVASPWNFPLAIPTGGV 657
Cdd:PRK11904   626 ELIALCVREAGKTLQDAIAEVREAVDFCRYYAaQARRLFGAPEKLPGptgesneLRLHGRGVFVCISPWNFPLAIFLGQV 705
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  658 AAALAAGSAVILKPAPPARRCAAELVRAFHDAGIPEDLVVLAPLEDGDVSRHLVTHKDVDRVVLTGSYDTARLF-RS--W 734
Cdd:PRK11904   706 AAALAAGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVGAALTADPRIAGVAFTGSTETARIInRTlaA 785
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  735 K--PDMHLLGETSGKNAIIVTPSADPDIAVRDAVYSAFAHAGQKCSAssLLVLVSSAGTSERIARQLVDATASLRVRLPL 812
Cdd:PRK11904   786 RdgPIVPLIAETGGQNAMIVDSTALPEQVVDDVVTSAFRSAGQRCSA--LRVLFVQEDIADRVIEMLKGAMAELKVGDPR 863
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  813 SLDSQMGPVVvpdDEKAVRGLTT---LGSGEHWVLKPRYLGDGlwtpGIRAGVVPGSEFHLT-------EYFAPVIGVMR 882
Cdd:PRK11904   864 LLSTDVGPVI---DAEAKANLDAhieRMKREARLLAQLPLPAG----TENGHFVAPTAFEIDsisqlerEVFGPILHVIR 936
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  883 VDT--LQEAIEAVNAVDYGLTSGIQT-LDATELAIwLEGVQAGNLYVNRGITGAIVRRQPFGGWKRSaiGSTTKAGGPSY 959
Cdd:PRK11904   937 YKAsdLDKVIDAINATGYGLTLGIHSrIEETADRI-ADRVRVGNVYVNRNQIGAVVGVQPFGGQGLS--GTGPKAGGPHY 1013

                   ..
gi 2219515474  960 LL 961
Cdd:PRK11904  1014 LL 1015
D1pyr5carbox2 TIGR01237
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ...
537-961 7.92e-76

delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of two in the degradation of proline to glutamate. This model represents one of several related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. Members of this branch may be associated with proline dehydrogenase (the other enzyme of the pathway from proline to glutamate) but have not been demonstrated experimentally. The branches are not as closely related to each other as some distinct aldehyde dehydrogenases are to some; separate models were built to let each model describe a set of equivalogs. [Energy metabolism, Amino acids and amines]


Pssm-ID: 200087 [Multi-domain]  Cd Length: 511  Bit Score: 260.57  E-value: 7.92e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  537 GAARLATNAEVDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDPEVSEAIDFCHHY 616
Cdd:TIGR01237   61 GTVSKASQEHAEHALQAAAKAFEAWKKTDPEERAAILFKAAAIVRRRRHEFSALLVKEVGKPWNEADAEVAEAIDFMEYY 140
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  617 AESSLLLHDG-------GHMVGARFIPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELVRAFHDA 689
Cdd:TIGR01237  141 ARQMIELAKGkpvnsreGETNQYVYTPTGVTVVISPWNFPFAIMVGMTVAPIVTGNCVVLKPAEAAPVIAAKFVEILEEA 220
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  690 GIPEDLVVLAPLEDGDVSRHLVTHKDVDRVVLTGSY--------DTARLFRSWKPDMHLLGETSGKNAIIVTPSADPDIA 761
Cdd:TIGR01237  221 GLPKGVVQFVPGSGSEVGDYLVDHPKTSLITFTGSRevgtrifeRAAKVQPGQKHLKRVIAEMGGKDTVIVDEDADIELA 300
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  762 VRDAVYSAFAHAGQKCSASSLLVLVSSagTSERIARQLVDATASLRVRLPLSLDSQMGPVVVPDDEKAVRGLTTLGSGEH 841
Cdd:TIGR01237  301 AQSAFTSAFGFAGQKCSAGSRAVVHEK--VYDEVVERFVEITESLKVGPPDSADVYVGPVIDQKSFNKIMEYIEIGKAEG 378
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  842 WVL--------KPRYLGdglwtPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLDATELA 913
Cdd:TIGR01237  379 RLVsggcgddsKGYFIG-----PTIFADVDRKARLAQEEIFGPVVAFIRASDFDEALEIANNTEYGLTGGVISNNRDHIN 453
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*...
gi 2219515474  914 IWLEGVQAGNLYVNRGITGAIVRRQPFGGWKRSAIGSttKAGGPSYLL 961
Cdd:TIGR01237  454 RAKAEFEVGNLYFNRNITGAIVGYQPFGGFKMSGTDS--KAGGPDYLA 499
PLN02681 PLN02681
proline dehydrogenase
270-428 2.54e-07

proline dehydrogenase


Pssm-ID: 215366 [Multi-domain]  Cd Length: 455  Bit Score: 54.71  E-value: 2.54e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  270 QAYLPDslgAMQRLQEwASRRVAAGGSRIKVRVVKGANLSMEKVDAEIHGWELTTWPSKQATDTNYKRMLSWAMTPERTR 349
Cdd:PLN02681   274 QAYLKD---ARERLRL-DLERSEREGVPLGAKLVRGAYLSLERRLAASLGVPSPVHDTIQDTHACYNRCAEFLLEKASNG 349
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  350 AIRLGVAGQNLFDIAFAYELRAARGVE---DGVEFEMLSGMATGLQEVVRRDTGHLLLYVPVvdpHEFDVAISYLVRRLE 426
Cdd:PLN02681   350 DGEVMLATHNVESGELAAAKMNELGLHkgdPRVQFAQLLGMSDNLSFGLGNAGFRVSKYLPY---GPVEEVIPYLLRRAE 426

                   ..
gi 2219515474  427 EN 428
Cdd:PLN02681   427 EN 428
 
Name Accession Description Interval E-value
ALDH_PutA-P5CDH cd07125
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ...
482-965 8.57e-164

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: 496.33  E-value: 8.57e-164
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  482 DAGVPEETgtLEERSRRLFVSEPDSDPALAANRQwARDIAAAIPDSTRGlaEVEAGAARLATNAEVDTLVTATAEAAGVW 561
Cdd:cd07125     11 DLEVPLEA--LADALKAFDEKEWEAIPIINGEET-ETGEGAPVIDPADH--ERTIGEVSLADAEDVDAALAIAAAAFAGW 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  562 QSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDPEVSEAIDFCHHYAESSLLLHDGGHMVG-------ARF 634
Cdd:cd07125     86 SATPVEERAEILEKAADLLEANRGELIALAAAEAGKTLADADAEVREAIDFCRYYAAQARELFSDPELPGptgelngLEL 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  635 IPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELVRAFHDAGIPEDLVVLAPLEDGDVSRHLVTHK 714
Cdd:cd07125    166 HGRGVFVCISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHP 245
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  715 DVDRVVLTGSYDTARLFRSWK-----PDMHLLGETSGKNAIIVTPSADPDIAVRDAVYSAFAHAGQKCSASSLLVLVSSA 789
Cdd:cd07125    246 RIDGVIFTGSTETAKLINRALaerdgPILPLIAETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEI 325
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  790 gtSERIARQLVDATASLRVRLPLSLDSQMGPVVVPDDEKAVRGLTTLGSGEHWVLKPRYLGDG---LWTPGIRAGVvpGS 866
Cdd:cd07125    326 --AERFIEMLKGAMASLKVGDPWDLSTDVGPLIDKPAGKLLRAHTELMRGEAWLIAPAPLDDGngyFVAPGIIEIV--GI 401
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  867 EFHLTEYFAPVIGVMR--VDTLQEAIEAVNAVDYGLTSGIQTLDATELAIWLEGVQAGNLYVNRGITGAIVRRQPFGGWK 944
Cdd:cd07125    402 FDLTTEVFGPILHVIRfkAEDLDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYINRNITGAIVGRQPFGGWG 481
                          490       500
                   ....*....|....*....|.
gi 2219515474  945 RSAIGSttKAGGPSYLLGLGE 965
Cdd:cd07125    482 LSGTGP--KAGGPNYLLRFGN 500
PutA COG0506
Proline dehydrogenase [Amino acid transport and metabolism]; Proline dehydrogenase is part of ...
27-982 9.83e-129

Proline dehydrogenase [Amino acid transport and metabolism]; Proline dehydrogenase is part of the Pathway/BioSystem: Proline degradation


Pssm-ID: 440272 [Multi-domain]  Cd Length: 975  Bit Score: 419.07  E-value: 9.83e-129
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474   27 ALGEKAVARARRWADESASEPVPRSAKLLSRILADPDGLTFTTRFVDDVVRPTDLDVAGDALKRLSSGRTDFLPPALAGA 106
Cdd:COG0506      8 ALRARAVALARRLVEAIRAAPEGGVEALLREYLLSPQEGVALMCLAEALLRLPDNATADRLIRDKLAKSPSFLVNASTWG 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  107 MGLGSAAsRLAPRTVTAVARRVFREIVGDLVVDATDKSLGPALARLRKGGNRLNVNLLGEAVLGEKEAARRLAEVSRLVT 186
Cdd:COG0506     88 LMLTLVG-RLGEPVIRPAVRRAMRRMARRFVAGETIEEALKAARKLRAKGYRVSLDLLGEAVLTEAEAERYLDAYLEALE 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  187 R-----EDVDYVSVKVSAVTGPHNPWGFDEVVAHGVQALLPLYRLARDNGTFLNLDMEDYKDLDLTIAVFTAILDQEDMY 261
Cdd:COG0506    167 AigaagVDRPGVSVKLSALGPRYSPAQRERVVEELLERLRPLARAAREAGIFVTIDMEEYDRLDLTLDVFERLLADPELA 246
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  262 GY-EAGIVLQAYLPDSLGAMQRLQEWASRrvaaGGSRIKVRVVKGANLSMEKVDAEIHGWELTTWPSKQATDTNYKRMLS 340
Cdd:COG0506    247 GWpGVGIVLQAYLKRAEADLDRLAALARR----GGRRIRVRLVKGAYWDPEIVRAQVHGWPYPVFTRKADTDANYLRCAR 322
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  341 WAMtpERTRAIRLGVAGQNLFDIAFAYELRAARGV-EDGVEFEMLSGMATGLQE-VVRRDTGHLLLYVPVVDPHEFDVAI 418
Cdd:COG0506    323 KLL--EAGDAIYPQFATHNARTIAAALALAGERGRpPDRFEFQMLYGMGEDLQRaLAAVDGGRLLLYCPVVAPVGGDAAL 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  419 SYLVRRLEENAAPENFMSGVFDLAADEVVFGRERDRFLAALSDLDPDAPVPEPNRRQDRLAERDAGVPEETGTLEERSRR 498
Cdd:COG0506    401 AYLLRRLLENNSFLNFFVADFDDDEDLLEFPREPPRFLAALAAPTPPPPPPLRRQRRRRRRARGGALAAALAAAAAAAAL 480
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  499 LFVSEPdSDPALAANRQWARDIAAAIPDSTRGLAEVEAGAARLATNAEVDTLVTATAEAAGVWQSLDPAERAAALHRVGD 578
Cdd:COG0506    481 AAAAAA-AAALAAAAAGAAAAAAAAAVAVVPAAAAAVVAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 559
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  579 VLAARRAELIEVAGSEAGKTIDQSDPEVSEAIDFCHHYAEsslllhDGGHMVGARFIPVDVTVVASPWNFPLAIPTGGVA 658
Cdd:COG0506    560 AEAAEAALLLAAAAAEAAAAAALAAAAAEAAAAAAAAAAA------AAAARAAAPPPPPPGGLVALLPLGPLAAAAAAAA 633
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  659 AALAAGSAVILKPAPPARRCAAELVRAFHDAGIPEDLVVLAPLEDGDVSRHLVTHKDVDRVVLTGSYDTARLFRswkpdm 738
Cdd:COG0506    634 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAALAALLLLLGGAGGGVLVLGAGGGAGGAAALTLAAAAAA------ 707
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  739 hllgeTSGKNAIIVTPSADPDIAVRDAVYSAFAHAGQKCSASSLLVLVSSAGTSERIARQLVDATASLRVRLPLSLDSQM 818
Cdd:COG0506    708 -----ATAATAAAAAAAAALAAAAAAAAAAAAAAAGGAAAAAAAAAAAAAVAAVAASAAASASASASLLSLLALLLLDAD 782
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  819 GPVVVPDDEKAVRGLTTLGSGEHWVLKPR--YLGDGLWTPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAV 896
Cdd:COG0506    783 LVILLLALAAAAAALLVGGPGAAALALGIveDAAAAALLLALAALELGEEELLLPGGGPLVPGLLTAPLLVALILGLIVL 862
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  897 DYGLTSGIQTLDATELAIWLEGVQAGNLYVNRGITGAIVRRQPFGGWKRSAIGSTTKAGGPSYLLGLGEVEPARGQGGKV 976
Cdd:COG0506    863 VLLEIVLVLALVLALALDLAALIGLGLTGGLLGGGGGIVGRRGGGGGAGGRVGGGGGGGGGGGGGGGGGGGGGGGGGGGG 942

                   ....*.
gi 2219515474  977 EQGTAA 982
Cdd:COG0506    943 GGGGGG 948
AdhE COG1012
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ...
537-949 3.41e-91

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: 302.05  E-value: 3.41e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  537 GAARLATNAEVDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDPEVSEAIDFCHHY 616
Cdd:COG1012     35 ARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERREELAALLTLETGKPLAEARGEVDRAADFLRYY 114
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  617 AESSLLLH-------DGGHMVGARFIPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELVRAFHDA 689
Cdd:COG1012    115 AGEARRLYgetipsdAPGTRAYVRREPLGVVGAITPWNFPLALAAWKLAPALAAGNTVVLKPAEQTPLSALLLAELLEEA 194
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  690 GIPEDLVVLAPLEDGDVSRHLVTHKDVDRVVLTGSYDTARLFRSWKPD--MHLLGETSGKNAIIVTPSADPDIAVRDAVY 767
Cdd:COG1012    195 GLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAAEnlKRVTLELGGKNPAIVLDDADLDAAVEAAVR 274
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  768 SAFAHAGQKCSASSLLVLVSSAgtSERIARQLVDATASLRVRLPLSLDSQMGPVVVPDDEKAVRGLTTLG--SGEHWVLK 845
Cdd:COG1012    275 GAFGNAGQRCTAASRLLVHESI--YDEFVERLVAAAKALKVGDPLDPGTDMGPLISEAQLERVLAYIEDAvaEGAELLTG 352
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  846 PRYLGDG---LWTPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLDATELAIWLEGVQAG 922
Cdd:COG1012    353 GRRPDGEggyFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAIALANDTEYGLAASVFTRDLARARRVARRLEAG 432
                          410       420
                   ....*....|....*....|....*..
gi 2219515474  923 NLYVNRGITGAIVrRQPFGGWKRSAIG 949
Cdd:COG1012    433 MVWINDGTTGAVP-QAPFGGVKQSGIG 458
ALDH_PutA-P5CDH-RocA cd07124
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ...
537-961 1.09e-88

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: 296.06  E-value: 1.09e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  537 GAARLATNAEVDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDPEVSEAIDFCHHY 616
Cdd:cd07124     61 GTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRRFELAAWMVLEVGKNWAEADADVAEAIDFLEYY 140
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  617 AESSLLLHDGGH-MV-----GARFIPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELVRAFHDAG 690
Cdd:cd07124    141 AREMLRLRGFPVeMVpgednRYVYRPLGVGAVISPWNFPLAILAGMTTAALVTGNTVVLKPAEDTPVIAAKLVEILEEAG 220
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  691 IPEDLVVLAPLEDGDVSRHLVTHKDVDRVVLTGSYDT--------ARLFRSWKPDMHLLGETSGKNAIIVTPSADPDIAV 762
Cdd:cd07124    221 LPPGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGSREVglriyeraAKVQPGQKWLKRVIAEMGGKNAIIVDEDADLDEAA 300
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  763 RDAVYSAFAHAGQKCSASSLLVLVSSAgtSERIARQLVDATASLRVRLPLSLDSQMGPVVVPDDEKAVRGLTTLGSGEHW 842
Cdd:cd07124    301 EGIVRSAFGFQGQKCSACSRVIVHESV--YDEFLERLVERTKALKVGDPEDPEVYMGPVIDKGARDRIRRYIEIGKSEGR 378
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  843 VLKPRyLGDGLWT------PGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLDATELAIWL 916
Cdd:cd07124    379 LLLGG-EVLELAAegyfvqPTIFADVPPDHRLAQEEIFGPVLAVIKAKDFDEALEIANDTEYGLTGGVFSRSPEHLERAR 457
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*
gi 2219515474  917 EGVQAGNLYVNRGITGAIVRRQPFGGWKRSaiGSTTKAGGPSYLL 961
Cdd:cd07124    458 REFEVGNLYANRKITGALVGRQPFGGFKMS--GTGSKAGGPDYLL 500
Aldedh pfam00171
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ...
540-960 5.56e-85

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: 284.04  E-value: 5.56e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  540 RLATNAEVDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDPEVSEAIDFCHHYAES 619
Cdd:pfam00171   24 PAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKPLAEARGEVDRAIDVLRYYAGL 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  620 SLLLH------DGGHMVGARFIPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELVRAFHDAGIPE 693
Cdd:pfam00171  104 ARRLDgetlpsDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPSELTPLTALLLAELFEEAGLPA 183
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  694 DLVVLAPLEDGDVSRHLVTHKDVDRVVLTGSYDTARLF-----RSWKPdmhLLGETSGKNAIIVTPSADPDIAVRDAVYS 768
Cdd:pfam00171  184 GVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIaeaaaQNLKR---VTLELGGKNPLIVLEDADLDAAVEAAVFG 260
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  769 AFAHAGQKCSASSLLVLVSSAgtSERIARQLVDATASLRVRLPLSLDSQMGPVVVPDDEKAVRGLTTLGSGEHWVLK--- 845
Cdd:pfam00171  261 AFGNAGQVCTATSRLLVHESI--YDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQLERVLKYVEDAKEEGAKLLtgg 338
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  846 PRYLGDGLW-TPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLDATELAIWLEGVQAGNL 924
Cdd:pfam00171  339 EAGLDNGYFvEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGVFTSDLERALRVARRLEAGMV 418
                          410       420       430
                   ....*....|....*....|....*....|....*.
gi 2219515474  925 YVNRGITGAIVRRqPFGGWKRSAIGsttKAGGPSYL 960
Cdd:pfam00171  419 WINDYTTGDADGL-PFGGFKQSGFG---REGGPYGL 450
Pro_dh pfam01619
Proline dehydrogenase;
148-436 4.44e-79

Proline dehydrogenase;


Pssm-ID: 426348 [Multi-domain]  Cd Length: 296  Bit Score: 261.66  E-value: 4.44e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  148 ALARLRKGGNRLNVNLLGEAVLGEKEAARRLAEVSRLVT----------REDVDYVSVKVSAVTGPHNPWGFDEVVAHGV 217
Cdd:pfam01619    4 TIEKLRKQGYRFSLDMLGEAALTEADADRYLDAYLRAIDalgkaagpwpLGPRPGISVKLSALHPRYEPLERERVMAELL 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  218 QALLPLYRLARDNGTFLNLDMEDYKDLDLTIAVFTAILDQEDMYGYE-AGIVLQAYLPDSLGAMQRLQEWASRRvaagGS 296
Cdd:pfam01619   84 ERLRPLCRLAKELGVRLNIDAEEADRLDLTLDLFERLLAEPELRGWNgVGITLQAYLKDALAVLDWLLELARRR----GR 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  297 RIKVRVVKGANLSMEKVDAEIHGWELTTWPSKQATDTNYKRMLSWAMtpERTRAIRLGVAGQNLFDIAFAYELRAARGVE 376
Cdd:pfam01619  160 PLGVRLVKGAYWDSEIKRAQQGGWPYPVFTRKEATDANYEACARFLL--ENHDRIYPQFATHNARSVAAALALAEELGIP 237
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2219515474  377 -DGVEFEMLSGMATGLQEVVRRDTGHLLLYVPVVDPHEFdvaISYLVRRLEENAAPENFMS 436
Cdd:pfam01619  238 pRRFEFQQLYGMGDNLSFALVAAGYRVRKYAPVGPHEEL---LAYLVRRLLENTANSSFVR 295
PRK11904 PRK11904
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
148-961 9.18e-77

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


Pssm-ID: 237017 [Multi-domain]  Cd Length: 1038  Bit Score: 275.15  E-value: 9.18e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  148 ALAR---LRKGGNRLNVNLLGEAVLGEKEAARRLAEVSRL---VTREDVDY-------VSVKVSAVTGPHNPWGFDEVVA 214
Cdd:PRK11904   189 ALKRarsARNKGYRYSFDMLGEAALTAADAERYFKAYARAieaIGRAAGGAdlparpgISIKLSALHPRYEAAQRERVLA 268
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  215 HGVQALLPLYRLARDNGTFLNLDMEDYKDLDLTIAVFTAILDQEDMYGYEA-GIVLQAYLPDSLGAMQRLQEWASRRvaa 293
Cdd:PRK11904   269 ELVPRVLELARLAKEANIGLTIDAEEADRLELSLDLFEALFRDPSLKGWGGfGLAVQAYQKRALPVLDWLADLARRQ--- 345
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  294 gGSRIKVRVVKGANLSMEKVDAEIHGweLTTWP---SKQATDTNY----KRMLSwamtpERTrAIRLGVAGQNLFDIAFA 366
Cdd:PRK11904   346 -GRRIPVRLVKGAYWDSEIKRAQELG--LPGYPvftRKAATDVSYlacaRKLLS-----ARG-AIYPQFATHNAHTVAAI 416
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  367 YELRAargvEDGVEFEMLSGMATGLQEVVRRDTG-HLLLYVPVvDPHEfDVaISYLVRRLEENAAPENFMSGVFD----- 440
Cdd:PRK11904   417 LEMAG----HRGFEFQRLHGMGEALYDALLDAPGiPCRIYAPV-GSHK-DL-LPYLVRRLLENGANSSFVHRLVDpdvpi 489
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  441 --LAADEVvfgrerdRFLAALSDL-DPDAPVPE----PNRRQDRlaerdaGVpeETGtlEERSRRLFVSEPDSdpalAAN 513
Cdd:PRK11904   490 eeLVADPV-------EKLRSFETLpNPKIPLPRdifgPERKNSK------GL--NLN--DRSELEPLAAAIAA----FLE 548
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  514 RQWArdiAAAIPDSTRGLAEV--------EAGAARLATNAEVDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRA 585
Cdd:PRK11904   549 KQWQ---AGPIINGEGEARPVvspadrrrVVGEVAFADAEQVEQALAAARAAFPAWSRTPVEERAAILERAADLLEANRA 625
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  586 ELIEVAGSEAGKTIDQSDPEVSEAIDFCHHYA-ESSLLLHDGGHMVG-------ARFIPVDVTVVASPWNFPLAIPTGGV 657
Cdd:PRK11904   626 ELIALCVREAGKTLQDAIAEVREAVDFCRYYAaQARRLFGAPEKLPGptgesneLRLHGRGVFVCISPWNFPLAIFLGQV 705
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  658 AAALAAGSAVILKPAPPARRCAAELVRAFHDAGIPEDLVVLAPLEDGDVSRHLVTHKDVDRVVLTGSYDTARLF-RS--W 734
Cdd:PRK11904   706 AAALAAGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVGAALTADPRIAGVAFTGSTETARIInRTlaA 785
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  735 K--PDMHLLGETSGKNAIIVTPSADPDIAVRDAVYSAFAHAGQKCSAssLLVLVSSAGTSERIARQLVDATASLRVRLPL 812
Cdd:PRK11904   786 RdgPIVPLIAETGGQNAMIVDSTALPEQVVDDVVTSAFRSAGQRCSA--LRVLFVQEDIADRVIEMLKGAMAELKVGDPR 863
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  813 SLDSQMGPVVvpdDEKAVRGLTT---LGSGEHWVLKPRYLGDGlwtpGIRAGVVPGSEFHLT-------EYFAPVIGVMR 882
Cdd:PRK11904   864 LLSTDVGPVI---DAEAKANLDAhieRMKREARLLAQLPLPAG----TENGHFVAPTAFEIDsisqlerEVFGPILHVIR 936
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  883 VDT--LQEAIEAVNAVDYGLTSGIQT-LDATELAIwLEGVQAGNLYVNRGITGAIVRRQPFGGWKRSaiGSTTKAGGPSY 959
Cdd:PRK11904   937 YKAsdLDKVIDAINATGYGLTLGIHSrIEETADRI-ADRVRVGNVYVNRNQIGAVVGVQPFGGQGLS--GTGPKAGGPHY 1013

                   ..
gi 2219515474  960 LL 961
Cdd:PRK11904  1014 LL 1015
PRK11905 PRK11905
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
148-1121 3.15e-76

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


Pssm-ID: 237018 [Multi-domain]  Cd Length: 1208  Bit Score: 275.59  E-value: 3.15e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  148 ALARLRKG---GNRLNVNLLGEAVLGEKEAAR-------RLAEVSRLVTREDV---DYVSVKVSAVtgpHNPWGF---DE 211
Cdd:PRK11905   188 ALKRARELearGYRYSYDMLGEAARTAADAERyyrdyerAIHAIGKAATGRGVydgPGISVKLSAL---HPRYERaqrER 264
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  212 VVAHGVQALLPLYRLARDNGTFLNLDMEDYKDLDLTIAVFTAILDQEDMYGYEA-GIVLQAYLPDSLGAMQRLQEWAsRR 290
Cdd:PRK11905   265 VMAELLPRLKALALLAKAYDIGLNIDAEEADRLELSLDLLEALCSDPDLAGWNGiGFVVQAYQKRCPFVIDYLIDLA-RR 343
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  291 VaagGSRIKVRVVKGANLsmekvDAEI--------HGWELTTwpSKQATDTNY----KRMLswamtpERTRAIRLGVAGQ 358
Cdd:PRK11905   344 S---GRRLMVRLVKGAYW-----DAEIkraqvdglEGFPVFT--RKVHTDVSYiacaRKLL------AARDVIYPQFATH 407
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  359 NLFDIAFAYELRAARgveDGVEFEMLSGMATGLQEVVRRDTGH---LLLYVPVvDPHEFDVAisYLVRRLEENAAPENFM 435
Cdd:PRK11905   408 NAQTLAAIYELAGGK---GDFEFQCLHGMGEPLYDQVVGKEKLgrpCRIYAPV-GTHETLLA--YLVRRLLENGANSSFV 481
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  436 SGVFD--LAADEVVfgreRDRFLAALSDLD---PDAPVPE----PNRRQDR---------LAERDAGVpEETGTLEERSR 497
Cdd:PRK11905   482 NRIVDenVPVEELI----ADPVEKVAAMGVaphPQIPLPRdlygPERRNSKgldlsdeatLAALDEAL-NAFAAKTWHAA 556
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  498 RLFVSEPDSDPALA----ANRqwaRDIAaaipdstrglaeveaGAARLATNAEVDTLVTATAEAAGVWQSLDPAERAAAL 573
Cdd:PRK11905   557 PLLAGGDVDGGTRPvlnpADH---DDVV---------------GTVTEASAEDVERALAAAQAAFPEWSATPAAERAAIL 618
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  574 HRVGDVLAARRAELIEVAGSEAGKTIDQSDPEVSEAIDFCHHYA-ESSLLLHDGGHMvgarfiPVDVTVVASPWNFPLAI 652
Cdd:PRK11905   619 ERAADLMEAHMPELFALAVREAGKTLANAIAEVREAVDFLRYYAaQARRLLNGPGHK------PLGPVVCISPWNFPLAI 692
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  653 PTGGVAAALAAGSAVILKPAPPARRCAAELVRAFHDAGIPEDLVVLAPLEDGDVSRHLVTHKDVDRVVLTGSYDTARLFR 732
Cdd:PRK11905   693 FTGQIAAALVAGNTVLAKPAEQTPLIAARAVRLLHEAGVPKDALQLLPGDGRTVGAALVADPRIAGVMFTGSTEVARLIQ 772
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  733 SW-----KPDMHLLGETSGKNAIIVTPSADPDIAVRDAVYSAFAHAGQKCSAssLLVLVSSAGTSERIARQLVDATASLR 807
Cdd:PRK11905   773 RTlakrsGPPVPLIAETGGQNAMIVDSSALPEQVVADVIASAFDSAGQRCSA--LRVLCLQEDVADRVLTMLKGAMDELR 850
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  808 VRLPLSLDSQMGPVVvpdDEKAVRGLTTlgsgehWVLKPRYLGDGLWTPGIRAGVVPGSEFHLT------------EYFA 875
Cdd:PRK11905   851 IGDPWRLSTDVGPVI---DAEAQANIEA------HIEAMRAAGRLVHQLPLPAETEKGTFVAPTlieidsisdlerEVFG 921
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  876 PVIGVMRV--DTLQEAIEAVNAVDYGLTSGIQT-LDATeLAIWLEGVQAGNLYVNRGITGAIVRRQPFGGWKRSaiGSTT 952
Cdd:PRK11905   922 PVLHVVRFkaDELDRVIDDINATGYGLTFGLHSrIDET-IAHVTSRIRAGNIYVNRNIIGAVVGVQPFGGEGLS--GTGP 998
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  953 KAGGPSYLLGLgeVEPARGQGGKvEQGTAALDPRVAnlcdAVSSQLDAADLAELRRALVADAAawRTAYGANRDVTGLAC 1032
Cdd:PRK11905   999 KAGGPLYLGRL--VREAPTPIPP-AHESVDTDAAAR----DFLAWLDKEGKAALAAAARDARA--RSALGLEQELPGPTG 1069
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 1033 ERNILRY--REVDVVVRAGQGTALADVVRVMAAG---VRAGGFISLSVADRLPqplqnALLAAGVQVA--VEDQGAWDAR 1105
Cdd:PRK11905  1070 ESNLLSLhpRGRVLCVADTEEALLRQLAAALATGnvaVVAADSGLAAALADLP-----GLVAARIDWTqdWEADDPFAGA 1144
                         1050
                   ....*....|....*.
gi 2219515474 1106 LAELAASGGLGTRVRV 1121
Cdd:PRK11905  1145 LLEGDAERARAVRQAL 1160
D1pyr5carbox2 TIGR01237
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ...
537-961 7.92e-76

delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of two in the degradation of proline to glutamate. This model represents one of several related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. Members of this branch may be associated with proline dehydrogenase (the other enzyme of the pathway from proline to glutamate) but have not been demonstrated experimentally. The branches are not as closely related to each other as some distinct aldehyde dehydrogenases are to some; separate models were built to let each model describe a set of equivalogs. [Energy metabolism, Amino acids and amines]


Pssm-ID: 200087 [Multi-domain]  Cd Length: 511  Bit Score: 260.57  E-value: 7.92e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  537 GAARLATNAEVDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDPEVSEAIDFCHHY 616
Cdd:TIGR01237   61 GTVSKASQEHAEHALQAAAKAFEAWKKTDPEERAAILFKAAAIVRRRRHEFSALLVKEVGKPWNEADAEVAEAIDFMEYY 140
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  617 AESSLLLHDG-------GHMVGARFIPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELVRAFHDA 689
Cdd:TIGR01237  141 ARQMIELAKGkpvnsreGETNQYVYTPTGVTVVISPWNFPFAIMVGMTVAPIVTGNCVVLKPAEAAPVIAAKFVEILEEA 220
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  690 GIPEDLVVLAPLEDGDVSRHLVTHKDVDRVVLTGSY--------DTARLFRSWKPDMHLLGETSGKNAIIVTPSADPDIA 761
Cdd:TIGR01237  221 GLPKGVVQFVPGSGSEVGDYLVDHPKTSLITFTGSRevgtrifeRAAKVQPGQKHLKRVIAEMGGKDTVIVDEDADIELA 300
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  762 VRDAVYSAFAHAGQKCSASSLLVLVSSagTSERIARQLVDATASLRVRLPLSLDSQMGPVVVPDDEKAVRGLTTLGSGEH 841
Cdd:TIGR01237  301 AQSAFTSAFGFAGQKCSAGSRAVVHEK--VYDEVVERFVEITESLKVGPPDSADVYVGPVIDQKSFNKIMEYIEIGKAEG 378
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  842 WVL--------KPRYLGdglwtPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLDATELA 913
Cdd:TIGR01237  379 RLVsggcgddsKGYFIG-----PTIFADVDRKARLAQEEIFGPVVAFIRASDFDEALEIANNTEYGLTGGVISNNRDHIN 453
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*...
gi 2219515474  914 IWLEGVQAGNLYVNRGITGAIVRRQPFGGWKRSAIGSttKAGGPSYLL 961
Cdd:TIGR01237  454 RAKAEFEVGNLYFNRNITGAIVGYQPFGGFKMSGTDS--KAGGPDYLA 499
PRK03137 PRK03137
1-pyrroline-5-carboxylate dehydrogenase; Provisional
542-961 1.02e-74

1-pyrroline-5-carboxylate dehydrogenase; Provisional


Pssm-ID: 179543  Cd Length: 514  Bit Score: 257.17  E-value: 1.02e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  542 ATNAEVDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDPEVSEAIDFCHHYAESSL 621
Cdd:PRK03137    70 ATKELAEKAMQAALEAFETWKKWSPEDRARILLRAAAIIRRRKHEFSAWLVKEAGKPWAEADADTAEAIDFLEYYARQML 149
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  622 LLHDG-------GHMVGARFIPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELVRAFHDAGIPED 694
Cdd:PRK03137   150 KLADGkpvesrpGEHNRYFYIPLGVGVVISPWNFPFAIMAGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAG 229
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  695 LVVLAPLEDGDVSRHLVTHKDVDRVVLTGSYDTA-RLF-RSWK--P-DMHL---LGETSGKNAIIVTPSADPDIAVRDAV 766
Cdd:PRK03137   230 VVNFVPGSGSEVGDYLVDHPKTRFITFTGSREVGlRIYeRAAKvqPgQIWLkrvIAEMGGKDAIVVDEDADLDLAAESIV 309
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  767 YSAFAHAGQKCSASSLLVLVSSAgtSERIARQLVDATASLRVRLPLSlDSQMGPVVVPDDEKAVRGLTTLGSGE-HWVLK 845
Cdd:PRK03137   310 ASAFGFSGQKCSACSRAIVHEDV--YDEVLEKVVELTKELTVGNPED-NAYMGPVINQASFDKIMSYIEIGKEEgRLVLG 386
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  846 prylGDGLWTPG------IRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLDATELAIWLEGV 919
Cdd:PRK03137   387 ----GEGDDSKGyfiqptIFADVDPKARIMQEEIFGPVVAFIKAKDFDHALEIANNTEYGLTGAVISNNREHLEKARREF 462
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|..
gi 2219515474  920 QAGNLYVNRGITGAIVRRQPFGGWKRSaiGSTTKAGGPSYLL 961
Cdd:PRK03137   463 HVGNLYFNRGCTGAIVGYHPFGGFNMS--GTDSKAGGPDYLL 502
ALDH cd07078
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ...
551-960 8.98e-70

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: 240.57  E-value: 8.98e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  551 VTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDPEVSEAIDFCHHYAESSLLLH------ 624
Cdd:cd07078      4 VAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRLHgevips 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  625 -DGGHMVGARFIPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELVRAFHDAGIPEDLVVLAPLED 703
Cdd:cd07078     84 pDPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVVTGDG 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  704 GDVSRHLVTHKDVDRVVLTGSYDTARLF-----RSWKPdmhLLGETSGKNAIIVTPSADPDIAVRDAVYSAFAHAGQKCS 778
Cdd:cd07078    164 DEVGAALASHPRVDKISFTGSTAVGKAImraaaENLKR---VTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQVCT 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  779 ASS-LLVLVSSAgtsERIARQLVDATASLRVRLPLSLDSQMGPVVVP----------DDEKAVRGLTTLGSGEHWVLKPR 847
Cdd:cd07078    241 AASrLLVHESIY---DEFVERLVERVKALKVGNPLDPDTDMGPLISAaqldrvlayiEDAKAEGAKLLCGGKRLEGGKGY 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  848 YLgdglwTPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLDATELAIWLEGVQAGNLYVN 927
Cdd:cd07078    318 FV-----PPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWIN 392
                          410       420       430
                   ....*....|....*....|....*....|...
gi 2219515474  928 RGITGAIVrRQPFGGWKRSAIGsttKAGGPSYL 960
Cdd:cd07078    393 DYSVGAEP-SAPFGGVKQSGIG---REGGPYGL 421
putA PRK11809
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ...
141-1084 1.14e-65

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


Pssm-ID: 236989 [Multi-domain]  Cd Length: 1318  Bit Score: 243.73  E-value: 1.14e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  141 TDKSLGPALARLRK---GGNRLNVNLLGEAVLGEKEAARRLAEvsrlvtredvdY---------------------VSVK 196
Cdd:PRK11809   261 TGETIAEALANARKleeKGFRYSYDMLGEAALTEADAQAYLAS-----------YeqaihaigkasngrgiyegpgISIK 329
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  197 VSAVTGPHNPWGFDEVVAHGVQALLPLYRLARDNGTFLNLDMEDYKDLDLTIAVFTAILDQEDMYGYEA-GIVLQAYLP- 274
Cdd:PRK11809   330 LSALHPRYSRAQYDRVMEELYPRLKSLTLLARQYDIGINIDAEEADRLEISLDLLEKLCFEPELAGWNGiGFVIQAYQKr 409
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  275 -----DSLGAMQRlqewASRRvaaggsRIKVRVVKGANLSMEKVDAEIHGWE-LTTWPSKQATDTNY----KRMLSwamT 344
Cdd:PRK11809   410 cpfviDYLIDLAR----RSRR------RLMIRLVKGAYWDSEIKRAQVDGLEgYPVYTRKVYTDVSYlacaRKLLA---V 476
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  345 PErtrAIRLGVAGQNLFDIAFAYELrAARGVEDG-VEFEMLSGMATGLQEVV--RRDTGHL----LLYVPVvDPHEFDVA 417
Cdd:PRK11809   477 PN---LIYPQFATHNAHTLAAIYHL-AGQNYYPGqYEFQCLHGMGEPLYEQVvgKVADGKLnrpcRIYAPV-GTHETLLA 551
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  418 isYLVRRLEENAAPENFMSGVfdlaADEVVfgrerdrflaALSDLDPDaPVPEpnrrqdrlAERDAGVPEETGTLEER-- 495
Cdd:PRK11809   552 --YLVRRLLENGANTSFVNRI----ADTSL----------PLDELVAD-PVEA--------VEKLAQQEGQLGLPHPKip 606
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  496 -SRRLFVSEPDSDPAL-AANRQWARDIAAAIPDSTRGL--------AEVEAGAA----------------RLATNAEVDT 549
Cdd:PRK11809   607 lPRDLYGKGRANSAGLdLANEHRLASLSSALLASAHQKwqaapmleDPVAAGEMspvinpadprdivgyvREATPAEVEQ 686
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  550 LVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDPEVSEAIDFCHHYAEsslllhdgghM 629
Cdd:PRK11809   687 ALESAVNAAPIWFATPPAERAAILERAADLMEAQMQTLMGLLVREAGKTFSNAIAEVREAVDFLRYYAG----------Q 756
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  630 VGARF-----IPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELVRAFHDAGIPEDLVVLAPLEDG 704
Cdd:PRK11809   757 VRDDFdndthRPLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKPAEQTPLIAAQAVRILLEAGVPAGVVQLLPGRGE 836
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  705 DVSRHLVTHKDVDRVVLTGSYDTARLF-----RSWKPDMH---LLGETSGKNAIIVTPSADPDIAVRDAVYSAFAHAGQK 776
Cdd:PRK11809   837 TVGAALVADARVRGVMFTGSTEVARLLqrnlaGRLDPQGRpipLIAETGGQNAMIVDSSALTEQVVADVLASAFDSAGQR 916
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  777 CSAssLLVLVSSAGTSERIARQLVDATASLRVRLPLSLDSQMGPVVvpdDEKAVRGL----TTLGSGEHWVLKPRYLGDG 852
Cdd:PRK11809   917 CSA--LRVLCLQDDVADRTLKMLRGAMAECRMGNPDRLSTDIGPVI---DAEAKANIerhiQAMRAKGRPVFQAARENSE 991
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  853 LWTPGirAGVVP-----GSEFHLT-EYFAPVIGVMRV--DTLQEAIEAVNAVDYGLTSGIQT-LDATeLAIWLEGVQAGN 923
Cdd:PRK11809   992 DWQSG--TFVPPtlielDSFDELKrEVFGPVLHVVRYnrNQLDELIEQINASGYGLTLGVHTrIDET-IAQVTGSAHVGN 1068
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  924 LYVNRGITGAIVRRQPFGGWKRSaiGSTTKAGGPSYLLGLGEVEPARGQGGKVEQgTAALDPRVANLCDAVSSQLDAadL 1003
Cdd:PRK11809  1069 LYVNRNMVGAVVGVQPFGGEGLS--GTGPKAGGPLYLYRLLATRPEDALAVTLAR-QDAEYPVDAQLRAALLAPLTA--L 1143
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474 1004 AELRRALVADAAAWRTAY------GANRDVTGLACERNilRY----REVDVVVRAGQGTALADVVRVMAAGVRA---GGF 1070
Cdd:PRK11809  1144 REWAAEREPELAALCDQYaelaqaGTTRLLPGPTGERN--TYtllpRERVLCLADTEQDALTQLAAVLAVGSQAlwpDDA 1221
                         1050
                   ....*....|....
gi 2219515474 1071 ISLSVADRLPQPLQ 1084
Cdd:PRK11809  1222 LHRALVAALPAAVQ 1235
PutA2 COG4230
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
217-1114 1.13e-63

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


Pssm-ID: 443374 [Multi-domain]  Cd Length: 1156  Bit Score: 236.76  E-value: 1.13e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  217 VQALLPLYRLARDNGTFLNLDMEDYKDLDLTIAVFTAILDQEDMYGYEAGIVLQAYLPDslgAMQRLQEWASRRVAAGGS 296
Cdd:COG4230    275 LPLLALLALAAININIDEEEDAEELLLLLLLLDLLAALLLDGGLGGGGGVGQAVQAYAK---ALLLVLDLLARRRRRRRR 351
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  297 RIKVRVVKGANLSMEKVDAEIHGweLTTWPSKQATDTNYKRMLswAMTPERTRAIRLGVAGQNLFDIAFAYELRAARGVE 376
Cdd:COG4230    352 RLVVRLVKGAEWDREIQRAQVLG--YVVYPVTTRKVLYDAAAL--ALALLLLAAQPAFAPQFATHAAATAAAAAAAGGGG 427
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  377 DGvEFEMLSGMATGLQEVVRRDTGHLLL--YVPVvDPHEFDVAisYLVRRLEENAAPENFMSGVFD--LAADEVVfgreR 452
Cdd:COG4230    428 EF-EFQCLHGMGEYLYDQVGRGKLGRPCriYAPV-GSHEDLLA--YLVRRLLENGANSSFVNRIADedVPVEELI----A 499
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  453 D--RFLAALSDLdPDAPVPEPNR--RQDRLAER--DAGVPEETGTLEERSRRlfvsepdsdpalAANRQWArdiAAAIPD 526
Cdd:COG4230    500 DpvEKARALGGA-PHPRIPLPRDlyGPERRNSAglDLSDEAVLAALSAALAA------------AAEKQWQ---AAPLIA 563
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  527 STRGLAEVEA-----------GAARLATNAEVDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEA 595
Cdd:COG4230    564 GEAASGEARPvrnpadhsdvvGTVVEATAADVEAALAAAQAAFPAWSATPVEERAAILERAADLLEAHRAELMALLVREA 643
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  596 GKTIDQSDPEVSEAIDFCHHYAESSLLLHDGGHMVGARFipvdvTVVA-SPWNFPLAIPTGGVAAALAAGSAVILKPAPP 674
Cdd:COG4230    644 GKTLPDAIAEVREAVDFCRYYAAQARRLFAAPTVLRGRG-----VFVCiSPWNFPLAIFTGQVAAALAAGNTVLAKPAEQ 718
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  675 ARRCAAELVRAFHDAGIPEDLVVLAPLEDGDVSRHLVTHKDVDRVVLTGSYDTAR-----LFRSWKPDMHLLGETSGKNA 749
Cdd:COG4230    719 TPLIAARAVRLLHEAGVPADVLQLLPGDGETVGAALVADPRIAGVAFTGSTETARlinrtLAARDGPIVPLIAETGGQNA 798
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  750 IIVTPSADPDIAVRDAVYSAFAHAGQKCSAssLLVLVSSAGTSERIARQLVDATASLRVRLPLSLDSQMGPVVvpdDEKA 829
Cdd:COG4230    799 MIVDSSALPEQVVDDVLASAFDSAGQRCSA--LRVLCVQEDIADRVLEMLKGAMAELRVGDPADLSTDVGPVI---DAEA 873
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  830 VRGLTTlgsgehWVLKPRYLGDGLWTPGIRAGVVPGSEF-----------HLT-EYFAPVIGVMRV--DTLQEAIEAVNA 895
Cdd:COG4230    874 RANLEA------HIERMRAEGRLVHQLPLPEECANGTFVaptlieidsisDLErEVFGPVLHVVRYkaDELDKVIDAINA 947
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  896 VDYGLTSGIQT-LDATELAIwLEGVQAGNLYVNRGITGAIVRRQPFGGWKRSaiGSTTKAGGPSYLLGLgevepARGQGG 974
Cdd:COG4230    948 TGYGLTLGVHSrIDETIDRV-AARARVGNVYVNRNIIGAVVGVQPFGGEGLS--GTGPKAGGPHYLLRF-----ATERTV 1019
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  975 KVEQGTAALDPRVANLCDAVSSQLDAADLAElrralvadaaawrtayganrdVTGlacERNILRY--REVDVVVRAGQGT 1052
Cdd:COG4230   1020 TVNTTAAGGNASLLALGDWLASLLGALTLPG---------------------PTG---ERNTLTLrpRGRVLCLADSLEA 1075
                          890       900       910       920       930       940
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2219515474 1053 ALADVVRVMAAGVRAggfisLSVADRLPQPLQNALLAAGVQVAVEdqGAWDARLAELAASGG 1114
Cdd:COG4230   1076 LLAQLAAALATGNRA-----VVAADLALAGLPAVLLPPFDAVLFE--GRLRALRQALAARDG 1130
ALDH_AldH-CAJ73105 cd07131
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ...
536-950 1.35e-62

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: 221.45  E-value: 1.35e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  536 AGAARLATNAEVDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDPEVSEAIDFCHH 615
Cdd:cd07131     28 VGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELARLVTREMGKPLAEGRGDVQEAIDMAQY 107
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  616 YAESSLLLHdgGHMVG---------ARFIPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELVRAF 686
Cdd:cd07131    108 AAGEGRRLF--GETVPselpnkdamTRRQPIGVVALITPWNFPVAIPSWKIFPALVCGNTVVFKPAEDTPACALKLVELF 185
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  687 HDAGIPEDLVVLAPLEDGDVSRHLVTHKDVDRVVLTGSYDTARLFR--SWKPDMHLLGETSGKNAIIVTPSADPDIAVRD 764
Cdd:cd07131    186 AEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGetCARPNKRVALEMGGKNPIIVMDDADLDLALEG 265
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  765 AVYSAFAHAGQKCSASSLLVLVSSagTSERIARQLVDATASLRVRLPLSLDSQMGPVVVPDD-EKAVR--------GLTT 835
Cdd:cd07131    266 ALWSAFGTTGQRCTATSRLIVHES--VYDEFLKRFVERAKRLRVGDGLDEETDMGPLINEAQlEKVLNyneigkeeGATL 343
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  836 LGSGEhwVLKPRYLGDGLW-TPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLDATELAI 914
Cdd:cd07131    344 LLGGE--RLTGGGYEKGYFvEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAIEIANDTEYGLSSAIYTEDVNKAFR 421
                          410       420       430
                   ....*....|....*....|....*....|....*.
gi 2219515474  915 WLEGVQAGNLYVNRGITGAIVrRQPFGGWKRSAIGS 950
Cdd:cd07131    422 ARRDLEAGITYVNAPTIGAEV-HLPFGGVKKSGNGH 456
ALDH_KGSADH-YcbD cd07097
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ...
537-950 2.86e-62

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: 220.58  E-value: 2.86e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  537 GAARLATNAEVDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDPEVSEAIDFCHHY 616
Cdd:cd07097     29 GKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELARLLTREEGKTLPEARGEVTRAGQIFRYY 108
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  617 AESSLLLH-------DGGHMVGARFIPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELVRAFHDA 689
Cdd:cd07097    109 AGEALRLSgetlpstRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIAPALAYGNTVVFKPAELTPASAWALVEILEEA 188
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  690 GIPEDLVVLAPLEDGDVSRHLVTHKDVDRVVLTGSYDT---------ARLFRswkpdMHLlgETSGKNAIIVTPSADPDI 760
Cdd:cd07097    189 GLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVgrriaaaaaARGAR-----VQL--EMGGKNPLVVLDDADLDL 261
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  761 AVRDAVYSAFAHAGQKCSASSLLVLVssAGTSERIARQLVDATASLRVRLPLSLDSQMGPVVVPDDEKAVRGLTTLGSGE 840
Cdd:cd07097    262 AVECAVQGAFFSTGQRCTASSRLIVT--EGIHDRFVEALVERTKALKVGDALDEGVDIGPVVSERQLEKDLRYIEIARSE 339
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  841 HWVL----KPRYLGDGLW--TPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLDATELAI 914
Cdd:cd07097    340 GAKLvyggERLKRPDEGYylAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALAIANDTEFGLSAGIVTTSLKHATH 419
                          410       420       430
                   ....*....|....*....|....*....|....*..
gi 2219515474  915 WLEGVQAGNLYVNRGITGaiVRRQ-PFGGWKRSAIGS 950
Cdd:cd07097    420 FKRRVEAGVVMVNLPTAG--VDYHvPFGGRKGSSYGP 454
D1pyr5carbox3 TIGR01238
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ...
517-968 3.70e-62

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: 220.94  E-value: 3.70e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  517 ARDIAAAIPDSTRGLAEVEAGAARLATNAEVDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAG 596
Cdd:TIGR01238   46 YKADGEAQPVTNPADRRDIVGQVFHANLAHVQAAIDSAQQAFPTWNATPAKERAAKLDRLADLLELHMPELMALCVREAG 125
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  597 KTIDQSDPEVSEAIDFCHHYAESslLLHDGGHMVGArfiPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPAR 676
Cdd:TIGR01238  126 KTIHNAIAEVREAVDFCRYYAKQ--VRDVLGEFSVE---SRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTS 200
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  677 RCAAELVRAFHDAGIPEDLVVLAPLEDGDVSRHLVTHKDVDRVVLTGSYDTARLF-----RSWKPDMHLLGETSGKNAII 751
Cdd:TIGR01238  201 LIAYRAVELMQEAGFPAGTIQLLPGRGADVGAALTSDPRIAGVAFTGSTEVAQLInqtlaQREDAPVPLIAETGGQNAMI 280
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  752 VTPSADPDIAVRDAVYSAFAHAGQKCSAssLLVLVSSAGTSERIARQLVDATASLRVRLPLSLDSQMGPVVvpdDEKAVR 831
Cdd:TIGR01238  281 VDSTALPEQVVRDVLRSAFDSAGQRCSA--LRVLCVQEDVADRVLTMIQGAMQELKVGVPHLLTTDVGPVI---DAEAKQ 355
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  832 GLttLGSGEHWVLKPRYL------GDGLWTPGIragVVPGSEFHLT-------EYFAPVIGVMR--VDTLQEAIEAVNAV 896
Cdd:TIGR01238  356 NL--LAHIEHMSQTQKKIaqltldDSRACQHGT---FVAPTLFELDdiaelseEVFGPVLHVVRykARELDQIVDQINQT 430
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2219515474  897 DYGLTSGIQTLDATELAiWLEG-VQAGNLYVNRGITGAIVRRQPFGGWKRSaiGSTTKAGGPSYLLGLGEVEP 968
Cdd:TIGR01238  431 GYGLTMGVHSRIETTYR-WIEKhARVGNCYVNRNQVGAVVGVQPFGGQGLS--GTGPKAGGPHYLYRLTQVQY 500
ALDH_P5CDH cd07083
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ...
542-961 2.53e-60

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: 215.52  E-value: 2.53e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  542 ATNAEVDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDPEVSEAIDFCHHYAESSL 621
Cdd:cd07083     52 ADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRRRELIATLTYEVGKNWVEAIDDVAEAIDFIRYYARAAL 131
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  622 LLHDGGHMVGAR--------FIPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELVRAFHDAGIPE 693
Cdd:cd07083    132 RLRYPAVEVVPYpgednesfYVGLGAGVVISPWNFPVAIFTGMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPP 211
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  694 DLVVLAPLEDGDVSRHLVTHKDVDRVVLTGSYDTARLFrsWK------PDMH----LLGETSGKNAIIVTPSADPDIAVR 763
Cdd:cd07083    212 GVVQFLPGVGEEVGAYLTEHERIRGINFTGSLETGKKI--YEaaarlaPGQTwfkrLYVETGGKNAIIVDETADFELVVE 289
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  764 DAVYSAFAHAGQKCSASSLLVLVSSAgtSERIARQLVDATASLRVRLPLSLDSQMGPVVVPDDEKAVRGLTTLGSGEHWV 843
Cdd:cd07083    290 GVVVSAFGFQGQKCSAASRLILTQGA--YEPVLERLLKRAERLSVGPPEENGTDLGPVIDAEQEAKVLSYIEHGKNEGQL 367
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  844 LKPRYLGDG---LWTPGIRAGVVPGSEFHLTEYFAPVIGVMRV--DTLQEAIEAVNAVDYGLTSGIQTLDATELAIWLEG 918
Cdd:cd07083    368 VLGGKRLEGegyFVAPTVVEEVPPKARIAQEEIFGPVLSVIRYkdDDFAEALEVANSTPYGLTGGVYSRKREHLEEARRE 447
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|...
gi 2219515474  919 VQAGNLYVNRGITGAIVRRQPFGGWKRSaiGSTTKAGGPSYLL 961
Cdd:cd07083    448 FHVGNLYINRKITGALVGVQPFGGFKLS--GTNAKTGGPHYLR 488
ALDH-SF cd06534
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ...
552-960 2.31e-59

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: 208.62  E-value: 2.31e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  552 TATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDPEVSEAIDFCHHYAESSLLLH------- 624
Cdd:cd06534      1 AAARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGgpelpsp 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  625 DGGHMVGARFIPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELVRAFHDAGIPEDLVVLAPLEDG 704
Cdd:cd06534     81 DPGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGGD 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  705 DVSRHLVTHKDVDRVVLTGSYDTARLFR-----SWKPdmhLLGETSGKNAIIVTPSADPDIAVRDAVYSAFAHAGQKCSA 779
Cdd:cd06534    161 EVGAALLSHPRVDKISFTGSTAVGKAIMkaaaeNLKP---VTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTA 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  780 SSLLVLvssagtSERIARQLVDAtaslrvrlplsldsqMGPVVVPDDekavrglttlgsgehwvlkprylgdglwtpgir 859
Cdd:cd06534    238 ASRLLV------HESIYDEFVEK---------------LVTVLVDVD--------------------------------- 263
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  860 agvvPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLDATELAIWLEGVQAGNLYVNRGITGAIVrRQP 939
Cdd:cd06534    264 ----PDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVGP-EAP 338
                          410       420
                   ....*....|....*....|.
gi 2219515474  940 FGGWKRSAIGSttkAGGPSYL 960
Cdd:cd06534    339 FGGVKNSGIGR---EGGPYGL 356
ALDH_F7_AASADH-like cd07086
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ...
535-946 1.49e-54

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: 198.17  E-value: 1.49e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  535 EAGAARLATNAEVDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDPEVSEAIDFCH 614
Cdd:cd07086     25 PIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRLVSLEMGKILPEGLGEVQEMIDICD 104
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  615 HYAESSLLLHdG--------GHMVGARFIPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELVRAF 686
Cdd:cd07086    105 YAVGLSRMLY-GltipserpGHRLMEQWNPLGVVGVITAFNFPVAVPGWNAAIALVCGNTVVWKPSETTPLTAIAVTKIL 183
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  687 HDA----GIPEDLVVLApLEDGDVSRHLVTHKDVDRVVLTGSYDT--------ARLFRswkpdMHLLgETSGKNAIIVTP 754
Cdd:cd07086    184 AEVleknGLPPGVVNLV-TGGGDGGELLVHDPRVPLVSFTGSTEVgrrvgetvARRFG-----RVLL-ELGGNNAIIVMD 256
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  755 SADPDIAVRDAVYSAFAHAGQKCSASSLLVLVSSagTSERIARQLVDATASLRVRLPLSLDSQMGPVV----VPDDEKAV 830
Cdd:cd07086    257 DADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHES--VYDEFLERLVKAYKQVRIGDPLDEGTLVGPLInqaaVEKYLNAI 334
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  831 R-----GLTTLGSGEhwvlKPRYLGDGLW-TPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGI 904
Cdd:cd07086    335 EiaksqGGTVLTGGK----RIDGGEPGNYvEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEEAIAINNDVPQGLSSSI 410
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....
gi 2219515474  905 QTLDATELAIWLE--GVQAGNLYVNRGITGAIVrRQPFGGWKRS 946
Cdd:cd07086    411 FTEDLREAFRWLGpkGSDCGIVNVNIPTSGAEI-GGAFGGEKET 453
ALDH_F21_LactADH-like cd07094
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ...
541-949 3.25e-47

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: 176.08  E-value: 3.25e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  541 LATNAEVDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDPEVSEAIDFCHHYAESS 620
Cdd:cd07094     17 ADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARVEVDRAIDTLRLAAEEA 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  621 LLLH------DGGHMVGARFI-----PVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELVRAFHDA 689
Cdd:cd07094     97 ERIRgeeiplDATQGSDNRLAwtirePVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASKTPLSALELAKILVEA 176
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  690 GIPEDLVVLAPLEDGDVSRHLVTHKDVDRVVLTGSYDTARLFRSWKPDMHLLGETSGKNAIIVTPSADPDIAVRDAVYSA 769
Cdd:cd07094    177 GVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRANAGGKRIALELGGNAPVIVDRDADLDAAIEALAKGG 256
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  770 FAHAGQKCSASSLLVLVSSagTSERIARQLVDATASLRVRLPLSLDSQMGPVVVPDD--------EKAVR-GLTTLGSGE 840
Cdd:cd07094    257 FYHAGQVCISVQRIYVHEE--LYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAaerverwvEEAVEaGARLLCGGE 334
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  841 hwvlkpryLGDGLWTPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLDATELAIWLEGVQ 920
Cdd:cd07094    335 --------RDGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRDLNVAFKAAEKLE 406
                          410       420
                   ....*....|....*....|....*....
gi 2219515474  921 AGNLYVNRGiTGAIVRRQPFGGWKRSAIG 949
Cdd:cd07094    407 VGGVMVNDS-SAFRTDWMPFGGVKESGVG 434
ALDH_F8_HMSADH cd07093
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ...
542-949 3.74e-47

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: 175.83  E-value: 3.74e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  542 ATNAEVDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDP-EVSEAIDFCHHYAESS 620
Cdd:cd07093     16 GGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARTrDIPRAAANFRFFADYI 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  621 LLL------HDGGHMVGARFIPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELVRAFHDAGIPED 694
Cdd:cd07093     96 LQLdgesypQDGGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLTAWLLAELANEAGLPPG 175
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  695 LVVLAPLEDGDVSRHLVTHKDVDRVVLTGSYDTARLF-----RSWKPdMHLlgETSGKNAIIVTPSADPDIAVRDAVYSA 769
Cdd:cd07093    176 VVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTImraaaPNLKP-VSL--ELGGKNPNIVFADADLDRAVDAAVRSS 252
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  770 FAHAGQKCSASSLLvLVSSAGTSERIARqLVDATASLRVRLPLSLDSQMGPVVVPDDEKAVRGLTTLGSGE----HW--- 842
Cdd:cd07093    253 FSNNGEVCLAGSRI-LVQRSIYDEFLER-FVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYVELARAEgatiLTggg 330
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  843 VLKPRYLGDGLW-TPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLDATELAIWLEGVQA 921
Cdd:cd07093    331 RPELPDLEGGYFvEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTRDLGRAHRVARRLEA 410
                          410       420       430
                   ....*....|....*....|....*....|
gi 2219515474  922 GNLYVNrgitGAIVR--RQPFGGWKRSAIG 949
Cdd:cd07093    411 GTVWVN----CWLVRdlRTPFGGVKASGIG 436
ALDH_DhaS cd07114
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ...
542-949 9.48e-47

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: 174.66  E-value: 9.48e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  542 ATNAEVDTLVTATAEA--AGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDPEVSEAIDFCHHYA-- 617
Cdd:cd07114     16 ASAADVDRAVAAARAAfeGGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRAQVRYLAEWYRYYAgl 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  618 ----ESSLL-LHDGGHMVGARFIPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELVRAFHDAGIP 692
Cdd:cd07114     96 adkiEGAVIpVDKGDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPASTLELAKLAEEAGFP 175
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  693 EDLVVLAPLEDGDVSRHLVTHKDVDRVVLTGSYDTARLF--RSWKPDMHLLGETSGKNAIIVTPSADPDIAVRDAVYSAF 770
Cdd:cd07114    176 PGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIarAAAENLAPVTLELGGKSPNIVFDDADLDAAVNGVVAGIF 255
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  771 AHAGQKCSASS-LLVlvsSAGTSERIARQLVDATASLRVRLPLSLDSQMGPVVVPDDEKAVRGL---------TTLGSGE 840
Cdd:cd07114    256 AAAGQTCVAGSrLLV---QRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVERYvarareegaRVLTGGE 332
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  841 hwVLKPRYLGDGLW-TPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLD---ATELAiwl 916
Cdd:cd07114    333 --RPSGADLGAGYFfEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWTRDlarAHRVA--- 407
                          410       420       430
                   ....*....|....*....|....*....|....*
gi 2219515474  917 EGVQAGNLYVN--RgitgAIVRRQPFGGWKRSAIG 949
Cdd:cd07114    408 RAIEAGTVWVNtyR----ALSPSSPFGGFKDSGIG 438
ALDH_LactADH-AldA cd07088
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ...
541-949 4.56e-46

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: 173.22  E-value: 4.56e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  541 LATNAEVDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDPEVSEAIDFCHHYAESS 620
Cdd:cd07088     31 AATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKLIVEEQGKTLSLARVEVEFTADYIDYMAEWA 110
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  621 LLLhDGGHMVGAR-----FI---PVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELVRAFHDAGIP 692
Cdd:cd07088    111 RRI-EGEIIPSDRpneniFIfkvPIGVVAGILPWNFPFFLIARKLAPALVTGNTIVIKPSEETPLNALEFAELVDEAGLP 189
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  693 EDLVVLAPLEDGDVSRHLVTHKDVDRVVLTGSYDT-ARLFRSWKPDM-HLLGETSGKNAIIVTPSADPDIAVRDAVYSAF 770
Cdd:cd07088    190 AGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAgQKIMEAAAENItKVSLELGGKAPAIVMKDADLDLAVKAIVDSRI 269
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  771 AHAGQKCSASSLlVLVSSAGTSERIARqLVDATASLRVRLPLSLDSQMGPVV-----------VpddEKAVRGLTTLGSG 839
Cdd:cd07088    270 INCGQVCTCAER-VYVHEDIYDEFMEK-LVEKMKAVKVGDPFDAATDMGPLVneaaldkveemV---ERAVEAGATLLTG 344
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  840 EHwvlkPRYLGDGLW-TPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLDATELAIWLEG 918
Cdd:cd07088    345 GK----RPEGEKGYFyEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELANDSEYGLTSYIYTENLNTAMRATNE 420
                          410       420       430
                   ....*....|....*....|....*....|..
gi 2219515474  919 VQAGNLYVNRGITGAIvrrQPF-GGWKRSAIG 949
Cdd:cd07088    421 LEFGETYINRENFEAM---QGFhAGWKKSGLG 449
ALDH_BenzADH-like cd07104
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ...
546-957 2.73e-44

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: 166.94  E-value: 2.73e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  546 EVDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDPEVSEAIDFCHHYAesSLLLHD 625
Cdd:cd07104      1 DVDRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILREAA--GLPRRP 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  626 GGHMVG---------ARFIPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELV-RAFHDAGIPEDL 695
Cdd:cd07104     79 EGEILPsdvpgkesmVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTGGLLIaEIFEEAGLPKGV 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  696 VVLAPLEDGDVSRHLVTHKDVDRVVLTGSYDTARLF-----RSWKPdMHLlgETSGKNAIIVTPSADPDIAVRDAVYSAF 770
Cdd:cd07104    159 LNVVPGGGSEIGDALVEHPRVRMISFTGSTAVGRHIgelagRHLKK-VAL--ELGGNNPLIVLDDADLDLAVSAAAFGAF 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  771 AHAGQKCSASSlLVLVSSAGTSERIARqLVDATASLRVRLPLSLDSQMGPVVVPDD--------EKAV-RGLTTLGSGEH 841
Cdd:cd07104    236 LHQGQICMAAG-RILVHESVYDEFVEK-LVAKAKALPVGDPRDPDTVIGPLINERQvdrvhaivEDAVaAGARLLTGGTY 313
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  842 wvlkprylgDGLW-TPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLD---ATELAiwlE 917
Cdd:cd07104    314 ---------EGLFyQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDlerAMAFA---E 381
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|...
gi 2219515474  918 GVQAGNLYVNrGIT---GAIVrrqPFGGWKRSAIGSttkAGGP 957
Cdd:cd07104    382 RLETGMVHIN-DQTvndEPHV---PFGGVKASGGGR---FGGP 417
ALDH_SGSD_AstD cd07095
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ...
546-946 7.20e-44

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: 165.52  E-value: 7.20e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  546 EVDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDPEVSE-------AIDFCHHYAe 618
Cdd:cd07095      1 QVDAAVAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEVAAmagkidiSIKAYHERT- 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  619 SSLLLHDGGHMVGARFIPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELVRAFHDAGIPEDLVVL 698
Cdd:cd07095     80 GERATPMAQGRAVLRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLPPGVLNL 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  699 ApLEDGDVSRHLVTHKDVDRVVLTGSYDTARLFR---SWKPDMHLLGETSGKNAIIVTPSADPDIAVRDAVYSAFAHAGQ 775
Cdd:cd07095    160 V-QGGRETGEALAAHEGIDGLLFTGSAATGLLLHrqfAGRPGKILALEMGGNNPLVVWDVADIDAAAYLIVQSAFLTAGQ 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  776 KCSASSLLVLVSSAGTSERIARqLVDATASLRVRLPLSLDSQMGPVVvpDDEKAVRGLTT----LGSGEHWVLKPRYL-- 849
Cdd:cd07095    239 RCTCARRLIVPDGAVGDAFLER-LVEAAKRLRIGAPDAEPPFMGPLI--IAAAAARYLLAqqdlLALGGEPLLAMERLva 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  850 GDGLWTPGI----RAGVVPGSEfhlteYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLDATELAIWLEGVQAGNLY 925
Cdd:cd07095    316 GTAFLSPGIidvtDAADVPDEE-----IFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAGIVN 390
                          410       420
                   ....*....|....*....|.
gi 2219515474  926 VNRGITGAIVRRqPFGGWKRS 946
Cdd:cd07095    391 WNRPTTGASSTA-PFGGVGLS 410
ALDH_F5_SSADH_GabD cd07103
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ...
542-950 1.31e-43

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: 165.30  E-value: 1.31e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  542 ATNAEVDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDPEVSEAIDFCHHYAESSL 621
Cdd:cd07103     16 AGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGEVDYAASFLEWFAEEAR 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  622 LLHD---GGHMVGARFI----PVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAP--PArrCAAELVRAFHDAGIP 692
Cdd:cd07103     96 RIYGrtiPSPAPGKRILvikqPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEetPL--SALALAELAEEAGLP 173
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  693 EDLVVLAPLEDGDVSRHLVTHKDVDRVVLTGSYDTARLFrswkpdMHLLGETS-------GKNA-IIVTPSADPDIAVRD 764
Cdd:cd07103    174 AGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLL------MAQAADTVkrvslelGGNApFIVFDDADLDKAVDG 247
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  765 AVYSAFAHAGQKC-SASSLLVLVSSAgtsERIARQLVDATASLRVRLPLSLDSQMGPVVvpdDEKAV------------R 831
Cdd:cd07103    248 AIASKFRNAGQTCvCANRIYVHESIY---DEFVEKLVERVKKLKVGNGLDEGTDMGPLI---NERAVekvealvedavaK 321
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  832 GLTTLGSGEHWVLKPRYlgdglWTPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLDATE 911
Cdd:cd07103    322 GAKVLTGGKRLGLGGYF-----YEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDLAR 396
                          410       420       430
                   ....*....|....*....|....*....|....*....
gi 2219515474  912 LAIWLEGVQAGNLYVNRGITGAIVrrQPFGGWKRSAIGS 950
Cdd:cd07103    397 AWRVAEALEAGMVGINTGLISDAE--APFGGVKESGLGR 433
ALDH_F6_MMSDH cd07085
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ...
525-951 3.26e-43

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: 165.00  E-value: 3.26e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  525 PDSTRGLAEVEagaarLATNAEVDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDP 604
Cdd:cd07085     23 PATGEVIARVP-----LATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDELARLITLEHGKTLADARG 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  605 EVSEAIDFCHHyAESSLLLHDGGHMVGAR--------FIPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPAR 676
Cdd:cd07085     98 DVLRGLEVVEF-ACSIPHLLKGEYLENVArgidtysyRQPLGVVAGITPFNFPAMIPLWMFPMAIACGNTFVLKPSERVP 176
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  677 RCAAELVRAFHDAGIPeDLVVLAPLEDGDVSRHLVTHKDVDRVVLTGS-------YDTARlfRSWKPDMHLLGetsGKNA 749
Cdd:cd07085    177 GAAMRLAELLQEAGLP-DGVLNVVHGGKEAVNALLDHPDIKAVSFVGStpvgeyiYERAA--ANGKRVQALGG---AKNH 250
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  750 IIVTPSADPDIAVRDAVYSAFAHAGQKCSASSLLVLVssAGTSERIARQLVDATASLRVRLPLSLDSQMGPVVVPDDEKA 829
Cdd:cd07085    251 AVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAV--GDEADEWIPKLVERAKKLKVGAGDDPGADMGPVISPAAKER 328
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  830 VRGLTTLG--SGEHWVL-----KPRYLGDGLWT-PGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLT 901
Cdd:cd07085    329 IEGLIESGveEGAKLVLdgrgvKVPGYENGNFVgPTILDNVTPDMKIYKEEIFGPVLSIVRVDTLDEAIAIINANPYGNG 408
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|
gi 2219515474  902 SGIQTLDATELAIWLEGVQAGNLYVNRGITgAIVRRQPFGGWKRSAIGST 951
Cdd:cd07085    409 AAIFTRSGAAARKFQREVDAGMVGINVPIP-VPLAFFSFGGWKGSFFGDL 457
ALDH_VaniDH_like cd07150
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ...
531-957 6.25e-43

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: 163.27  E-value: 6.25e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  531 LAEVEAGAARLATNAevdtlVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDPEVSEAI 610
Cdd:cd07150     12 YARVAVGSRQDAERA-----IAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWFETTFTP 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  611 DF-------CHHYAESSLLLHDGGHMVGARFIPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELV 683
Cdd:cd07150     87 ELlraaageCRRVRGETLPSDSPGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVIGLKIA 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  684 RAFHDAGIPEDLVVLAPLEDGDVSRHLVTHKDVDRVVLTGSYDTARLF-----RSWKPDMHLLGetsGKNAIIVTPSADP 758
Cdd:cd07150    167 EIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIaekagRHLKKITLELG---GKNPLIVLADADL 243
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  759 DIAVRDAVYSAFAHAGQKCSASSlLVLVSSAGTSERIARqLVDATASLRVRLPLSLDSQMGPVVVPDD--------EKAV 830
Cdd:cd07150    244 DYAVRAAAFGAFMHQGQICMSAS-RIIVEEPVYDEFVKK-FVARASKLKVGDPRDPDTVIGPLISPRQverikrqvEDAV 321
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  831 -RGLTTLGSGEHwvlkprylgDGLW-TPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLD 908
Cdd:cd07150    322 aKGAKLLTGGKY---------DGNFyQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTND 392
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2219515474  909 ---ATELAIWLEgvqAGNLYVNrgitGAIVRRQ---PFGGWKRSAIGsttKAGGP 957
Cdd:cd07150    393 lqrAFKLAERLE---SGMVHIN----DPTILDEahvPFGGVKASGFG---REGGE 437
ALDH_SNDH cd07118
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ...
542-949 6.53e-43

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: 163.28  E-value: 6.53e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  542 ATNAEVDTLVTATAEA--AGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDPEVSEAIDFCHHYAES 619
Cdd:cd07118     16 GTVEDVDAAVAAARKAfdKGPWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGEIEGAADLWRYAASL 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  620 SLLLHDGGH-MVGARFI------PVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELVRAFHDAGIP 692
Cdd:cd07118     96 ARTLHGDSYnNLGDDMLglvlrePIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTTLMLAELLIEAGLP 175
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  693 EDLVVLAPLEDGDVSRHLVTHKDVDRVVLTGSYDTAR-LFRSWKPDMHLLG-ETSGKNAIIVTPSADPDIAVRDAVYSAF 770
Cdd:cd07118    176 AGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKaIAAAAARNLKKVSlELGGKNPQIVFADADLDAAADAVVFGVY 255
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  771 AHAGQKCSASSLLVLVSSagTSERIARQLVDATASLRVRLPLSLDSQMGPVVVPDDEKAVRGLTTLG--SGEHWVLKPRY 848
Cdd:cd07118    256 FNAGECCNSGSRLLVHES--IADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVDAGraEGATLLLGGER 333
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  849 L--GDGLW-TPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLDATELAIWLEGVQAGNLY 925
Cdd:cd07118    334 LasAAGLFyQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDTALTVARRIRAGTVW 413
                          410       420
                   ....*....|....*....|....
gi 2219515474  926 VNRGITGAIvrRQPFGGWKRSAIG 949
Cdd:cd07118    414 VNTFLDGSP--ELPFGGFKQSGIG 435
ALDH_HMSADH_HapE cd07115
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ...
525-949 7.41e-43

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: 163.38  E-value: 7.41e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  525 PDSTRGLAEVEAGAArlatnAEVDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTI-DQSD 603
Cdd:cd07115      4 PATGELIARVAQASA-----EDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIrAARR 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  604 PEVSEAIDFCHHYA------ESSLLLHDGGHMVGARFIPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARR 677
Cdd:cd07115     79 LDVPRAADTFRYYAgwadkiEGEVIPVRGPFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPL 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  678 CAAELVRAFHDAGIPEDLVVLAPLEDGDVSRHLVTHKDVDRVVLTGSYDTAR-LFRSWKPDMHLLG-ETSGKNAIIVTPS 755
Cdd:cd07115    159 SALRIAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRkIMQGAAGNLKRVSlELGGKSANIVFAD 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  756 ADPDIAVRDAVYSAFAHAGQKCSASSLLVLVSSAgtSERIARQLVDATASLRVRLPLSLDSQMGPVVVPDDEKAVRGLTT 835
Cdd:cd07115    239 ADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESI--YDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVD 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  836 LGSGEHWVLKPRYLGDG----LWTPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLDATE 911
Cdd:cd07115    317 VGREEGARLLTGGKRPGargfFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGR 396
                          410       420       430
                   ....*....|....*....|....*....|....*...
gi 2219515474  912 LAIWLEGVQAGNLYVNrgITGAIVRRQPFGGWKRSAIG 949
Cdd:cd07115    397 AHRVAAALKAGTVWIN--TYNRFDPGSPFGGYKQSGFG 432
ALDH_DDALDH cd07099
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ...
537-956 1.13e-42

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: 162.78  E-value: 1.13e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  537 GAARLATNAEVDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDPEVSEAIDFCHHY 616
Cdd:cd07099     10 GEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEVLLALEAIDWA 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  617 AE------------SSLLLHDGGHMVgaRFIPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELVR 684
Cdd:cd07099     90 ARnaprvlaprkvpTGLLMPNKKATV--EYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPLVGELLAE 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  685 AFHDAGIPEDLVVLApLEDGDVSRHLVTHKdVDRVVLTGSYDTARLF-----RSWKPDMHLLGetsGKNAIIVTPSADPD 759
Cdd:cd07099    168 AWAAAGPPQGVLQVV-TGDGATGAALIDAG-VDKVAFTGSVATGRKVmaaaaERLIPVVLELG---GKDPMIVLADADLE 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  760 IAVRDAVYSAFAHAGQKCSASSLLVLVSSAgtSERIARQLVDATASLRVRLPLSLDSQMGPVVVP----------DDEKA 829
Cdd:cd07099    243 RAAAAAVWGAMVNAGQTCISVERVYVHESV--YDEFVARLVAKARALRPGADDIGDADIGPMTTArqldivrrhvDDAVA 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  830 vRGLTTLGSGEHWVLKPRYLGdglwtPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLD- 908
Cdd:cd07099    321 -KGAKALTGGARSNGGGPFYE-----PTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRDl 394
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|
gi 2219515474  909 --ATELAIWLEgvqAGNLYVNRGITGAIVRRQPFGGWKRSAIGSTTKAGG 956
Cdd:cd07099    395 arAEAIARRLE---AGAVSINDVLLTAGIPALPFGGVKDSGGGRRHGAEG 441
ALDH_SSADH1_GabD1 cd07100
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ...
547-949 1.50e-42

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: 161.47  E-value: 1.50e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  547 VDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDPEVSEAIDFCHHYAE--SSLL-- 622
Cdd:cd07100      1 IEAALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRYYAEnaEAFLad 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  623 ---LHDGGH-MVgaRFIPVDVTVVASPWNFPL------AIPTggvaaaLAAGSAVILKPAPPARRCAAELVRAFHDAGIP 692
Cdd:cd07100     81 epiETDAGKaYV--RYEPLGVVLGIMPWNFPFwqvfrfAAPN------LMAGNTVLLKHASNVPGCALAIEELFREAGFP 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  693 EDLVVLAPLeDGDVSRHLVTHKDVDRVVLTGSydtARLFRSwkpdmhlLGETSGKN------------AIIVTPSADPDI 760
Cdd:cd07100    153 EGVFQNLLI-DSDQVEAIIADPRVRGVTLTGS---ERAGRA-------VAAEAGKNlkksvlelggsdPFIVLDDADLDK 221
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  761 AVRDAVYSAFAHAGQKCSASSLLVLVSSAgtSERIARQLVDATASLRVRLPLSLDSQMGPVVVPDD--------EKAV-R 831
Cdd:cd07100    222 AVKTAVKGRLQNAGQSCIAAKRFIVHEDV--YDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLrdelheqvEEAVaA 299
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  832 GLTTLGSGEhwvlkpRYLGDGLW-TPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLD-- 908
Cdd:cd07100    300 GATLLLGGK------RPDGPGAFyPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDle 373
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*
gi 2219515474  909 -ATELAiwlEGVQAGNLYVNrgitgAIVR---RQPFGGWKRSAIG 949
Cdd:cd07100    374 rAERVA---RRLEAGMVFIN-----GMVKsdpRLPFGGVKRSGYG 410
ALDH_BenzADH cd07152
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ...
537-958 7.04e-42

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: 160.15  E-value: 7.04e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  537 GAARLATNAEVDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDPEVSEAIDFCHHY 616
Cdd:cd07152      5 GEVGVADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGELHEA 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  617 AEssLLLHDGGHMVG--------ARFIPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELV-RAFH 687
Cdd:cd07152     85 AG--LPTQPQGEILPsapgrlslARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGGVVIaRLFE 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  688 DAGIPEDLVVLAPlEDGDVSRHLVTHKDVDRVVLTGSYDTARLF-----RSWKpDMHLlgETSGKNAIIVTPSADPDIAV 762
Cdd:cd07152    163 EAGLPAGVLHVLP-GGADAGEALVEDPNVAMISFTGSTAVGRKVgeaagRHLK-KVSL--ELGGKNALIVLDDADLDLAA 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  763 RDAVYSAFAHAGQKCSASSL-LVLVSSAgtsERIARQLVDATASLRVRLPLSLDSQMGPVVvpDDEKAVR---------- 831
Cdd:cd07152    239 SNGAWGAFLHQGQICMAAGRhLVHESVA---DAYTAKLAAKAKHLPVGDPATGQVALGPLI--NARQLDRvhaivddsva 313
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  832 -GLTTLGSGEHwvlkprylgDGL-WTPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLD- 908
Cdd:cd07152    314 aGARLEAGGTY---------DGLfYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDv 384
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2219515474  909 --ATELAiwlEGVQAGNLYVNRG--ITGAIVrrqPFGGWKRSaiGSTTKAGGPS 958
Cdd:cd07152    385 grAMALA---DRLRTGMLHINDQtvNDEPHN---PFGGMGAS--GNGSRFGGPA 430
ALDH_AldA-AAD23400 cd07106
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ...
533-949 9.73e-42

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: 159.62  E-value: 9.73e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  533 EVEAGAARlATNAEVDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDPEVSEAIDF 612
Cdd:cd07106      8 EVFASAPV-ASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFEVGGAVAW 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  613 CHHYAESSL---LLHDG-GHMVGARFIPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELVRAFHD 688
Cdd:cd07106     87 LRYTASLDLpdeVIEDDdTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCTLKLGELAQE 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  689 AgIPEDlVVLAPLEDGDVSRHLVTHKDVDRVVLTGSYDTARL-FRSWKPDM-HLLGETSGKNAIIVTPSADPDIAVRDAV 766
Cdd:cd07106    167 V-LPPG-VLNVVSGGDELGPALTSHPDIRKISFTGSTATGKKvMASAAKTLkRVTLELGGNDAAIVLPDVDIDAVAPKLF 244
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  767 YSAFAHAGQKCSASSLLVLVSSAGtsERIARQLVDATASLRVRLPLSLDSQMGPV-------VVPD--DEKAVRGLTTLG 837
Cdd:cd07106    245 WGAFINSGQVCAAIKRLYVHESIY--DEFCEALVALAKAAVVGDGLDPGTTLGPVqnkmqydKVKElvEDAKAKGAKVLA 322
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  838 SGEhwVLKprylGDGLW-TPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLD---ATELA 913
Cdd:cd07106    323 GGE--PLD----GPGYFiPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDlerAEAVA 396
                          410       420       430
                   ....*....|....*....|....*....|....*.
gi 2219515474  914 IWLEgvqAGNLYVNRgiTGAIVRRQPFGGWKRSAIG 949
Cdd:cd07106    397 RRLE---AGTVWINT--HGALDPDAPFGGHKQSGIG 427
ALDH_F11_NP-GAPDH cd07082
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ...
548-950 1.11e-41

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: 160.04  E-value: 1.11e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  548 DTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDPEVSEAIDFCHHYAESSLLLhDGG 627
Cdd:cd07082     42 EAAETAYDAGRGWWPTMPLEERIDCLHKFADLLKENKEEVANLLMWEIGKTLKDALKEVDRTIDYIRDTIEELKRL-DGD 120
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  628 HMVGARF------------IPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELVRAFHDAGIPEDL 695
Cdd:cd07082    121 SLPGDWFpgtkgkiaqvrrEPLGVVLAIGPFNYPLNLTVSKLIPALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGV 200
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  696 VVLAPLEDGDVSRHLVTHKDVDRVVLTGSYDTARLFRSWKPDMHLLGETSGKNAIIVTPSADPDIAVRDAVYSAFAHAGQ 775
Cdd:cd07082    201 VNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNRLKKQHPMKRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQ 280
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  776 KCSASSlLVLVssagtSERIARQLVD----ATASLRVRLPLSLDSQMGPVVVPDDEKAVRGLT--TLGSGEHWVLKPRYL 849
Cdd:cd07082    281 RCTAIK-RVLV-----HESVADELVEllkeEVAKLKVGMPWDNGVDITPLIDPKSADFVEGLIddAVAKGATVLNGGGRE 354
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  850 GDGLWTPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLDATELAIWLEGVQAGNLYVN-- 927
Cdd:cd07082    355 GGNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVNDIEEAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINsk 434
                          410       420
                   ....*....|....*....|....*
gi 2219515474  928 --RGITgaivrRQPFGGWKRSAIGS 950
Cdd:cd07082    435 cqRGPD-----HFPFLGRKDSGIGT 454
ALDH_y4uC cd07149
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ...
535-949 1.70e-41

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: 159.30  E-value: 1.70e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  535 EAGAARLATNAEVDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDPEVSEAIDFCH 614
Cdd:cd07149     11 VIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARKEVDRAIETLR 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  615 HYAESSLLLHdgGHMV--------GARF-----IPVDVTVVASPWNFPL---------AIptggvaaalAAGSAVILKPA 672
Cdd:cd07149     91 LSAEEAKRLA--GETIpfdaspggEGRIgftirEPIGVVAAITPFNFPLnlvahkvgpAI---------AAGNAVVLKPA 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  673 PPARRCAAELVRAFHDAGIPEDLVVLAPLEDGDVSRHLVTHKDVDRVVLTGSYDTARLFRSWKPDMHLLGETSGKNAIIV 752
Cdd:cd07149    160 SQTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAIARKAGLKKVTLELGSNAAVIV 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  753 TPSADPDIAVRDAVYSAFAHAGQKCsASSLLVLVSSAGTSERIARqLVDATASLRVRLPLSLDSQMGPVVvpdDEKAVRG 832
Cdd:cd07149    240 DADADLEKAVERCVSGAFANAGQVC-ISVQRIFVHEDIYDEFLER-FVAATKKLVVGDPLDEDTDVGPMI---SEAEAER 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  833 LttlgsgEHWVLKPRYLGDGLWTPGIRAG----------VVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTS 902
Cdd:cd07149    315 I------EEWVEEAVEGGARLLTGGKRDGaileptvltdVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQA 388
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*....
gi 2219515474  903 GIQT--LDATELAIwlEGVQAGNLYVNrGITGAIVRRQPFGGWKRSAIG 949
Cdd:cd07149    389 GVFTndLQKALKAA--RELEVGGVMIN-DSSTFRVDHMPYGGVKESGTG 434
ALDH_F10_BADH cd07110
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ...
525-949 3.31e-41

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: 158.28  E-value: 3.31e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  525 PDSTRGLAEVEAgaarlATNAEVDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDP 604
Cdd:cd07110      4 PATEATIGEIPA-----ATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAW 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  605 EVSEAIDFCHHYA----------ESSLLLHDGGHMVGARFIPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPP 674
Cdd:cd07110     79 DVDDVAGCFEYYAdlaeqldakaERAVPLPSEDFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSEL 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  675 ARRCAAELVRAFHDAGIPEDLVVLAPLEDGDVSRHLVTHKDVDRVVLTGSYDTAR-LFRSWKPDMHLLG-ETSGKNAIIV 752
Cdd:cd07110    159 TSLTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSqVMQAAAQDIKPVSlELGGKSPIIV 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  753 TPSADPDIAVRDAVYSAFAHAGQKCSASSLLvLVSSAGTSERIARqLVDATASLRVRLPLSLDSQMGPVVVPDDEKAVR- 831
Cdd:cd07110    239 FDDADLEKAVEWAMFGCFWNNGQICSATSRL-LVHESIADAFLER-LATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVLs 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  832 --------GLTTLGSGEHwvlkPRYLGDGLW-TPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTS 902
Cdd:cd07110    317 fiargkeeGARLLCGGRR----PAHLEKGYFiAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAA 392
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*..
gi 2219515474  903 GIQTLDATELAIWLEGVQAGNLYVNrgITGAIVRRQPFGGWKRSAIG 949
Cdd:cd07110    393 AVISRDAERCDRVAEALEAGIVWIN--CSQPCFPQAPWGGYKRSGIG 437
ALDH_EDX86601 cd07102
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ...
540-951 5.75e-40

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: 154.71  E-value: 5.75e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  540 RLATNAEVDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDPEVSEAIDFCHHY--- 616
Cdd:cd07102     13 PLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEIRGMLERARYMisi 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  617 AESSLLLHDGGHMVGA-RFI---PVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELVRAFHDAGIP 692
Cdd:cd07102     93 AEEALADIRVPEKDGFeRYIrrePLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCGERFAAAFAEAGLP 172
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  693 EDLVVLAPLeDGDVSRHLVTHKDVDRVVLTGSYDT-ARLFRSWKPDMHLLG-ETSGKNAIIVTPSADPDIAVRDAVYSAF 770
Cdd:cd07102    173 EGVFQVLHL-SHETSAALIADPRIDHVSFTGSVAGgRAIQRAAAGRFIKVGlELGGKDPAYVRPDADLDAAAESLVDGAF 251
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  771 AHAGQKCSAssllvlvssagtSERI----------ARQLVDATASLRVRLPLSLDSQMGPVVVPDDEKAVRGLT------ 834
Cdd:cd07102    252 FNSGQSCCS------------IERIyvhesiydafVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQIadaiak 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  835 --TLGSGEHwvLKPRYLGDGLW-TPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLDATE 911
Cdd:cd07102    320 gaRALIDGA--LFPEDKAGGAYlAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDIAR 397
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|
gi 2219515474  912 LAIWLEGVQAGNLYVNRGItgAIVRRQPFGGWKRSAIGST 951
Cdd:cd07102    398 AEALGEQLETGTVFMNRCD--YLDPALAWTGVKDSGRGVT 435
ALDH_PhpJ cd07146
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ...
531-950 4.99e-39

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: 151.74  E-value: 4.99e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  531 LAEVEAGAArlatnaevDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDPEVSEAI 610
Cdd:cd07146     12 VGTVPAGTE--------EALREALALAASYRSTLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTRYEVGRAA 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  611 D---FCHHYA---ESSLLLHDGGHMVGARFI-----PVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCA 679
Cdd:cd07146     84 DvlrFAAAEAlrdDGESFSCDLTANGKARKIftlrePLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEKTPLSA 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  680 AELVRAFHDAGIPEDLVVLAPLEDGDVSRHLVTHKDVDRVVLTGSYDTARLFRSWKPDMHLLGETSGKNAIIVTPSADPD 759
Cdd:cd07146    164 IYLADLLYEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAIAATAGYKRQLLELGGNDPLIVMDDADLE 243
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  760 IAVRDAVYSAFAHAGQKCSA-SSLLVLVSSAgtsERIARQLVDATASLRVRLPLSLDSQMGPVVvpDDEKAV----RGLT 834
Cdd:cd07146    244 RAATLAVAGSYANSGQRCTAvKRILVHESVA---DEFVDLLVEKSAALVVGDPMDPATDMGTVI--DEEAAIqienRVEE 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  835 TLGSGEHWVLKPRYLGDGLWtPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLD---ATE 911
Cdd:cd07146    319 AIAQGARVLLGNQRQGALYA-PTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTNDldtIKR 397
                          410       420       430
                   ....*....|....*....|....*....|....*....
gi 2219515474  912 LAiwlEGVQAGNLYVNrGITGAIVRRQPFGGWKRSAIGS 950
Cdd:cd07146    398 LV---ERLDVGTVNVN-EVPGFRSELSPFGGVKDSGLGG 432
ALDH_AAS00426 cd07109
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ...
525-949 1.31e-38

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: 150.46  E-value: 1.31e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  525 PDSTRGLAEVEAGAArlatnAEVDTLVTATAEA-AGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSD 603
Cdd:cd07109      4 PSTGEVFARIARGGA-----ADVDRAVQAARRAfESGWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQAR 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  604 PEVSEAIDFCHHYAESSLLLH------DGGHMVGARFIPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARR 677
Cdd:cd07109     79 ADVEAAARYFEYYGGAADKLHgetiplGPGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPL 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  678 CAAELVRAFHDAGIPEDLVVLAPLEDGDVSRHLVTHKDVDRVVLTGSYDTARLFRSWKPDMH--LLGETSGKNAIIVTPS 755
Cdd:cd07109    159 TALRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAENVvpVTLELGGKSPQIVFAD 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  756 ADPDIAVRDAVYSAFAHAGQKCSASSLLVLVSSAgtSERIARQLVDATASLRVRLPLSlDSQMGPVVVPDDEKAVRGLT- 834
Cdd:cd07109    239 ADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSI--YDEVLERLVERFRALRVGPGLE-DPDLGPLISAKQLDRVEGFVa 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  835 --------TLGSGEhwVLKPRYLGDGLWTPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQT 906
Cdd:cd07109    316 rarargarIVAGGR--IAEGAPAGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWT 393
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....
gi 2219515474  907 LDaTELAIWL-EGVQAGNLYVNRGITGAIVRRqPFGGWKRSAIG 949
Cdd:cd07109    394 RD-GDRALRVaRRLRAGQVFVNNYGAGGGIEL-PFGGVKKSGHG 435
ALDH_PhdK-like cd07107
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ...
525-950 2.72e-38

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: 149.83  E-value: 2.72e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  525 PDSTRGLAEVEAGAArlatnAEVDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDP 604
Cdd:cd07107      4 PATGQVLARVPAASA-----ADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLG 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  605 EVSEAIDFCHHYAESSLLLH------DGGHMVGARFIPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKP---APPA 675
Cdd:cd07107     79 DVMVAAALLDYFAGLVTELKgetipvGGRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPpeqAPLS 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  676 RRCAAELVRAFhdagIPEDLVVLAPLEDGDVSRHLVTHKDVDRVVLTGSYDTARLFRSWKPDM--HLLGETSGKNAIIVT 753
Cdd:cd07107    159 ALRLAELAREV----LPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEGikHVTLELGGKNALIVF 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  754 PSADPDIAVRDAVYSA-FAHAGQKCSASSLLvLVSSAGTSERIARqLVDATASLRVRLPLSLDSQMGPVV-------VPD 825
Cdd:cd07107    235 PDADPEAAADAAVAGMnFTWCGQSCGSTSRL-FVHESIYDEVLAR-VVERVAAIKVGDPTDPATTMGPLVsrqqydrVMH 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  826 --DEKAVRGLTTLGSGEHwvLKPRYLGDGLWT-PGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTS 902
Cdd:cd07107    313 yiDSAKREGARLVTGGGR--PEGPALEGGFYVePTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTA 390
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2219515474  903 GIQTLDATELAIWLEGVQAGNLYVN---RGITGAivrrqPFGGWKRSAIGS 950
Cdd:cd07107    391 AIWTNDISQAHRTARRVEAGYVWINgssRHFLGA-----PFGGVKNSGIGR 436
ALDH_AldA-Rv0768 cd07139
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ...
537-957 3.71e-38

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: 149.65  E-value: 3.71e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  537 GAARLATNAEVDTLVTATAEA--AGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQS-DPEVSEAIDFC 613
Cdd:cd07139     28 GRVPEATPADVDAAVAAARRAfdNGPWPRLSPAERAAVLRRLADALEARADELARLWTAENGMPISWSrRAQGPGPAALL 107
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  614 HHYAE-----------SSLllhDGGHMVGARfIPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAEL 682
Cdd:cd07139    108 RYYAAlardfpfeerrPGS---GGGHVLVRR-EPVGVVAAIVPWNAPLFLAALKIAPALAAGCTVVLKPSPETPLDAYLL 183
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  683 VRAFHDAGIPEDLVVLAPlEDGDVSRHLVTHKDVDRVVLTGSYDTARLFrswkpdMHLLG--------ETSGKNAIIVTP 754
Cdd:cd07139    184 AEAAEEAGLPPGVVNVVP-ADREVGEYLVRHPGVDKVSFTGSTAAGRRI------AAVCGerlarvtlELGGKSAAIVLD 256
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  755 SADPDIAVRDAVYSAFAHAGQKCSASSlLVLVSSAGTSERIARqLVDATASLRVRLPLSLDSQMGPVVVPDDEKAVRGLT 834
Cdd:cd07139    257 DADLDAAVPGLVPASLMNNGQVCVALT-RILVPRSRYDEVVEA-LAAAVAALKVGDPLDPATQIGPLASARQRERVEGYI 334
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  835 TLGSGEHWVL-----KPRYLGDGLW-TPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLD 908
Cdd:cd07139    335 AKGRAEGARLvtgggRPAGLDRGWFvEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDAVRIANDSDYGLSGSVWTAD 414
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2219515474  909 ---ATELAiwlEGVQAGNLYVNrGITGAIVrrQPFGGWKRSAIGsttKAGGP 957
Cdd:cd07139    415 verGLAVA---RRIRTGTVGVN-GFRLDFG--APFGGFKQSGIG---REGGP 457
ALDH_SSADH2_GabD2 cd07101
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ...
543-949 5.50e-38

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: 149.00  E-value: 5.50e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  543 TNAEVDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDPEVSEAIDFCHHYAESSLL 622
Cdd:cd07101     16 TPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEVLDVAIVARYYARRAER 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  623 L-----HDGGHMVGARFI----PVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELVRAFHDAGIPE 693
Cdd:cd07101     96 LlkprrRRGAIPVLTRTTvnrrPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTALTALWAVELLIEAGLPR 175
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  694 DLVVLAPLEDGDVSRHLVTHkdVDRVVLTGSYDTARLFRSWKPDmHLLG---ETSGKNAIIVTPSADPDIAVRDAVYSAF 770
Cdd:cd07101    176 DLWQVVTGPGSEVGGAIVDN--ADYVMFTGSTATGRVVAERAGR-RLIGcslELGGKNPMIVLEDADLDKAAAGAVRACF 252
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  771 AHAGQKC-SASSLLVLVSSAgtsERIARQLVDATASLRVRLPLSLDSQMGPVVVPD---------DEKAVRGLTTLGSGe 840
Cdd:cd07101    253 SNAGQLCvSIERIYVHESVY---DEFVRRFVARTRALRLGAALDYGPDMGSLISQAqldrvtahvDDAVAKGATVLAGG- 328
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  841 hwvlKPRY-LGDGLWTPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLDATELAIWLEGV 919
Cdd:cd07101    329 ----RARPdLGPYFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTRDGARGRRIAARL 404
                          410       420       430
                   ....*....|....*....|....*....|.
gi 2219515474  920 QAGNLYVNRGITGAIVRRQ-PFGGWKRSAIG 949
Cdd:cd07101    405 RAGTVNVNEGYAAAWASIDaPMGGMKDSGLG 435
ALDH_GABALDH-PuuC cd07112
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ...
531-949 6.15e-38

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: 148.90  E-value: 6.15e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  531 LAEVEAGAArlatnAEVDTLVTATAEA--AGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTI-DQSDPEVS 607
Cdd:cd07112     15 LAEVAACDA-----ADVDRAVAAARRAfeSGVWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPIsDALAVDVP 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  608 EAIDFCHHYAESSLLLHDGGHMVGARFI------PVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAE 681
Cdd:cd07112     90 SAANTFRWYAEAIDKVYGEVAPTGPDALalitrePLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPAEQSPLTALR 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  682 LVRAFHDAGIPEDLVVLAPLEDGDVSRHLVTHKDVDRVVLTGSYDTARLFRSWKPDMHLLG---ETSGKNAIIVTPSA-D 757
Cdd:cd07112    170 LAELALEAGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSGQSNLKRvwlECGGKSPNIVFADApD 249
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  758 PDIAVRDAVYSAFAHAGQKCSASS-LLVlvsSAGTSERIARQLVDATASLRVRLPLSLDSQMGPVVvpDDEKAVRGLTTL 836
Cdd:cd07112    250 LDAAAEAAAAGIFWNQGEVCSAGSrLLV---HESIKDEFLEKVVAAAREWKPGDPLDPATRMGALV--SEAHFDKVLGYI 324
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  837 GSGEHWVLKPRYLGDGLWT--------PGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLD 908
Cdd:cd07112    325 ESGKAEGARLVAGGKRVLTetggffvePTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAASVWTSD 404
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|.
gi 2219515474  909 ATELAIWLEGVQAGNLYVNRGITGAIvrRQPFGGWKRSAIG 949
Cdd:cd07112    405 LSRAHRVARRLRAGTVWVNCFDEGDI--TTPFGGFKQSGNG 443
ALDH_CddD-AldA-like cd07089
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ...
533-949 7.23e-38

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: 148.54  E-value: 7.23e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  533 EVEAGAARLATNAEVDTLVTATAEA--AGVWqSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTI----DQSDPEV 606
Cdd:cd07089      7 EEVIGTAPDAGAADVDAAIAAARRAfdTGDW-STDAEERARCLRQLHEALEARKEELRALLVAEVGAPVmtarAMQVDGP 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  607 SEAIDFCHHYAESSLLLHDGG-----HMVGARFI---PVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRC 678
Cdd:cd07089     86 IGHLRYFADLADSFPWEFDLPvpalrGGPGRRVVrrePVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAPDTPLS 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  679 AAELVRAFHDAGIPEDLVVLAPLEDGDVSRHLVTHKDVDRVVLTGSYDTARLFRSWKPDM--HLLGETSGKNAIIVTPSA 756
Cdd:cd07089    166 ALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAATlkRVLLELGGKSANIVLDDA 245
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  757 DPDIAVRDAVYSAFAHAGQKCSASSLLVLVSSagTSERIARQLVDATASLRVRLPLSLDSQMGPVVVPDDEKAVRGLTTL 836
Cdd:cd07089    246 DLAAAAPAAVGVCMHNAGQGCALTTRLLVPRS--RYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRVEGYIAR 323
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  837 GSGEHWVL-----KPRYLGDGLWT-PGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLDAT 910
Cdd:cd07089    324 GRDEGARLvtgggRPAGLDKGFYVePTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVWSADVD 403
                          410       420       430
                   ....*....|....*....|....*....|....*....
gi 2219515474  911 ELAIWLEGVQAGNLYVNRGITGAIvrRQPFGGWKRSAIG 949
Cdd:cd07089    404 RAYRVARRIRTGSVGINGGGGYGP--DAPFGGYKQSGLG 440
ALDH_SaliADH cd07105
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ...
546-949 8.72e-38

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: 147.72  E-value: 8.72e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  546 EVDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDPEVSEAIDFCHHYAeSSLLLHD 625
Cdd:cd07105      1 DADQAVEAAAAAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGFNVDLAAGMLREAA-SLITQII 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  626 GGHM------VGARFI--PVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELVRAFHDAGIPED--- 694
Cdd:cd07105     80 GGSIpsdkpgTLAMVVkePVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGvln 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  695 LVVLAPLEDGDVSRHLVTHKDVDRVVLTGSYDTARLFRSW-----KPdmhLLGETSGKNAIIVTPSADPDIAVRDAVYSA 769
Cdd:cd07105    160 VVTHSPEDAPEVVEALIAHPAVRKVNFTGSTRVGRIIAETaakhlKP---VLLELGGKAPAIVLEDADLDAAANAALFGA 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  770 FAHAGQKCSASSLLVLVSSagtserIARQLVDATASLRVRLPLSlDSQMGPVVVPDDEKAVRGLTT--LGSGEHWVL--K 845
Cdd:cd07105    237 FLNSGQICMSTERIIVHES------IADEFVEKLKAAAEKLFAG-PVVLGSLVSAAAADRVKELVDdaLSKGAKLVVggL 309
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  846 PRYLGDGL-WTPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLD---ATELAiwlEGVQA 921
Cdd:cd07105    310 ADESPSGTsMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDlarALAVA---KRIES 386
                          410       420       430
                   ....*....|....*....|....*....|.
gi 2219515474  922 GNLYVNrgitGAIVRRQ---PFGGWKRSAIG 949
Cdd:cd07105    387 GAVHIN----GMTVHDEptlPHGGVKSSGYG 413
ALDH_BADH-GbsA cd07119
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ...
531-949 1.07e-37

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: 148.61  E-value: 1.07e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  531 LAEVEAGAARLATNAevdtlVTATAEA--AGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDPEVSE 608
Cdd:cd07119     26 IATVPEGTAEDAKRA-----IAAARRAfdSGEWPHLPAQERAALLFRIADKIREDAEELARLETLNTGKTLRESEIDIDD 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  609 AIDFCHHYAESSLLLHDGGHMVGARFI------PVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAEL 682
Cdd:cd07119    101 VANCFRYYAGLATKETGEVYDVPPHVIsrtvrePVGVCGLITPWNYPLLQAAWKLAPALAAGNTVVIKPSEVTPLTTIAL 180
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  683 VRAFHDAGIPEDLVVLAPLEDGDVSRHLVTHKDVDRVVLTGSYDTAR-LFRSWKPDMHLLG-ETSGKNAIIVTPSADPDI 760
Cdd:cd07119    181 FELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRsIMRAAAGNVKKVAlELGGKNPNIVFADADFET 260
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  761 AVRDAVYSAFAHAGQKCSASSLLVLVSSagTSERIARQLVDATASLRVRLPLSLDSQMGPVVVPDDEKAVRGLTTLGSGE 840
Cdd:cd07119    261 AVDQALNGVFFNAGQVCSAGSRLLVEES--IHDKFVAALAERAKKIKLGNGLDADTEMGPLVSAEHREKVLSYIQLGKEE 338
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  841 HWVLK-------PRYLGDGLW-TPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLDATEL 912
Cdd:cd07119    339 GARLVcggkrptGDELAKGYFvEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIRLANDTPYGLAGAVWTKDIARA 418
                          410       420       430
                   ....*....|....*....|....*....|....*...
gi 2219515474  913 AIWLEGVQAGNLYVNR-GITGAivrRQPFGGWKRSAIG 949
Cdd:cd07119    419 NRVARRLRAGTVWINDyHPYFA---EAPWGGYKQSGIG 453
ALDH_ABALDH-YdcW cd07092
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ...
537-949 4.94e-37

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: 145.93  E-value: 4.94e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  537 GAARLATNAEVDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTID-QSDPEVSEAIDFCHH 615
Cdd:cd07092     11 ATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHlVRDDELPGAVDNFRF 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  616 YAESSLLLHDG-------GHMVGARFIPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELVRAFHD 688
Cdd:cd07092     91 FAGAARTLEGPaageylpGHTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPLTTLLLAELAAE 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  689 aGIPeDLVVLAPLEDGD-VSRHLVTHKDVDRVVLTGSYDTARLF-----RSWKpDMHLlgETSGKNAIIVTPSADPDIAV 762
Cdd:cd07092    171 -VLP-PGVVNVVCGGGAsAGDALVAHPRVRMVSLTGSVRTGKKVaraaaDTLK-RVHL--ELGGKAPVIVFDDADLDAAV 245
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  763 RDAVYSAFAHAGQKCSASSlLVLVsSAGTSERIARQLVDATASLRVRLPLSLDSQMGPVVVPDD--------EKAVRGLT 834
Cdd:cd07092    246 AGIATAGYYNAGQDCTAAC-RVYV-HESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQrervagfvERAPAHAR 323
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  835 TLGSGEhwvlkpRYLGDGLW-TPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLD---AT 910
Cdd:cd07092    324 VLTGGR------RAEGPGYFyEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDvgrAM 397
                          410       420       430
                   ....*....|....*....|....*....|....*....
gi 2219515474  911 ELAIWLegvQAGNLYVNRGITgaIVRRQPFGGWKRSAIG 949
Cdd:cd07092    398 RLSARL---DFGTVWVNTHIP--LAAEMPHGGFKQSGYG 431
astD PRK09457
succinylglutamic semialdehyde dehydrogenase; Reviewed
542-946 1.26e-36

succinylglutamic semialdehyde dehydrogenase; Reviewed


Pssm-ID: 181873  Cd Length: 487  Bit Score: 145.49  E-value: 1.26e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  542 ATNAEVDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDPEVSE-----AIDFcHHY 616
Cdd:PRK09457    34 ATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAEVIARETGKPLWEAATEVTAminkiAISI-QAY 112
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  617 AESSLllHDGGHMVGA----RFIPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELVRAFHDAGIP 692
Cdd:PRK09457   113 HERTG--EKRSEMADGaavlRHRPHGVVAVFGPYNFPGHLPNGHIVPALLAGNTVVFKPSELTPWVAELTVKLWQQAGLP 190
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  693 EDLVVLAPLEDgDVSRHLVTHKDVDRVVLTGSYDTARLFR---SWKPDMHLLGETSGKNAIIVTPSADPDIAVRDAVYSA 769
Cdd:PRK09457   191 AGVLNLVQGGR-ETGKALAAHPDIDGLLFTGSANTGYLLHrqfAGQPEKILALEMGGNNPLVIDEVADIDAAVHLIIQSA 269
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  770 FAHAGQKCS-ASSLLVLVSSAGtsERIARQLVDATASLRVRLPlslDSQ----MGPVVvpdDEKAVRGLTT-----LGSG 839
Cdd:PRK09457   270 FISAGQRCTcARRLLVPQGAQG--DAFLARLVAVAKRLTVGRW---DAEpqpfMGAVI---SEQAAQGLVAaqaqlLALG 341
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  840 EHWVLKPRYL--GDGLWTPGIrAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLDATELAIWLE 917
Cdd:PRK09457   342 GKSLLEMTQLqaGTGLLTPGI-IDVTGVAELPDEEYFGPLLQVVRYDDFDEAIRLANNTRFGLSAGLLSDDREDYDQFLL 420
                          410       420
                   ....*....|....*....|....*....
gi 2219515474  918 GVQAGNLYVNRGITGAiVRRQPFGGWKRS 946
Cdd:PRK09457   421 EIRAGIVNWNKPLTGA-SSAAPFGGVGAS 448
gabD2 PRK09407
succinic semialdehyde dehydrogenase; Reviewed
502-949 2.44e-36

succinic semialdehyde dehydrogenase; Reviewed


Pssm-ID: 236501 [Multi-domain]  Cd Length: 524  Bit Score: 145.41  E-value: 2.44e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  502 SEPDSDPALAANRQWARDIAAAIPDSTRGLAEVEA-------GAARLATNAEVDTLVTATAEAAGVWQSLDPAERAAALH 574
Cdd:PRK09407     4 TALPMPAPSALTFERLRRLTARVDGAAGPTREVTApftgeplATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLL 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  575 RVGDVLAARRAELIEVAGSEAGKTIDQSDPEVSEAIDFCHHYAESSL-LLHD---GGHMVGA-----RFIPVDVTVVASP 645
Cdd:PRK09407    84 RFHDLVLENREELLDLVQLETGKARRHAFEEVLDVALTARYYARRAPkLLAPrrrAGALPVLtktteLRQPKGVVGVISP 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  646 WNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELVRAFHDAGIPEDLVVLAPLEDGDVSRHLVTHkdVDRVVLTGSY 725
Cdd:PRK09407   164 WNYPLTLAVSDAIPALLAGNAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGPVVGTALVDN--ADYLMFTGST 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  726 DTARLFRSwKPDMHLLG---ETSGKNAIIVTPSADPDIAVRDAVYSAFAHAGQKC-SASSLLVLVSSAgtsERIARQLVD 801
Cdd:PRK09407   242 ATGRVLAE-QAGRRLIGfslELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCiSIERIYVHESIY---DEFVRAFVA 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  802 ATASLRVRLPLSLDSQMGPVVVPDDEKAV---------RGLTTLGSGehwvlKPRY-LGDGLWTPGIRAGVVPGSEFHLT 871
Cdd:PRK09407   318 AVRAMRLGAGYDYSADMGSLISEAQLETVsahvddavaKGATVLAGG-----KARPdLGPLFYEPTVLTGVTPDMELARE 392
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2219515474  872 EYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLDATELAIWLEGVQAGNLYVNRGITGAIVRRQ-PFGGWKRSAIG 949
Cdd:PRK09407   393 ETFGPVVSVYPVADVDEAVERANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNEGYAAAWGSVDaPMGGMKDSGLG 471
ALDH_CddD_SSP0762 cd07138
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ...
533-949 4.50e-36

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: 143.41  E-value: 4.50e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  533 EVEAGAARLATNAEVDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDP-------- 604
Cdd:cd07138     24 EEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQAITLEMGAPITLARAaqvglgig 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  605 ------EVSEAIDFCHHyAESSLLLHDgghmvgarfiPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRC 678
Cdd:cd07138    104 hlraaaDALKDFEFEER-RGNSLVVRE----------PIGVCGLITPWNWPLNQIVLKVAPALAAGCTVVLKPSEVAPLS 172
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  679 AAELVRAFHDAGIPE---DLVvlapleDGD---VSRHLVTHKDVDRVVLTGSYDTARLFrswkpdMHLLGET-------- 744
Cdd:cd07138    173 AIILAEILDEAGLPAgvfNLV------NGDgpvVGEALSAHPDVDMVSFTGSTRAGKRV------AEAAADTvkrvalel 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  745 SGKNAIIVTPSADPDIAVRDAVYSAFAHAGQKCSA-SSLLVLVSSAGTSERIARQLVDATaslRVRLPLSLDSQMGPVVV 823
Cdd:cd07138    241 GGKSANIILDDADLEKAVPRGVAACFANSGQSCNApTRMLVPRSRYAEAEEIAAAAAEAY---VVGDPRDPATTLGPLAS 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  824 PDDEKAVRGLTTLGSGEHWVL------KPRYLGDGLWT-PGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAV 896
Cdd:cd07138    318 AAQFDRVQGYIQKGIEEGARLvaggpgRPEGLERGYFVkPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDEAIAIANDT 397
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2219515474  897 DYGLTSGIQTLDATELAIWLEGVQAGNLYVNRGITGAivrRQPFGGWKRSAIG 949
Cdd:cd07138    398 PYGLAGYVWSADPERARAVARRLRAGQVHINGAAFNP---GAPFGGYKQSGNG 447
ALDH_F9_TMBADH cd07090
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ...
525-949 7.70e-36

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: 142.44  E-value: 7.70e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  525 PDSTRGLAEVEAgaarlATNAEVDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDP 604
Cdd:cd07090      4 PATGEVLATVHC-----AGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARV 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  605 EVSEAIDFCHHYAESSLLLH------DGGHMVGARFIPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRC 678
Cdd:cd07090     79 DIDSSADCLEYYAGLAPTLSgehvplPGGSFAYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLT 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  679 AAELVRAFHDAGIPEDL--VVLApleDGDVSRHLVTHKDVDRVVLTGSYDTAR-LFRSWKPDM-HLLGETSGKNAIIVTP 754
Cdd:cd07090    159 ALLLAEILTEAGLPDGVfnVVQG---GGETGQLLCEHPDVAKVSFTGSVPTGKkVMSAAAKGIkHVTLELGGKSPLIIFD 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  755 SADPDIAVRDAVYSAFAHAGQKCSASSlLVLVSSaGTSERIARQLVDATASLRVRLPLSLDSQMGPVVVPDDEKAVR--- 831
Cdd:cd07090    236 DADLENAVNGAMMANFLSQGQVCSNGT-RVFVQR-SIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLgyi 313
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  832 ------GLTTLGSGEHWVLKPRYLGDGLWTPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQ 905
Cdd:cd07090    314 esakqeGAKVLCGGERVVPEDGLENGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVF 393
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*
gi 2219515474  906 TLDATELAIWLEGVQAGNLYVNR-GITGAIVrrqPFGGWKRSAIG 949
Cdd:cd07090    394 TRDLQRAHRVIAQLQAGTCWINTyNISPVEV---PFGGYKQSGFG 435
ALDH_F4-17_P5CDH cd07123
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ...
542-961 1.05e-35

Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1)-pyrroline-5-carboxylate dehydrogenase (EC=1.5.1.12 ), families 4 and 17: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH), also known as ALDH4A1 in humans, is a mitochondrial homodimer involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. This is a necessary step in the pathway interconnecting the urea and tricarboxylic acid cycles. The preferred substrate is glutamic gamma-semialdehyde, other substrates include succinic, glutaric and adipic semialdehydes. Also included in this CD is the Aldh17 Drosophila melanogaster (Q9VUC0) P5CDH and similar sequences.


Pssm-ID: 143441 [Multi-domain]  Cd Length: 522  Bit Score: 143.50  E-value: 1.05e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  542 ATNAEVDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAAR-RAELIEVAGSEAGKTIDQSDPEVS-EAIDFCH---HY 616
Cdd:cd07123     66 ADAALVEKAIEAALEARKEWARMPFEDRAAIFLKAADLLSGKyRYELNAATMLGQGKNVWQAEIDAAcELIDFLRfnvKY 145
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  617 AESslLLHD-----GGHMVGA-RFIPVDVTVVA-SPWNFPlAIPTGGVAAALAAGSAVILKPAPPARRCAAELVRAFHDA 689
Cdd:cd07123    146 AEE--LYAQqplssPAGVWNRlEYRPLEGFVYAvSPFNFT-AIGGNLAGAPALMGNVVLWKPSDTAVLSNYLVYKILEEA 222
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  690 GIPEDLVVLAPLEDGDVSRHLVTHKDVDRVVLTGSYDTarlFRS-WK------------PdmHLLGETSGKNAIIVTPSA 756
Cdd:cd07123    223 GLPPGVINFVPGDGPVVGDTVLASPHLAGLHFTGSTPT---FKSlWKqigenldryrtyP--RIVGETGGKNFHLVHPSA 297
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  757 DPDIAVRDAVYSAFAHAGQKCSASSLLVLVSSAgtSERIARQLVDATASLRVRLPLSLDSQMGPVVvpdDEKAVRGLTTL 836
Cdd:cd07123    298 DVDSLVTATVRGAFEYQGQKCSAASRAYVPESL--WPEVKERLLEELKEIKMGDPDDFSNFMGAVI---DEKAFDRIKGY 372
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  837 -----GSGEHWVLkprYLGDGLWTPG--IRAGVV----PGSEFHLTEYFAPVIGVMRVD--TLQEAIEAVNAV-DYGLTS 902
Cdd:cd07123    373 idhakSDPEAEII---AGGKCDDSVGyfVEPTVIettdPKHKLMTEEIFGPVLTVYVYPdsDFEETLELVDTTsPYALTG 449
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2219515474  903 GI--QTLDATELAiwLEGVQ--AGNLYVNRGITGAIVRRQPFGGWKRSaiGSTTKAGGPSYLL 961
Cdd:cd07123    450 AIfaQDRKAIREA--TDALRnaAGNFYINDKPTGAVVGQQPFGGARAS--GTNDKAGSPLNLL 508
ALDH_MGR_2402 cd07108
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ...
525-949 1.41e-35

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: 141.73  E-value: 1.41e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  525 PDSTRGLAEVEAGAArlatnAEVDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTI-DQSD 603
Cdd:cd07108      4 PATGQVIGEVPRSRA-----ADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALrTQAR 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  604 PEVSEAIDFCHHYA------ESSLLLHDGGHMVGARFIPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARR 677
Cdd:cd07108     79 PEAAVLADLFRYFGglagelKGETLPFGPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPL 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  678 CAAELVRAFHDAgIPEDLVVLAPLEDGDVSRHLVTHKDVDRVVLTGSYDTARLFRSWKPD--MHLLGETSGKNAIIVTPS 755
Cdd:cd07108    159 AVLLLAEILAQV-LPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAADrlIPVSLELGGKSPMIVFPD 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  756 ADPDIAVRDAVYSA-FAHAGQKCSASSLLVLVSSagTSERIARQLVDATASLRVRLPLSLDSQMGPVVVPDDEKAVRGLT 834
Cdd:cd07108    238 ADLDDAVDGAIAGMrFTRQGQSCTAGSRLFVHED--IYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVCGYI 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  835 TLG---SGEHWVL-----KPRYLGDGLW-TPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQ 905
Cdd:cd07108    316 DLGlstSGATVLRggplpGEGPLADGFFvQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVW 395
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....
gi 2219515474  906 TLDATELAIWLEGVQAGNLYVNRGitGAIVRRQPFGGWKRSAIG 949
Cdd:cd07108    396 TRDLGRALRAAHALEAGWVQVNQG--GGQQPGQSYGGFKQSGLG 437
gabD1 PRK09406
succinic semialdehyde dehydrogenase; Reviewed
542-956 3.50e-35

succinic semialdehyde dehydrogenase; Reviewed


Pssm-ID: 181826 [Multi-domain]  Cd Length: 457  Bit Score: 140.64  E-value: 3.50e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  542 ATNAEVDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDPEVSEAIDFCHHYAE-SS 620
Cdd:PRK09406    20 LTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKAEALKCAKGFRYYAEhAE 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  621 LLLHD--------GGHMVGARFIPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELVRAFHDAGIP 692
Cdd:PRK09406   100 ALLADepadaaavGASRAYVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHASNVPQTALYLADLFRRAGFP 179
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  693 EDLVVLAPLEDGDVSRHLvthKDvDRVV---LTGSYDTARLFRSWKPDM--HLLGETSGKNAIIVTPSADPDIAVRDAVY 767
Cdd:PRK09406   180 DGCFQTLLVGSGAVEAIL---RD-PRVAaatLTGSEPAGRAVAAIAGDEikKTVLELGGSDPFIVMPSADLDRAAETAVT 255
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  768 SAFAHAGQKCSASSLLVLvsSAGTSERIARQLVDATASLRVRLPLSLDSQMGPVVVPD---------DEKAVRGLTTLGS 838
Cdd:PRK09406   256 ARVQNNGQSCIAAKRFIV--HADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQgrdevekqvDDAVAAGATILCG 333
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  839 GEhwvlkpRYLGDGLW-TPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLDATELAIWLE 917
Cdd:PRK09406   334 GK------RPDGPGWFyPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAWTRDEAEQERFID 407
                          410       420       430
                   ....*....|....*....|....*....|....*....
gi 2219515474  918 GVQAGNLYVNrGITgAIVRRQPFGGWKRSAIGSTTKAGG 956
Cdd:PRK09406   408 DLEAGQVFIN-GMT-VSYPELPFGGVKRSGYGRELSAHG 444
ALDH_LactADH_F420-Bios cd07145
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ...
546-949 1.04e-33

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: 135.94  E-value: 1.04e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  546 EVDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDPEVSEAIDFCHHYAESSLLLH- 624
Cdd:cd07145     22 EVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRVEVERTIRLFKLAAEEAKVLRg 101
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  625 -----DGGHMVGARFI-----PVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELVRAFHDAGIPED 694
Cdd:cd07145    102 etipvDAYEYNERRIAftvrePIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSSNTPLTAIELAKILEEAGLPPG 181
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  695 LVVLAPLEDGDVSRHLVTHKDVDRVVLTGSYDTARLFRS-----WKPDMHLLGetsGKNAIIVTPSADPDIAVRDAVYSA 769
Cdd:cd07145    182 VINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASkaggtGKKVALELG---GSDPMIVLKDADLERAVSIAVRGR 258
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  770 FAHAGQKCSASSlLVLVSSAGTSERIARqLVDATASLRVRLPLSLDSQMGPVVVPDDEKAVRGLT--TLGSGEHWVLKPR 847
Cdd:cd07145    259 FENAGQVCNAVK-RILVEEEVYDKFLKL-LVEKVKKLKVGDPLDESTDLGPLISPEAVERMENLVndAVEKGGKILYGGK 336
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  848 YLGDGLWTPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLD---ATELAIWLEgvqAGNL 924
Cdd:cd07145    337 RDEGSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVFTNDinrALKVARELE---AGGV 413
                          410       420
                   ....*....|....*....|....*..
gi 2219515474  925 YVNRGITgaiVRRQ--PFGGWKRSAIG 949
Cdd:cd07145    414 VINDSTR---FRWDnlPFGGFKKSGIG 437
ALDH_F1-2_Ald2-like cd07091
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ...
542-949 6.08e-33

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: 134.26  E-value: 6.08e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  542 ATNAEVDTLVTAtAEAA---GVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQS-DPEVSEAIDFCHHYA 617
Cdd:cd07091     38 ADEEDVDAAVKA-ARAAfetGWWRKMDPRERGRLLNKLADLIERDRDELAALESLDNGKPLEESaKGDVALSIKCLRYYA 116
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  618 ------ESSLLLHDGGHMVGARFIPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELVRAFHDAGI 691
Cdd:cd07091    117 gwadkiQGKTIPIDGNFLAYTRREPIGVCGQIIPWNFPLLMLAWKLAPALAAGNTVVLKPAEQTPLSALYLAELIKEAGF 196
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  692 PEDLVVLAPLEDGDVSRHLVTHKDVDRVVLTGSYDTARLFRSWKPDMHL------LGetsGKNAIIVTPSADPDIAVRDA 765
Cdd:cd07091    197 PPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAAAKSNLkkvtleLG---GKSPNIVFDDADLDKAVEWA 273
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  766 VYSAFAHAGQKCSASS-LLVlvsSAGTSERIARQLVDATASLRVRLPLSLDSQMGPVVVPDD--------EKAVR-GLTT 835
Cdd:cd07091    274 AFGIFFNQGQCCCAGSrIFV---QESIYDEFVEKFKARAEKRVVGDPFDPDTFQGPQVSKAQfdkilsyiESGKKeGATL 350
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  836 LGSGEHWVLKPRYLgdglwTPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLDATELAIW 915
Cdd:cd07091    351 LTGGERHGSKGYFI-----QPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEVIERANDTEYGLAAGVFTKDINKALRV 425
                          410       420       430
                   ....*....|....*....|....*....|....*
gi 2219515474  916 LEGVQAGNLYVNrgiTGAIVRRQ-PFGGWKRSAIG 949
Cdd:cd07091    426 SRALKAGTVWVN---TYNVFDAAvPFGGFKQSGFG 457
ALDH_F7_AASADH cd07130
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ...
540-933 6.37e-33

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: 134.26  E-value: 6.37e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  540 RLATNAEVDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDPEVSEAIDFCHHYAES 619
Cdd:cd07130     29 RQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLVSLEMGKILPEGLGEVQEMIDICDFAVGL 108
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  620 SLLLHdG--------GHMVGARFIPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAE----LVRAFH 687
Cdd:cd07130    109 SRQLY-GltipserpGHRMMEQWNPLGVVGVITAFNFPVAVWGWNAAIALVCGNVVVWKPSPTTPLTAIAvtkiVARVLE 187
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  688 DAGIPEDLVVLApLEDGDVSRHLVTHKDVDRVVLTGSYDT---------ARLFRSwkpdmhLLgETSGKNAIIVTPSADP 758
Cdd:cd07130    188 KNGLPGAIASLV-CGGADVGEALVKDPRVPLVSFTGSTAVgrqvgqavaARFGRS------LL-ELGGNNAIIVMEDADL 259
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  759 DIAVRDAVYSAFAHAGQKCSASSLLVLVSSagTSERIARQLVDATASLRVRLPLSLDSQMGPVV----VPDDEKAVR--- 831
Cdd:cd07130    260 DLAVRAVLFAAVGTAGQRCTTTRRLIVHES--IYDEVLERLKKAYKQVRIGDPLDDGTLVGPLHtkaaVDNYLAAIEeak 337
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  832 --GLTTLGSGEhwvlkpRYLGDGLW-TPGIRAGVVPGSEFHlTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLD 908
Cdd:cd07130    338 sqGGTVLFGGK------VIDGPGNYvEPTIVEGLSDAPIVK-EETFAPILYVLKFDTLEEAIAWNNEVPQGLSSSIFTTD 410
                          410       420
                   ....*....|....*....|....*..
gi 2219515474  909 ATELAIWL--EGVQAGNLYVNRGITGA 933
Cdd:cd07130    411 LRNAFRWLgpKGSDCGIVNVNIGTSGA 437
ALDH_StaphAldA1 cd07117
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ...
542-952 1.66e-32

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: 132.96  E-value: 1.66e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  542 ATNAEVDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDP-EVSEAIDFCHHYA--- 617
Cdd:cd07117     35 ATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLAMVETLDNGKPIRETRAvDIPLAADHFRYFAgvi 114
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  618 ---ESSLLLHDGGHMVGARFIPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELVRAFHDAgIPED 694
Cdd:cd07117    115 raeEGSANMIDEDTLSIVLREPIGVVGQIIPWNFPFLMAAWKLAPALAAGNTVVIKPSSTTSLSLLELAKIIQDV-LPKG 193
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  695 LVVLAPLEDGDVSRHLVTHKDVDRVVLTGSYDTARLFRSWKPDmHLLGET---SGKNAIIVTPSADPDIAVRDAVYSAFA 771
Cdd:cd07117    194 VVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAK-KLIPATlelGGKSANIIFDDANWDKALEGAQLGILF 272
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  772 HAGQKCSASSLLVLVSsaGTSERIARQLVDATASLRVRLPLSLDSQMGPVVVPDDEKAVRGLTTLGSGEHWVL---KPRY 848
Cdd:cd07117    273 NQGQVCCAGSRIFVQE--GIYDEFVAKLKEKFENVKVGNPLDPDTQMGAQVNKDQLDKILSYVDIAKEEGAKIltgGHRL 350
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  849 LGDGL-----WTPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLDATELAIWLEGVQAGN 923
Cdd:cd07117    351 TENGLdkgffIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEVIDMANDSEYGLGGGVFTKDINRALRVARAVETGR 430
                          410       420
                   ....*....|....*....|....*....
gi 2219515474  924 LYVNrgITGAIVRRQPFGGWKRSAIGSTT 952
Cdd:cd07117    431 VWVN--TYNQIPAGAPFGGYKKSGIGRET 457
ALDH_F21_RNP123 cd07147
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ...
541-949 2.35e-32

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: 131.98  E-value: 2.35e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  541 LATNAEVDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDPEVSEAIDFCHHYAESS 620
Cdd:cd07147     17 LAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARGEVARAIDTFRIAAEEA 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  621 LLLHD-----------GGHMVGARFIPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELVRAFHDA 689
Cdd:cd07147     97 TRIYGevlpldisargEGRQGLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPASRTPLSALILGEVLAET 176
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  690 GIPEDLVVLAPLeDGDVSRHLVTHKDVDRVVLTGSYDTARLFRSWKPDMHLLGETSGKNAIIVTPSADPDIAVRDAVYSA 769
Cdd:cd07147    177 GLPKGAFSVLPC-SRDDADLLVTDERIKLLSFTGSPAVGWDLKARAGKKKVVLELGGNAAVIVDSDADLDFAAQRIIFGA 255
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  770 FAHAGQKC-SASSLLVlvsSAGTSERIARQLVDATASLRVRLPLSLDSQMGPVVVPDDEKAVrglttlgsgEHWVLKPRY 848
Cdd:cd07147    256 FYQAGQSCiSVQRVLV---HRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEAERV---------EGWVNEAVD 323
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  849 LGDGLWTPGIRAG----------VVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLDATELAIWLEG 918
Cdd:cd07147    324 AGAKLLTGGKRDGalleptiledVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVFTRDLEKALRAWDE 403
                          410       420       430
                   ....*....|....*....|....*....|.
gi 2219515474  919 VQAGNLYVNRgITGAIVRRQPFGGWKRSAIG 949
Cdd:cd07147    404 LEVGGVVIND-VPTFRVDHMPYGGVKDSGIG 433
ALDH_PsfA-ACA09737 cd07120
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ...
543-949 6.73e-32

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: 130.54  E-value: 6.73e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  543 TNAEVDTLVTATAEA--AGVWqSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDPEVSEAIDFCHHYAesS 620
Cdd:cd07120     17 GVAEAEAAIAAARRAfdETDW-AHDPRLRARVLLELADAFEANAERLARLLALENGKILGEARFEISGAISELRYYA--G 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  621 LLLHDGGHMVGAR--------FIPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELVRAFHDA-GI 691
Cdd:cd07120     94 LARTEAGRMIEPEpgsfslvlREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQINAAIIRILAEIpSL 173
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  692 PEDLVVLAPLEDGDVSRHLVTHKDVDRVVLTGSYDTAR-LFRSWKPDMHLLG-ETSGKNAIIVTPSADPDIAVRDAVYSA 769
Cdd:cd07120    174 PAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRaIMAAAAPTLKRLGlELGGKTPCIVFDDADLDAALPKLERAL 253
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  770 FAHAGQKC-SASSLLVLVSSAgtsERIARQLVDATASLRVRLPLSLDSQMGPVVVPDDEKAVRGLTT--LGSGEHWVLKP 846
Cdd:cd07120    254 TIFAGQFCmAGSRVLVQRSIA---DEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRMVEraIAAGAEVVLRG 330
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  847 RYLGDGL-----WTPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLDATELAIWLEGVQA 921
Cdd:cd07120    331 GPVTEGLakgafLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTRDLARAMRVARAIRA 410
                          410       420
                   ....*....|....*....|....*...
gi 2219515474  922 GNLYVNRgiTGAIVRRQPFGGWKRSAIG 949
Cdd:cd07120    411 GTVWIND--WNKLFAEAEEGGYRQSGLG 436
gabD PRK11241
NADP-dependent succinate-semialdehyde dehydrogenase I;
545-960 1.75e-31

NADP-dependent succinate-semialdehyde dehydrogenase I;


Pssm-ID: 183050 [Multi-domain]  Cd Length: 482  Bit Score: 130.03  E-value: 1.75e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  545 AEVDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDPEVSEAIDFCHHYAESSLLLH 624
Cdd:PRK11241    48 DETRAAIDAANRALPAWRALTAKERANILRRWFNLMMEHQDDLARLMTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIY 127
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  625 DG---GHMVGARFI----PVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELVRAFHDAGIPEDLVV 697
Cdd:PRK11241   128 GDtipGHQADKRLIvikqPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFN 207
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  698 LAPLEDGDVSRHLVTHKDVDRVVLTGSYDTAR-LFRSWKPDMHLLGETSGKNA-IIVTPSADPDIAVRDAVYSAFAHAGQ 775
Cdd:PRK11241   208 VVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRqLMEQCAKDIKKVSLELGGNApFIVFDDADLDKAVEGALASKFRNAGQ 287
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  776 KCSASSLLVLvsSAGTSERIARQLVDATASLRVRLPLSLDSQMGPVVvpdDEKAV------------RGLTTLGSGehwv 843
Cdd:PRK11241   288 TCVCANRLYV--QDGVYDRFAEKLQQAVSKLHIGDGLEKGVTIGPLI---DEKAVakveehiadaleKGARVVCGG---- 358
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  844 lKPRYLGDGLWTPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLDATELAIWLEGVQAGN 923
Cdd:PRK11241   359 -KAHELGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGI 437
                          410       420       430
                   ....*....|....*....|....*....|....*...
gi 2219515474  924 LYVNRGITGAIVrrQPFGGWKRSAIGST-TKAGGPSYL 960
Cdd:PRK11241   438 VGINTGIISNEV--APFGGIKASGLGREgSKYGIEDYL 473
PLN02467 PLN02467
betaine aldehyde dehydrogenase
542-949 2.83e-31

betaine aldehyde dehydrogenase


Pssm-ID: 215260 [Multi-domain]  Cd Length: 503  Bit Score: 129.85  E-value: 2.83e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  542 ATNAEVDTLVTATAEA-----AGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSD------------- 603
Cdd:PLN02467    42 ATAEDVDAAVEAARKAfkrnkGKDWARTTGAVRAKYLRAIAAKITERKSELAKLETLDCGKPLDEAAwdmddvagcfeyy 121
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  604 PEVSEAIDfchHYAESSLLLHDGGHMVGARFIPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELV 683
Cdd:PLN02467   122 ADLAEALD---AKQKAPVSLPMETFKGYVLKEPLGVVGLITPWNYPLLMATWKVAPALAAGCTAVLKPSELASVTCLELA 198
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  684 RAFHDAGIPED-LVVLAPLEDgDVSRHLVTHKDVDRVVLTGSYDTARLFRSW-----KPDMHLLGetsGKNAIIVTPSAD 757
Cdd:PLN02467   199 DICREVGLPPGvLNVVTGLGT-EAGAPLASHPGVDKIAFTGSTATGRKIMTAaaqmvKPVSLELG---GKSPIIVFDDVD 274
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  758 PDIAVRDAVYSAFAHAGQKCSASSLLVLvssagtSERIA----RQLVDATASLRVRLPLSLDSQMGPVVVPDDEKAV--- 830
Cdd:PLN02467   275 LDKAVEWAMFGCFWTNGQICSATSRLLV------HERIAseflEKLVKWAKNIKISDPLEEGCRLGPVVSEGQYEKVlkf 348
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  831 ------RGLTTLGSGEhwvlKPRYLGDGLWT-PGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSG 903
Cdd:PLN02467   349 istaksEGATILCGGK----RPEHLKKGFFIePTIITDVTTSMQIWREEVFGPVLCVKTFSTEDEAIELANDSHYGLAGA 424
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*.
gi 2219515474  904 IQTLDATELAIWLEGVQAGNLYVNrgITGAIVRRQPFGGWKRSAIG 949
Cdd:PLN02467   425 VISNDLERCERVSEAFQAGIVWIN--CSQPCFCQAPWGGIKRSGFG 468
ALDH_F2BC cd07142
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ...
525-949 4.82e-31

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: 128.38  E-value: 4.82e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  525 PDSTRGLAEVEAGAArlatnAEVDTLVTATAEA--AGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQS 602
Cdd:cd07142     26 PRNGEVIAHVAEGDA-----EDVDRAVKAARKAfdEGPWPRMTGYERSRILLRFADLLEKHADELAALETWDNGKPYEQA 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  603 D-PEVSEAIDFCHHYAESSLLLH------DGGHMVGARFIPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPA 675
Cdd:cd07142    101 RyAEVPLAARLFRYYAGWADKIHgmtlpaDGPHHVYTLHEPIGVVGQIIPWNFPLLMFAWKVGPALACGNTIVLKPAEQT 180
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  676 RRCAAELVRAFHDAGIPEDLVVLAPLEDGDVSRHLVTHKDVDRVVLTGSYDTARLF------RSWKPDMHLLGetsGKNA 749
Cdd:cd07142    181 PLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKIImqlaakSNLKPVTLELG---GKSP 257
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  750 IIVTPSADPDIAVRDAVYSAFAHAGQKCSASSLLVLvssagtSERIARQLVD-ATASLRVRL---PLSLDSQMGPVVvpD 825
Cdd:cd07142    258 FIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFV------HESIYDEFVEkAKARALKRVvgdPFRKGVEQGPQV--D 329
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  826 DEKAVRGLTTLGSGEHWVLKPRYLGDGLWT------PGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYG 899
Cdd:cd07142    330 KEQFEKILSYIEHGKEEGATLITGGDRIGSkgyyiqPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEVIKRANNSKYG 409
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2219515474  900 LTSGIQTLDATELAIWLEGVQAGNLYVN--RGITGAIvrrqPFGGWKRSAIG 949
Cdd:cd07142    410 LAAGVFSKNIDTANTLSRALKAGTVWVNcyDVFDASI----PFGGYKMSGIG 457
ALDH_PADH_NahF cd07113
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ...
533-949 5.77e-31

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: 128.33  E-value: 5.77e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  533 EVEAGAARLATNAEVDTLVtATAEAA--GVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDP-EVSEA 609
Cdd:cd07113     25 EQVIASVASATEADVDAAV-ASAWRAfvSAWAKTTPAERGRILLRLADLIEQHGEELAQLETLCSGKSIHLSRAfEVGQS 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  610 IDFCHHYA-----------ESSLLLhdgghMVGARFI------PVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKP- 671
Cdd:cd07113    104 ANFLRYFAgwatkingetlAPSIPS-----MQGERYTaftrrePVGVVAGIVPWNFSVMIAVWKIGAALATGCTIVIKPs 178
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  672 --APPARRCAAELVRafhDAGIPeDLVVLAPLEDGDVSRHLVTHKDVDRVVLTGSYDTARLFRSWKPDmHLLG---ETSG 746
Cdd:cd07113    179 efTPLTLLRVAELAK---EAGIP-DGVLNVVNGKGAVGAQLISHPDVAKVSFTGSVATGKKIGRQAAS-DLTRvtlELGG 253
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  747 KNAIIVTPSADPDIAVRDAVYSAFAHAGQKCSASSLLVLVSSagTSERIARQLVDATASLRVRLPLSLDSQMGPVV-VPD 825
Cdd:cd07113    254 KNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRS--KFDELVTKLKQALSSFQVGSPMDESVMFGPLAnQPH 331
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  826 DEKAVRGLTTLGSGEHWVLkprYLGDGLWTPGI----RAGVVPGSEFHLT--EYFAPVIGVMRVDTLQEAIEAVNAVDYG 899
Cdd:cd07113    332 FDKVCSYLDDARAEGDEIV---RGGEALAGEGYfvqpTLVLARSADSRLMreETFGPVVSFVPYEDEEELIQLINDTPFG 408
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2219515474  900 LTSGIQTLDATELAIWLEGVQAGNLYVN-RGITGAIVrrqPFGGWKRSAIG 949
Cdd:cd07113    409 LTASVWTNNLSKALRYIPRIEAGTVWVNmHTFLDPAV---PFGGMKQSGIG 456
ALDH_ACDHII_AcoD-like cd07559
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ...
542-952 1.55e-30

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: 127.07  E-value: 1.55e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  542 ATNAEVDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARrAELIEVAgseagKTIDQSDP-------EVSEAIDFCH 614
Cdd:cd07559     35 STAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEEN-LELLAVA-----ETLDNGKPiretlaaDIPLAIDHFR 108
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  615 HYA------ESSLLLHDGGHMVGARFIPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELVRAFHD 688
Cdd:cd07559    109 YFAgviraqEGSLSEIDEDTLSYHFHEPLGVVGQIIPWNFPLLMAAWKLAPALAAGNTVVLKPASQTPLSILVLMELIGD 188
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  689 AgIPEDLVVLAPLEDGDVSRHLVTHKDVDRVVLTGSYDTARLFRSWKPDmHLLG---ETSGKNAIIVTPSA-DPDIAVRD 764
Cdd:cd07559    189 L-LPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYAAE-NLIPvtlELGGKSPNIFFDDAmDADDDFDD 266
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  765 AVYSAFA----HAGQKCSASS-LLVlvsSAGTSERIARQLVDATASLRVRLPLSLDSQMGPVVVPDDEKAV--------- 830
Cdd:cd07559    267 KAEEGQLgfafNQGEVCTCPSrALV---QESIYDEFIERAVERFEAIKVGNPLDPETMMGAQVSKDQLEKIlsyvdigke 343
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  831 RGLTTLGSGEHWVLkPRYLGDGLWTPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLDAT 910
Cdd:cd07559    344 EGAEVLTGGERLTL-GGLDKGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFKDEEEAIAIANDTEYGLGGGVWTRDIN 422
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|..
gi 2219515474  911 ELAIWLEGVQAGNLYVNrgITGAIVRRQPFGGWKRSAIGSTT 952
Cdd:cd07559    423 RALRVARGIQTGRVWVN--CYHQYPAHAPFGGYKKSGIGRET 462
ALDH_F16 cd07111
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ...
542-949 2.50e-30

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: 126.36  E-value: 2.50e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  542 ATNAEVDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQS-DPEVSEAIDFCHHYAESS 620
Cdd:cd07111     56 AEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQKHQRLFAVLESLDNGKPIRESrDCDIPLVARHFYHHAGWA 135
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  621 LLLHDGGHMVGarfiPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELVRAFHDAGIPEDlVVLAP 700
Cdd:cd07111    136 QLLDTELAGWK----PVGVVGQIVPWNFPLLMLAWKICPALAMGNTVVLKPAEYTPLTALLFAEICAEAGLPPG-VLNIV 210
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  701 LEDGDVSRHLVTHKDVDRVVLTGSYDTARLFRS----WKPDMHLlgETSGKNAIIVTPSADPDIAVRDAVYSAFAHAGQK 776
Cdd:cd07111    211 TGNGSFGSALANHPGVDKVAFTGSTEVGRALRRatagTGKKLSL--ELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQV 288
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  777 CSASS-LLVLVSSAgtsERIARQLVDATASLRVRLPLSLDSQMGPVVVPDDEKAVRGLTTLGSGEH---WVLKPRYLGDG 852
Cdd:cd07111    289 CCAGSrLLVQESVA---EELIRKLKERMSHLRVGDPLDKAIDMGAIVDPAQLKRIRELVEEGRAEGadvFQPGADLPSKG 365
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  853 LW-TPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLD---ATELAIwleGVQAGNLYVN- 927
Cdd:cd07111    366 PFyPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVALANNTPYGLAASVWSENlslALEVAL---SLKAGVVWINg 442
                          410       420
                   ....*....|....*....|..
gi 2219515474  928 RGITGAIVrrqPFGGWKRSAIG 949
Cdd:cd07111    443 HNLFDAAA---GFGGYRESGFG 461
ALDH_HBenzADH cd07151
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ...
538-949 2.79e-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: 125.88  E-value: 2.79e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  538 AARLATNAEVDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDPEVSEAIDFCHHYA 617
Cdd:cd07151     25 EIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIRESGSTRIKANIEWGAAMAITREAA 104
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  618 ESSLLLH--------DGGHMVGARfIPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELV-RAFHD 688
Cdd:cd07151    105 TFPLRMEgrilpsdvPGKENRVYR-EPLGVVGVISPWNFPLHLSMRSVAPALALGNAVVLKPASDTPITGGLLLaKIFEE 183
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  689 AGIPEDL---VVLAPLEDGDvsrHLVTHKdVDRVV-LTGSYDTARLF-----RSWKpdmHLLGETSGKNAIIVTPSADPD 759
Cdd:cd07151    184 AGLPKGVlnvVVGAGSEIGD---AFVEHP-VPRLIsFTGSTPVGRHIgelagRHLK---KVALELGGNNPFVVLEDADID 256
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  760 IAVRDAVYSAFAHAGQKC-SASSLLVlvsSAGTSERIARQLVDATASLRVRLPLSLDSQMGPVVVPDD--------EKAV 830
Cdd:cd07151    257 AAVNAAVFGKFLHQGQICmAINRIIV---HEDVYDEFVEKFVERVKALPYGDPSDPDTVVGPLINESQvdglldkiEQAV 333
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  831 R-GLTTLGSGEHwvlkprylGDGLWTPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLD- 908
Cdd:cd07151    334 EeGATLLVGGEA--------EGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELANDTEYGLSGAVFTSDl 405
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*
gi 2219515474  909 --ATELAiwlEGVQAGNLYVNRGITG--AIVrrqPFGGWKRSAIG 949
Cdd:cd07151    406 erGVQFA---RRIDAGMTHINDQPVNdePHV---PFGGEKNSGLG 444
PRK13473 PRK13473
aminobutyraldehyde dehydrogenase;
539-950 6.76e-30

aminobutyraldehyde dehydrogenase;


Pssm-ID: 237391  Cd Length: 475  Bit Score: 125.02  E-value: 6.76e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  539 ARLATNAEVDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQS-DPEVSEAIDFCHHYA 617
Cdd:PRK13473    33 IAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEFARLESLNCGKPLHLAlNDEIPAIVDVFRFFA 112
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  618 ESSLLLH-------DGGHMVGARFIPVDVtvVAS--PWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELVRAFHD 688
Cdd:PRK13473   113 GAARCLEgkaageyLEGHTSMIRRDPVGV--VASiaPWNYPLMMAAWKLAPALAAGNTVVLKPSEITPLTALKLAELAAD 190
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  689 AgIPEDLVVLAPLEDGDVSRHLVTHKDVDRVVLTGSYDTARLF-----RSWKpDMHLlgETSGKNAIIVTPSADPDIAVR 763
Cdd:PRK13473   191 I-LPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKHVlsaaaDSVK-RTHL--ELGGKAPVIVFDDADLDAVVE 266
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  764 DAVYSAFAHAGQKCSASS-LLVlvsSAGTSERIARQLVDATASLRVRLPLSLDSQMGPVV----------VPDDEKAVRG 832
Cdd:PRK13473   267 GIRTFGYYNAGQDCTAACrIYA---QRGIYDDLVAKLAAAVATLKVGDPDDEDTELGPLIsaahrdrvagFVERAKALGH 343
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  833 LTTLGSGEhwvlkpRYLGDG-LWTPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLD--- 908
Cdd:PRK13473   344 IRVVTGGE------APDGKGyYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDEDQAVRWANDSDYGLASSVWTRDvgr 417
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|..
gi 2219515474  909 ATELAIWLegvQAGNLYVNRGITgaIVRRQPFGGWKRSAIGS 950
Cdd:PRK13473   418 AHRVSARL---QYGCTWVNTHFM--LVSEMPHGGQKQSGYGK 454
ALDH_F1AB_F2_RALDH1 cd07141
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ...
531-949 1.16e-29

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: 124.38  E-value: 1.16e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  531 LAEVEAGaarlaTNAEVDTLVTATAEA---AGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTI-DQSDPEV 606
Cdd:cd07141     35 ICEVQEG-----DKADVDKAVKAARAAfklGSPWRTMDASERGRLLNKLADLIERDRAYLASLETLDNGKPFsKSYLVDL 109
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  607 SEAIDFCHHYAESSLLLH------DGGHMVGARFIPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPA---PPARR 677
Cdd:cd07141    110 PGAIKVLRYYAGWADKIHgktipmDGDFFTYTRHEPVGVCGQIIPWNFPLLMAAWKLAPALACGNTVVLKPAeqtPLTAL 189
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  678 CAAELVRafhDAGIPEDLVVLAPLEDGDVSRHLVTHKDVDRVVLTGSYDTARLFR--SWKPDMHLLG-ETSGKNAIIVTP 754
Cdd:cd07141    190 YLASLIK---EAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVGKLIQqaAGKSNLKRVTlELGGKSPNIVFA 266
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  755 SADPDIAVRDAVYSAFAHAGQKCSASSlLVLVSSAGTSERIARqLVDATASLRVRLPLSLDSQMGPVVvpDDE--KAVRG 832
Cdd:cd07141    267 DADLDYAVEQAHEALFFNMGQCCCAGS-RTFVQESIYDEFVKR-SVERAKKRVVGNPFDPKTEQGPQI--DEEqfKKILE 342
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  833 LTTLG---------SGEHWVLKPRYLgdglwTPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSG 903
Cdd:cd07141    343 LIESGkkegaklecGGKRHGDKGYFI-----QPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTIDEVIERANNTTYGLAAA 417
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*.
gi 2219515474  904 IQTLDATELAIWLEGVQAGNLYVNrgITGAIVRRQPFGGWKRSAIG 949
Cdd:cd07141    418 VFTKDIDKAITFSNALRAGTVWVN--CYNVVSPQAPFGGYKMSGNG 461
PLN02278 PLN02278
succinic semialdehyde dehydrogenase
545-949 2.57e-29

succinic semialdehyde dehydrogenase


Pssm-ID: 215157 [Multi-domain]  Cd Length: 498  Bit Score: 123.65  E-value: 2.57e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  545 AEVDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDPEVSEAIDFCHHYAESS---- 620
Cdd:PLN02278    62 AETNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIANKEDLAQLMTLEQGKPLKEAIGEVAYGASFLEYFAEEAkrvy 141
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  621 ---LLLHDGGHMVGARFIPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPA---PPARRCAAELVRafhDAGIPED 694
Cdd:PLN02278   142 gdiIPSPFPDRRLLVLKQPVGVVGAITPWNFPLAMITRKVGPALAAGCTVVVKPSeltPLTALAAAELAL---QAGIPPG 218
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  695 LVVLAPLEDGDVSRHLVTHKDVDRVVLTGSYDTARLFrswkpdMHLLGETS-------GKNA-IIVTPSADPDIAVRDAV 766
Cdd:PLN02278   219 VLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKL------MAGAAATVkrvslelGGNApFIVFDDADLDVAVKGAL 292
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  767 YSAFAHAGQKC-SASSLLVlvsSAGTSERIARQLVDATASLRVRLPLSLDSQMGPVVvpdDEKAVRGLTT-----LGSGE 840
Cdd:PLN02278   293 ASKFRNSGQTCvCANRILV---QEGIYDKFAEAFSKAVQKLVVGDGFEEGVTQGPLI---NEAAVQKVEShvqdaVSKGA 366
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  841 HWVL--KPRYLGDGLWTPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLDATELAIWLEG 918
Cdd:PLN02278   367 KVLLggKRHSLGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEEAIAIANDTEAGLAAYIFTRDLQRAWRVSEA 446
                          410       420       430
                   ....*....|....*....|....*....|.
gi 2219515474  919 VQAGNLYVNRGITGAIVrrQPFGGWKRSAIG 949
Cdd:PLN02278   447 LEYGIVGVNEGLISTEV--APFGGVKQSGLG 475
PLN00412 PLN00412
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
543-950 3.45e-29

NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional


Pssm-ID: 215110 [Multi-domain]  Cd Length: 496  Bit Score: 123.33  E-value: 3.45e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  543 TNAEVDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDPEVSEAIDFCHHYAESSL- 621
Cdd:PLN00412    51 TQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKAPIAECLVKEIAKPAKDAVTEVVRSGDLISYTAEEGVr 130
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  622 LLHDGGHMVGARF-------------IPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELVRAFHD 688
Cdd:PLN00412   131 ILGEGKFLVSDSFpgnernkycltskIPLGVVLAIPPFNYPVNLAVSKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHL 210
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  689 AGIPEDLVVLAPLEDGDVSRHLVTHKDVDRVVLTGSyDTArLFRSWKPDM-HLLGETSGKNAIIVTPSADPDIAVRDAVY 767
Cdd:PLN00412   211 AGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTGG-DTG-IAISKKAGMvPLQMELGGKDACIVLEDADLDLAAANIIK 288
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  768 SAFAHAGQKCSASSlLVLVssagtSERIARQLVDA----TASLRVRLPLSlDSQMGPVVVPDDEKAVRGLTT--LGSGEH 841
Cdd:PLN00412   289 GGFSYSGQRCTAVK-VVLV-----MESVADALVEKvnakVAKLTVGPPED-DCDITPVVSESSANFIEGLVMdaKEKGAT 361
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  842 WVLKPRYLGDGLWtPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLDATELAIWLEGVQA 921
Cdd:PLN00412   362 FCQEWKREGNLIW-PLLLDNVRPDMRIAWEEPFGPVLPVIRINSVEEGIHHCNASNFGLQGCVFTRDINKAILISDAMET 440
                          410       420       430
                   ....*....|....*....|....*....|..
gi 2219515474  922 GNLYVNrgitGAIVR---RQPFGGWKRSAIGS 950
Cdd:PLN00412   441 GTVQIN----SAPARgpdHFPFQGLKDSGIGS 468
PRK13968 PRK13968
putative succinate semialdehyde dehydrogenase; Provisional
541-949 3.56e-29

putative succinate semialdehyde dehydrogenase; Provisional


Pssm-ID: 184426 [Multi-domain]  Cd Length: 462  Bit Score: 122.66  E-value: 3.56e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  541 LATNAEVDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDPEVSEAIDFCHHYAE-- 618
Cdd:PRK13968    25 WAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARAEVAKSANLCDWYAEhg 104
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  619 ------SSLLLHDGGHMVGARfiPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELVRAFHDAGIP 692
Cdd:PRK13968   105 pamlkaEPTLVENQQAVIEYR--PLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNVMGCAQLIAQVFKDAGIP 182
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  693 EDLVVLAPLEDGDVSRhLVTHKDVDRVVLTGSYDT-----ARLFRSWKPDMHLLGetsGKNAIIVTPSADPDIAVRDAVY 767
Cdd:PRK13968   183 QGVYGWLNADNDGVSQ-MINDSRIAAVTVTGSVRAgaaigAQAGAALKKCVLELG---GSDPFIVLNDADLELAVKAAVA 258
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  768 SAFAHAGQKCSASSLLVLvsSAGTSERIARQLVDATASLRVRLPLSLDSQMGPVVVPD--DEKAVRGLTTLGSGEHWVLK 845
Cdd:PRK13968   259 GRYQNTGQVCAAAKRFII--EEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDlrDELHHQVEATLAEGARLLLG 336
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  846 PRYL-GDG-LWTPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLDATELAIWLEGVQAGN 923
Cdd:PRK13968   337 GEKIaGAGnYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTTDETQARQMAARLECGG 416
                          410       420
                   ....*....|....*....|....*.
gi 2219515474  924 LYVNrGITgAIVRRQPFGGWKRSAIG 949
Cdd:PRK13968   417 VFIN-GYC-ASDARVAFGGVKKSGFG 440
ALDH_F15-22 cd07098
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ...
543-963 3.40e-27

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: 116.63  E-value: 3.40e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  543 TNAEVDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKT-IDQSDPEV---SEAIDFCHHYAE 618
Cdd:cd07098     16 TPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTmVDASLGEIlvtCEKIRWTLKHGE 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  619 SSL----------LLHDGGHMvgaRFIPVDVTVVASPWNFPLaiptggvaaalaagsAVILKPAPPAR--------RCA- 679
Cdd:cd07098     96 KALrpesrpggllMFYKRARV---EYEPLGVVGAIVSWNYPF---------------HNLLGPIIAALfagnaivvKVSe 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  680 ---------AELVR-AFHDAGIPEDLVVLAPLEdGDVSRHLVTHKDVDRVVLTGSYDTARLF-----RSWKPdmhLLGET 744
Cdd:cd07098    158 qvawssgffLSIIReCLAACGHDPDLVQLVTCL-PETAEALTSHPVIDHITFIGSPPVGKKVmaaaaESLTP---VVLEL 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  745 SGKNAIIVTPSADPDIAVRDAVYSAFAHAGQKCsASSLLVLVSSaGTSERIARQLVDATASLRVRLPLSLDSQMGPVVVP 824
Cdd:cd07098    234 GGKDPAIVLDDADLDQIASIIMRGTFQSSGQNC-IGIERVIVHE-KIYDKLLEILTDRVQALRQGPPLDGDVDVGAMISP 311
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  825 DDEKAVRGL--------TTLGSGEHWVLKPRYLGDGLWTPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAV 896
Cdd:cd07098    312 ARFDRLEELvadavekgARLLAGGKRYPHPEYPQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANST 391
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2219515474  897 DYGLTSGIQTLDATELAIWLEGVQAGNLYVNRGITGAIVRRQPFGGWKRSAIGsttKAGGPSYLLGL 963
Cdd:cd07098    392 EYGLGASVFGKDIKRARRIASQLETGMVAINDFGVNYYVQQLPFGGVKGSGFG---RFAGEEGLRGL 455
ALDH_RL0313 cd07148
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ...
564-949 2.50e-25

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: 110.97  E-value: 2.50e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  564 LDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDPEVSEAIDFCHHYAESslLLHDGGHMV-------GARFI- 635
Cdd:cd07148     41 LPAHERIAILERLADLMEERADELALLIAREGGKPLVDAKVEVTRAIDGVELAADE--LGQLGGREIpmgltpaSAGRIa 118
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  636 -----PVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELVRAFHDAGIPEDLVVLAPLEDgDVSRHL 710
Cdd:cd07148    119 fttrePIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPALATPLSCLAFVDLLHEAGLPEGWCQAVPCEN-AVAEKL 197
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  711 VTHKDVDRVVLTGSYDTARLFRS-WKPDMHLLGETSGKNAIIVTPSADPDIAVRDAVYSAFAHAGQKCsaSSLLVLVSSA 789
Cdd:cd07148    198 VTDPRVAFFSFIGSARVGWMLRSkLAPGTRCALEHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVC--VSVQRVFVPA 275
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  790 GTSERIARQLVDATASLRVRLPLSLDSQMGPVVVPD---------DEKAVRGLTTLGSGehwvlkpRYLGDGLWTPGIRA 860
Cdd:cd07148    276 EIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPRevdrveewvNEAVAAGARLLCGG-------KRLSDTTYAPTVLL 348
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  861 GVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGI--QTLDATELAIwlEGVQAGNLYVNRGiTGAIVRRQ 938
Cdd:cd07148    349 DPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAVftKDLDVALKAV--RRLDATAVMVNDH-TAFRVDWM 425
                          410
                   ....*....|.
gi 2219515474  939 PFGGWKRSAIG 949
Cdd:cd07148    426 PFAGRRQSGYG 436
ALDH_AldA_AN0554 cd07143
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ...
542-949 2.71e-25

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: 111.08  E-value: 2.71e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  542 ATNAEVDTLVTAtAEAA--GVW-QSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDP-EVSEAIDFCHHYA 617
Cdd:cd07143     41 ATEADVDIAVEV-AHAAfeTDWgLKVSGSKRGRCLSKLADLMERNLDYLASIEALDNGKTFGTAKRvDVQASADTFRYYG 119
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  618 ESSLLLH------DGGHMVGARFIPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELVRAFHDAGI 691
Cdd:cd07143    120 GWADKIHgqvietDIKKLTYTRHEPIGVCGQIIPWNFPLLMCAWKIAPALAAGNTIVLKPSELTPLSALYMTKLIPEAGF 199
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  692 PEDLVVLAPLEDGDVSRHLVTHKDVDRVVLTGSYDTARLFRSWKPDMHLLG---ETSGKNAIIVTPSADPDIAVRDAVYS 768
Cdd:cd07143    200 PPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRKVMEAAAKSNLKKvtlELGGKSPNIVFDDADLESAVVWTAYG 279
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  769 AFAHAGQKCSASSlLVLVSSaGTSERIARQLVDATASLRVRLPLSLDSQMGPVVvpDDEKAVRGLTTLGSGehwvlkpRY 848
Cdd:cd07143    280 IFFNHGQVCCAGS-RIYVQE-GIYDKFVKRFKEKAKKLKVGDPFAEDTFQGPQV--SQIQYERIMSYIESG-------KA 348
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  849 LGDGLWTPGIRAG-------------VVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLD---ATEL 912
Cdd:cd07143    349 EGATVETGGKRHGnegyfieptiftdVTEDMKIVKEEIFGPVVAVIKFKTEEEAIKRANDSTYGLAAAVFTNNinnAIRV 428
                          410       420       430
                   ....*....|....*....|....*....|....*..
gi 2219515474  913 AIWLEgvqAGNLYVNrgITGAIVRRQPFGGWKRSAIG 949
Cdd:cd07143    429 ANALK---AGTVWVN--CYNLLHHQVPFGGYKQSGIG 460
ALDH_ALD2-YMR170C cd07144
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ...
541-949 7.73e-25

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: 109.80  E-value: 7.73e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  541 LATNAEVDTLVTAtAEAA--GVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQ-SDPEVSEAIDFCHHYA 617
Cdd:cd07144     41 AAGEEDVDKAVKA-ARKAfeSWWSKVTGEERGELLDKLADLVEKNRDLLAAIEALDSGKPYHSnALGDLDEIIAVIRYYA 119
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  618 ESSLLLHdgghmvGARFI------------PVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELVRA 685
Cdd:cd07144    120 GWADKIQ------GKTIPtspnklaytlhePYGVCGQIIPWNYPLAMAAWKLAPALAAGNTVVIKPAENTPLSLLYFANL 193
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  686 FHDAGIPEDLVVLAPLEDGDVSRHLVTHKDVDRVVLTGSYDTARLFrswkpdMHLLG--------ETSGKNAIIVTPSAD 757
Cdd:cd07144    194 VKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLV------MKAAAqnlkavtlECGGKSPALVFEDAD 267
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  758 PDIAVRDAVYSAFAHAGQKCSASSlLVLVssagtSERIARQLVD-----ATASLRVRLPLSLDSQMGPVVVPDDEKAVRG 832
Cdd:cd07144    268 LDQAVKWAAAGIMYNSGQNCTATS-RIYV-----QESIYDKFVEkfvehVKQNYKVGSPFDDDTVVGPQVSKTQYDRVLS 341
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  833 LTTLGS--GEHWVL----KPRYLGDGLW-TPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQ 905
Cdd:cd07144    342 YIEKGKkeGAKLVYggekAPEGLGKGYFiPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYEEAIKKANDTTYGLAAAVF 421
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....
gi 2219515474  906 TLDATELAIWLEGVQAGNLYVNRGITGAIvrRQPFGGWKRSAIG 949
Cdd:cd07144    422 TKDIRRAHRVARELEAGMVWINSSNDSDV--GVPFGGFKMSGIG 463
PRK09847 PRK09847
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
525-949 4.28e-24

gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional


Pssm-ID: 182108 [Multi-domain]  Cd Length: 494  Bit Score: 107.67  E-value: 4.28e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  525 PDSTRGLAEVEAGaarlaTNAEVDTLVTATAEA--AGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQS 602
Cdd:PRK09847    42 PVTQAPLAKIARG-----KSVDIDRAVSAARGVfeRGDWSLSSPAKRKAVLNKLADLMEAHAEELALLETLDTGKPIRHS 116
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  603 -DPEVSEAIDFCHHYAESSLLLH------DGGHMVGARFIPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPA 675
Cdd:PRK09847   117 lRDDIPGAARAIRWYAEAIDKVYgevattSSHELAMIVREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKS 196
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  676 RRCAAELVRAFHDAGIPEDLVVLAPLEDGDVSRHLVTHKDVDRVVLTGSYDTARLFRSWKPDMHLLG---ETSGKNA-II 751
Cdd:PRK09847   197 PLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGDSNMKRvwlEAGGKSAnIV 276
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  752 VTPSADPDIAVRDAVYSAFAHAGQKCSASSLLVLVSSAgTSERIARqLVDATASLRVRLPLSLDSQMGPVVVPDDEKAVR 831
Cdd:PRK09847   277 FADCPDLQQAASATAAGIFYNQGQVCIAGTRLLLEESI-ADEFLAL-LKQQAQNWQPGHPLDPATTMGTLIDCAHADSVH 354
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  832 GLTTLGSGEHWVL-------KPRYLGdglwtPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGI 904
Cdd:PRK09847   355 SFIREGESKGQLLldgrnagLAAAIG-----PTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAV 429
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*
gi 2219515474  905 QTLDATELAIWLEGVQAGNLYVNRGITGAIVrrQPFGGWKRSAIG 949
Cdd:PRK09847   430 WTRDLSRAHRMSRRLKAGSVFVNNYNDGDMT--VPFGGYKQSGNG 472
PLN02766 PLN02766
coniferyl-aldehyde dehydrogenase
542-949 8.99e-24

coniferyl-aldehyde dehydrogenase


Pssm-ID: 215410 [Multi-domain]  Cd Length: 501  Bit Score: 106.83  E-value: 8.99e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  542 ATNAEVDTLVTATAEA--AGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGK------TIDqsdpeVSEAIDFC 613
Cdd:PLN02766    55 GDKEDVDLAVKAAREAfdHGPWPRMSGFERGRIMMKFADLIEEHIEELAALDTIDAGKlfalgkAVD-----IPAAAGLL 129
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  614 HHYAESSLLLHDGGHMVGARFI------PVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELVRAFH 687
Cdd:PLN02766   130 RYYAGAADKIHGETLKMSRQLQgytlkePIGVVGHIIPWNFPSTMFFMKVAPALAAGCTMVVKPAEQTPLSALFYAHLAK 209
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  688 DAGIPEDLVVLAPLEDGDVSRHLVTHKDVDRVVLTGSYDTARLF-----RSWKPDMHLlgETSGKNAIIVTPSADPDIAV 762
Cdd:PLN02766   210 LAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEVGRKImqaaaTSNLKQVSL--ELGGKSPLLIFDDADVDMAV 287
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  763 RDAVYSAFAHAGQKCSASSLlVLVSSaGTSERIARQLVDATASLRVRLPLSLDSQMGPVVVPDDEKAVRGLTTLGSGEHW 842
Cdd:PLN02766   288 DLALLGIFYNKGEICVASSR-VYVQE-GIYDEFVKKLVEKAKDWVVGDPFDPRARQGPQVDKQQFEKILSYIEHGKREGA 365
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  843 VL----KPryLGD-GLWT-PGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLDATELAIWL 916
Cdd:PLN02766   366 TLltggKP--CGDkGYYIePTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEEAIKKANNTKYGLAAGIVTKDLDVANTVS 443
                          410       420       430
                   ....*....|....*....|....*....|...
gi 2219515474  917 EGVQAGNLYVNrgITGAIVRRQPFGGWKRSAIG 949
Cdd:PLN02766   444 RSIRAGTIWVN--CYFAFDPDCPFGGYKMSGFG 474
PRK13252 PRK13252
betaine aldehyde dehydrogenase; Provisional
531-949 1.34e-23

betaine aldehyde dehydrogenase; Provisional


Pssm-ID: 183918  Cd Length: 488  Bit Score: 106.12  E-value: 1.34e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  531 LAEVEAgaarlATNAEVDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQS---DPeVS 607
Cdd:PRK13252    35 LATVQA-----ATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRERNDELAALETLDTGKPIQETsvvDI-VT 108
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  608 EAiDFCHHYA------ESSLLLHDGGHMVGARFIPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAE 681
Cdd:PRK13252   109 GA-DVLEYYAglapalEGEQIPLRGGSFVYTRREPLGVCAGIGAWNYPIQIACWKSAPALAAGNAMIFKPSEVTPLTALK 187
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  682 LVRAFHDAGIPEDL--VVLApleDGDVSRHLVTHKDVDRVVLTGSYDTARLF-----RSWKpdmHLLGETSGKNAIIVTP 754
Cdd:PRK13252   188 LAEIYTEAGLPDGVfnVVQG---DGRVGAWLTEHPDIAKVSFTGGVPTGKKVmaaaaASLK---EVTMELGGKSPLIVFD 261
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  755 SADPDIAVRDAVYSAFAHAGQKCSASSlLVLVSSAGTSERIARqLVDATASLRVRLPLSLDSQMGPVVVPDDEKAVRGLT 834
Cdd:PRK13252   262 DADLDRAADIAMLANFYSSGQVCTNGT-RVFVQKSIKAAFEAR-LLERVERIRIGDPMDPATNFGPLVSFAHRDKVLGYI 339
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  835 TLGSGEH-------WVLKPRYLGDGLWT-PGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQT 906
Cdd:PRK13252   340 EKGKAEGarllcggERLTEGGFANGAFVaPTVFTDCTDDMTIVREEIFGPVMSVLTFDDEDEVIARANDTEYGLAAGVFT 419
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....
gi 2219515474  907 LDATELAIWLEGVQAGNLYVNR-GITGAivrRQPFGGWKRSAIG 949
Cdd:PRK13252   420 ADLSRAHRVIHQLEAGICWINTwGESPA---EMPVGGYKQSGIG 460
PLN02466 PLN02466
aldehyde dehydrogenase family 2 member
525-949 2.32e-21

aldehyde dehydrogenase family 2 member


Pssm-ID: 215259 [Multi-domain]  Cd Length: 538  Bit Score: 99.50  E-value: 2.32e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  525 PDSTRGLAEVEAGAARlatnaEVDTLVTATAEA--AGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQS 602
Cdd:PLN02466    80 PRTGEVIAHVAEGDAE-----DVNRAVAAARKAfdEGPWPKMTAYERSRILLRFADLLEKHNDELAALETWDNGKPYEQS 154
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  603 -DPEVSEAIDFCHHYAESSLLLH------DGGHMVGARFIPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPA 675
Cdd:PLN02466   155 aKAELPMFARLFRYYAGWADKIHgltvpaDGPHHVQTLHEPIGVAGQIIPWNFPLLMFAWKVGPALACGNTIVLKTAEQT 234
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  676 RRCAAELVRAFHDAGIPEDLVVLAPLEDGDVSRHLVTHKDVDRVVLTGSYDTARLF-----RS-WKPDMHLLGetsGKNA 749
Cdd:PLN02466   235 PLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGSTDTGKIVlelaaKSnLKPVTLELG---GKSP 311
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  750 IIVTPSADPDIAVRDAVYSAFAHAGQKCSASSLLVLvssagtSERIARQLVD---ATASLR-VRLPLSLDSQMGPVVVPD 825
Cdd:PLN02466   312 FIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFV------HERVYDEFVEkakARALKRvVGDPFKKGVEQGPQIDSE 385
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  826 D-EKAVR--------GLTTLGSGEHWVLKPRYLgdglwTPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAV 896
Cdd:PLN02466   386 QfEKILRyiksgvesGATLECGGDRFGSKGYYI-----QPTVFSNVQDDMLIAQDEIFGPVQSILKFKDLDEVIRRANNT 460
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2219515474  897 DYGLTSGIQTLDATELAIWLEGVQAGNLYVN--RGITGAIvrrqPFGGWKRSAIG 949
Cdd:PLN02466   461 RYGLAAGVFTQNLDTANTLSRALRVGTVWVNcfDVFDAAI----PFGGYKMSGIG 511
PLN02419 PLN02419
methylmalonate-semialdehyde dehydrogenase [acylating]
541-927 3.48e-21

methylmalonate-semialdehyde dehydrogenase [acylating]


Pssm-ID: 166060 [Multi-domain]  Cd Length: 604  Bit Score: 99.44  E-value: 3.48e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  541 LATNAEVDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDPEVSEAIDFCHHYAESS 620
Cdd:PLN02419   147 LTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDKLAMNITTEQGKTLKDSHGDIFRGLEVVEHACGMA 226
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  621 LL-----LHDGGHMVGARFI--PVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPA---PPARRCAAELVRafhDAG 690
Cdd:PLN02419   227 TLqmgeyLPNVSNGVDTYSIrePLGVCAGICPFNFPAMIPLWMFPVAVTCGNTFILKPSekdPGASVILAELAM---EAG 303
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  691 IPEDLVVLAPLEDgDVSRHLVTHKDVDRVVLTGSyDTARLF---RSWKPDMHLLGETSGKNAIIVTPSADPDIAVRDAVY 767
Cdd:PLN02419   304 LPDGVLNIVHGTN-DTVNAICDDEDIRAVSFVGS-NTAGMHiyaRAAAKGKRIQSNMGAKNHGLVLPDANIDATLNALLA 381
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  768 SAFAHAGQKCSASSLLVLVSSAGTSERiarQLVDATASLRVRLPLSLDSQMGPVVVPDDEKAVRGLTTLG--SGEHWVLK 845
Cdd:PLN02419   382 AGFGAAGQRCMALSTVVFVGDAKSWED---KLVERAKALKVTCGSEPDADLGPVISKQAKERICRLIQSGvdDGAKLLLD 458
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  846 ------PRYLGDGLWTPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLDATELAIWLEGV 919
Cdd:PLN02419   459 grdivvPGYEKGNFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEAISIINKNKYGNGAAIFTSSGAAARKFQMDI 538

                   ....*...
gi 2219515474  920 QAGNLYVN 927
Cdd:PLN02419   539 EAGQIGIN 546
PRK10090 PRK10090
aldehyde dehydrogenase A; Provisional
573-949 4.44e-21

aldehyde dehydrogenase A; Provisional


Pssm-ID: 182233 [Multi-domain]  Cd Length: 409  Bit Score: 97.11  E-value: 4.44e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  573 LHRVGDVLAARRAELIEVAGSEAGKTIDQSDPEVSEAIDFCHHYA------ESSLLLHDGGH---MVGARfiPVDVTVVA 643
Cdd:PRK10090     1 LRKIAAGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYMAewarryEGEIIQSDRPGeniLLFKR--ALGVTTGI 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  644 SPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELVRAFHDAGIPEDLVVLAPLEDGDVSRHLVTHKDVDRVVLTG 723
Cdd:PRK10090    79 LPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMVSMTG 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  724 SYDT-ARLFRSWKPDMHLLG-ETSGKNAIIVTPSADPDIAVRDAVYSAFAHAGQKCSASSLlVLVSSaGTSERIARQLVD 801
Cdd:PRK10090   159 SVSAgEKIMAAAAKNITKVClELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAER-VYVQK-GIYDQFVNRLGE 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  802 ATASLRVRLPLS-LDSQMGPVVVPDD--------EKAV-RGLTTLGSGEhwvlkpRYLGDG-LWTPGIRAGVVPGSEFHL 870
Cdd:PRK10090   237 AMQAVQFGNPAErNDIAMGPLINAAAlerveqkvARAVeEGARVALGGK------AVEGKGyYYPPTLLLDVRQEMSIMH 310
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  871 TEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLDATELAIWLEGVQAGNLYVNRGITGAIvrrQPF-GGWKRSAIG 949
Cdd:PRK10090   311 EETFGPVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENFEAM---QGFhAGWRKSGIG 387
ALDH_F1L_FTFDH cd07140
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ...
541-949 1.13e-20

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: 96.80  E-value: 1.13e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  541 LATNAEVDTLVTATAEA--AGVWQSLDPAERAAALHRVGDVLAARRAEL--IEVAGSEAGKTIdQSDPEVSEAIDFCHHY 616
Cdd:cd07140     39 LATVEDVDRAVAAAKEAfeNGEWGKMNARDRGRLMYRLADLMEEHQEELatIESLDSGAVYTL-ALKTHVGMSIQTFRYF 117
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  617 AESSLLLHD----------GGHMVGARFIPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELVRAF 686
Cdd:cd07140    118 AGWCDKIQGktipinqarpNRNLTLTKREPIGVCGIVIPWNYPLMMLAWKMAACLAAGNTVVLKPAQVTPLTALKFAELT 197
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  687 HDAGIPEDLVVLAPLEDGDVSRHLVTHKDVDRVVLTGSYDTARLFRSWKPDMHLLG---ETSGKNAIIVTPSADPDIAVR 763
Cdd:cd07140    198 VKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGKHIMKSCAVSNLKKvslELGGKSPLIIFADCDMDKAVR 277
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  764 DAVYSAFAHAGQKCSASSLLVLVSSagTSERIARQLVDATASLRVRLPLSLDSQMGP--------VVVPDDEKAVRGLTT 835
Cdd:cd07140    278 MGMSSVFFNKGENCIAAGRLFVEES--IHDEFVRRVVEEVKKMKIGDPLDRSTDHGPqnhkahldKLVEYCERGVKEGAT 355
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  836 LGSGEHWVLKPRYlgdgLWTPGIRAGVVPGSEFHLTEYFAPVIGVMRVDT--LQEAIEAVNAVDYGLTSGIQTLDATELA 913
Cdd:cd07140    356 LVYGGKQVDRPGF----FFEPTVFTDVEDHMFIAKEESFGPIMIISKFDDgdVDGVLQRANDTEYGLASGVFTKDINKAL 431
                          410       420       430
                   ....*....|....*....|....*....|....*.
gi 2219515474  914 IWLEGVQAGNLYVNRGITGAIVrrQPFGGWKRSAIG 949
Cdd:cd07140    432 YVSDKLEAGTVFVNTYNKTDVA--APFGGFKQSGFG 465
PLN02315 PLN02315
aldehyde dehydrogenase family 7 member
525-959 1.19e-19

aldehyde dehydrogenase family 7 member


Pssm-ID: 177949  Cd Length: 508  Bit Score: 94.13  E-value: 1.19e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  525 PDSTRGLAEVEAGAARlatnaEVDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDP 604
Cdd:PLN02315    41 PANNQPIAEVVEASLE-----DYEEGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAKLDYLGRLVSLEMGKILAEGIG 115
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  605 EVSEAIDFCHHYAESSLLLHDG-------GHMVGARFIPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAP--PA 675
Cdd:PLN02315   116 EVQEIIDMCDFAVGLSRQLNGSiipserpNHMMMEVWNPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPttPL 195
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  676 RRCAAELVRA--FHDAGIPeDLVVLAPLEDGDVSRHLVTHKDVDRVVLTGSYDTARLFRSWKPDMH--LLGETSGKNAII 751
Cdd:PLN02315   196 ITIAMTKLVAevLEKNNLP-GAIFTSFCGGAEIGEAIAKDTRIPLVSFTGSSKVGLMVQQTVNARFgkCLLELSGNNAII 274
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  752 VTPSADPDIAVRDAVYSAFAHAGQKCSASSLLVLVSSagTSERIARQLVDATASLRVRLPLSLDSQMGPVVVPDDEKAV- 830
Cdd:PLN02315   275 VMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHES--IYDDVLEQLLTVYKQVKIGDPLEKGTLLGPLHTPESKKNFe 352
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  831 RGLTTLGS--GEHWVLKPRYLGDGLWTPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLD 908
Cdd:PLN02315   353 KGIEIIKSqgGKILTGGSAIESEGNFVQPTIVEISPDADVVKEELFGPVLYVMKFKTLEEAIEINNSVPQGLSSSIFTRN 432
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2219515474  909 ATELAIWL--EGVQAGNLYVNRGITGAIVrRQPFGGWKrsAIGSTTKAGGPSY 959
Cdd:PLN02315   433 PETIFKWIgpLGSDCGIVNVNIPTNGAEI-GGAFGGEK--ATGGGREAGSDSW 482
ALDH_ACDHII-AcoD cd07116
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ...
538-952 2.41e-18

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: 89.82  E-value: 2.41e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  538 AARlATNAEVDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARrAELIEVAGS-EAGKTI-DQSDPEVSEAIDFCHH 615
Cdd:cd07116     32 VPR-STAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEAN-LEMLAVAETwDNGKPVrETLAADIPLAIDHFRY 109
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  616 YA------ESSLLLHDGGHMVGARFIPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELVRAFHDA 689
Cdd:cd07116    110 FAgciraqEGSISEIDENTVAYHFHEPLGVVGQIIPWNFPLLMATWKLAPALAAGNCVVLKPAEQTPASILVLMELIGDL 189
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  690 gIPEDLVVLAPLEDGDVSRHLVTHKDVDRVVLTGSYDTARLFRSWKPD--MHLLGETSGKNAIIVTPS-ADPDIAVRDAV 766
Cdd:cd07116    190 -LPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYASEniIPVTLELGGKSPNIFFADvMDADDAFFDKA 268
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  767 YSAFA----HAGQKCSASSLLVLVSSagTSERIARQLVDATASLRVRLPLSLDSQMGPVVVPDD-EKAVR--------GL 833
Cdd:cd07116    269 LEGFVmfalNQGEVCTCPSRALIQES--IYDRFMERALERVKAIKQGNPLDTETMIGAQASLEQlEKILSyidigkeeGA 346
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  834 TTLGSGEHWVLkPRYLGDGLWTPGIRAGVVPGSEFHlTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLDATELA 913
Cdd:cd07116    347 EVLTGGERNEL-GGLLGGGYYVPTTFKGGNKMRIFQ-EEIFGPVLAVTTFKDEEEALEIANDTLYGLGAGVWTRDGNTAY 424
                          410       420       430
                   ....*....|....*....|....*....|....*....
gi 2219515474  914 IWLEGVQAGNLYVNrgITGAIVRRQPFGGWKRSAIGSTT 952
Cdd:cd07116    425 RMGRGIQAGRVWTN--CYHLYPAHAAFGGYKQSGIGREN 461
aldehy_Rv0768 TIGR04284
aldehyde dehydrogenase, Rv0768 family; This family describes a branch of the aldehyde ...
533-949 3.38e-18

aldehyde dehydrogenase, Rv0768 family; This family describes a branch of the aldehyde dehydrogenase (NAD) family (see pfam00171) that includes Rv0768 from Mycobacterium tuberculosis. All members of this family belong to species predicted to synthesize mycofactocin, suggesting that this enzyme or another upstream or downstream in the same pathway might be mycofactocin-dependent. However, the taxonomic range of this family is not nearly broad enough to make that relationship conclusive. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 275104  Cd Length: 480  Bit Score: 89.06  E-value: 3.38e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  533 EVEAGAARLATNAEVDTLVTATAEA--AGVWqSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTID-QSDPEVSEA 609
Cdd:TIGR04284   25 EEVLGVAADATAADMDAAIAAARRAfdETDW-SRDTALRVRCLRQLRDALRAHVEELRELTIAEVGAPRMlTAGAQLEGP 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  610 ID---FCHHYAESSLLLHDGGHMV--------GARFIPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRC 678
Cdd:TIGR04284  104 VDdlgFAADLAESYAWTTDLGVASpmgiptrrTLRREAVGVVGAITPWNFPHQINLAKLGPALAAGNTVVLKPAPDTPWC 183
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  679 AAELVR-AFHDAGIPEDLVVLAPLEDGDVSRHLVTHKDVDRVVLTGSYDTAR--LFRSWKPDMHLLGETSGKNAIIVTPS 755
Cdd:TIGR04284  184 AAVLGElIAEHTDFPPGVVNIVTSSDHRLGALLAKDPRVDMVSFTGSTATGRavMADAAATLKKVFLELGGKSAFIVLDD 263
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  756 ADPDIAVRDAVYSAFAHAGQKCSASSLLVlVSSAGTSERIArQLVDATASLRVRLPLSLDSQMGPVVVPDDEKAVRGLTT 835
Cdd:TIGR04284  264 ADLAAACSMAAFTVCMHAGQGCAITTRLV-VPRARYDEAVA-AAAATMGSIKPGDPADPGTVCGPVISARQRDRVQSYLD 341
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  836 LGSGEHWVL-----KPRYLGDGLWT-PGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLDA 909
Cdd:TIGR04284  342 LAVAEGGRFacgggRPADRDRGFFVePTVIAGLDNNARVAREEIFGPVLTVIAHDGDDDAVRIANDSPYGLSGTVFGADP 421
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|.
gi 2219515474  910 TELAIWLEGVQAGNLYVNRGI-TGAIVrrqPFGGWKRSAIG 949
Cdd:TIGR04284  422 ERAAAVAARVRTGTVNVNGGVwYSADA---PFGGYKQSGIG 459
ALDH_KGSADH-like cd07084
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ...
547-957 3.60e-17

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: 85.75  E-value: 3.60e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  547 VDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQsdpevseAIDFCHHYAE-------- 618
Cdd:cd07084      1 PERALLAADISTKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMF-------AENICGDQVQlrarafvi 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  619 SSLLLHDG-------GHMVGARF--IPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELVRAFHDA 689
Cdd:cd07084     74 YSYRIPHEpgnhlgqGLKQQSHGyrWPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYA 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  690 GI--PEDLVVLAplEDGDVSRHLVTHKDVDRVVLTGSYDTARLFRSWKPDMHLLGETSGKNAIIVTPSADP-DIAVRDAV 766
Cdd:cd07084    154 GLlpPEDVTLIN--GDGKTMQALLLHPNPKMVLFTGSSRVAEKLALDAKQARIYLELAGFNWKVLGPDAQAvDYVAWQCV 231
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  767 YSAFAHAGQKCSASS-LLVLVSSAGtseriaRQLVDATASLRVRLPLSlDSQMGPVVVPDDEKAV--------RGLTTLG 837
Cdd:cd07084    232 QDMTACSGQKCTAQSmLFVPENWSK------TPLVEKLKALLARRKLE-DLLLGPVQTFTTLAMIahmenllgSVLLFSG 304
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  838 SGEHWVLKPRYLGdglwtPGIRAGV-VPGSE------FHLTEYFAPV--IGVMRVDTLQEAIEAVNAVDYGLTSGIQT-- 906
Cdd:cd07084    305 KELKNHSIPSIYG-----ACVASALfVPIDEilktyeLVTEEIFGPFaiVVEYKKDQLALVLELLERMHGSLTAAIYSnd 379
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2219515474  907 ---LDATELAIWLEGVQagnLYVNRGITGAIVRRQPFGGWKRSAIGstTKAGGP 957
Cdd:cd07084    380 pifLQELIGNLWVAGRT---YAILRGRTGVAPNQNHGGGPAADPRG--AGIGGP 428
ALDH_AlkH-like cd07134
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ...
558-950 4.09e-11

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: 66.48  E-value: 4.09e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  558 AGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSD-----PEVSEAIDFCHHYAE--------SSLLlh 624
Cdd:cd07134     11 ALALRASTAAERIAKLKRLKKAILARREEIIAALAADFRKPAAEVDlteilPVLSEINHAIKHLKKwmkpkrvrTPLL-- 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  625 dgghMVGA----RFIPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKP---APPARRCAAELVR-AFhdagiPEDLV 696
Cdd:cd07134     89 ----LFGTkskiRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPselTPHTSAVIAKIIReAF-----DEDEV 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  697 vlAPLE-DGDVSRHLVThKDVDRVVLTGSYDTARLFrswkpdM-----HLLG---ETSGKNAIIVTPSADPDIAVRDAVY 767
Cdd:cd07134    160 --AVFEgDAEVAQALLE-LPFDHIFFTGSPAVGKIV------MaaaakHLASvtlELGGKSPTIVDETADLKKAAKKIAW 230
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  768 SAFAHAGQKCSA-----------SSLLVLVSSA-----GTSERIAR-----QLVDATASLRVRLPLsldsqmgpvvvpdD 826
Cdd:cd07134    231 GKFLNAGQTCIApdyvfvhesvkDAFVEHLKAEiekfyGKDAARKAspdlaRIVNDRHFDRLKGLL-------------D 297
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  827 EKAVRGLTTLGSGEHwVLKPRYLGdglwtPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQT 906
Cdd:cd07134    298 DAVAKGAKVEFGGQF-DAAQRYIA-----PTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFS 371
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....
gi 2219515474  907 LDATELAIWLEGVQAGNLYVNRGITGAIVRRQPFGGWKRSAIGS 950
Cdd:cd07134    372 KDKANVNKVLARTSSGGVVVNDVVLHFLNPNLPFGGVNNSGIGS 415
ALDH_F14-YMR110C cd07135
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ...
633-950 1.27e-10

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: 64.93  E-value: 1.27e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  633 RFIPVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCA---AELVRAFHD--------AGIPEdlvvlapl 701
Cdd:cd07135    105 RKEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAallAELVPKYLDpdafqvvqGGVPE-------- 176
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  702 edgdVSRhLVTHKdVDRVVLTGSYDTARLFrSWKPDMHL------LGetsGKNAIIVTPSADPDIAVRDAVYSAFAHAGQ 775
Cdd:cd07135    177 ----TTA-LLEQK-FDKIFYTGSGRVGRII-AEAAAKHLtpvtleLG---GKSPVIVTKNADLELAAKRILWGKFGNAGQ 246
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  776 KC-SASSLLV-------LVSSAGT--SERIARQLVDATASLRV-------RLPLSLDSQMGPVVVPDDEKAvrglttlgs 838
Cdd:cd07135    247 ICvAPDYVLVdpsvydeFVEELKKvlDEFYPGGANASPDYTRIvnprhfnRLKSLLDTTKGKVVIGGEMDE--------- 317
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  839 gehwvlKPRYLgdglwTPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLDATELAIWLEG 918
Cdd:cd07135    318 ------ATRFI-----PPTIVSDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTR 386
                          330       340       350
                   ....*....|....*....|....*....|..
gi 2219515474  919 VQAGNLYVNRGITGAIVRRQPFGGWKRSAIGS 950
Cdd:cd07135    387 TRSGGVVINDTLIHVGVDNAPFGGVGDSGYGA 418
ALDH_F3-13-14_CALDH-like cd07087
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ...
636-950 1.79e-10

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: 64.47  E-value: 1.79e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  636 PVDVTVVASPWNFP--LAIP----------TGgvaaalaagsavILKPAPPARRCAAELVRAFHDAgIPEDLVVLAPLeD 703
Cdd:cd07087    100 PLGVVLIIGPWNYPlqLALApligaiaagnTV------------VLKPSELAPATSALLAKLIPKY-FDPEAVAVVEG-G 165
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  704 GDVSRHLVTHKdVDRVVLTGSYDTARLFrswkpdM-----HL------LGetsGKNAIIVTPSADPDIAVRDAVYSAFAH 772
Cdd:cd07087    166 VEVATALLAEP-FDHIFFTGSPAVGKIV------MeaaakHLtpvtleLG---GKSPCIVDKDANLEVAARRIAWGKFLN 235
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  773 AGQKCSASS-LLVlvssagtSERIARQLVDAtaslrvrLPLSLDSQMG--PVVVPD-----DEKAVRGLTTLGSGEHWVL 844
Cdd:cd07087    236 AGQTCIAPDyVLV-------HESIKDELIEE-------LKKAIKEFYGedPKESPDygriiNERHFDRLASLLDDGKVVI 301
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  845 KPRYLGDGLW-TPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLDATELAIWLEGVQAGN 923
Cdd:cd07087    302 GGQVDKEERYiAPTILDDVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGG 381
                          330       340
                   ....*....|....*....|....*..
gi 2219515474  924 LYVNRGITGAIVRRQPFGGWKRSAIGS 950
Cdd:cd07087    382 VCVNDVLLHAAIPNLPFGGVGNSGMGA 408
PRK11903 PRK11903
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
562-913 6.43e-09

3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;


Pssm-ID: 237016 [Multi-domain]  Cd Length: 521  Bit Score: 60.10  E-value: 6.43e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  562 QSLDPAERAAALHRVGDVLAARRAELIEVAGSEAGKTIDQSDPEVSEAIDFCHHYAESSLLLHDGGHMVGA--------- 632
Cdd:PRK11903    58 RALTYAQRAALLAAIVKVLQANRDAYYDIATANSGTTRNDSAVDIDGGIFTLGYYAKLGAALGDARLLRDGeavqlgkdp 137
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  633 ----RFIPVDVTVVA---SPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELVRAFHDAGI-PEDLVVLAPLEDG 704
Cdd:PRK11903   138 afqgQHVLVPTRGVAlfiNAFNFPAWGLWEKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGIlPAGALSVVCGSSA 217
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  705 DVSRHLvthKDVDRVVLTGSYDTARLFRSW----KPDMHLLGETSGKNAIIVTPSADP-----DIAVRDAVYSAFAHAGQ 775
Cdd:PRK11903   218 GLLDHL---QPFDVVSFTGSAETAAVLRSHpavvQRSVRVNVEADSLNSALLGPDAAPgseafDLFVKEVVREMTVKSGQ 294
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  776 KCSASSlLVLVSSAgTSERIARQLVDATASLRVRLPLSLDSQMGPVVVPDDEKAVR-GLTTLGSGEHWVLKPRYLGDGLW 854
Cdd:PRK11903   295 KCTAIR-RIFVPEA-LYDAVAEALAARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRaGLAALRAQAEVLFDGGGFALVDA 372
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2219515474  855 TPGIRAGVVP----------GSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLDATELA 913
Cdd:PRK11903   373 DPAVAACVGPtllgasdpdaATAVHDVEVFGPVATLLPYRDAAHALALARRGQGSLVASVYSDDAAFLA 441
PTZ00381 PTZ00381
aldehyde dehydrogenase family protein; Provisional
636-950 1.25e-08

aldehyde dehydrogenase family protein; Provisional


Pssm-ID: 240392  Cd Length: 493  Bit Score: 58.89  E-value: 1.25e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  636 PVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAaELVRAFHDAGIPEDLVVLapLEDG-DVSRHLVTHK 714
Cdd:PTZ00381   109 PLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTS-KLMAKLLTKYLDPSYVRV--IEGGvEVTTELLKEP 185
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  715 dVDRVVLTGSYDTARLFRSWKPDmHLLG---ETSGKNAIIVTPSADPDIAVRDAVYSAFAHAGQKCSASSLLVLvssagt 791
Cdd:PTZ00381   186 -FDHIFFTGSPRVGKLVMQAAAE-NLTPctlELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLV------ 257
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  792 SERIARQLVDAtaslrvrLPLSLDSQMGP----------VVVPDDEKAVRGLTTLGSGEHWV-----LKPRYLgdglwTP 856
Cdd:PTZ00381   258 HRSIKDKFIEA-------LKEAIKEFFGEdpkksedysrIVNEFHTKRLAELIKDHGGKVVYggevdIENKYV-----AP 325
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  857 GIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLDATELAIWLEGVQAGNLYVNRGITGAIVR 936
Cdd:PTZ00381   326 TIIVNPDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDCVFHLLNP 405
                          330
                   ....*....|....
gi 2219515474  937 RQPFGGWKRSAIGS 950
Cdd:PTZ00381   406 NLPFGGVGNSGMGA 419
ALDH_F3FHI cd07137
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ...
636-950 2.75e-08

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: 57.81  E-value: 2.75e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  636 PVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKP---APPARRCAAELVRAFHDAGipedlvVLAPLEDG-DVSRHLV 711
Cdd:cd07137    101 PLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPselAPATSALLAKLIPEYLDTK------AIKVIEGGvPETTALL 174
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  712 THKdVDRVVLTGSYDTARLFRSwKPDMHLLG---ETSGKNAIIVTPSADPDIAVRDAVYSAF-AHAGQKCSASSLLVlvs 787
Cdd:cd07137    175 EQK-WDKIFFTGSPRVGRIIMA-AAAKHLTPvtlELGGKCPVIVDSTVDLKVAVRRIAGGKWgCNNGQACIAPDYVL--- 249
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  788 sagTSERIARQLVDAtaslrvrLPLSLDSQMGPvvvpdDEKAVRGLTTLGSGEHWVLKPRYLGDglwtPGIRAGVVPG-- 865
Cdd:cd07137    250 ---VEESFAPTLIDA-------LKNTLEKFFGE-----NPKESKDLSRIVNSHHFQRLSRLLDD----PSVADKIVHGge 310
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  866 -------------------SEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLDATELAIWLEGVQAGNLYV 926
Cdd:cd07137    311 rdeknlyieptilldppldSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTF 390
                          330       340
                   ....*....|....*....|....
gi 2219515474  927 NRGITGAIVRRQPFGGWKRSAIGS 950
Cdd:cd07137    391 NDTVVQYAIDTLPFGGVGESGFGA 414
PLN02681 PLN02681
proline dehydrogenase
270-428 2.54e-07

proline dehydrogenase


Pssm-ID: 215366 [Multi-domain]  Cd Length: 455  Bit Score: 54.71  E-value: 2.54e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  270 QAYLPDslgAMQRLQEwASRRVAAGGSRIKVRVVKGANLSMEKVDAEIHGWELTTWPSKQATDTNYKRMLSWAMTPERTR 349
Cdd:PLN02681   274 QAYLKD---ARERLRL-DLERSEREGVPLGAKLVRGAYLSLERRLAASLGVPSPVHDTIQDTHACYNRCAEFLLEKASNG 349
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  350 AIRLGVAGQNLFDIAFAYELRAARGVE---DGVEFEMLSGMATGLQEVVRRDTGHLLLYVPVvdpHEFDVAISYLVRRLE 426
Cdd:PLN02681   350 DGEVMLATHNVESGELAAAKMNELGLHkgdPRVQFAQLLGMSDNLSFGLGNAGFRVSKYLPY---GPVEEVIPYLLRRAE 426

                   ..
gi 2219515474  427 EN 428
Cdd:PLN02681   427 EN 428
ALDH-like cd07077
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ...
563-806 5.69e-07

NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde dehydrogenase-like (ALDH-like) group of the ALDH superfamily of NAD(P)+-dependent enzymes which, 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. This group includes families ALDH18, ALDH19, and ALDH20 and represents 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: 143396 [Multi-domain]  Cd Length: 397  Bit Score: 53.38  E-value: 5.69e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  563 SLDPAERAAALHRVGDVLAARRAELIEVAGSEAG-------------------KTIDQSDPEVSEAIDFCHHYAEssLLL 623
Cdd:cd07077     12 VNHDEQRDLIINAIANALYDTRQRLASEAVSERGayirslianwiammgcsesKLYKNIDTERGITASVGHIQDV--LLP 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  624 HDGGHMVgaRFIPVDVTVVASPWNFPLAIPTGGVAAALAAGSAvILKPAPPA---RRCAAELVRAFHDAGIPEDLVVLAP 700
Cdd:cd07077     90 DNGETYV--RAFPIGVTMHILPSTNPLSGITSALRGIATRNQC-IFRPHPSApftNRALALLFQAADAAHGPKILVLYVP 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  701 LEDGDVSRHLVTHKDVDRVVLTGSYDTARLFRSWKPDMHLLGETSGKNAIIVTPSADPDIAVRDAVYSAFaHAGQKCSAS 780
Cdd:cd07077    167 HPSDELAEELLSHPKIDLIVATGGRDAVDAAVKHSPHIPVIGFGAGNSPVVVDETADEERASGSVHDSKF-FDQNACASE 245
                          250       260
                   ....*....|....*....|....*...
gi 2219515474  781 SLLVLVSSAGTS--ERIARQLVDATASL 806
Cdd:cd07077    246 QNLYVVDDVLDPlyEEFKLKLVVEGLKV 273
ALDH_MaoC-N cd07128
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ...
668-913 1.48e-06

N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC dehydratase, a monoamine oxidase regulatory protein. Orthologs of MaoC include PaaZ (Escherichia coli) and PaaN (Pseudomonas putida), which are putative ring-opening enzymes of the aerobic phenylacetic acid (PA) catabolic pathway. The C-terminal domain of MaoC has sequence similarity to enoyl-CoA hydratase. Also included in this CD is a novel Burkholderia xenovorans LB400 ALDH of the aerobic benzoate oxidation (box) pathway. This pathway involves first the synthesis of a CoA thio-esterified aromatic acid, with subsequent dihydroxylation and cleavage steps, yielding the CoA thio-esterified aliphatic aldehyde, 3,4-dehydroadipyl-CoA semialdehyde, which is further converted into its corresponding CoA acid by the Burkholderia LB400 ALDH.


Pssm-ID: 143446 [Multi-domain]  Cd Length: 513  Bit Score: 52.27  E-value: 1.48e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  668 ILKPAPPARRCAAELVRAFHDAGI-PEDLVVLAPLEDGDVSRHLvTHKDVdrVVLTGSYDTARLFRSwKPDMHLLG---- 742
Cdd:cd07128    176 IVKPATATAYLTEAVVKDIVESGLlPEGALQLICGSVGDLLDHL-GEQDV--VAFTGSAATAAKLRA-HPNIVARSirfn 251
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  743 -ETSGKNAIIVTPSADP-----DIAVRDAVYSAFAHAGQKCSASSlLVLVsSAGTSERIARQLVDATASLRVRLPLSLDS 816
Cdd:cd07128    252 aEADSLNAAILGPDATPgtpefDLFVKEVAREMTVKAGQKCTAIR-RAFV-PEARVDAVIEALKARLAKVVVGDPRLEGV 329
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  817 QMGPVVVPDDEKAVR-GLTTLGSGEHWVLKPRYLGDGLWTPGIRAGVVP-----------GSEFHLTEYFAPVIGVMRVD 884
Cdd:cd07128    330 RMGPLVSREQREDVRaAVATLLAEAEVVFGGPDRFEVVGADAEKGAFFPptlllcddpdaATAVHDVEAFGPVATLMPYD 409
                          250       260
                   ....*....|....*....|....*....
gi 2219515474  885 TLQEAIEAVNAVDYGLTSGIQTLDATELA 913
Cdd:cd07128    410 SLAEAIELAARGRGSLVASVVTNDPAFAR 438
ALDH_KGSADH cd07129
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ...
547-596 3.49e-05

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: 47.92  E-value: 3.49e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2219515474  547 VDTLVTATAEAAGVWQSLDPAERAAALHRVGDVLAARRAELIEVAGSEAG 596
Cdd:cd07129      1 VDAAAAAAAAAFESYRALSPARRAAFLEAIADEIEALGDELVARAHAETG 50
ALDH_F20_ACDH cd07122
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ...
668-964 4.91e-05

Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH, EC=1.2.1.10), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA . The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH and may be critical enzymes in the fermentative pathway.


Pssm-ID: 143440 [Multi-domain]  Cd Length: 436  Bit Score: 47.10  E-value: 4.91e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  668 ILKPAPPARRC---AAELVR-AFHDAGIPEDLVVLAPLEDGDVSRHLVTHKDVDRVVLTGSydtarlfrswkPDMHLLGE 743
Cdd:cd07122    127 IFSPHPRAKKCsieAAKIMReAAVAAGAPEGLIQWIEEPSIELTQELMKHPDVDLILATGG-----------PGMVKAAY 195
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  744 TSGKNAIIVTP---------SADPDIAVRDAVYS-AFAHaGQKCSASSLLVLVSSagtserIARQLVDATaslrvrlpls 813
Cdd:cd07122    196 SSGKPAIGVGPgnvpayideTADIKRAVKDIILSkTFDN-GTICASEQSVIVDDE------IYDEVRAEL---------- 258
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  814 ldSQMGPVVVPDDEKAvrglttlgsgehwvlkprYLGDGLWTPG--------------I--RAGV-VP------------ 864
Cdd:cd07122    259 --KRRGAYFLNEEEKE------------------KLEKALFDDGgtlnpdivgksaqkIaeLAGIeVPedtkvlvaeetg 318
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  865 -GSEFHLT-EYFAPVIGVMRVDTLQEAIEAVNA-VDY---GLTSGIQTLD---ATELAIwleGVQAGNLYVNRGitgaiv 935
Cdd:cd07122    319 vGPEEPLSrEKLSPVLAFYRAEDFEEALEKARElLEYggaGHTAVIHSNDeevIEEFAL---RMPVSRILVNTP------ 389
                          330       340
                   ....*....|....*....|....*....
gi 2219515474  936 rrQPFGGwkrsaIGSTTKAGGPSYLLGLG 964
Cdd:cd07122    390 --SSLGG-----IGDTYNGLAPSLTLGCG 411
ALDH_F12_P5CDH cd07126
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ...
624-803 9.31e-05

Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12), family 12: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. P5CDH is a mitochondrial enzyme involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. The P5CDH, ALDH12A1 gene, in Arabidopsis, has been identified as an osmotic-stress-inducible ALDH gene. This CD contains both Viridiplantae and Alveolata P5CDH sequences.


Pssm-ID: 143444  Cd Length: 489  Bit Score: 46.33  E-value: 9.31e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  624 HDGGHMVGARFIPVDVTVVAsPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELVRAFHDAGIP-EDLVVLAplE 702
Cdd:cd07126    131 HQGQQSSGYRWPYGPVAIIT-PFNFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPaTDVDLIH--S 207
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  703 DGDVSRHLVTHKDVDRVVLTGSYDTA-RLFRSWKPDMHLlgETSGKNAIIVTPS-ADPDIAVRDAVYSAFAHAGQKCSAS 780
Cdd:cd07126    208 DGPTMNKILLEANPRMTLFTGSSKVAeRLALELHGKVKL--EDAGFDWKILGPDvSDVDYVAWQCDQDAYACSGQKCSAQ 285
                          170       180       190
                   ....*....|....*....|....*....|.
gi 2219515474  781 SLLVLVSS---AGTSERIA-----RQLVDAT 803
Cdd:cd07126    286 SILFAHENwvqAGILDKLKalaeqRKLEDLT 316
ALDH_F3AB cd07132
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ...
636-950 1.99e-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: 45.29  E-value: 1.99e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  636 PVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCA---AELvrafhdagIPEDL------VVLAPLEDgdv 706
Cdd:cd07132    100 PLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAkllAEL--------IPKYLdkecypVVLGGVEE--- 168
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  707 SRHLVTHKdVDRVVLTGSYDTARLFRSwKPDMHL------LGetsGKNAIIVTPSADPDIAVRDAVYSAFAHAGQKCSAS 780
Cdd:cd07132    169 TTELLKQR-FDYIFYTGSTSVGKIVMQ-AAAKHLtpvtleLG---GKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIAP 243
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  781 SlLVLVssagtSERIARQLVDAtaslrvrLPLSLDSQMG--PVVVPD------DEKAVRGLTTLGSGE-----HWVLKPR 847
Cdd:cd07132    244 D-YVLC-----TPEVQEKFVEA-------LKKTLKEFYGedPKESPDygriinDRHFQRLKKLLSGGKvaiggQTDEKER 310
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  848 YLgdglwTPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLDATELAIWLEGVQAGNLYVN 927
Cdd:cd07132    311 YI-----APTVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCVN 385
                          330       340
                   ....*....|....*....|...
gi 2219515474  928 RGITGAIVRRQPFGGWKRSAIGS 950
Cdd:cd07132    386 DTIMHYTLDSLPFGGVGNSGMGA 408
PLN02203 PLN02203
aldehyde dehydrogenase
636-949 6.29e-04

aldehyde dehydrogenase


Pssm-ID: 165847 [Multi-domain]  Cd Length: 484  Bit Score: 43.95  E-value: 6.29e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  636 PVDVTVVASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAaelvrAFHDAGIPE--DLVVLAPLEDG-DVSRHLVT 712
Cdd:PLN02203   108 PLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATS-----AFLAANIPKylDSKAVKVIEGGpAVGEQLLQ 182
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  713 HKdVDRVVLTGSYDTARLFRSwKPDMHLLG---ETSGKNAIIV---TPSADPDIAVRDAVYSAF-AHAGQKCSASSlLVL 785
Cdd:PLN02203   183 HK-WDKIFFTGSPRVGRIIMT-AAAKHLTPvalELGGKCPCIVdslSSSRDTKVAVNRIVGGKWgSCAGQACIAID-YVL 259
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  786 VssagtSERIARQLVDAtaslrvrLPLSLDSQMGpvvvpDDEKAVRGLTTLGSGEHWVLKPRYLGDglwtPGIRAGVVPG 865
Cdd:PLN02203   260 V-----EERFAPILIEL-------LKSTIKKFFG-----ENPRESKSMARILNKKHFQRLSNLLKD----PRVAASIVHG 318
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  866 ---------------------SEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLDATELAIWLEGVQAGNL 924
Cdd:PLN02203   319 gsidekklfieptillnppldSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSV 398
                          330       340
                   ....*....|....*....|....*
gi 2219515474  925 YVNRGITGAIVRRQPFGGWKRSAIG 949
Cdd:PLN02203   399 TFNDAIIQYACDSLPFGGVGESGFG 423
PRK15398 PRK15398
aldehyde dehydrogenase;
671-900 9.29e-04

aldehyde dehydrogenase;


Pssm-ID: 237956  Cd Length: 465  Bit Score: 43.35  E-value: 9.29e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  671 PAPPARRCAAELVRAFHDA----GIPEDLVVLAPLEDGDVSRHLVTHKDVDRVVLTGSydtarlfrswkPDMHLLGETSG 746
Cdd:PRK15398   164 PHPGAKKVSLRAIELLNEAivaaGGPENLVVTVAEPTIETAQRLMKHPGIALLVVTGG-----------PAVVKAAMKSG 232
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  747 KNAI---------IVTPSADPDIAVRDAVYSAFAHAGQKCSASSLLVLVSSAgtSERIARQLVDATAslrVRLPLSLDSQ 817
Cdd:PRK15398   233 KKAIgagagnppvVVDETADIEKAARDIVKGASFDNNLPCIAEKEVIVVDSV--ADELMRLMEKNGA---VLLTAEQAEK 307
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  818 MGPVVVPDDEKAVRGlttlgsgehWVLK-PRYLGD--GLWTP-GIRAGVVPGSEFH---LTEYFAPVIGVMRVDTLQEAI 890
Cdd:PRK15398   308 LQKVVLKNGGTVNKK---------WVGKdAAKILEaaGINVPkDTRLLIVETDANHpfvVTELMMPVLPVVRVKDVDEAI 378
                          250
                   ....*....|
gi 2219515474  891 EAVNAVDYGL 900
Cdd:PRK15398   379 ALAVKLEHGN 388
ALDH_F20_ACDH_EutE-like cd07081
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ...
668-906 6.94e-03

Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and related proteins; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA. The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH, and may be critical enzymes in the fermentative pathway.


Pssm-ID: 143400 [Multi-domain]  Cd Length: 439  Bit Score: 40.33  E-value: 6.94e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  668 ILKPAPPAR----RCAAELVRAFHDAGIPEDLVVLAPLEDGDVSRHLVTHKDVDRVVLTGSYDTAR-LFRSWKPdmhLLG 742
Cdd:cd07081    127 IFSPHPRAKkvtqRAATLLLQAAVAAGAPENLIGWIDNPSIELAQRLMKFPGIGLLLATGGPAVVKaAYSSGKP---AIG 203
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  743 ETSGKNAIIVTPSADPDIAVRDAVYSAFAHAGQKCSASSLLVLVSSagtserIARQLVDataslrvrlplSLDSQMGPVV 822
Cdd:cd07081    204 VGAGNTPVVIDETADIKRAVQSIVKSKTFDNGVICASEQSVIVVDS------VYDEVMR-----------LFEGQGAYKL 266
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  823 VPDDEKAVRG--LTTLGSGEHWVLKPRY---LGDGLWTPG------IRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIE 891
Cdd:cd07081    267 TAEELQQVQPviLKNGDVNRDIVGQDAYkiaAAAGLKVPQetriliGEVTSLAEHEPFAHEKLSPVLAMYRAANFADADA 346
                          250
                   ....*....|....*....
gi 2219515474  892 AVNAV----DYGLTSGIQT 906
Cdd:cd07081    347 KALALklegGCGHTSAMYS 365
ALDH_CALDH_CalB cd07133
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ...
567-950 9.94e-03

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: 39.78  E-value: 9.94e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  567 AERAAALHRVGDVLAARRAELIEvagseagkTIDQsdpevseaiDFCHHYAESSLLL--------------HDGGHM--- 629
Cdd:cd07133     20 EERRDRLDRLKALLLDNQDALAE--------AISA---------DFGHRSRHETLLAeilpsiagikharkHLKKWMkps 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  630 ---VGARFIPVDVTV---------VASPWNFPLAIPTGGVAAALAAGSAVILKPAPPARRCAAELVRAFHDAGIPEDLVV 697
Cdd:cd07133     83 rrhVGLLFLPAKAEVeyqplgvvgIIVPWNYPLYLALGPLIAALAAGNRVMIKPSEFTPRTSALLAELLAEYFDEDEVAV 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  698 LapLEDGDVSRHlVTHKDVDRVVLTGSYDTARLFrswkpdM-----HL------LGetsGKNAIIVTPSADPDIAVRDAV 766
Cdd:cd07133    163 V--TGGADVAAA-FSSLPFDHLLFTGSTAVGRHV------MraaaeNLtpvtleLG---GKSPAIIAPDADLAKAAERIA 230
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  767 YSAFAHAGQKCSASSlLVLVsSAGTSERIARQLVDATASLRVRLPLSLDsqMGPVV----------VPDD--EKAVRGLT 834
Cdd:cd07133    231 FGKLLNAGQTCVAPD-YVLV-PEDKLEEFVAAAKAAVAKMYPTLADNPD--YTSIInerhyarlqgLLEDarAKGARVIE 306
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2219515474  835 TLGSGEhwvlkpRYLGDGLWTPGIRAGVVPGSEFHLTEYFAPVIGVMRVDTLQEAIEAVNAVDYGLTSGIQTLDATELAI 914
Cdd:cd07133    307 LNPAGE------DFAATRKLPPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDR 380
                          410       420       430
                   ....*....|....*....|....*....|....*.
gi 2219515474  915 WLEGVQAGNLYVNRGITGAIVRRQPFGGWKRSAIGS 950
Cdd:cd07133    381 VLRRTHSGGVTINDTLLHVAQDDLPFGGVGASGMGA 416
 
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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