|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
54-542 |
0e+00 |
|
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: 947.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 54 NLVQGKWVGSSNWSTVVDPLNGESFIKVAEVDGTGIQPFVESLSSCPKHGVHNPFKAPERYLMLGDVSTKAAHMLSLPKV 133
Cdd:cd07126 1 NLVAGKWKGASNYTTLLDPLNGDKFISVPDTDEDEINEFVDSLRQCPKSGLHNPLKNPERYLLYGDVSHRVAHELRKPEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 134 SDFFTRLIQRVSPKSYQQAFGEVYVTQKFLENFCGDQVRFLARSFAVPGNHLGQQSHGFRWPYGPVAIITPFNFPLEIPV 213
Cdd:cd07126 81 EDFFARLIQRVAPKSDAQALGEVVVTRKFLENFAGDQVRFLARSFNVPGDHQGQQSSGYRWPYGPVAIITPFNFPLEIPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 214 LQLMGALYMGNKPVLKVDTKVSIVMEQMLRLLHTCGLPVEDVDFINSDGKTMNKLLLEGNPRMTLFTGSSKVAEKLANDL 293
Cdd:cd07126 161 LQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKILLEANPRMTLFTGSSKVAERLALEL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 294 NGRVKLEDAGFDWKILGPDVHQEDYIAWVCDQDAYACSGQKCSAQSLLFMHENWSSTSLIRKMKDLAERRKLADLTIGPV 373
Cdd:cd07126 241 HGKVKLEDAGFDWKILGPDVSDVDYVAWQCDQDAYACSGQKCSAQSILFAHENWVQAGILDKLKALAEQRKLEDLTIGPV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 374 LTFTTDSMLEHTNKLLEIPGSKLLFGGQPLENHLIPSIYGAIKPTAVYVPIEEIVKDKNYELVTKEIFGPFQIITDYKSS 453
Cdd:cd07126 321 LTWTTERILDHVDKLLAIPGAKVLFGGKPLTNHSIPSIYGAYEPTAVFVPLEEIAIEENFELVTTEVFGPFQVVTEYKDE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 454 QLSVVLDLIERMHAHLTAAVVSNDPLFLQEVIGKSVNGTTYAGLRARTTGAPQNHWFGPAGDPRGAGIGTPEAIKLVWSC 533
Cdd:cd07126 401 QLPLVLEALERMHAHLTAAVVSNDIRFLQEVLANTVNGTTYAGIRARTTGAPQNHWFGPAGDPRGAGIGTPEAIRLVWSC 480
|
....*....
gi 1540552764 534 HREIIYDLG 542
Cdd:cd07126 481 HREIITDIG 489
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
111-538 |
0e+00 |
|
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: 519.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 111 PERYLMLGDVSTKAAHMLSLPKVSDFFTRLIQRVSPKSYQQAFGEVYVTQK---FLENFCGDQVRFLARSFAV------- 180
Cdd:cd07084 1 PERALLAADISTKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKgwmFAENICGDQVQLRARAFVIysyriph 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 181 -PGNHLGQ----QSHGFRWPYGPVAIITPFNFPLEIPVLQLMGALYMGNKPVLKVDTKVSIVMEQMLRLLHTCG-LPVED 254
Cdd:cd07084 81 ePGNHLGQglkqQSHGYRWPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGlLPPED 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 255 VDFINSDGKTMNKLLLEGNPRMTLFTGSSKVAEKLANDLN-GRVKLEDAGFDWKILGPDVHQEDYIAWVCDQDAYACSGQ 333
Cdd:cd07084 161 VTLINGDGKTMQALLLHPNPKMVLFTGSSRVAEKLALDAKqARIYLELAGFNWKVLGPDAQAVDYVAWQCVQDMTACSGQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 334 KCSAQSLLFMHENWSSTSLIRKMKDLAERRKLADLTIGPVLTFTTDSMLEHTNKLLeipGSKLLFGGQPLENHLIPSIYG 413
Cdd:cd07084 241 KCTAQSMLFVPENWSKTPLVEKLKALLARRKLEDLLLGPVQTFTTLAMIAHMENLL---GSVLLFSGKELKNHSIPSIYG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 414 AIKPTAVYVPIEEIvkDKNYELVTKEIFGPFQIITDYKSSQLSVVLDLIERMHAHLTAAVVSNDPLFLQEVIGKS-VNGT 492
Cdd:cd07084 318 ACVASALFVPIDEI--LKTYELVTEEIFGPFAIVVEYKKDQLALVLELLERMHGSLTAAIYSNDPIFLQELIGNLwVAGR 395
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1540552764 493 TYAGLRARTTGAP-QNHWFGPAGDPRGAGIGTPEAIKLVWSCHREII 538
Cdd:cd07084 396 TYAILRGRTGVAPnQNHGGGPAADPRGAGIGGPEAIKLVWRCHAEQA 442
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
123-538 |
3.20e-69 |
|
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: 229.02 E-value: 3.20e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 123 KAAHMLSLPKVSDFFTRLIQRVSPKSYQQAFGEVYVTQK----FLENFCGDQVRFLARSFAVPGNH--------LGQQSH 190
Cdd:cd07078 12 KAWAALPPAERAAILRKLADLLEERREELAALETLETGKpieeALGEVARAADTFRYYAGLARRLHgevipspdPGELAI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 191 GFRWPYGPVAIITPFNFPLEIPVLQLMGALYMGNKPVLKVDTKVSIVMEQMLRLLHTCGLPVEDVDFINSDGK-TMNKLL 269
Cdd:cd07078 92 VRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVVTGDGDeVGAALA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 270 LEGNPRMTLFTGSSKVAEKLANDLNGRVK---LEDAGFDWKILGPDVhQEDYIAWVCDQDAYACSGQKCSAQSLLFMHEN 346
Cdd:cd07078 172 SHPRVDKISFTGSTAVGKAIMRAAAENLKrvtLELGGKSPLIVFDDA-DLDAAVKGAVFGAFGNAGQVCTAASRLLVHES 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 347 wSSTSLIRKMKDLAERRKLADLT-----IGPVLT----FTTDSMLEHTNKlleiPGSKLLFGGQPLENHlipsiYGA-IK 416
Cdd:cd07078 251 -IYDEFVERLVERVKALKVGNPLdpdtdMGPLISaaqlDRVLAYIEDAKA----EGAKLLCGGKRLEGG-----KGYfVP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 417 PTaVYVPIeeivkDKNYELVTKEIFGPFQIITDYKSsqLSVVLDLIERMHAHLTAAVVSNDPLFLQEVIGKSVNGTTYAG 496
Cdd:cd07078 321 PT-VLTDV-----DPDMPIAQEEIFGPVLPVIPFKD--EEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWIN 392
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1540552764 497 LRARTTGAPQNhwFGPAGDPRGAGIGTPEAIKLVWSCHREII 538
Cdd:cd07078 393 DYSVGAEPSAP--FGGVKQSGIGREGGPYGLEEYTEPKTVTI 432
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
123-538 |
2.10e-52 |
|
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: 182.81 E-value: 2.10e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 123 KAAHMLSLPKVSDFFTRLIQRVSPKSYQQAFGEVYVTQKFLENFCGD------QVRFLA------RSFAVPGNHLGQQSH 190
Cdd:cd06534 8 KAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEvaraidTFRYAAgladklGGPELPSPDPGGEAY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 191 GFRWPYGPVAIITPFNFPLEIPVLQLMGALYMGNKPVLKVDTKVSIVMEQMLRLLHTCGLPVEDVDFINSDGKT-MNKLL 269
Cdd:cd06534 88 VRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGGDEvGAALL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 270 LEGNPRMTLFTGSSKVAEKLANDLNGRVK---LEDAGFDWKILGPDVhQEDYIAWVCDQDAYACSGQKCSAQSLLFMHEn 346
Cdd:cd06534 168 SHPRVDKISFTGSTAVGKAIMKAAAENLKpvtLELGGKSPVIVDEDA-DLDAAVEGAVFGAFFNAGQICTAASRLLVHE- 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 347 wsstslirkmkdlaerrkladltigpvltfttdsmlehtnklleipgskllfggqplenhlipSIYGAIKptAVYVPIEE 426
Cdd:cd06534 246 ---------------------------------------------------------------SIYDEFV--EKLVTVLV 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 427 IVKDKNyELVTKEIFGPFQIITDYKSSQLsvVLDLIERMHAHLTAAVVSNDPLFLQEVIGKSVNGTTYAGLRARTTGAPQ 506
Cdd:cd06534 261 DVDPDM-PIAQEEIFGPVLPVIRFKDEEE--AIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVGPEA 337
|
410 420 430
....*....|....*....|....*....|..
gi 1540552764 507 NHWFGPAGDPRGAGIgtPEAIKLVWSCHREII 538
Cdd:cd06534 338 PFGGVKNSGIGREGG--PYGLEEYTRTKTVVI 367
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
51-478 |
1.73e-27 |
|
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: 115.61 E-value: 1.73e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 51 EVLNLVQGKWV--GSSNWSTVVDPLNGESFIKVAEVDGTGIQPFVESlsscpkhgVHNPFKA------PERYLMLgdvsT 122
Cdd:COG1012 5 EYPLFIGGEWVaaASGETFDVINPATGEVLARVPAATAEDVDAAVAA--------ARAAFPAwaatppAERAAIL----L 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 123 KAAHMLSlpKVSDFFTRLIQRVSPKSYQQAFGEVYVTQKFLENFCGdqvrfLARSF---AVPGNHLGQQSHGFRWPYGPV 199
Cdd:COG1012 73 RAADLLE--ERREELAALLTLETGKPLAEARGEVDRAADFLRYYAG-----EARRLygeTIPSDAPGTRAYVRREPLGVV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 200 AIITPFNFPLEIPVLQLMGALYMGNKPVLKVDTKVSIVMEQMLRLLHTCGLPVEDVDFINSDGKTMNKLLLEgNP--RMT 277
Cdd:COG1012 146 GAITPWNFPLALAAWKLAPALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVA-HPdvDKI 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 278 LFTGSSKVAEKL---ANDLNGRVKLE----DAGfdwkILGPDvhqedyiawvCDQD---------AYACSGQKCSAQSLL 341
Cdd:COG1012 225 SFTGSTAVGRRIaaaAAENLKRVTLElggkNPA----IVLDD----------ADLDaaveaavrgAFGNAGQRCTAASRL 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 342 FMHEnwsstSLIRKMKD-LAERrkLADLTIGPVLTFTT-----------DSMLEHTNKLLEiPGSKLLFGGQPLEN---H 406
Cdd:COG1012 291 LVHE-----SIYDEFVErLVAA--AKALKVGDPLDPGTdmgpliseaqlERVLAYIEDAVA-EGAELLTGGRRPDGeggY 362
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1540552764 407 LIPsiygaikPTavyvpieeIVKD--KNYELVTKEIFGPFQIITDYKSSQlsvvlDLIERMHAH---LTAAVVSNDP 478
Cdd:COG1012 363 FVE-------PT--------VLADvtPDMRIAREEIFGPVLSVIPFDDEE-----EAIALANDTeygLAASVFTRDL 419
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
56-504 |
2.06e-27 |
|
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: 115.75 E-value: 2.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 56 VQGKWVGSSNWSTVVDPLN-GESFIKVAEVDGTGIQPFVESLSSCPKHGVHNPFKAPERYLMlgdvstKAAHMLSLPKVS 134
Cdd:cd07083 23 IGGEWVDTKERMVSVSPFApSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLL------KAADLLRRRRRE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 135 DFFTRLiqRVSPKSYQQAFGEVYVTQKFLENFCGDQVRFLARSFAVPGnHLGQQSHGFRWPYGPVAIITPFNFPLEIPVL 214
Cdd:cd07083 97 LIATLT--YEVGKNWVEAIDDVAEAIDFIRYYARAALRLRYPAVEVVP-YPGEDNESFYVGLGAGVVISPWNFPVAIFTG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 215 QLMGALYMGNKPVLKVDTKVSIVMEQMLRLLHTCGLPVEDVDFINSDGKTMNKLLLEgNPRMTL--FTGSSKVA----EK 288
Cdd:cd07083 174 MIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTE-HERIRGinFTGSLETGkkiyEA 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 289 LANDLNG-----RVKLEDAGFDWKILGPDVHQEDYIAWVCdQDAYACSGQKCSAQSLLFMHENWSSTSLIRKMKDlAERR 363
Cdd:cd07083 253 AARLAPGqtwfkRLYVETGGKNAIIVDETADFELVVEGVV-VSAFGFQGQKCSAASRLILTQGAYEPVLERLLKR-AERL 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 364 KLADLT-----IGPVLTFTT----DSMLEHTNKLLeipgsKLLFGGQPLEnhlipSIYGAIKPTAVyvpiEEivKDKNYE 434
Cdd:cd07083 331 SVGPPEengtdLGPVIDAEQeakvLSYIEHGKNEG-----QLVLGGKRLE-----GEGYFVAPTVV----EE--VPPKAR 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 435 LVTKEIFGPFQIITDYKSSQLSVVLDLIERMHAHLTAAVVSNDPLFLQEVIGKSVNGTTYagLRARTTGA 504
Cdd:cd07083 395 IAQEEIFGPVLSVIRYKDDDFAEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLY--INRKITGA 462
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
137-478 |
4.30e-27 |
|
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: 114.17 E-value: 4.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 137 FTRLIQRVSPKSYQQAFGEVYVTQKFLENFCGDQVRFLARSFAVPGNHLGQQshgFRWPYGPVAIITPFNFPLEIPVLQL 216
Cdd:pfam00171 71 LAELETLENGKPLAEARGEVDRAIDVLRYYAGLARRLDGETLPSDPGRLAYT---RREPLGVVGAITPWNFPLLLPAWKI 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 217 MGALYMGNKPVLKVDTKVSIVMEQMLRLLHTCGLPVEDVDFINSDGKTMNKLLLEgNP--RMTLFTGSSKVAEKLANDLN 294
Cdd:pfam00171 148 APALAAGNTVVLKPSELTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVE-HPdvRKVSFTGSTAVGRHIAEAAA 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 295 GRVK---LEDAGFDWKILGPDVHQEDYIAWVCdQDAYACSGQKCSAQSLLFMHEnwsstS----LIRKMKDLAERRKLAD 367
Cdd:pfam00171 227 QNLKrvtLELGGKNPLIVLEDADLDAAVEAAV-FGAFGNAGQVCTATSRLLVHE-----SiydeFVEKLVEAAKKLKVGD 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 368 -----LTIGPVltfTTDSMLEHTNKLLEI---PGSKLLFGGQPLENHlipsiyGA-IKPTAVYVPieeivkDKNYELVTK 438
Cdd:pfam00171 301 pldpdTDMGPL---ISKAQLERVLKYVEDakeEGAKLLTGGEAGLDN------GYfVEPTVLANV------TPDMRIAQE 365
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1540552764 439 EIFGPFQIITDYKSSQlsvvlDLIERMHAH---LTAAVVSNDP 478
Cdd:pfam00171 366 EIFGPVLSVIRFKDEE-----EAIEIANDTeygLAAGVFTSDL 403
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
147-511 |
6.91e-23 |
|
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: 101.92 E-value: 6.91e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 147 KSYQQAFGEVYVTQKFLENFCgDQVRFLA--RSFAVPGNHlgqqSHGFRWPYGPVAIITPFNFPLEIPVLQLMGALYMGN 224
Cdd:cd07124 121 KNWAEADADVAEAIDFLEYYA-REMLRLRgfPVEMVPGED----NRYVYRPLGVGAVISPWNFPLAILAGMTTAALVTGN 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 225 KPVLKVDTKVSIVMEQMLRLLHTCGLPVEDVDFINSDGKTMNKLLLEgNPRMTL--FTGSSKVA----EKLANDLNG--- 295
Cdd:cd07124 196 TVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVGDYLVE-HPDVRFiaFTGSREVGlriyERAAKVQPGqkw 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 296 --RVKLEDAGFDWKILGPDVHQEDYIAWVCdQDAYACSGQKCSAQSLLFMHENWSSTsLIRKMKDLAERRKLAD-----L 368
Cdd:cd07124 275 lkRVIAEMGGKNAIIVDEDADLDEAAEGIV-RSAFGFQGQKCSACSRVIVHESVYDE-FLERLVERTKALKVGDpedpeV 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 369 TIGPVLtftTDSMLEHTNKLLEI--PGSKLLFGGQPLEN----HLI-PSIYGAIKPTAvyvpieeivkdknyELVTKEIF 441
Cdd:cd07124 353 YMGPVI---DKGARDRIRRYIEIgkSEGRLLLGGEVLELaaegYFVqPTIFADVPPDH--------------RLAQEEIF 415
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1540552764 442 GPFQIITDYKSsqLSVVLDLIERMHAHLTAAVVSNDPLFLQEVIGKSVNGTTYAGlRaRTTGA-PQNHWFG 511
Cdd:cd07124 416 GPVLAVIKAKD--FDEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYAN-R-KITGAlVGRQPFG 482
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
112-477 |
2.79e-22 |
|
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: 99.81 E-value: 2.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 112 ERYLMLgdvsTKAAHMLSLPKvsDFFTRLIQRVSPKSYQQAFGEVYVTQKFLENFCGDQVRFLARSFAVPGNHLGQQSHG 191
Cdd:cd07094 44 ERMAIL----ERAADLLKKRA--EEFAKIIACEGGKPIKDARVEVDRAIDTLRLAAEEAERIRGEEIPLDATQGSDNRLA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 192 F--RWPYGPVAIITPFNFPLEIPVLQLMGALYMGNKPVLKVDTKVSIVMEQMLRLLHTCGLPVEDVDFINSDGKTM-NKL 268
Cdd:cd07094 118 WtiREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASKTPLSALELAKILVEAGVPEGVLQVVTGEREVLgDAF 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 269 LLEGNPRMTLFTGSSKVAEKLANDLNG-RVKLEDAGFDWKILGPDVhQEDYIAWVCDQDAYACSGQKCSAQSLLFMHEnw 347
Cdd:cd07094 198 AADERVAMLSFTGSAAVGEALRANAGGkRIALELGGNAPVIVDRDA-DLDAAIEALAKGGFYHAGQVCISVQRIYVHE-- 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 348 sstSLIRKMKDLAERR--KL-------ADLTIGPVLTFTTDSMLE-HTNKLLEiPGSKLLFGGQPLENHLIPSIYGAIKP 417
Cdd:cd07094 275 ---ELYDEFIEAFVAAvkKLkvgdpldEDTDVGPLISEEAAERVErWVEEAVE-AGARLLCGGERDGALFKPTVLEDVPR 350
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 418 TAvyvpieeivkdknyELVTKEIFGPFQIItdYKSSQLSVVLDLIERMHAHLTAAVVSND 477
Cdd:cd07094 351 DT--------------KLSTEETFGPVVPI--IRYDDFEEAIRIANSTDYGLQAGIFTRD 394
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
195-477 |
6.66e-19 |
|
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: 89.95 E-value: 6.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 195 PYGPVAIITPFNFPLEIPVLQLMGALYMGNKPVLKVDTKVSIVMEQMLRLLHTCGLPVEDVDFINSDGKTMNKLLLEgNP 274
Cdd:cd07125 167 GRGVFVCISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVA-HP 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 275 R--MTLFTGSSKVAEKLANDLNGRVkledagfdwkilGPDVHqedYIA-----------------WVCD---QDAYACSG 332
Cdd:cd07125 246 RidGVIFTGSTETAKLINRALAERD------------GPILP---LIAetggknamivdstalpeQAVKdvvQSAFGSAG 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 333 QKCSAQSLLFMHENwSSTSLIRKMKDLAerrklADLTIGPVLTFTTDsmlehTNKLLEIPGSKLLFGGQPLEN----HLI 408
Cdd:cd07125 311 QRCSALRLLYLQEE-IAERFIEMLKGAM-----ASLKVGDPWDLSTD-----VGPLIDKPAGKLLRAHTELMRgeawLIA 379
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1540552764 409 PSIYGAIKPTavYVP--IEEIVKDKNYelvTKEIFGPFQIITDYKSSQLSVVLDLIERMHAHLTAAVVSND 477
Cdd:cd07125 380 PAPLDDGNGY--FVApgIIEIVGIFDL---TTEVFGPILHVIRFKAEDLDEAIEDINATGYGLTLGIHSRD 445
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
68-477 |
3.23e-18 |
|
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: 87.27 E-value: 3.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 68 TVVDPLNGEsfiKVAEVDGTGIQPFVESLSSCpKHGVHNPFKAP--ERYLMLgdvsTKAAHMLSlpKVSDFFTRLIQRVS 145
Cdd:cd07149 2 EVISPYDGE---VIGRVPVASEEDVEKAIAAA-KEGAKEMKSLPayERAEIL----ERAAQLLE--ERREEFARTIALEA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 146 PKSYQQAFGEVYVTQKFLEnFCGDQVRFLARSF----AVPGnhlGQQSHGF--RWPYGPVAIITPFNFPLEIPVLQLMGA 219
Cdd:cd07149 72 GKPIKDARKEVDRAIETLR-LSAEEAKRLAGETipfdASPG---GEGRIGFtiREPIGVVAAITPFNFPLNLVAHKVGPA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 220 LYMGNKPVLKVDTKVSIVMEQMLRLLHTCGLPVEDVDFINSDGKTMNKLLLEG-NPRMTLFTGSSKVAEKLANDLnG--R 296
Cdd:cd07149 148 IAAGNAVVLKPASQTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDpRVRMISFTGSPAVGEAIARKA-GlkK 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 297 VKLEDAGFDWKILGPDVHQEDYIAwVCDQDAYACSGQKC-SAQSlLFMHENWSStSLIRKMKDlaerrKLADLTIGPVLT 375
Cdd:cd07149 227 VTLELGSNAAVIVDADADLEKAVE-RCVSGAFANAGQVCiSVQR-IFVHEDIYD-EFLERFVA-----ATKKLVVGDPLD 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 376 FTTD-SMLEHTNKLLEI---------PGSKLLFGGQPLENHLIPSIYGAIKPTAvyvpieeivkdknyELVTKEIFGPFQ 445
Cdd:cd07149 299 EDTDvGPMISEAEAERIeewveeaveGGARLLTGGKRDGAILEPTVLTDVPPDM--------------KVVCEEVFAPVV 364
|
410 420 430
....*....|....*....|....*....|..
gi 1540552764 446 IITDYKSsqLSVVLDLIERMHAHLTAAVVSND 477
Cdd:cd07149 365 SLNPFDT--LDEAIAMANDSPYGLQAGVFTND 394
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
68-477 |
4.64e-18 |
|
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: 86.64 E-value: 4.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 68 TVVDPLNGESfikVAEVDGTGIQPFVESLSScpKHGVHNPFKAPERYlmlgDVSTKAAHMLSlpKVSDFFTRLIQRVSPK 147
Cdd:cd07146 2 EVRNPYTGEV---VGTVPAGTEEALREALAL--AASYRSTLTRYQRS----AILNKAAALLE--ARREEFARLITLESGL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 148 SYQQAFGEVYVTQKFLEnFCGDQV-RFLARSFAVPGNHLGQQSHGF--RWPYGPVAIITPFNFPLEIPVLQLMGALYMGN 224
Cdd:cd07146 71 CLKDTRYEVGRAADVLR-FAAAEAlRDDGESFSCDLTANGKARKIFtlREPLGVVLAITPFNHPLNQVAHKIAPAIAANN 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 225 KPVLKVDTKVSIVMEQMLRLLHTCGLPVEDVDFINSD-GKTMNKLLLEGNPRMTLFTGSSKVAEKLANDLNG-RVKLEDA 302
Cdd:cd07146 150 RIVLKPSEKTPLSAIYLADLLYEAGLPPDMLSVVTGEpGEIGDELITHPDVDLVTFTGGVAVGKAIAATAGYkRQLLELG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 303 GFDWKILGPDVHQEDYIAWVCDqDAYACSGQKCSAQSLLFMHENwSSTSLIRKMKDLAERRKLAD-----LTIGPVLTFT 377
Cdd:cd07146 230 GNDPLIVMDDADLERAATLAVA-GSYANSGQRCTAVKRILVHES-VADEFVDLLVEKSAALVVGDpmdpaTDMGTVIDEE 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 378 TDSMLEHTNKLLEIPGSKLLFGGQPLENHLIPSIYGAIKPTAvyvpieeivkdknyELVTKEIFGPFQIItdYKSSQLSV 457
Cdd:cd07146 308 AAIQIENRVEEAIAQGARVLLGNQRQGALYAPTVLDHVPPDA--------------ELVTEETFGPVAPV--IRVKDLDE 371
|
410 420
....*....|....*....|
gi 1540552764 458 VLDLIERMHAHLTAAVVSND 477
Cdd:cd07146 372 AIAISNSTAYGLSSGVCTND 391
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
54-452 |
7.04e-18 |
|
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: 86.47 E-value: 7.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 54 NLVQGKWVGSS-NWSTVVDPLNGESFIKVA-----EVDGTGIQPFVESLSSCPKHGVHnpfkapERYLMLgdvsTKAAHM 127
Cdd:cd07082 4 YLINGEWKESSgKTIEVYSPIDGEVIGSVPalsalEILEAAETAYDAGRGWWPTMPLE------ERIDCL----HKFADL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 128 LSlpKVSDFFTRLIQRVSPKSYQQAFGEV-----YVTQKFLE--NFCGDQVRFlaRSFAVPGNHLGQQShgfRWPYGPVA 200
Cdd:cd07082 74 LK--ENKEEVANLLMWEIGKTLKDALKEVdrtidYIRDTIEElkRLDGDSLPG--DWFPGTKGKIAQVR---REPLGVVL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 201 IITPFNFPLEIPVLQLMGALYMGNKPVLKVDTKVSIVMEQMLRLLHTCGLPVEDVDFINSDGK-TMNKLLLEGNPRMTLF 279
Cdd:cd07082 147 AIGPFNYPLNLTVSKLIPALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGReIGDPLVTHGRIDVISF 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 280 TGSSKVAEKLAnDLNGRVK--LEDAGFDWKILGPDVHQEDYIAwVCDQDAYACSGQKCSAQSLLFMHENWSSTsLIRKMK 357
Cdd:cd07082 227 TGSTEVGNRLK-KQHPMKRlvLELGGKDPAIVLPDADLELAAK-EIVKGALSYSGQRCTAIKRVLVHESVADE-LVELLK 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 358 DLAERRKLAD-----LTIGPVL-TFTTDSMLEHTNKLLEiPGSKLLFGGQPLENHLipsiygaIKPTAVYVPIEEIVkdk 431
Cdd:cd07082 304 EEVAKLKVGMpwdngVDITPLIdPKSADFVEGLIDDAVA-KGATVLNGGGREGGNL-------IYPTLLDPVTPDMR--- 372
|
410 420
....*....|....*....|.
gi 1540552764 432 nyeLVTKEIFGPFQIITDYKS 452
Cdd:cd07082 373 ---LAWEEPFGPVLPIIRVND 390
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
192-443 |
2.29e-16 |
|
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; Uncharacterized aldehyde dehydrogenase of Candidatus kuenenia AldH (locus CAJ73105) and similar sequences with similarity to alpha-aminoadipic semialdehyde dehydrogenase (AASADH, human ALDH7A1, EC=1.2.1.31), Arabidopsis ALDH7B4, and Streptomyces clavuligerus delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH) are included in this CD.
Pssm-ID: 143449 [Multi-domain] Cd Length: 478 Bit Score: 81.62 E-value: 2.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 192 FRWPYGPVAIITPFNFPLEIPVLQLMGALYMGNKPVLKVDTKVSIVMEQMLRLLHTCGLPVEDVDFINSDGKTMNKLLLE 271
Cdd:cd07131 132 RRQPIGVVALITPWNFPVAIPSWKIFPALVCGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVE 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 272 gNPRM--TLFTGSSKVAE---KLANDLNGRVKLEDAGFDWKILGPDVHQE---DYIAWvcdqDAYACSGQKCSAQSLLFM 343
Cdd:cd07131 212 -HPDVdvVSFTGSTEVGErigETCARPNKRVALEMGGKNPIIVMDDADLDlalEGALW----SAFGTTGQRCTATSRLIV 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 344 HENWSStSLIRKMKDLAERRKL-----ADLTIGPVLtftTDSMLEHTNKLLEI---PGSKLLFGGQPLENHLIPSIYgAI 415
Cdd:cd07131 287 HESVYD-EFLKRFVERAKRLRVgdgldEETDMGPLI---NEAQLEKVLNYNEIgkeEGATLLLGGERLTGGGYEKGY-FV 361
|
250 260 270
....*....|....*....|....*....|
gi 1540552764 416 KPTavyvpieeIVKDKNYEL--VTKEIFGP 443
Cdd:cd07131 362 EPT--------VFTDVTPDMriAQEEIFGP 383
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
68-477 |
5.96e-16 |
|
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: 80.47 E-value: 5.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 68 TVVDPLNGESfikVAEVDGTGIQPFVESLSSCPKH-GVHNPFKAPERYLMLgdvsTKAAHMLSLPKvsDFFTRLIQRVSP 146
Cdd:cd07145 2 EVRNPANGEV---IDTVPSLSREEVREAIEVAEKAkDVMSNLPAYKRYKIL----MKVAELIERRK--EELAKLLTIEVG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 147 KSYQQAFGEVYVTQKFLENFCGDQVRFLARSFAVPGNHLGQQSHGF--RWPYGPVAIITPFNFPLEIPVLQLMGALYMGN 224
Cdd:cd07145 73 KPIKQSRVEVERTIRLFKLAAEEAKVLRGETIPVDAYEYNERRIAFtvREPIGVVGAITPFNFPANLFAHKIAPAIAVGN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 225 KPVLKVDTKVSIVMEQMLRLLHTCGLPVEDVDFINSDGKTMNKLLLEgNPR--MTLFTGSSKVAEKLANDLNG---RVKL 299
Cdd:cd07145 153 SVVVKPSSNTPLTAIELAKILEEAGLPPGVINVVTGYGSEVGDEIVT-NPKvnMISFTGSTAVGLLIASKAGGtgkKVAL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 300 EDAGFDWKILGPDVHQEDyIAWVCDQDAYACSGQKCSAQSLLFMHENWSST---SLIRKMKDLAERRKLADLT-IGPVLT 375
Cdd:cd07145 232 ELGGSDPMIVLKDADLER-AVSIAVRGRFENAGQVCNAVKRILVEEEVYDKflkLLVEKVKKLKVGDPLDESTdLGPLIS 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 376 FTTDSMLEHT-NKLLEiPGSKLLFGGQPLENHLIPsiygaikPTAVYVPIEEIVkdknyeLVTKEIFGPFQIITDYKSSQ 454
Cdd:cd07145 311 PEAVERMENLvNDAVE-KGGKILYGGKRDEGSFFP-------PTVLENDTPDMI------VMKEEVFGPVLPIAKVKDDE 376
|
410 420
....*....|....*....|...
gi 1540552764 455 LSVvlDLIERMHAHLTAAVVSND 477
Cdd:cd07145 377 EAV--EIANSTEYGLQASVFTND 397
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
195-515 |
6.75e-16 |
|
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: 80.01 E-value: 6.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 195 PYGPVAIITPFNFPLEIPVLQLMGALYMGNKPVLKVDTKVSIVMEQMLRLLHTCGLPVEDVDFINSDGKTMNKLLLEGNP 274
Cdd:cd07095 97 PHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLPPGVLNLVQGGRETGEALAAHEGI 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 275 RMTLFTGSSKVAEKLANDLNGRVkledagfdWKILG-------P----DVHQEDYIAWVCDQDAYACSGQKCSAQSLLFM 343
Cdd:cd07095 177 DGLLFTGSAATGLLLHRQFAGRP--------GKILAlemggnnPlvvwDVADIDAAAYLIVQSAFLTAGQRCTCARRLIV 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 344 HENWSSTSLIRKMKDLAERRKLADLT------IGPVLTFTTDSMLEHTNKLLEIpgskllfGGQPL-ENHLIPSIYGAIK 416
Cdd:cd07095 249 PDGAVGDAFLERLVEAAKRLRIGAPDaeppfmGPLIIAAAAARYLLAQQDLLAL-------GGEPLlAMERLVAGTAFLS 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 417 PTAVYVPIEEIVKDknyelvtKEIFGPFqiitdykssqLSVVL--DLIERMHAH------LTAAVVSNDP----LFLQEV 484
Cdd:cd07095 322 PGIIDVTDAADVPD-------EEIFGPL----------LQVYRydDFDEAIALAnatrfgLSAGLLSDDEalfeRFLARI 384
|
330 340 350
....*....|....*....|....*....|..
gi 1540552764 485 IGKSVNgttyaglRAR-TTGAPQNHWFGPAGD 515
Cdd:cd07095 385 RAGIVN-------WNRpTTGASSTAPFGGVGL 409
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
192-477 |
7.55e-16 |
|
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: 80.18 E-value: 7.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 192 FRWPYGPVAIITPFNFPLEIPVLQLMGALYMGNKPVLKVDTKVSIVMEQMLRLLHTCGLPVEDVDFINSDGKTMNKLLLE 271
Cdd:cd07113 139 RREPVGVVAGIVPWNFSVMIAVWKIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKGAVGAQLISH 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 272 GNPRMTLFTGSS----KVAEKLANDLNgRVKLEDAGFDWKILGPDVHqedyIAWVCD---QDAYACSGQKCSAQSLLFMH 344
Cdd:cd07113 219 PDVAKVSFTGSVatgkKIGRQAASDLT-RVTLELGGKNAAAFLKDAD----IDWVVEgllTAGFLHQGQVCAAPERFYVH 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 345 ENWSSTsLIRKMKdlaerRKLADLTIGPVLT----FTTDSMLEHTNKLLEI------PGSKLLFGGQPLENhliPSIYga 414
Cdd:cd07113 294 RSKFDE-LVTKLK-----QALSSFQVGSPMDesvmFGPLANQPHFDKVCSYlddaraEGDEIVRGGEALAG---EGYF-- 362
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1540552764 415 IKPTAVyvpieeIVKDKNYELVTKEIFGPFQIITDYKSSQlsVVLDLIERMHAHLTAAVVSND 477
Cdd:cd07113 363 VQPTLV------LARSADSRLMREETFGPVVSFVPYEDEE--ELIQLINDTPFGLTASVWTNN 417
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
193-452 |
8.20e-16 |
|
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: 79.99 E-value: 8.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 193 RWPYGPVAIITPFNFPLEIPVLQLMGALYMGNKPVLKVDTKVSIVMEQMLRLLHTCGLPVEDVDFINSDGKTMNKLLLEg 272
Cdd:cd07097 133 REPLGVVGLITPWNFPIAIPAWKIAPALAYGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVE- 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 273 NPRMTL--FTGSS----KVAEKLANDLnGRVKLEDAGFDWKILGPDVHQEDYIAWVCdQDAYACSGQKCSAQSLLFMHEN 346
Cdd:cd07097 212 HPDVDAvsFTGSTavgrRIAAAAAARG-ARVQLEMGGKNPLVVLDDADLDLAVECAV-QGAFFSTGQRCTASSRLIVTEG 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 347 WSST---SLIRKMKDLAERRKLADLT-IGPVltfTTDSMLEHTNKLLEI---PGSKLLFGGQPLEN-----HLIPSIYGA 414
Cdd:cd07097 290 IHDRfveALVERTKALKVGDALDEGVdIGPV---VSERQLEKDLRYIEIarsEGAKLVYGGERLKRpdegyYLAPALFAG 366
|
250 260 270
....*....|....*....|....*....|....*...
gi 1540552764 415 IKPTAvyvpieEIVKDknyelvtkEIFGPFQIITDYKS 452
Cdd:cd07097 367 VTNDM------RIARE--------EIFGPVAAVIRVRD 390
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
147-478 |
9.76e-16 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 79.98 E-value: 9.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 147 KSYQQAFGEVYVTQKFLEnfcgdqvrFLARS-----FAVPGNHL-GQQSHGFRWPYGPVAIITPFNFPLEIPVLQLMGAL 220
Cdd:PRK03137 125 KPWAEADADTAEAIDFLE--------YYARQmlklaDGKPVESRpGEHNRYFYIPLGVGVVISPWNFPFAIMAGMTLAAI 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 221 YMGNKPVLKVDTKVSIVMEQMLRLLHTCGLPVEDVDFINSDGKTMNKLLLEgNP--RMTLFTGSSKVA----EKLANDLN 294
Cdd:PRK03137 197 VAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVGDYLVD-HPktRFITFTGSREVGlriyERAAKVQP 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 295 G-----RVKLEDAGFDWKILGPDVHQEDYIAWVCdQDAYACSGQKCSAQSLLFMHENWSSTsLIRKMKDLAERRKLADLT 369
Cdd:PRK03137 276 GqiwlkRVIAEMGGKDAIVVDEDADLDLAAESIV-ASAFGFSGQKCSACSRAIVHEDVYDE-VLEKVVELTKELTVGNPE 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 370 ----IGPVLtfTTDSMlehtNKLL---EIpGS---KLLFGGQPLEN---HLIPSIYGAIKPTAVyvpieeivkdknyeLV 436
Cdd:PRK03137 354 dnayMGPVI--NQASF----DKIMsyiEI-GKeegRLVLGGEGDDSkgyFIQPTIFADVDPKAR--------------IM 412
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1540552764 437 TKEIFGPFQIITdyKSSQLSVVLDLIERMHAHLTAAVVSNDP 478
Cdd:PRK03137 413 QEEIFGPVVAFI--KAKDFDHALEIANNTEYGLTGAVISNNR 452
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
193-477 |
6.58e-15 |
|
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: 77.02 E-value: 6.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 193 RWPYGPVAIITPFNFPLEIPVLQLMGALYMGNKPVLKVDTKVSIVMEQMLRLLHTCgLPVEDVDFINSDGKTMNKLLLEg 272
Cdd:cd07108 115 REPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLAVLLLAEILAQV-LPAGVLNVITGYGEECGAALVD- 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 273 NP--RMTLFTGSSKVAEKLANDLNGR---VKLEDAGFDWKILGPDVHQEDYIAWVCDQDAYACSGQKCSAQSLLFMHENW 347
Cdd:cd07108 193 HPdvDKVTFTGSTEVGKIIYRAAADRlipVSLELGGKSPMIVFPDADLDDAVDGAIAGMRFTRQGQSCTAGSRLFVHEDI 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 348 SStSLIRKMKDlaerrKLADLTIGPVLTFTTD-----------SMLEHTNKLLEIPGSKLLFGG-QPLENHLIPSIYgaI 415
Cdd:cd07108 273 YD-AFLEKLVA-----KLSKLKIGDPLDEATDigaiisekqfaKVCGYIDLGLSTSGATVLRGGpLPGEGPLADGFF--V 344
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1540552764 416 KPTaVYVPIeeivkDKNYELVTKEIFGPFQIITDYKSSqlSVVLDLIERMHAHLTAAVVSND 477
Cdd:cd07108 345 QPT-IFSGV-----DNEWRLAREEIFGPVLCAIPWKDE--DEVIAMANDSHYGLAAYVWTRD 398
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
56-478 |
6.83e-15 |
|
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: 76.92 E-value: 6.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 56 VQGKWVGSSN--WSTVVDPLNGESFIKV-----AEVDGT-----GIQPFVESLSscpkhgvhnpfkAPERylmlGDVSTK 123
Cdd:cd07088 2 INGEFVPSSSgeTIDVLNPATGEVVATVpaataEDADRAvdaaeAAQKAWERLP------------AIER----AAYLRK 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 124 AAHMLSlpKVSDFFTRLIQRVSPKSYQQAFGEVYVTQKFLENFCGdqvrfLARSFA-------VPGNHLGQqshgFRWPY 196
Cdd:cd07088 66 LADLIR--ENADELAKLIVEEQGKTLSLARVEVEFTADYIDYMAE-----WARRIEgeiipsdRPNENIFI----FKVPI 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 197 GPVAIITPFNFPLEIPVLQLMGALYMGNKPVLK--VDTKVSIVmeQMLRLLHTCGLPVEDVDFINSDGKTMNKLLLEgNP 274
Cdd:cd07088 135 GVVAGILPWNFPFFLIARKLAPALVTGNTIVIKpsEETPLNAL--EFAELVDEAGLPAGVLNIVTGRGSVVGDALVA-HP 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 275 --RMTLFTGS----SKVAEKLANDLNgRVKLEDAGFDWKILGPDVHQE---DYIAWvcdqDAYACSGQKCSAQSLLFMHE 345
Cdd:cd07088 212 kvGMISLTGSteagQKIMEAAAENIT-KVSLELGGKAPAIVMKDADLDlavKAIVD----SRIINCGQVCTCAERVYVHE 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 346 NWSSTsLIRKMKDLAERRKL-----ADLTIGPVLtftTDSMLEHTNKLLEIP---GSKLLFGGQPLE----NHLIPSIYG 413
Cdd:cd07088 287 DIYDE-FMEKLVEKMKAVKVgdpfdAATDMGPLV---NEAALDKVEEMVERAveaGATLLTGGKRPEgekgYFYEPTVLT 362
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1540552764 414 AIkptavyvpieeivkDKNYELVTKEIFGPFQIITDYKSsqLSVVLDLIERMHAHLTAAVVSNDP 478
Cdd:cd07088 363 NV--------------RQDMEIVQEEIFGPVLPVVKFSS--LDEAIELANDSEYGLTSYIYTENL 411
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
54-443 |
1.02e-14 |
|
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: 76.45 E-value: 1.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 54 NLVQGKWVGSSNWS-TVVDPLNGEsfiKVAEVDGTGIQPFVESLSSCpkhgvHNPFK------APERylmlGDVSTKAAH 126
Cdd:cd07086 1 GVIGGEWVGSGGETfTSRNPANGE---PIARVFPASPEDVEAAVAAA-----REAFKewrkvpAPRR----GEIVRQIGE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 127 MLSLPKvsDFFTRLIQRVSPKSYQQAFGEVyvtQKFLenfcgDQVRF---LARSFA-------VPGNHLGQQSHgfrwPY 196
Cdd:cd07086 69 ALRKKK--EALGRLVSLEMGKILPEGLGEV---QEMI-----DICDYavgLSRMLYgltipseRPGHRLMEQWN----PL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 197 GPVAIITPFNFPLEIPVLQLMGALYMGNKPVLKVDTKVS----IVMEQMLRLLHTCGLPVEDVDFINSDGKTMNklLLEG 272
Cdd:cd07086 135 GVVGVITAFNFPVAVPGWNAAIALVCGNTVVWKPSETTPltaiAVTKILAEVLEKNGLPPGVVNLVTGGGDGGE--LLVH 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 273 NPRMTL--FTGSSKVAEKLA---NDLNGRVKLEDAGFDWKILGPDVHQE---DYIAWvcdqDAYACSGQKCSAQSLLFMH 344
Cdd:cd07086 213 DPRVPLvsFTGSTEVGRRVGetvARRFGRVLLELGGNNAIIVMDDADLDlavRAVLF----AAVGTAGQRCTTTRRLIVH 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 345 ENWSStSLIRKMKDLAERRKLADLT-----IGPVLTFTTDSMLEHTNKLLEIPGSKLLFGGQPLENHLiPSIYgaIKPTA 419
Cdd:cd07086 289 ESVYD-EFLERLVKAYKQVRIGDPLdegtlVGPLINQAAVEKYLNAIEIAKSQGGTVLTGGKRIDGGE-PGNY--VEPTI 364
|
410 420
....*....|....*....|....
gi 1540552764 420 VyvpieEIVKDKNyELVTKEIFGP 443
Cdd:cd07086 365 V-----TGVTDDA-RIVQEETFAP 382
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
140-494 |
1.74e-14 |
|
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: 76.10 E-value: 1.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 140 LIQRVSPKSYQQAFGEVYVTQKFLENFcGDQVRflarsfavpgNHLGQQSHGfrwPYGPVAIITPFNFPLEIPVLQLMGA 219
Cdd:TIGR01238 119 LCVREAGKTIHNAIAEVREAVDFCRYY-AKQVR----------DVLGEFSVE---SRGVFVCISPWNFPLAIFTGQISAA 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 220 LYMGNKPVLKVDTKVSIVMEQMLRLLHTCGLPVEDVDFINSDGKTMNKlLLEGNPRM--TLFTGSSKVAEKLANDLNGR- 296
Cdd:TIGR01238 185 LAAGNTVIAKPAEQTSLIAYRAVELMQEAGFPAGTIQLLPGRGADVGA-ALTSDPRIagVAFTGSTEVAQLINQTLAQRe 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 297 ---VKL--EDAGFDWKILGPDVHQEDYIAWVCdQDAYACSGQKCSAQSLLFMHENWS--STSLIRKMKDLAERRKLADLT 369
Cdd:TIGR01238 264 dapVPLiaETGGQNAMIVDSTALPEQVVRDVL-RSAFDSAGQRCSALRVLCVQEDVAdrVLTMIQGAMQELKVGVPHLLT 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 370 --IGPVL-TFTTDSMLEHTNKLLEIPGSkllFGGQPLENHLIPSIYGAIKPTAVyvpieEIvkdKNYELVTKEIFGPFQI 446
Cdd:TIGR01238 343 tdVGPVIdAEAKQNLLAHIEHMSQTQKK---IAQLTLDDSRACQHGTFVAPTLF-----EL---DDIAELSEEVFGPVLH 411
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1540552764 447 ITDYKSSQLSVVLDLIERMHAHLTAAVVSNDPLFLQEVIGKSVNGTTY 494
Cdd:TIGR01238 412 VVRYKARELDQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCY 459
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
56-494 |
2.07e-14 |
|
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: 75.81 E-value: 2.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 56 VQGKWVGSSNWST--VVDPLNGESFIKVAEVDGTGIQPFVESLSSCPKHGVHNPFKAPERylmlGDVSTKAAHMLSLPKv 133
Cdd:cd07119 2 IDGEWVEAASGKTrdIINPANGEVIATVPEGTAEDAKRAIAAARRAFDSGEWPHLPAQER----AALLFRIADKIREDA- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 134 sDFFTRLIQRVSPKSYQQAFGEVYVTQKFLENFCGDQVRFLARSFAVPGNhlgQQSHGFRWPYGPVAIITPFNFPLEIPV 213
Cdd:cd07119 77 -EELARLETLNTGKTLRESEIDIDDVANCFRYYAGLATKETGEVYDVPPH---VISRTVREPVGVCGLITPWNYPLLQAA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 214 LQLMGALYMGNKPVLKVDTKVSIVMEQMLRLLHTCGLPVEDVDFINSDGKTMNKLLLEgNPRMTL--FTGSSKVAEKLAN 291
Cdd:cd07119 153 WKLAPALAAGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAE-SPDVDLvsFTGGTATGRSIMR 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 292 DLNGRVK---LEDAGFDWKILGPDVHQEDYIAWVCDQdAYACSGQKCSAQSLLFMHENWSStSLIRKMKDLAERRKL--- 365
Cdd:cd07119 232 AAAGNVKkvaLELGGKNPNIVFADADFETAVDQALNG-VFFNAGQVCSAGSRLLVEESIHD-KFVAALAERAKKIKLgng 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 366 --ADLTIGPVLTfttdsmLEHTNKLLEI------PGSKLLFGGQ-PLENHLIPSIYgaIKPTAVY-VpieeivkDKNYEL 435
Cdd:cd07119 310 ldADTEMGPLVS------AEHREKVLSYiqlgkeEGARLVCGGKrPTGDELAKGYF--VEPTIFDdV-------DRTMRI 374
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1540552764 436 VTKEIFGPFQIITDYKSSQLSVVL--DLIermhAHLTAAVVSNDPLFLQEVIGKSVNGTTY 494
Cdd:cd07119 375 VQEEIFGPVLTVERFDTEEEAIRLanDTP----YGLAGAVWTKDIARANRVARRLRAGTVW 431
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
55-477 |
2.64e-14 |
|
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: 75.22 E-value: 2.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 55 LVQGKWVGSSNWST--VVDPLNGESFIKVAEVDGTGIQPFVESLSSCPKHGVHNPFKAPERylmlGDVSTKAAHMLSlpK 132
Cdd:cd07142 7 FINGQFVDAASGKTfpTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDEGPWPRMTGYER----SRILLRFADLLE--K 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 133 VSDFFTRLIQRVSPKSYQQA-FGEVYVTQKFLENFCGDQVRFLARSFAVPGNHLGQQSHGfrwPYGPVAIITPFNFPLEI 211
Cdd:cd07142 81 HADELAALETWDNGKPYEQArYAEVPLAARLFRYYAGWADKIHGMTLPADGPHHVYTLHE---PIGVVGQIIPWNFPLLM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 212 PVLQLMGALYMGNKPVLKVDTKVSIVMEQMLRLLHTCGLPVEDVDFINSDGKTMNKLLLEgnpRM----TLFTGSSKVAE 287
Cdd:cd07142 158 FAWKVGPALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIAS---HMdvdkVAFTGSTEVGK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 288 K---LANDLNGR-VKLEDAGFDWKILGPDVHQeDYIAWVCDQDAYACSGQKCSAQSLLFMHENWSStSLIRKMKDLAERR 363
Cdd:cd07142 235 IimqLAAKSNLKpVTLELGGKSPFIVCEDADV-DKAVELAHFALFFNQGQCCCAGSRTFVHESIYD-EFVEKAKARALKR 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 364 KLAD-----LTIGPVLTfttdsmLEHTNKLLEI------PGSKLLFGGQPLENHlipSIYgaIKPTavyvpIEEIVKDkN 432
Cdd:cd07142 313 VVGDpfrkgVEQGPQVD------KEQFEKILSYiehgkeEGATLITGGDRIGSK---GYY--IQPT-----IFSDVKD-D 375
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1540552764 433 YELVTKEIFGPFQIITDYKSsqlsvVLDLIERMHAH---LTAAVVSND 477
Cdd:cd07142 376 MKIARDEIFGPVQSILKFKT-----VDEVIKRANNSkygLAAGVFSKN 418
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
140-462 |
8.56e-14 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 74.62 E-value: 8.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 140 LIQRVSPKSYQQAFGEVYVTQKFLENFCGdQVRflarsfavpgNHLGQQSHgfRwPYGPVAIITPFNFPLEIPVLQLMGA 219
Cdd:PRK11809 727 LLVREAGKTFSNAIAEVREAVDFLRYYAG-QVR----------DDFDNDTH--R-PLGPVVCISPWNFPLAIFTGQVAAA 792
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 220 LYMGNkPVL-KVDTKVSIVMEQMLRLLHTCGLPVEDVDFINSDGKTMNKLLLeGNPRM--TLFTGSSKVAEKLANDLNGR 296
Cdd:PRK11809 793 LAAGN-SVLaKPAEQTPLIAAQAVRILLEAGVPAGVVQLLPGRGETVGAALV-ADARVrgVMFTGSTEVARLLQRNLAGR 870
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 297 vkLEDAG----------------FDWKILGPDVhqedyiawVCD--QDAYACSGQKCSAQSLLFMHEnwsstslirkmkD 358
Cdd:PRK11809 871 --LDPQGrpipliaetggqnamiVDSSALTEQV--------VADvlASAFDSAGQRCSALRVLCLQD------------D 928
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 359 LAERR------KLADLTIGPVLTFTTD-----------SMLEHTNKLLEipgskllfGGQPLenHLIPSIYGAIKPTAVY 421
Cdd:PRK11809 929 VADRTlkmlrgAMAECRMGNPDRLSTDigpvidaeakaNIERHIQAMRA--------KGRPV--FQAARENSEDWQSGTF 998
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1540552764 422 VPIEEIVKDKNYELvTKEIFGPFQIITDYKSSQLSVVLDLI 462
Cdd:PRK11809 999 VPPTLIELDSFDEL-KREVFGPVLHVVRYNRNQLDELIEQI 1038
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
134-443 |
8.66e-14 |
|
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: 73.72 E-value: 8.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 134 SDFFTRLIQRVSPKSYQQAFGEVyvtqkfleNFCGDQVRFLArSFAVPGNHLGQQSHGF----RWPYGPVAIITPFNFPL 209
Cdd:cd07106 58 AEELARLLTLEQGKPLAEAQFEV--------GGAVAWLRYTA-SLDLPDEVIEDDDTRRvelrRKPLGVVAAIVPWNFPL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 210 EIPVLQLMGALYMGNKPVLK--VDTKVSIVMeqMLRLLHTCgLPVEDVDFINSDGktmnklllEGNPRMTL--------F 279
Cdd:cd07106 129 LLAAWKIAPALLAGNTVVLKpsPFTPLCTLK--LGELAQEV-LPPGVLNVVSGGD--------ELGPALTShpdirkisF 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 280 TGSS----KVAEKLANDLNgRVKLEDAGFDWKILGPDVhqeDY------IAWVcdqdAYACSGQKCSAQSLLFMHEnwss 349
Cdd:cd07106 198 TGSTatgkKVMASAAKTLK-RVTLELGGNDAAIVLPDV---DIdavapkLFWG----AFINSGQVCAAIKRLYVHE---- 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 350 tS----LIRKMKDLAERRKLAD-----LTIGPVltftTDSM-LEHTNKLLE---IPGSKLLFGGQPLENhliPSIYgaIK 416
Cdd:cd07106 266 -SiydeFCEALVALAKAAVVGDgldpgTTLGPV----QNKMqYDKVKELVEdakAKGAKVLAGGEPLDG---PGYF--IP 335
|
330 340
....*....|....*....|....*..
gi 1540552764 417 PTAVYVPieeivkDKNYELVTKEIFGP 443
Cdd:cd07106 336 PTIVDDP------PEGSRIVDEEQFGP 356
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
195-452 |
1.46e-13 |
|
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: 72.83 E-value: 1.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 195 PYGPVAIITPFNFPLEIPVLQLMGALYMGNKPVLKVDTKVSIVMEQMLRLLHTCGLPVEDVDFINSDGKTMNKLLLEgNP 274
Cdd:cd07144 144 PYGVCGQIIPWNYPLAMAAWKLAPALAAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAE-HP 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 275 RM--TLFTGSSKVAEKLANDLNGRVK---LEDAGFDWKILGPDVHQEDYIAWVCDQDAYAcSGQKCSAQSLLFMHENWSS 349
Cdd:cd07144 223 DVdkIAFTGSTATGRLVMKAAAQNLKavtLECGGKSPALVFEDADLDQAVKWAAAGIMYN-SGQNCTATSRIYVQESIYD 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 350 TSLIRKMKDLAERRKLA-----DLTIGPVLTFTT-DSMLEHTNKLLEiPGSKLLFGGQPLENHLIPSIYgaIKPTavyvp 423
Cdd:cd07144 302 KFVEKFVEHVKQNYKVGspfddDTVVGPQVSKTQyDRVLSYIEKGKK-EGAKLVYGGEKAPEGLGKGYF--IPPT----- 373
|
250 260 270
....*....|....*....|....*....|.
gi 1540552764 424 ieeIVKD--KNYELVTKEIFGPFQIITDYKS 452
Cdd:cd07144 374 ---IFTDvpQDMRIVKEEIFGPVVVISKFKT 401
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
54-375 |
1.65e-13 |
|
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: 72.93 E-value: 1.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 54 NLVQGKWVGSSN--WSTVVDPLNGESFIKV-----AEVDgtgiqpfvESLSSCpkhgvHNPFKAPERYlmlgDVSTKAAH 126
Cdd:cd07085 3 LFINGEWVESKTteWLDVYNPATGEVIARVplataEEVD--------AAVAAA-----KAAFPAWSAT----PVLKRQQV 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 127 MLS----LPKVSDFFTRLIQRVSPKSYQQAFGEVyvtQKFLENF---CGDQVRFLARSFAVPGNhlGQQSHGFRWPYGPV 199
Cdd:cd07085 66 MFKfrqlLEENLDELARLITLEHGKTLADARGDV---LRGLEVVefaCSIPHLLKGEYLENVAR--GIDTYSYRQPLGVV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 200 AIITPFNFPLEIPVLQLMGALYMGNKPVLKVDTKVSIVMEQMLRLLHTCGLPVEDVDFINSDGKTMNKLLLEGNPRMTLF 279
Cdd:cd07085 141 AGITPFNFPAMIPLWMFPMAIACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHGGKEAVNALLDHPDIKAVSF 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 280 TGSSKVAE---KLANDLNGRVKLEDAGFDWKILGPDVHQEDYIAWVCDQdAYACSGQKCSAQSLLFMHENwSSTSLIRKM 356
Cdd:cd07085 221 VGSTPVGEyiyERAAANGKRVQALGGAKNHAVVMPDADLEQTANALVGA-AFGAAGQRCMALSVAVAVGD-EADEWIPKL 298
|
330 340
....*....|....*....|....*.
gi 1540552764 357 KDLAERRKL-------ADLtiGPVLT 375
Cdd:cd07085 299 VERAKKLKVgagddpgADM--GPVIS 322
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
137-477 |
2.91e-13 |
|
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: 71.98 E-value: 2.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 137 FTRLIQRVSPKSYQQAFGEVYVTQKFLENFCGDQVRFlaRSFAVPGNHLGQQSHGFRWPYGPVAIITPFNFPLEIPVLQL 216
Cdd:cd07150 63 LIDLLIDEGGSTYGKAWFETTFTPELLRAAAGECRRV--RGETLPSDSPGTVSMSVRRPLGVVAGITPFNYPLILATKKV 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 217 MGALYMGNKPVLKVDTKVSIVMEQMLRLLHTCGLPVEDVDFINSDGKTMNKLLLEgNPR--MTLFTGSSKV----AEKLA 290
Cdd:cd07150 141 AFALAAGNTVVLKPSEETPVIGLKIAEIMEEAGLPKGVFNVVTGGGAEVGDELVD-DPRvrMVTFTGSTAVgreiAEKAG 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 291 NDLNgRVKLEDAGFDWKILGPDVhQEDYIAWVCDQDAYACSGQKCSAQSLLFMHENWSS------TSLIRKMK--DLAER 362
Cdd:cd07150 220 RHLK-KITLELGGKNPLIVLADA-DLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDefvkkfVARASKLKvgDPRDP 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 363 rklaDLTIGPVLTFT-TDSMLEHTNKLLEiPGSKLLFGGQPLENHLIPSIYGAIKPTAVyvpieeIVKDknyelvtkEIF 441
Cdd:cd07150 298 ----DTVIGPLISPRqVERIKRQVEDAVA-KGAKLLTGGKYDGNFYQPTVLTDVTPDMR------IFRE--------ETF 358
|
330 340 350
....*....|....*....|....*....|....*.
gi 1540552764 442 GPFQIITDYKSSQLSvvLDLIERMHAHLTAAVVSND 477
Cdd:cd07150 359 GPVTSVIPAKDAEEA--LELANDTEYGLSAAILTND 392
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
197-483 |
3.35e-13 |
|
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: 71.85 E-value: 3.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 197 GPVAIITPFNFPLEIPVLQLMGALyMGNKPVLK-VDTKVS---IVMEqmlrLLHTCGLPVEDVDFINSDGKTMNKLLLeG 272
Cdd:cd07123 172 GFVYAVSPFNFTAIGGNLAGAPAL-MGNVVLWKpSDTAVLsnyLVYK----ILEEAGLPPGVINFVPGDGPVVGDTVL-A 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 273 NPRMT--LFTGSS--------KVAEKLANDLN-GRVKLEDAGFDWKILGP--DVhqeDYIAWVCDQDAYACSGQKCSAQS 339
Cdd:cd07123 246 SPHLAglHFTGSTptfkslwkQIGENLDRYRTyPRIVGETGGKNFHLVHPsaDV---DSLVTATVRGAFEYQGQKCSAAS 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 340 LLFMHEnwsstSLIRKMKD-LAErrKLADLTIGPVLTFTT--------------DSMLEHTNkllEIPGSKLLFGGQPLE 404
Cdd:cd07123 323 RAYVPE-----SLWPEVKErLLE--ELKEIKMGDPDDFSNfmgavidekafdriKGYIDHAK---SDPEAEIIAGGKCDD 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 405 nhlipSIYGAIKPTaVYVpieeiVKDKNYELVTKEIFGPFQIITDYKSSQLSVVLDLIERMHAH-LTAAVVSNDPLFLQE 483
Cdd:cd07123 393 -----SVGYFVEPT-VIE-----TTDPKHKLMTEEIFGPVLTVYVYPDSDFEETLELVDTTSPYaLTGAIFAQDRKAIRE 461
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
193-452 |
4.78e-13 |
|
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: 71.12 E-value: 4.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 193 RWPYGPVAIITPFNFPLEIPVLQLMGALYMGNKPVLKVDTKVSIVMEQMLRLLHTCGLPVEDVDFINSDGKTMNKLLLEg 272
Cdd:cd07147 121 RFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPASRTPLSALILGEVLAETGLPKGAFSVLPCSRDDADLLVTD- 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 273 nPRMTL--FTGSSKVAEKLaNDLNGR--VKLEDAGFDWKILGPDVHQeDYIAWVCDQDAYACSGQKCSAQSLLFMHENWS 348
Cdd:cd07147 200 -ERIKLlsFTGSPAVGWDL-KARAGKkkVVLELGGNAAVIVDSDADL-DFAAQRIIFGAFYQAGQSCISVQRVLVHRSVY 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 349 StSLIRKMKDLAERRKLAD-----LTIGPVLtftTDSMLEHTNKLLE---IPGSKLLFGGQPLENHLIPSIygaikptav 420
Cdd:cd07147 277 D-EFKSRLVARVKALKTGDpkddaTDVGPMI---SESEAERVEGWVNeavDAGAKLLTGGKRDGALLEPTI--------- 343
|
250 260 270
....*....|....*....|....*....|..
gi 1540552764 421 yvpIEEIvkDKNYELVTKEIFGPFQIITDYKS 452
Cdd:cd07147 344 ---LEDV--PPDMEVNCEEVFGPVVTVEPYDD 370
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
52-443 |
7.19e-13 |
|
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, methylmalonate-semialdehyde dehydrogenase catalyzes the irreversible NAD+- and CoA-dependent oxidative decarboxylation of methylmalonate semialdehyde to propionyl-CoA. Methylmalonate-semialdehyde dehydrogenase has been characterized in both prokaryotes and eukaryotes, functioning as a mammalian tetramer and a bacterial homodimer. Although similar in monomeric molecular mass and enzymatic activity, the N-terminal sequence in P.aeruginosa does not correspond with the N-terminal sequence predicted for rat liver. Sequence homology to a variety of prokaryotic and eukaryotic aldehyde dehydrogenases places MMSDH in the aldehyde dehydrogenase (NAD+) superfamily (pfam00171), making MMSDH's CoA requirement unique among known ALDHs. Methylmalonate semialdehyde dehydrogenase is closely related to betaine aldehyde dehydrogenase, 2-hydroxymuconic semialdehyde dehydrogenase, and class 1 and 2 aldehyde dehydrogenase. In Bacillus, a highly homologous protein to methylmalonic acid semialdehyde dehydrogenase, groups out from the main MMSDH clade with Listeria and Sulfolobus. This Bacillus protein has been suggested to be located in an iol operon and/or involved in myo-inositol catabolism, converting malonic semialdehyde to acetyl CoA ad CO2. The preceeding enzymes responsible for valine catabolism are present in Bacillus, Listeria, and Sulfolobus. [Energy metabolism, Amino acids and amines]
Pssm-ID: 130783 Cd Length: 477 Bit Score: 70.68 E-value: 7.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 52 VLNLVQGKWV--GSSNWSTVVDPLNGESFIKVAEVDGTGIQPFVESlsscpkhgvhnpfkAPERYLMLGD--VSTKAAHM 127
Cdd:TIGR01722 1 VNHWIGGKFAegASGTYIPVTNPATNEVTTKVAFASVDEVDAAVAS--------------ARETFLTWGQtsLAQRTSVL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 128 LS----LPKVSDFFTRLIQRVSPKSYQQAFGEVYVTQKFLENFCGDQVRFLARSfaVPGNHLGQQSHGFRWPYGPVAIIT 203
Cdd:TIGR01722 67 LRyqalLKEHRDEIAELITAEHGKTHSDALGDVARGLEVVEHACGVNSLLKGET--STQVATRVDVYSIRQPLGVCAGIT 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 204 PFNFPLEIPVLQLMGALYMGNKPVLKVDTKVSIVMEQMLRLLHTCGLPVEDVDFINSDGKTMNKLLLEGNPRMTLFTGSS 283
Cdd:TIGR01722 145 PFNFPAMIPLWMFPIAIACGNTFVLKPSEKVPSAAVKLAELFSEAGAPDGVLNVVHGDKEAVDRLLEHPDVKAVSFVGST 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 284 KVAEKL---ANDLNGRVKLEDAGFDWKILGPDVHQEDYIAWVCDQdAYACSGQKCSAQSLLFMHEnwSSTSLIRKMKDLA 360
Cdd:TIGR01722 225 PIGRYIhttGSAHGKRVQALGGAKNHMVVMPDADKDAAADALVGA-AYGAAGQRCMAISAAVLVG--AADEWVPEIRERA 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 361 ERRKLADLT-----IGPVLT---------FTTDSMLEHTNKLLEIPGSKLlfGGQPLENHLIPSIYGAIKPTAvyvpiee 426
Cdd:TIGR01722 302 EKIRIGPGDdpgaeMGPLITpqakdrvasLIAGGAAEGAEVLLDGRGYKV--DGYEEGNWVGPTLLERVPPTM------- 372
|
410
....*....|....*..
gi 1540552764 427 ivkdKNYElvtKEIFGP 443
Cdd:TIGR01722 373 ----KAYQ---EEIFGP 382
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
193-443 |
1.43e-12 |
|
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: 69.89 E-value: 1.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 193 RWPYGPVAIITPFNFPLEIPVLQLMGALYMGNKPVLKVDTKVSIVMEQMLRLLHTCGLPVEDVDFINSDGKTMNKLLLEG 272
Cdd:cd07114 117 REPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPASTLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEH 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 273 NP-RMTLFTGSSKV--------AEKLAndlngRVKLEDAGFDWKILGPDVHQEDYIAWVCDqDAYACSGQKCSAQSLLFM 343
Cdd:cd07114 197 PLvAKIAFTGGTETgrhiaraaAENLA-----PVTLELGGKSPNIVFDDADLDAAVNGVVA-GIFAAAGQTCVAGSRLLV 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 344 HENWSStSLIRKMKDLAERRKL-----ADLTIGPVLTFTtdsMLEHTNKLLEI---PGSKLLFGGQPLEnhliPSIYGA- 414
Cdd:cd07114 271 QRSIYD-EFVERLVARARAIRVgdpldPETQMGPLATER---QLEKVERYVARareEGARVLTGGERPS----GADLGAg 342
|
250 260 270
....*....|....*....|....*....|.
gi 1540552764 415 --IKPTAVYVPieeivkDKNYELVTKEIFGP 443
Cdd:cd07114 343 yfFEPTILADV------TNDMRIAQEEVFGP 367
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
138-477 |
3.29e-12 |
|
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: 68.79 E-value: 3.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 138 TRLIQRVSPKSYQQAFGEVYVTQKFLENFCGDQVRFLARSFAVPGNHL-GQQSHGFRWPYGPVAIITPFNFPLEIPVLQL 216
Cdd:cd07099 61 AELLHAETGKPRADAGLEVLLALEAIDWAARNAPRVLAPRKVPTGLLMpNKKATVEYRPYGVVGVISPWNYPLLTPMGDI 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 217 MGALYMGNKPVLKVDTKVSIVMEQMLRLLHTCGLPVEDVDFINSDGKTMNKLLLEGnPRMTLFTGSS----KVAEKLAND 292
Cdd:cd07099 141 IPALAAGNAVVLKPSEVTPLVGELLAEAWAAAGPPQGVLQVVTGDGATGAALIDAG-VDKVAFTGSVatgrKVMAAAAER 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 293 LNgRVKLEDAGFDWKILGPDVHQE---DYIAWvcdqDAYACSGQKCSAQSLLFMHENWSStSLIRKMKDLAERRKLA--- 366
Cdd:cd07099 220 LI-PVVLELGGKDPMIVLADADLEraaAAAVW----GAMVNAGQTCISVERVYVHESVYD-EFVARLVAKARALRPGadd 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 367 --DLTIGPVltfTTDSMLE----HTNKLLEiPGSKLLFGGQPLEnhlIPSIYgaIKPTaVYVPIeeivkDKNYELVTKEI 440
Cdd:cd07099 294 igDADIGPM---TTARQLDivrrHVDDAVA-KGAKALTGGARSN---GGGPF--YEPT-VLTDV-----PHDMDVMREET 358
|
330 340 350
....*....|....*....|....*....|....*..
gi 1540552764 441 FGPfqIITDYKSSQLSVVLDLIERMHAHLTAAVVSND 477
Cdd:cd07099 359 FGP--VLPVMPVADEDEAIALANDSRYGLSASVFSRD 393
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
167-478 |
8.38e-12 |
|
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: 67.38 E-value: 8.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 167 CGDQVRFLARSFAVPGNhlGQQSHGFRWPYGPVAIITPFNFPLEIPVLQLMGALYMGNKPVLKVDTKVSIVMEQMLRLLH 246
Cdd:cd07110 94 AEQLDAKAERAVPLPSE--DFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTSLTELELAEIAA 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 247 TCGLPVEDVDFINSDGKTMNKLLLEgNPRM--TLFTGS----SKVAEKLANDLNGrVKLEDAGFDWKILGPDVHQEDYIA 320
Cdd:cd07110 172 EAGLPPGVLNVVTGTGDEAGAPLAA-HPGIdkISFTGStatgSQVMQAAAQDIKP-VSLELGGKSPIIVFDDADLEKAVE 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 321 WVCdQDAYACSGQKCSAQSLLFMHENWSStSLIRKMKDLAERRKLAD-----LTIGPVLTFTT-DSMLEHTNKLLEiPGS 394
Cdd:cd07110 250 WAM-FGCFWNNGQICSATSRLLVHESIAD-AFLERLATAAEAIRVGDpleegVRLGPLVSQAQyEKVLSFIARGKE-EGA 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 395 KLLFGGQPLEnHLIPSIYgaIKPTaVYVpieEIVKDKnyELVTKEIFGPFQIITDYKSSQLSVvlDLIERMHAHLTAAVV 474
Cdd:cd07110 327 RLLCGGRRPA-HLEKGYF--IAPT-VFA---DVPTDS--RIWREEIFGPVLCVRSFATEDEAI--ALANDSEYGLAAAVI 395
|
....
gi 1540552764 475 SNDP 478
Cdd:cd07110 396 SRDA 399
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
186-477 |
9.99e-12 |
|
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: 66.93 E-value: 9.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 186 GQQSHGFRWPYGPVAIITPFNFPLEIPVLQLMGALYMGNKPVLKVDTKVSIVMEQML-RLLHTCGLPVEDVDFINSDGKT 264
Cdd:cd07152 101 GRLSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGGVVIaRLFEEAGLPAGVLHVLPGGADA 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 265 MNKLLLEGNPRMTLFTGSSKVAEK---LANDLNGRVKLEDAGFDWKILGPDVHQE---DYIAWvcdqDAYACSGQKCSAQ 338
Cdd:cd07152 181 GEALVEDPNVAMISFTGSTAVGRKvgeAAGRHLKKVSLELGGKNALIVLDDADLDlaaSNGAW----GAFLHQGQICMAA 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 339 SLLFMHENWSStSLIRKMKDLAERRKLAD-----LTIGPVLtftTDSMLEHTNKLLEIP---GSKLLFGGQPLENHLIPS 410
Cdd:cd07152 257 GRHLVHESVAD-AYTAKLAAKAKHLPVGDpatgqVALGPLI---NARQLDRVHAIVDDSvaaGARLEAGGTYDGLFYRPT 332
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1540552764 411 IYGAIKPTAvyvpieeivkdknyELVTKEIFGPFQIITDYKSSQLSVVldLIERMHAHLTAAVVSND 477
Cdd:cd07152 333 VLSGVKPGM--------------PAFDEEIFGPVAPVTVFDSDEEAVA--LANDTEYGLSAGIISRD 383
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
145-522 |
1.15e-11 |
|
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: 66.98 E-value: 1.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 145 SPKSYQQAFGEVyvtqkfleNFCGDQVRF---LARsfAVPG---NHLGQQSHGF--RWPYGPVAIITPFNFPLEIPVLQL 216
Cdd:cd07118 71 SGKPISQARGEI--------EGAADLWRYaasLAR--TLHGdsyNNLGDDMLGLvlREPIGVVGIITPWNFPFLILSQKL 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 217 MGALYMGNKPVLKVD--TKVSIVMeqMLRLLHTCGLPVEDVDFINSDGKTMNKLLLEgNPR--MTLFTGSSKVAEKLAND 292
Cdd:cd07118 141 PFALAAGCTVVVKPSefTSGTTLM--LAELLIEAGLPAGVVNIVTGYGATVGQAMTE-HPDvdMVSFTGSTRVGKAIAAA 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 293 LNGRVK---LEDAGFDWKILGPDvhqedyiawvCDQDA---------YACSGQKCSAQSLLFMHENWSStSLIRKMKDLA 360
Cdd:cd07118 218 AARNLKkvsLELGGKNPQIVFAD----------ADLDAaadavvfgvYFNAGECCNSGSRLLVHESIAD-AFVAAVVARS 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 361 ERRKLAD-----LTIGPVltfTTDSMLEHTNKLLEI---PGSKLLFGGQPLEN----HLIPSIYGAIKPtavyvpieeiv 428
Cdd:cd07118 287 RKVRVGDpldpeTKVGAI---INEAQLAKITDYVDAgraEGATLLLGGERLASaaglFYQPTIFTDVTP----------- 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 429 kdkNYELVTKEIFGPFQIITDYKSsqLSVVLDLIERMHAHLTAAVVSNDplfLQEVIgksvngTTYAGLRART------- 501
Cdd:cd07118 353 ---DMAIAREEIFGPVLSVLTFDT--VDEAIALANDTVYGLSAGVWSKD---IDTAL------TVARRIRAGTvwvntfl 418
|
410 420
....*....|....*....|.
gi 1540552764 502 TGAPQNhwfgPAGDPRGAGIG 522
Cdd:cd07118 419 DGSPEL----PFGGFKQSGIG 435
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
176-477 |
1.59e-11 |
|
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: 66.46 E-value: 1.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 176 RSFAVPGNHLGQQSHGfrwPYGPVAIITPFNFPLEIPVLQLMGALYMGNKPVLKVDTKVSIVMEQMLRLLHTCGLPVEDV 255
Cdd:cd07091 125 KTIPIDGNFLAYTRRE---PIGVCGQIIPWNFPLLMLAWKLAPALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVV 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 256 DFINSDGKTMNKLLLEgNPRM--TLFTGSSKVAE---KLANDLN-GRVKLEDAGFDWKILGPDVHQEDYIAWVcdqdAYA 329
Cdd:cd07091 202 NIVPGFGPTAGAAISS-HMDVdkIAFTGSTAVGRtimEAAAKSNlKKVTLELGGKSPNIVFDDADLDKAVEWA----AFG 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 330 C---SGQKCSAQSLLFMHENWSStSLIRKMKDLAERRKLADltigPVLTFTTDSML---EHTNKLLEI------PGSKLL 397
Cdd:cd07091 277 IffnQGQCCCAGSRIFVQESIYD-EFVEKFKARAEKRVVGD----PFDPDTFQGPQvskAQFDKILSYiesgkkEGATLL 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 398 FGGQPLENhliPSIYgaIKPTaVYVPIEEIVKdknyeLVTKEIFGPFQIITDYKSSQlsvvlDLIERMHAH---LTAAVV 474
Cdd:cd07091 352 TGGERHGS---KGYF--IQPT-VFTDVKDDMK-----IAKEEIFGPVVTILKFKTED-----EVIERANDTeygLAAGVF 415
|
...
gi 1540552764 475 SND 477
Cdd:cd07091 416 TKD 418
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
164-452 |
2.55e-11 |
|
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: 65.66 E-value: 2.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 164 ENFcgdqvRFLA--------RSFAVPGNHLgqqSHGFRWPYGPVAIITPFNFPLEIPVLQLMGALYMGNKPVLKV--DTK 233
Cdd:cd07093 86 ANF-----RFFAdyilqldgESYPQDGGAL---NYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPseWTP 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 234 VSIVMeqMLRLLHTCGLPVEDVDFINSDGKTMNKLLLEgNPRMTL--FTGSSKVAEKL---ANDLNGRVKLEDAGFDWKI 308
Cdd:cd07093 158 LTAWL--LAELANEAGLPPGVVNVVHGFGPEAGAALVA-HPDVDLisFTGETATGRTImraAAPNLKPVSLELGGKNPNI 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 309 LGPDVHQEDYIAWVCDQdAYACSGQKCSAQSLLFMHENWSStSLIRKMKDLAERRKLADLT-----IGPVLTfttdsmLE 383
Cdd:cd07093 235 VFADADLDRAVDAAVRS-SFSNNGEVCLAGSRILVQRSIYD-EFLERFVERAKALKVGDPLdpdteVGPLIS------KE 306
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1540552764 384 HTNKLL---EIP---GSKLLFGGQPLE-NHLIPSIYgaIKPTAVYVPieeivkDKNYELVTKEIFGPFQIITDYKS 452
Cdd:cd07093 307 HLEKVLgyvELAraeGATILTGGGRPElPDLEGGYF--VEPTVITGL------DNDSRVAQEEIFGPVVTVIPFDD 374
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
135-345 |
5.18e-11 |
|
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: 65.02 E-value: 5.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 135 DFFTRLIQRVSPKSYQQAFGE---VYVTQKFLENFCGDQVRFLARSFAVPGnhLGQQSHgFRWPYGPVAIITPFNFPLEI 211
Cdd:cd07101 58 DELLDLIQLETGKARRHAFEEvldVAIVARYYARRAERLLKPRRRRGAIPV--LTRTTV-NRRPKGVVGVISPWNYPLTL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 212 PVLQLMGALYMGNKPVLKVDTKVSIVMEQMLRLLHTCGLPVEDVDFINSDGKTMNKLLLEgNPRMTLFTGSS----KVAE 287
Cdd:cd07101 135 AVSDAIPALLAGNAVVLKPDSQTALTALWAVELLIEAGLPRDLWQVVTGPGSEVGGAIVD-NADYVMFTGSTatgrVVAE 213
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1540552764 288 KLANDLNGrVKLEDAGFDWKILGPDVHqedyIAWVCDQDAYAC---SGQKCSAQSLLFMHE 345
Cdd:cd07101 214 RAGRRLIG-CSLELGGKNPMIVLEDAD----LDKAAAGAVRACfsnAGQLCVSIERIYVHE 269
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
193-494 |
5.29e-11 |
|
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (locus EDX86601) and other similar sequences, are present in this CD.
Pssm-ID: 143420 [Multi-domain] Cd Length: 452 Bit Score: 64.96 E-value: 5.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 193 RWPYGPVAIITPFNFPLEIPVLQLMGALYMGNKPVLKVDTKVSIVMEQMLRLLHTCGLPVEDVDFINSDGKTMNKLLLEG 272
Cdd:cd07102 114 REPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCGERFAAAFAEAGLPEGVFQVLHLSHETSAALIADP 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 273 NPRMTLFTGSSKVAEKLANDLNGR---VKLEDAGFDWKILGPDVHQEDYIAWVCDqDAYACSGQKCSAQSLLFMHENWSS 349
Cdd:cd07102 194 RIDHVSFTGSVAGGRAIQRAAAGRfikVGLELGGKDPAYVRPDADLDAAAESLVD-GAFFNSGQSCCSIERIYVHESIYD 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 350 TsLIRKMKDLAERRKLAD-----LTIGPVLTFT-TDSMLEHTNKLLEiPGSKLLFGGQPLENHLIPSIYgaIKPTaVYVP 423
Cdd:cd07102 273 A-FVEAFVAVVKGYKLGDpldpsTTLGPVVSARaADFVRAQIADAIA-KGARALIDGALFPEDKAGGAY--LAPT-VLTN 347
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1540552764 424 IeeivkDKNYELVTKEIFGPfqIITDYKSSQLSVVLDLIERMHAHLTAAVVSNDPLFLQEVIGKSVNGTTY 494
Cdd:cd07102 348 V-----DHSMRVMREETFGP--VVGIMKVKSDAEAIALMNDSEYGLTASVWTKDIARAEALGEQLETGTVF 411
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
169-451 |
1.25e-10 |
|
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: 63.80 E-value: 1.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 169 DQVRFLARSFAVPGNHL-GQQSHGFRW--PYGPVAIITPFNFPLEIPVLQLMGALYMGNKPVLK--VDTKVSIVMeqMLR 243
Cdd:cd07089 94 DLADSFPWEFDLPVPALrGGPGRRVVRrePVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKpaPDTPLSALL--LGE 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 244 LLHTCGLPVEDVDFINSDGKTMNKLLLEgNPR--MTLFTGSSKVAEKLANDLNGRVK---LEDAGFDWKILGPDVhqeDY 318
Cdd:cd07089 172 IIAETDLPAGVVNVVTGSDNAVGEALTT-DPRvdMVSFTGSTAVGRRIMAQAAATLKrvlLELGGKSANIVLDDA---DL 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 319 IAWVCDQDAYAC--SGQKCSAQSLLFMHENwSSTSLIRKMKDLAERRKLAD-----LTIGPVLtftTDSMLEHTNKLLEI 391
Cdd:cd07089 248 AAAAPAAVGVCMhnAGQGCALTTRLLVPRS-RYDEVVEALAAAFEALPVGDpadpgTVMGPLI---SAAQRDRVEGYIAR 323
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1540552764 392 ---PGSKLLFGGQPLEnHLIPSIYgaIKPTaVYVPIeeivkDKNYELVTKEIFGPFQIITDYK 451
Cdd:cd07089 324 grdEGARLVTGGGRPA-GLDKGFY--VEPT-LFADV-----DNDMRIAQEEIFGPVLVVIPYD 377
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
195-477 |
1.99e-10 |
|
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: 63.32 E-value: 1.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 195 PYGPVAIITPFNFPLEIPVLQLMGALYMGNKPVLKVDTKVSIVMEQMLRLLHTCGLPVEDVDFINSDGKTMNKlLLEGNP 274
Cdd:cd07143 144 PIGVCGQIIPWNFPLLMCAWKIAPALAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGN-AISSHM 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 275 RM--TLFTGSS----KVAEKLANDLNGRVKLEDAGFDWKILGPDVHQEDYIAWVcDQDAYACSGQKCSAQSLLFMHENWS 348
Cdd:cd07143 223 DIdkVAFTGSTlvgrKVMEAAAKSNLKKVTLELGGKSPNIVFDDADLESAVVWT-AYGIFFNHGQVCCAGSRIYVQEGIY 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 349 StSLIRKMKDLAERRKLAD-----LTIGP-VLTFTTDSMLEHTNKLLEiPGSKLLFGGQPLENH---LIPSIYGAIKPta 419
Cdd:cd07143 302 D-KFVKRFKEKAKKLKVGDpfaedTFQGPqVSQIQYERIMSYIESGKA-EGATVETGGKRHGNEgyfIEPTIFTDVTE-- 377
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1540552764 420 vyvpieeivkdkNYELVTKEIFGPFQIITDYKSSQlsvvlDLIERMHAH---LTAAVVSND 477
Cdd:cd07143 378 ------------DMKIVKEEIFGPVVAVIKFKTEE-----EAIKRANDStygLAAAVFTNN 421
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
193-452 |
2.32e-10 |
|
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: 63.00 E-value: 2.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 193 RWPYGPVAIITPFNFPLEIPVLQLMGALYMGNKPVLKVDTKVSIVMEQMLRLLHTCGLPVEDVDFINSDGKTMNKLL-LE 271
Cdd:cd07112 122 REPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPAEQSPLTALRLAELALEAGLPAGVLNVVPGFGHTAGEALgLH 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 272 GNPRMTLFTGSSKVAEKL---ANDLNG-RVKLEDAGFDWKILGPDVHQEDYIAwvcDQDAYAC---SGQKCSAQSLLFMH 344
Cdd:cd07112 202 MDVDALAFTGSTEVGRRFleySGQSNLkRVWLECGGKSPNIVFADAPDLDAAA---EAAAAGIfwnQGEVCSAGSRLLVH 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 345 ENWSStSLIRKMKDLAERRKLAD-----LTIGPVLTFttdsmlEHTNKLL------EIPGSKLLFGGQPLEN-----HLI 408
Cdd:cd07112 279 ESIKD-EFLEKVVAAAREWKPGDpldpaTRMGALVSE------AHFDKVLgyiesgKAEGARLVAGGKRVLTetggfFVE 351
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1540552764 409 PSIYGAIKPTAvyvpieeivkdknyELVTKEIFGPFQIITDYKS 452
Cdd:cd07112 352 PTVFDGVTPDM--------------RIAREEIFGPVLSVITFDS 381
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
169-454 |
2.51e-10 |
|
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: 62.73 E-value: 2.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 169 DQVRFLA---RsfAVPGNHLGQQSHGF-----RWPYGPVAIITPFNFPLEIPVLQLMGALYMGNKPVLKVD--TKVSIvm 238
Cdd:cd07092 86 DNFRFFAgaaR--TLEGPAAGEYLPGHtsmirREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSetTPLTT-- 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 239 eQMLRLLHTCGLPVEDVDFINSDGKTMNKLLLEG-NPRMTLFTGSS----KVAEKLANDLNgRVKLEDAG------FDWK 307
Cdd:cd07092 162 -LLLAELAAEVLPPGVVNVVCGGGASAGDALVAHpRVRMVSLTGSVrtgkKVARAAADTLK-RVHLELGGkapvivFDDA 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 308 ILGPDVHQedyIAWVcdqdAYACSGQKCSAQSLLFMHENWSSTsLIRKMKDLAERRKL-----ADLTIGPVLTFTT-DSM 381
Cdd:cd07092 240 DLDAAVAG---IATA----GYYNAGQDCTAACRVYVHESVYDE-FVAALVEAVSAIRVgdpddEDTEMGPLNSAAQrERV 311
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1540552764 382 LEHTNKLLEipGSKLLFGGQPLENhliPSIYgaIKPTAVYVPieeivkDKNYELVTKEIFGPFQIITDYKSSQ 454
Cdd:cd07092 312 AGFVERAPA--HARVLTGGRRAEG---PGYF--YEPTVVAGV------AQDDEIVQEEIFGPVVTVQPFDDED 371
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
147-443 |
2.95e-10 |
|
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: 62.45 E-value: 2.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 147 KSYQQAFGEVYVTQKFLENFCGDQVRFLARSfaVPGNHLGQQSHGFRWPYGPVAIITPFNFPLEIPVLQLMGALYMGNKP 226
Cdd:cd07103 71 KPLAEARGEVDYAASFLEWFAEEARRIYGRT--IPSPAPGKRILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTV 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 227 VLKVDTKVSIVMEQMLRLLHTCGLPVEDVDFINSDGKTMNKLLLEgNPRMTL--FTGSSKVAEKLANDLNGRVK---LEd 301
Cdd:cd07103 149 VLKPAEETPLSALALAELAEEAGLPAGVLNVVTGSPAEIGEALCA-SPRVRKisFTGSTAVGKLLMAQAADTVKrvsLE- 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 302 agfdwkiLG---PdvhqedYIawVCDqDA-------------YACSGQKCSAQSLLFMHEnwsstSL----IRKMKDLAE 361
Cdd:cd07103 227 -------LGgnaP------FI--VFD-DAdldkavdgaiaskFRNAGQTCVCANRIYVHE-----SIydefVEKLVERVK 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 362 RRKL-----ADLTIGPVLTFTT-DSMLEHTNKLLEiPGSKLLFGGQPLENHliPSIYgaiKPTavyvpieeIVKD--KNY 433
Cdd:cd07103 286 KLKVgngldEGTDMGPLINERAvEKVEALVEDAVA-KGAKVLTGGKRLGLG--GYFY---EPT--------VLTDvtDDM 351
|
330
....*....|
gi 1540552764 434 ELVTKEIFGP 443
Cdd:cd07103 352 LIMNEETFGP 361
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
139-444 |
4.37e-10 |
|
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: 61.98 E-value: 4.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 139 RLIQRVSPKSYQQAFGEVyvtqkfleNFCGDQVRF---LARSfaVPGNHL----GQQSHGFRWPYGPVAIITPFNFPLEI 211
Cdd:cd07120 64 RLLALENGKILGEARFEI--------SGAISELRYyagLART--EAGRMIepepGSFSLVLREPMGVAGIIVPWNSPVVL 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 212 PVLQLMGALYMGNKPVLKVDTKVSIVMEQMLRLLHTC-GLPVEDVDFINSDGKTMNKLLLEGNPRMTL-FTGSSKVAEKL 289
Cdd:cd07120 134 LVRSLAPALAAGCTVVVKPAGQTAQINAAIIRILAEIpSLPAGVVNLFTESGSEGAAHLVASPDVDVIsFTGSTATGRAI 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 290 ANDLNGRVK---LEDAGFDWKILGPDVHQEDYIAwVCDQDAYACSGQKCSAQSLLFMHEnwsstSLIRKMKD-LAERrkL 365
Cdd:cd07120 214 MAAAAPTLKrlgLELGGKTPCIVFDDADLDAALP-KLERALTIFAGQFCMAGSRVLVQR-----SIADEVRDrLAAR--L 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 366 ADLTIGPVLTFTTD-------SMLEHTNKLLEIP---GSKLLFGGQPLENHLIPsiyGA-IKPTAVYVPieeivkDKNYE 434
Cdd:cd07120 286 AAVKVGPGLDPASDmgplidrANVDRVDRMVERAiaaGAEVVLRGGPVTEGLAK---GAfLRPTLLEVD------DPDAD 356
|
330
....*....|
gi 1540552764 435 LVTKEIFGPF 444
Cdd:cd07120 357 IVQEEIFGPV 366
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
5-451 |
4.89e-10 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 62.13 E-value: 4.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 5 LANRAARVSISPNRNACAAFNFSSRCVHSLPFATVEAEEISgSKPAEV---LNLVQGKWVGSSNWST--VVDPLNGESFI 79
Cdd:PLN02466 9 LLSRSLSASSSALLRSRGRNGGRGRGIRRFSTAAAAVEEPI-TPPVQVsytQLLINGQFVDAASGKTfpTLDPRTGEVIA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 80 KVAEVDGTGIQPFVESLSSCPKHGVHNPFKAPERYLMLgdvsTKAAHMLSlpKVSDFFTRLIQRVSPKSYQQAFG-EVYV 158
Cdd:PLN02466 88 HVAEGDAEDVNRAVAAARKAFDEGPWPKMTAYERSRIL----LRFADLLE--KHNDELAALETWDNGKPYEQSAKaELPM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 159 TQKFLENFCG--DQVRFLArsfaVP--GNHLGQQSHGfrwPYGPVAIITPFNFPLEIPVLQLMGALYMGNKPVLKVDTKV 234
Cdd:PLN02466 162 FARLFRYYAGwaDKIHGLT----VPadGPHHVQTLHE---PIGVAGQIIPWNFPLLMFAWKVGPALACGNTIVLKTAEQT 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 235 SIVMEQMLRLLHTCGLPVEDVDFINSDGKTMNKLLLEgnpRMTL----FTGSS---KVAEKLANDLNGR-VKLEDAGFDW 306
Cdd:PLN02466 235 PLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALAS---HMDVdklaFTGSTdtgKIVLELAAKSNLKpVTLELGGKSP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 307 KILGPDVHQED-----YIAWVCDQdayacsGQKCSAQSLLFMHENwSSTSLIRKMKDLAERRKLAD-----LTIGPVLtf 376
Cdd:PLN02466 312 FIVCEDADVDKavelaHFALFFNQ------GQCCCAGSRTFVHER-VYDEFVEKAKARALKRVVGDpfkkgVEQGPQI-- 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 377 ttDSmlEHTNKLLEI------PGSKLLFGGQPLENHlipSIYgaIKPTaVYVPIEEivkdkNYELVTKEIFGPFQIITDY 450
Cdd:PLN02466 383 --DS--EQFEKILRYiksgveSGATLECGGDRFGSK---GYY--IQPT-VFSNVQD-----DMLIAQDEIFGPVQSILKF 447
|
.
gi 1540552764 451 K 451
Cdd:PLN02466 448 K 448
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
49-443 |
5.06e-10 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 62.07 E-value: 5.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 49 PAEVLNLVQGKWVGSSNwSTVVDPLNGESFIKVAEVDGTGIQPFVESLSSCPKH---GVHNPFKAPERYLMlgdvstKAA 125
Cdd:PLN02419 111 PPRVPNLIGGSFVESQS-SSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAfplWRNTPITTRQRVML------KFQ 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 126 HMLSlpKVSDFFTRLIQRVSPKSYQQAFGEVYVTQKFLENFCGdqVRFLARSFAVPGNHLGQQSHGFRWPYGPVAIITPF 205
Cdd:PLN02419 184 ELIR--KNMDKLAMNITTEQGKTLKDSHGDIFRGLEVVEHACG--MATLQMGEYLPNVSNGVDTYSIREPLGVCAGICPF 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 206 NFPLEIPVLQLMGALYMGNKPVLKVDTK---VSIVMEQmlrLLHTCGLPVEDVDFINSDGKTMNKLLLEGNPRMTLFTGS 282
Cdd:PLN02419 260 NFPAMIPLWMFPVAVTCGNTFILKPSEKdpgASVILAE---LAMEAGLPDGVLNIVHGTNDTVNAICDDEDIRAVSFVGS 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 283 SKVAEKL---ANDLNGRVKLEDAGFDWKILGPDVHQEDYIAWVCdQDAYACSGQKCSAQSLLFM---HENWSStSLIRKM 356
Cdd:PLN02419 337 NTAGMHIyarAAAKGKRIQSNMGAKNHGLVLPDANIDATLNALL-AAGFGAAGQRCMALSTVVFvgdAKSWED-KLVERA 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 357 KDLAER-RKLADLTIGPVLtftTDSMLEHTNKLLEI---PGSKLLFGGQPL-------ENHLIPSIYGAIKPtavyvpie 425
Cdd:PLN02419 415 KALKVTcGSEPDADLGPVI---SKQAKERICRLIQSgvdDGAKLLLDGRDIvvpgyekGNFIGPTILSGVTP-------- 483
|
410
....*....|....*...
gi 1540552764 426 eivkdkNYELVTKEIFGP 443
Cdd:PLN02419 484 ------DMECYKEEIFGP 495
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
197-464 |
5.51e-10 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 62.14 E-value: 5.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 197 GPVAIITPFNFPLEIPVLQLMGALYMGNKPVLKVDTKVSIVMEQMLRLLHTCGLPVEDVDFINSDGKTMNKLLLEgNPRM 276
Cdd:PRK11904 686 GVFVCISPWNFPLAIFLGQVAAALAAGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVGAALTA-DPRI 764
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 277 T--LFTGSSKVAEKLANDLNGRvkledagfDWKILgPdvhqedYIA-----------------WVCD---QDAYACSGQK 334
Cdd:PRK11904 765 AgvAFTGSTETARIINRTLAAR--------DGPIV-P------LIAetggqnamivdstalpeQVVDdvvTSAFRSAGQR 829
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 335 CSAQSLLFMHEnwsstslirkmkDLAER---------RKL-----ADLT--IGPVLTFTTDSMLE-HTNKLLEipGSKLL 397
Cdd:PRK11904 830 CSALRVLFVQE------------DIADRviemlkgamAELkvgdpRLLStdVGPVIDAEAKANLDaHIERMKR--EARLL 895
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1540552764 398 F----GGQPLENHLIPsiygaikPTAVyvpieEIvkdKNYELVTKEIFGPFQIITDYKSSQLSVVLDLIER 464
Cdd:PRK11904 896 AqlplPAGTENGHFVA-------PTAF-----EI---DSISQLEREVFGPILHVIRYKASDLDKVIDAINA 951
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
58-452 |
9.52e-10 |
|
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: 61.07 E-value: 9.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 58 GKWVGSSNWSTVVDPLNGEsfiKVAEVDGTGIQPFVESLSSCpkhgvHNPFK------APERYLM---LGDVSTKAAHML 128
Cdd:cd07130 5 GEWGGGGGVVTSISPANGE---PIARVRQATPEDYESTIKAA-----QEAFKewrdvpAPKRGEIvrqIGDALRKKKEAL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 129 SlpkvsdfftRLIQRVSPKSYQQAFGEVyvtQKFLEnFCgDQVRFLARSFA-------VPGNHLGQQSHgfrwPYGPVAI 201
Cdd:cd07130 77 G---------KLVSLEMGKILPEGLGEV---QEMID-IC-DFAVGLSRQLYgltipseRPGHRMMEQWN----PLGVVGV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 202 ITPFNFPLEIPVLQLMGALYMGNKPVLKVDTKVSI----VMEQMLRLLHTCGLPvEDVDFINSDGKTMNKLLLEgNPRMT 277
Cdd:cd07130 139 ITAFNFPVAVWGWNAAIALVCGNVVVWKPSPTTPLtaiaVTKIVARVLEKNGLP-GAIASLVCGGADVGEALVK-DPRVP 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 278 L--FTGSS----KVAEKLANDLnGRVKLEDAGFDWKILGPDVHqedyIAWVCDQDAYAC---SGQKCSAQSLLFMHENWS 348
Cdd:cd07130 217 LvsFTGSTavgrQVGQAVAARF-GRSLLELGGNNAIIVMEDAD----LDLAVRAVLFAAvgtAGQRCTTTRRLIVHESIY 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 349 STSLIRKMKDLAERR---KLADLTI-GPVLTFTTDSMLEHTNKLLEIPGSKLLFGGQPLENhliPSIYgaIKPTAVYVPi 424
Cdd:cd07130 292 DEVLERLKKAYKQVRigdPLDDGTLvGPLHTKAAVDNYLAAIEEAKSQGGTVLFGGKVIDG---PGNY--VEPTIVEGL- 365
|
410 420
....*....|....*....|....*...
gi 1540552764 425 eeivkdKNYELVTKEIFGPFQIITDYKS 452
Cdd:cd07130 366 ------SDAPIVKEETFAPILYVLKFDT 387
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
135-477 |
1.12e-09 |
|
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: 60.62 E-value: 1.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 135 DFFTRLIQRVSPKSYQQAFGEVYVTQKFLENfcgdqvrflARSFA-------VPGNHLGQQSHGFRWPYGPVAIITPFNF 207
Cdd:cd07104 40 DEIADWLIRESGSTRPKAAFEVGAAIAILRE---------AAGLPrrpegeiLPSDVPGKESMVRRVPLGVVGVISPFNF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 208 PLEIPVLQLMGALYMGNKPVLKVDTKVSIVMEQML-RLLHTCGLP-------VEDVDFINsdgktmNKLLLEGNPRMTLF 279
Cdd:cd07104 111 PLILAMRSVAPALALGNAVVLKPDSRTPVTGGLLIaEIFEEAGLPkgvlnvvPGGGSEIG------DALVEHPRVRMISF 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 280 TGSS----KVAEKLANDLNgRVKLEDAGFDWKILGPDVHQE---DYIAWvcdqDAYACSGQKCSAQSLLFMHEnwsstSL 352
Cdd:cd07104 185 TGSTavgrHIGELAGRHLK-KVALELGGNNPLIVLDDADLDlavSAAAF----GAFLHQGQICMAAGRILVHE-----SV 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 353 ----IRKMKDLAERRKLADLT-----IGPVLTFT-TDSMLEHTNKLLEiPGSKLLFGGQPLENHLIPSIYGAIKPtavyv 422
Cdd:cd07104 255 ydefVEKLVAKAKALPVGDPRdpdtvIGPLINERqVDRVHAIVEDAVA-AGARLLTGGTYEGLFYQPTVLSDVTP----- 328
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 423 pieeivkdkNYELVTKEIFGPFQIITDYKSSQLSVVLdliermhAH-----LTAAVVSND 477
Cdd:cd07104 329 ---------DMPIFREEIFGPVAPVIPFDDDEEAVEL-------ANdteygLSAAVFTRD 372
|
|
| lactal_redase_Meth |
NF040648 |
lactaldehyde dehydrogenase; |
55-443 |
1.33e-09 |
|
lactaldehyde dehydrogenase;
Pssm-ID: 468615 [Multi-domain] Cd Length: 463 Bit Score: 60.39 E-value: 1.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 55 LVQGKWVGSSNWStVVDPLNGESFIKVAEVDGTGIQPFVESLSSCPKhgVHNPFKAPERYLMLGDVSTKaahmlsLPKVS 134
Cdd:NF040648 2 FINGKWIDREDID-VINPYNLEVIDKIPSLSREEVKEAIEIANEAKE--VMKNLSPRKRYNILMDIAEE------LKKNK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 135 DFFTRLIQRVSPKSYQQAFGEVyvtQKFLENFcgdqvRFLA------RSFAVPGNhlgqQSHGF--RWPYGPVAIITPFN 206
Cdd:NF040648 73 EELAKLITIDAGKPIKQSIIEV---DRSIETF-----KLAAfyakeiRGETIPSD----AGLIFtkKEPLGVVGAITPFN 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 207 FPLEIPVLQLMGALYMGNKPVLKVDTKVSIVMEQMLRL----LHTCGLPVEDVDFINSDGKTMNKLLLEgNPR--MTLFT 280
Cdd:NF040648 141 YPLNLAAHKIAPAIATGNSVVLHPSSKAPLAAIELAKIiekvLKKMNIPLGVFNLVTGYGEVVGDEIVK-NEKvnKISFT 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 281 GSSKVAEKLANDLN-GRVKLEDAGFDWKILGPDVHQEDYIAwVCDQDAYACSGQKCSAQSLLFMHENWSST---SLIRKM 356
Cdd:NF040648 220 GSVEVGESISKKAGmKKITLELGGNNPLIVLKDADIEKAVE-SAVKGSFLNSGQVCISVGRVIVEEEIADEfikKLVEET 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 357 KDLAERRKLADLT-IGPVLTFTTDSMLEHT-NKLLEiPGSKLLFGGQPlENHLipsiygaIKPTAVYVpieeivkDKNYE 434
Cdd:NF040648 299 KKLKVGNPLDEKTdIGPLITEEAAIRVENLvNEAIE-EGAKLLCGGNR-EGSL-------FYPTVLDV-------DEDNI 362
|
....*....
gi 1540552764 435 LVTKEIFGP 443
Cdd:NF040648 363 LVKVETFGP 371
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
180-478 |
1.38e-09 |
|
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, p-hydroxybenzaldehyde dehydrogenase (PchA, HBenzADH) which catalyzes oxidation of p-hydroxybenzaldehyde to p-hydroxybenzoic acid and other related sequences are included in this CD.
Pssm-ID: 143469 [Multi-domain] Cd Length: 465 Bit Score: 60.40 E-value: 1.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 180 VPGNHLGQQSHGFRWPYGPVAIITPFNFPLEIPVLQLMGALYMGNKPVLKVDTKVSIVMEQML-RLLHTCGLPVEDVDFI 258
Cdd:cd07151 115 LPSDVPGKENRVYREPLGVVGVISPWNFPLHLSMRSVAPALALGNAVVLKPASDTPITGGLLLaKIFEEAGLPKGVLNVV 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 259 NSDGKTMNKLLLEGN-PRMTLFTGSSKVA-----------EKLANDLNGR---VKLEDAGFDWKI----LGPDVHQedyi 319
Cdd:cd07151 195 VGAGSEIGDAFVEHPvPRLISFTGSTPVGrhigelagrhlKKVALELGGNnpfVVLEDADIDAAVnaavFGKFLHQ---- 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 320 awvcdqdayacsGQKCSAQSLLFMHENWSStSLIRKMKDLAERRKLADLT-----IGPVLtftTDSMLEHTNKLLEIP-- 392
Cdd:cd07151 271 ------------GQICMAINRIIVHEDVYD-EFVEKFVERVKALPYGDPSdpdtvVGPLI---NESQVDGLLDKIEQAve 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 393 -GSKLLFGGQPLENHLIPSIYGAIKPtavyvpieeivkdkNYELVTKEIFGPFQIITDYKSSQlsVVLDLIERMHAHLTA 471
Cdd:cd07151 335 eGATLLVGGEAEGNVLEPTVLSDVTN--------------DMEIAREEIFGPVAPIIKADDEE--EALELANDTEYGLSG 398
|
....*..
gi 1540552764 472 AVVSNDP 478
Cdd:cd07151 399 AVFTSDL 405
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
189-478 |
1.71e-09 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 60.13 E-value: 1.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 189 SHGFRWPYGPVAIITPFNFPLEIPVLQLMGALYMGNKPVLKVDTKVSIVMEQMLRLLHTCGLPVEDVDFINSDGKTMNKL 268
Cdd:PLN02467 145 GYVLKEPLGVVGLITPWNYPLLMATWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAP 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 269 LlEGNPRM--TLFTGSSKVAEKLANDLNGRVK---LEDAGFDWKILGPDVHQEDYIAWVcdqdAYAC---SGQKCSAQSL 340
Cdd:PLN02467 225 L-ASHPGVdkIAFTGSTATGRKIMTAAAQMVKpvsLELGGKSPIIVFDDVDLDKAVEWA----MFGCfwtNGQICSATSR 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 341 LFMHENWSStSLIRKMKDLAERRKLAD-LT----IGPVLtftTDSMLEHTNKLLEIP---GSKLLFGG-QPleNHLIPSI 411
Cdd:PLN02467 300 LLVHERIAS-EFLEKLVKWAKNIKISDpLEegcrLGPVV---SEGQYEKVLKFISTAkseGATILCGGkRP--EHLKKGF 373
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1540552764 412 YgaIKPTAVY-VPieeivkdKNYELVTKEIFGPFQIITDYKSSQLSVvlDLIERMHAHLTAAVVSNDP 478
Cdd:PLN02467 374 F--IEPTIITdVT-------TSMQIWREEVFGPVLCVKTFSTEDEAI--ELANDSHYGLAGAVISNDL 430
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
193-452 |
2.64e-09 |
|
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: 59.37 E-value: 2.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 193 RWPYGPVAIITPFNFPLEIPVLQLMGALYMGNKPVLKVDTKVSIVMEQMLRLLHTCGLPVEDVDFINSDGKTMNKLLLE- 271
Cdd:cd07115 115 REPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSALRIAELMAEAGFPAGVLNVVTGFGEVAGAALVEh 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 272 -GNPRMTlFTGSSKVAEKLANDLNG---RVKLEDAGFDWKILGPDVHQEDYI---AWvcdqDAYACSGQKCSAQSLLFMH 344
Cdd:cd07115 195 pDVDKIT-FTGSTAVGRKIMQGAAGnlkRVSLELGGKSANIVFADADLDAAVraaAT----GIFYNQGQMCTAGSRLLVH 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 345 ENWSS------TSLIRKMK--DLAERRKladlTIGPVLTfttdsmLEHTNKLLEI------PGSKLLFGGQPLENH---L 407
Cdd:cd07115 270 ESIYDeflerfTSLARSLRpgDPLDPKT----QMGPLVS------QAQFDRVLDYvdvgreEGARLLTGGKRPGARgffV 339
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1540552764 408 IPSIYGAIKPTavyvpieeivkdknYELVTKEIFGPFQIITDYKS 452
Cdd:cd07115 340 EPTIFAAVPPE--------------MRIAQEEIFGPVVSVMRFRD 370
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
195-452 |
2.88e-09 |
|
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: 59.24 E-value: 2.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 195 PYGPVAIITPFNFPLEIPVLQLMGALYMGNKPVLKVDTKVSIVMEQMLRLLHT----CGLPVEDVDFINSDGKTMNKLLL 270
Cdd:cd07098 120 PLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQVAWSSGFFLSIIREclaaCGHDPDLVQLVTCLPETAEALTS 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 271 EGNPRMTLFTGSSKVAEKLAN---DLNGRVKLEDAGFDWKILGPDvHQEDYIAWVCDQDAYACSGQKCSAQSLLFMHENW 347
Cdd:cd07098 200 HPVIDHITFIGSPPVGKKVMAaaaESLTPVVLELGGKDPAIVLDD-ADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKI 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 348 SSTsLIRKMKDLAERrkladLTIGPVLTFTTD--SML--EHTNKLLEI------PGSKLLFGGQPLENHLIPSiyGAIKP 417
Cdd:cd07098 279 YDK-LLEILTDRVQA-----LRQGPPLDGDVDvgAMIspARFDRLEELvadaveKGARLLAGGKRYPHPEYPQ--GHYFP 350
|
250 260 270
....*....|....*....|....*....|....*
gi 1540552764 418 TAVYVPIeeivkDKNYELVTKEIFGPFQIITDYKS 452
Cdd:cd07098 351 PTLLVDV-----TPDMKIAQEEVFGPVMVVMKASD 380
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
195-367 |
3.77e-09 |
|
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: 58.95 E-value: 3.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 195 PYGPVAIITPFNFPLEIPVLQLMGALYMGNKPVLKVDTKVSIVMEQMLRLLHTCGLPVEDVDFINSDGKTMNKLLLEGNP 274
Cdd:cd07111 147 PVGVVGQIVPWNFPLLMLAWKICPALAMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNGSFGSALANHPGV 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 275 RMTLFTGSSKVAEKLANDLNGRVK---LEDAGFDWKILGPDVHQEDYIAWVCDQdAYACSGQKCSAQSLLFMHENWSStS 351
Cdd:cd07111 227 DKVAFTGSTEVGRALRRATAGTGKklsLELGGKSPFIVFDDADLDSAVEGIVDA-IWFNQGQVCCAGSRLLVQESVAE-E 304
|
170
....*....|....*.
gi 1540552764 352 LIRKMKDLAERRKLAD 367
Cdd:cd07111 305 LIRKLKERMSHLRVGD 320
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
140-462 |
4.55e-09 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 59.49 E-value: 4.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 140 LIQRVSPKSYQQAFGEVYvtqkflE--NFCgdqvRFLA---RSFAVPGNHLgqqshgfrwPYGPVAIITPFNFPLEIPVL 214
Cdd:PRK11905 635 LAVREAGKTLANAIAEVR------EavDFL----RYYAaqaRRLLNGPGHK---------PLGPVVCISPWNFPLAIFTG 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 215 QLMGALYMGNkPVL-KVDTKVSIVMEQMLRLLHTCGLPVEDVDFINSDGKTMNKLLLeGNPRMT--LFTGSSKVAEK--- 288
Cdd:PRK11905 696 QIAAALVAGN-TVLaKPAEQTPLIAARAVRLLHEAGVPKDALQLLPGDGRTVGAALV-ADPRIAgvMFTGSTEVARLiqr 773
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 289 -LANDLNGRVKL--EDAGFDWKI-----LGPDVHQeDYIAwvcdqDAYACSGQKCSAQSLLFMHEnwsstslirkmkDLA 360
Cdd:PRK11905 774 tLAKRSGPPVPLiaETGGQNAMIvdssaLPEQVVA-DVIA-----SAFDSAGQRCSALRVLCLQE------------DVA 835
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 361 ERR------KLADLTI----------GPVLTFTT-DSMLEHTNKLLEIpgskllfgGQPLENHLIPSIYGA---IKPTAV 420
Cdd:PRK11905 836 DRVltmlkgAMDELRIgdpwrlstdvGPVIDAEAqANIEAHIEAMRAA--------GRLVHQLPLPAETEKgtfVAPTLI 907
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1540552764 421 yvpieEIvkdKNYELVTKEIFGP-FQIITdYKSSQLSVVLDLI 462
Cdd:PRK11905 908 -----EI---DSISDLEREVFGPvLHVVR-FKADELDRVIDDI 941
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
193-459 |
5.02e-09 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 58.75 E-value: 5.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 193 RWPYGPVAIITPFNFPLEIPVLQLMGALYMGNKPVLKVDTKVSIVMEQMLRLLHTCGLPVEDVDFINSDGKTMNKLL-LE 271
Cdd:PRK09847 155 REPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALsRH 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 272 GNPRMTLFTGSSKVAEKL---ANDLN-GRVKLEDAGFDWKILGPDVHQEDYIAWVCDQDAYACSGQKCSAQSLLFMHENW 347
Cdd:PRK09847 235 NDIDAIAFTGSTRTGKQLlkdAGDSNmKRVWLEAGGKSANIVFADCPDLQQAASATAAGIFYNQGQVCIAGTRLLLEESI 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 348 SSTSLIRKmkdlaeRRKLADLTIG-PVLTFTTDSML------EHTNKLLEIPGSKllfgGQPLENHLIPSIYGAIKPTaV 420
Cdd:PRK09847 315 ADEFLALL------KQQAQNWQPGhPLDPATTMGTLidcahaDSVHSFIREGESK----GQLLLDGRNAGLAAAIGPT-I 383
|
250 260 270
....*....|....*....|....*....|....*....
gi 1540552764 421 YVPIeeivkDKNYELVTKEIFGPFQIITDYKSSQLSVVL 459
Cdd:PRK09847 384 FVDV-----DPNASLSREEIFGPVLVVTRFTSEEQALQL 417
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
149-477 |
5.27e-09 |
|
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: 58.54 E-value: 5.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 149 YQQAFGEVYVTQKFLENFCGDQVRFLARSFAVPGNHLgqqSHGFRWPYGPVAIITPFNFPLEIPVLQLMGALYMGNKPVL 228
Cdd:cd07107 73 VSAMLGDVMVAAALLDYFAGLVTELKGETIPVGGRNL---HYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVV 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 229 KVDTKV---SIVMEQMLRLLhtcgLPVEDVDFINSDGKTMNKLLLEgNP--RMTLFTGSSKVAEKLANDLNGRVK---LE 300
Cdd:cd07107 150 KPPEQAplsALRLAELAREV----LPPGVFNILPGDGATAGAALVR-HPdvKRIALIGSVPTGRAIMRAAAEGIKhvtLE 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 301 DAGFDWKILGPDVHQEDYIAWVCDQDAYACSGQKCSAQSLLFMHENWSSTSLIRKMKDLAERR----KLADLTIGPVLtf 376
Cdd:cd07107 225 LGGKNALIVFPDADPEAAADAAVAGMNFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKvgdpTDPATTMGPLV-- 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 377 tTDSMLEHTNKLLEIP---GSKLLFGGQPLENHLIPSIYgAIKPTaVYVPIeeivkDKNYELVTKEIFGPFQIITDYKSS 453
Cdd:cd07107 303 -SRQQYDRVMHYIDSAkreGARLVTGGGRPEGPALEGGF-YVEPT-VFADV-----TPGMRIAREEIFGPVLSVLRWRDE 374
|
330 340
....*....|....*....|....
gi 1540552764 454 QlsVVLDLIERMHAHLTAAVVSND 477
Cdd:cd07107 375 A--EMVAQANGVEYGLTAAIWTND 396
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
69-443 |
8.96e-09 |
|
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: 57.63 E-value: 8.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 69 VVDPLNGESFIKVA-----EVDGtGIQPFVESLSSCPKHgvhnpFKAPERYLMLGDVstkAAHMLslpKVSDFFTRLIQR 143
Cdd:cd07109 1 VFDPSTGEVFARIArggaaDVDR-AVQAARRAFESGWLR-----LSPAERGRLLLRI---ARLIR---EHADELARLESL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 144 VSPKSYQQAFGEVYVTQKFLENFCGDQVRFLARSFAvpgnhLGQQSHGF--RWPYGPVAIITPFNFPLEIPVLQLMGALY 221
Cdd:cd07109 69 DTGKPLTQARADVEAAARYFEYYGGAADKLHGETIP-----LGPGYFVYtvREPHGVTGHIIPWNYPLQITGRSVAPALA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 222 MGNKPVLKV--DTKVSIVMeqMLRLLHTCGLPVEDVDFINSDGKTMNKLLLEgNPRM--TLFTGS----SKVAEKLANDL 293
Cdd:cd07109 144 AGNAVVVKPaeDAPLTALR--LAELAEEAGLPAGALNVVTGLGAEAGAALVA-HPGVdhISFTGSvetgIAVMRAAAENV 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 294 NGrVKLEDAGFDWKILGPDVHQE---DYIAWVCDQDAyacsGQKCSAQSLLFMHENWSStSLIRKMKDLAERRK----LA 366
Cdd:cd07109 221 VP-VTLELGGKSPQIVFADADLEaalPVVVNAIIQNA----GQTCSAGSRLLVHRSIYD-EVLERLVERFRALRvgpgLE 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 367 DLTIGPVLtftTDSMLEHTNKLLEIP---GSKLLFGGQPLENHL------IPSIYGAIKPtavyvpieeivkdkNYELVT 437
Cdd:cd07109 295 DPDLGPLI---SAKQLDRVEGFVARArarGARIVAGGRIAEGAPaggyfvAPTLLDDVPP--------------DSRLAQ 357
|
....*.
gi 1540552764 438 KEIFGP 443
Cdd:cd07109 358 EEIFGP 363
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
55-444 |
4.72e-08 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 55.68 E-value: 4.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 55 LVQGKWVGSSNWST--VVDPLNGESfikvaevdgtgiqpfvesLSSCPKHGVHNPFKAPE---------RYLMLGDVSTK 123
Cdd:PRK11241 14 LINGEWLDANNGEVidVTNPANGDK------------------LGSVPKMGADETRAAIDaanralpawRALTAKERANI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 124 AAHMLSLP-KVSDFFTRLIQRVSPKSYQQAFGEVYVTQKFLENFCGDQVRFLARSfaVPGNHLGQQSHGFRWPYGPVAII 202
Cdd:PRK11241 76 LRRWFNLMmEHQDDLARLMTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGDT--IPGHQADKRLIVIKQPIGVTAAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 203 TPFNFPLEIPVLQLMGALYMGNKPVLKVDTKVSIVMEQMLRLLHTCGLPVEDVDFIN-SDGKTMNKllLEGNP--RMTLF 279
Cdd:PRK11241 154 TPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTgSAGAVGGE--LTSNPlvRKLSF 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 280 TGSSKVAEKL----ANDLNgRVKLEDAG------FDWKILgpDVHQEDYIAwvcdqDAYACSGQKCSAQSLLFMHENwSS 349
Cdd:PRK11241 232 TGSTEIGRQLmeqcAKDIK-KVSLELGGnapfivFDDADL--DKAVEGALA-----SKFRNAGQTCVCANRLYVQDG-VY 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 350 TSLIRKMKDLAERRKL-----ADLTIGPVLTFTTDSML-EHTNKLLEiPGSKLLFGGQPLE---NHLIPSIYgaikptaV 420
Cdd:PRK11241 303 DRFAEKLQQAVSKLHIgdgleKGVTIGPLIDEKAVAKVeEHIADALE-KGARVVCGGKAHElggNFFQPTIL-------V 374
|
410 420
....*....|....*....|....
gi 1540552764 421 YVPieeivkdKNYELVTKEIFGPF 444
Cdd:PRK11241 375 DVP-------ANAKVAKEETFGPL 391
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
140-462 |
7.22e-08 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 55.71 E-value: 7.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 140 LIQRVSPKSYQQAFGEVYvtqkflE--NFC---GDQVRflaRSFAVPGNHLGQqshgfrwpyGPVAIITPFNFPLEIPVL 214
Cdd:COG4230 638 LLVREAGKTLPDAIAEVR------EavDFCryyAAQAR---RLFAAPTVLRGR---------GVFVCISPWNFPLAIFTG 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 215 QLMGALYMGN----KPVlkvdtkvsivmEQ-------MLRLLHTCGLPVEDVDFINSDGKTMNKLLLeGNPRMT--LFTG 281
Cdd:COG4230 700 QVAAALAAGNtvlaKPA-----------EQtpliaarAVRLLHEAGVPADVLQLLPGDGETVGAALV-ADPRIAgvAFTG 767
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 282 SSKVAEKLANDLNGRvkledagfdwkiLGPDVhqeDYIA-----------------WVCD---QDAYACSGQKCSAQSLL 341
Cdd:COG4230 768 STETARLINRTLAAR------------DGPIV---PLIAetggqnamivdssalpeQVVDdvlASAFDSAGQRCSALRVL 832
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 342 FMHEnwsstslirkmkDLAER------RKLADLT----------IGPVLTFTTDSMLE-HTNKLLEIpgSKLLF----GG 400
Cdd:COG4230 833 CVQE------------DIADRvlemlkGAMAELRvgdpadlstdVGPVIDAEARANLEaHIERMRAE--GRLVHqlplPE 898
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1540552764 401 QPLENHLIPsiygaikPTAVYVP-IEEIvkdknyelvTKEIFGPF-QIITdYKSSQLSVVLDLI 462
Cdd:COG4230 899 ECANGTFVA-------PTLIEIDsISDL---------EREVFGPVlHVVR-YKADELDKVIDAI 945
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
179-494 |
7.52e-08 |
|
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: 55.00 E-value: 7.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 179 AVPGNH--LGQQSHGF--RWPYGPVAIITPFNFPLEIPVLQLMGALYMGNKPVLKVD--TKVSIVMeqMLRLLHTCGLPV 252
Cdd:cd07090 96 TLSGEHvpLPGGSFAYtrREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSpfTPLTALL--LAEILTEAGLPD 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 253 EDVDFINSDGKTMNKLLLEGNPRMTLFTGS----SKVAEKLANDLNgRVKLEDAGFDWKILGPDvhqedyiawvCDQDAy 328
Cdd:cd07090 174 GVFNVVQGGGETGQLLCEHPDVAKVSFTGSvptgKKVMSAAAKGIK-HVTLELGGKSPLIIFDD----------ADLEN- 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 329 ACS----------GQKCSAQSLLFMHenwsstsliRKMKD-----LAERRK--------LADLTIGPVLTFttdsmlEHT 385
Cdd:cd07090 242 AVNgammanflsqGQVCSNGTRVFVQ---------RSIKDefterLVERTKkirigdplDEDTQMGALISE------EHL 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 386 NKLLEI------PGSKLLFGGQPL--ENHLIPSIYgaIKPTaVYVPIEEivkdkNYELVTKEIFGPFQIITDYKSSQlsv 457
Cdd:cd07090 307 EKVLGYiesakqEGAKVLCGGERVvpEDGLENGFY--VSPC-VLTDCTD-----DMTIVREEIFGPVMSILPFDTEE--- 375
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1540552764 458 vlDLIER---MHAHLTAAVVSNDPLFLQEVIGKSVNGTTY 494
Cdd:cd07090 376 --EVIRRandTTYGLAAGVFTRDLQRAHRVIAQLQAGTCW 413
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
192-477 |
1.32e-07 |
|
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: 54.27 E-value: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 192 FRWPYGPVAIITPFNFPLEIPVLQLMGALYMGNKPVLK--VDTKVSI--VMEQMLRLlhtcgLPVEDVDFINSDGKTMNK 267
Cdd:cd07559 133 FHEPLGVVGQIIPWNFPLLMAAWKLAPALAAGNTVVLKpaSQTPLSIlvLMELIGDL-----LPKGVVNVVTGFGSEAGK 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 268 LLLEgNPRMT--LFTGSSKVAEKLANDLNGR---VKLEDAGFDWKILGPDVHQED---YIAWVCDQDAYAC-SGQKCSAQ 338
Cdd:cd07559 208 PLAS-HPRIAklAFTGSTTVGRLIMQYAAENlipVTLELGGKSPNIFFDDAMDADddfDDKAEEGQLGFAFnQGEVCTCP 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 339 SLLFMHENwsstslI--RKMKDLAERrkLADLTIGPVLtfTTDSML------EHTNKLL---EI---PGSKLLFGGQPL- 403
Cdd:cd07559 287 SRALVQES------IydEFIERAVER--FEAIKVGNPL--DPETMMgaqvskDQLEKILsyvDIgkeEGAEVLTGGERLt 356
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1540552764 404 ENHLIPSIYgaIKPTAVYVPieeivkDKNYELVTKEIFGPFQIITDYKSSQlsVVLDLIERMHAHLTAAVVSND 477
Cdd:cd07559 357 LGGLDKGYF--YEPTLIKGG------NNDMRIFQEEIFGPVLAVITFKDEE--EAIAIANDTEYGLGGGVWTRD 420
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
195-491 |
1.58e-07 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 53.88 E-value: 1.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 195 PYGPVAIITPFNFPLEIPVLQLMGALYMGNKPVLKVDTKVSIVMEQMLRLLhTCGLPVEDVDFINSdGKTMNKLLLEGNP 274
Cdd:PTZ00381 109 PLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLL-TKYLDPSYVRVIEG-GVEVTTELLKEPF 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 275 RMTLFTGSSKV--------AEKLANdlngrVKLEDAGFDWKILGPDVHQE---DYIAWVCDQDAyacsGQKCSAQSLLFM 343
Cdd:PTZ00381 187 DHIFFTGSPRVgklvmqaaAENLTP-----CTLELGGKSPVIVDKSCNLKvaaRRIAWGKFLNA----GQTCVAPDYVLV 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 344 HENwSSTSLIRKMKdlaerRKLADLtIGP-----------VLTFTTDSMLEhtnkLLEIPGSKLLFGGQPLENHLIpsiy 412
Cdd:PTZ00381 258 HRS-IKDKFIEALK-----EAIKEF-FGEdpkksedysriVNEFHTKRLAE----LIKDHGGKVVYGGEVDIENKY---- 322
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1540552764 413 gaIKPTAVYVPieeivkDKNYELVTKEIFGPFQIITDYKSSQLsvVLDLIERMHAHLTAAVVSNDPLFLQEVIGKSVNG 491
Cdd:PTZ00381 323 --VAPTIIVNP------DLDSPLMQEEIFGPILPILTYENIDE--VLEFINSRPKPLALYYFGEDKRHKELVLENTSSG 391
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
193-454 |
5.92e-07 |
|
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: 52.07 E-value: 5.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 193 RWPYGPVAIITPFNFPLEIPVLQLMGALYMGNKPVLKVDTKVSIVMEQMLRLLHTCgLPVEDVDFINSDGKTMNKLLLEG 272
Cdd:cd07117 134 REPIGVVGQIIPWNFPFLMAAWKLAPALAAGNTVVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIVTGKGSKSGEYLLNH 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 273 NPRMTL-FTGSSKVAEKLAN-----------DLNGR---VKLEDAGFDWKILGPDVHqedyIAWvcDQdayacsGQKCSA 337
Cdd:cd07117 213 PGLDKLaFTGSTEVGRDVAIaaakklipatlELGGKsanIIFDDANWDKALEGAQLG----ILF--NQ------GQVCCA 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 338 QSLLFMHENWSStSLIRKMKDlaerrKLADLTIGPVLTFTT-------DSMLEHTNKLLEI---PGSKLLFGGQPL-ENH 406
Cdd:cd07117 281 GSRIFVQEGIYD-EFVAKLKE-----KFENVKVGNPLDPDTqmgaqvnKDQLDKILSYVDIakeEGAKILTGGHRLtENG 354
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1540552764 407 LIPSIYgaIKPTAVyvpieeIVKDKNYELVTKEIFGPFQIITDYKSSQ 454
Cdd:cd07117 355 LDKGFF--IEPTLI------VNVTNDMRVAQEEIFGPVATVIKFKTED 394
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
55-452 |
8.26e-07 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 51.61 E-value: 8.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 55 LVQGKWVGSSNWST--VVDPLNGESfikVAEVDGTGIQPFVESLSSCpkHGVHNPFK---APERYLMLgdvstKAAHMLS 129
Cdd:PLN02278 28 LIGGKWTDAYDGKTfpVYNPATGEV---IANVPCMGRAETNDAIASA--HDAFPSWSkltASERSKIL-----RRWYDLI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 130 LPKVSDFfTRLIQRVSPKSYQQAFGEVYVTQKFLENFCGDQVRflARSFAVPGNHLGQQSHGFRWPYGPVAIITPFNFPL 209
Cdd:PLN02278 98 IANKEDL-AQLMTLEQGKPLKEAIGEVAYGASFLEYFAEEAKR--VYGDIIPSPFPDRRLLVLKQPVGVVGAITPWNFPL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 210 EIPVLQLMGALYMGNKPVLKVDTKVSIVMEQMLRLLHTCGLPVEDVDFINSDGKTMNKLLLEgNP--RMTLFTGSSKVAE 287
Cdd:PLN02278 175 AMITRKVGPALAAGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEIGDALLA-SPkvRKITFTGSTAVGK 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 288 KLANDLNGRVK---LEDAGFDWKILGPDVHQEdyiawVCDQDAYAC----SGQKCSAQSLLFMHENWS---STSLIRKMK 357
Cdd:PLN02278 254 KLMAGAAATVKrvsLELGGNAPFIVFDDADLD-----VAVKGALASkfrnSGQTCVCANRILVQEGIYdkfAEAFSKAVQ 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 358 DLAERRKL-ADLTIGPVLTFTT-DSMLEHTNKLLEiPGSKLLFGGQPLenHLIPSIYgaiKPTAvyvpieeIVKDKNYEL 435
Cdd:PLN02278 329 KLVVGDGFeEGVTQGPLINEAAvQKVESHVQDAVS-KGAKVLLGGKRH--SLGGTFY---EPTV-------LGDVTEDML 395
|
410
....*....|....*...
gi 1540552764 436 VTK-EIFGPFQIITDYKS 452
Cdd:PLN02278 396 IFReEVFGPVAPLTRFKT 413
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
186-443 |
1.36e-06 |
|
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: 50.65 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 186 GQQSHGFRWPYGPVAIITPFNFPLEIPVLQLMGALYMGNKPVLKVDTKVSIVMEQMLRLLHTCGLPVEDVDFINSD---- 261
Cdd:cd07105 89 GTLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVLNVVTHSpeda 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 262 GKTMNKLLLEGNPRMTLFTGSSKV----AEKLAN-------DLNGR---VKLEDAGFDWKILGpdvhqedyIAWvcdqDA 327
Cdd:cd07105 169 PEVVEALIAHPAVRKVNFTGSTRVgriiAETAAKhlkpvllELGGKapaIVLEDADLDAAANA--------ALF----GA 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 328 YACSGQKCSAQSLLFMHENWSSTsLIRKMKDLAERRKLADLTIGPVLtftTDSMLEHTNKLLE---IPGSKLLFGGQPLE 404
Cdd:cd07105 237 FLNSGQICMSTERIIVHESIADE-FVEKLKAAAEKLFAGPVVLGSLV---SAAAADRVKELVDdalSKGAKLVVGGLADE 312
|
250 260 270
....*....|....*....|....*....|....*....
gi 1540552764 405 nhlipSIYGAIKPTAVyvpIEEIvkDKNYELVTKEIFGP 443
Cdd:cd07105 313 -----SPSGTSMPPTI---LDNV--TPDMDIYSEESFGP 341
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
180-492 |
1.43e-06 |
|
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: 50.68 E-value: 1.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 180 VPGNHLGQQSHGFRW---PYGPVAIITPFNFPLEIPVLQLMGALYMGNKPVLK---VDTKVSIVMEQMLrllhTCGLPVE 253
Cdd:cd07135 90 VKDGPLAFMFGKPRIrkePLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKpseLTPHTAALLAELV----PKYLDPD 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 254 DVDFINSDGKTMNKlLLEGNPRMTLFTGSSKV----AEKLANDLNgRVKLE---------DAGFDWKILGPDvhqedyIA 320
Cdd:cd07135 166 AFQVVQGGVPETTA-LLEQKFDKIFYTGSGRVgriiAEAAAKHLT-PVTLElggkspvivTKNADLELAAKR------IL 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 321 WVcdqdAYACSGQKCSAQSLLFMHENwSSTSLIRKMKDLAERRKLADLTIGPVLTF-TTDSMLEHTNKLLEIPGSKLLFG 399
Cdd:cd07135 238 WG----KFGNAGQICVAPDYVLVDPS-VYDEFVEELKKVLDEFYPGGANASPDYTRiVNPRHFNRLKSLLDTTKGKVVIG 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 400 GQ-PLENHLIPsiygaikPTAVYVpieeiVKDkNYELVTKEIFGPfqIITDYKSSQLSVVLDLIERMHAHLTAAVVSNDP 478
Cdd:cd07135 313 GEmDEATRFIP-------PTIVSD-----VSW-DDSLMSEELFGP--VLPIIKVDDLDEAIKVINSRDTPLALYIFTDDK 377
|
330 340
....*....|....*....|
gi 1540552764 479 LFLQEVI------GKSVNGT 492
Cdd:cd07135 378 SEIDHILtrtrsgGVVINDT 397
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
134-443 |
2.56e-06 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 49.73 E-value: 2.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 134 SDFFTRLIQRVSPKSYQQAFGEVYVTQKFLenfcgDQVRFLARSFA---VPGNHLGQQSHGFRWPYGPVAIITPFNFPLE 210
Cdd:PRK10090 12 ASEISALIVEEGGKIQQLAEVEVAFTADYI-----DYMAEWARRYEgeiIQSDRPGENILLFKRALGVTTGILPWNFPFF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 211 IPVLQLMGALYMGNKPVLKVDTKVSIVMEQMLRLLHTCGLPVEDVDFINSDGKTMNKlLLEGNPR--MTLFTGS----SK 284
Cdd:PRK10090 87 LIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQ-ELAGNPKvaMVSMTGSvsagEK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 285 VAEKLANDLNgRVKLEDAGFDWKILGPDVHQEDYIAWVCDQDAYAcSGQKCSAQSLLFMHENWSSTSLIR---KMK---- 357
Cdd:PRK10090 166 IMAAAAKNIT-KVCLELGGKAPAIVMDDADLDLAVKAIVDSRVIN-SGQVCNCAERVYVQKGIYDQFVNRlgeAMQavqf 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 358 -DLAERRKLAdltIGPVLtftTDSMLEHTNKLLEIP---GSKLLFGGQPLENHlipsiyGAIKPTAVYVPIeeivkDKNY 433
Cdd:PRK10090 244 gNPAERNDIA---MGPLI---NAAALERVEQKVARAveeGARVALGGKAVEGK------GYYYPPTLLLDV-----RQEM 306
|
330
....*....|
gi 1540552764 434 ELVTKEIFGP 443
Cdd:PRK10090 307 SIMHEETFGP 316
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
193-290 |
3.47e-06 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 49.88 E-value: 3.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 193 RWPYGPVAIITPFNFPLEIPVLQLMGALYMGNKPVLKVDTKVSIVMEQMLRLLHTCGLPVEDVDFINSDGKTMNKLLLEg 272
Cdd:PRK09407 152 RQPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGPVVGTALVD- 230
|
90
....*....|....*...
gi 1540552764 273 NPRMTLFTGSSKVAEKLA 290
Cdd:PRK09407 231 NADYLMFTGSTATGRVLA 248
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
56-460 |
4.30e-06 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 49.45 E-value: 4.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 56 VQGKWVGSSNWSTVVDPLNGEsfiKVAEVDGTGIQPFVESLSSCPKHG-VHNPFKAPER---YLMLGDVSTKAAHMLSlp 131
Cdd:PLN02315 25 VGGEWRANGPLVSSVNPANNQ---PIAEVVEASLEDYEEGLRACEEAAkIWMQVPAPKRgeiVRQIGDALRAKLDYLG-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 132 kvsdfftRLIQRVSPKSYQQAFGEVyvtQKFLEnFCgDQVRFLARSFA---VPG---NHLGQQShgfrW-PYGPVAIITP 204
Cdd:PLN02315 100 -------RLVSLEMGKILAEGIGEV---QEIID-MC-DFAVGLSRQLNgsiIPSerpNHMMMEV----WnPLGIVGVITA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 205 FNFPLEIPVLQLMGALYMGNKPVLK---VDTKVSIVMEQML-RLLHTCGLPVEDVDFINSDGKTMNKLLLEGNPRMTLFT 280
Cdd:PLN02315 164 FNFPCAVLGWNACIALVCGNCVVWKgapTTPLITIAMTKLVaEVLEKNNLPGAIFTSFCGGAEIGEAIAKDTRIPLVSFT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 281 GSSKVA---EKLANDLNGRVKLEDAGFDWKILGPDVHQEDYIAWVCDQdAYACSGQKCSAQSLLFMHENWSSTsLIRKMK 357
Cdd:PLN02315 244 GSSKVGlmvQQTVNARFGKCLLELSGNNAIIVMDDADIQLAVRSVLFA-AVGTAGQRCTTCRRLLLHESIYDD-VLEQLL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 358 DLAERRKLAD-----LTIGPVLTFTTDSMLEHTNKLLEIPGSKLLFGGQPLE---NHLIPSIYgAIKPTAvyvpieeivk 429
Cdd:PLN02315 322 TVYKQVKIGDplekgTLLGPLHTPESKKNFEKGIEIIKSQGGKILTGGSAIEsegNFVQPTIV-EISPDA---------- 390
|
410 420 430
....*....|....*....|....*....|.
gi 1540552764 430 dknyELVTKEIFGPFQIITDYKSSQLSVVLD 460
Cdd:PLN02315 391 ----DVVKEELFGPVLYVMKFKTLEEAIEIN 417
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
171-372 |
7.73e-06 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 48.60 E-value: 7.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 171 VRFLAR-----SFAVPGNHLGQQSHGFRWPYGPVAIITPFNFPLEIPVLQLMGALYMGNKPVLKVDTKVSIVMEQMLRLL 245
Cdd:PLN00412 129 VRILGEgkflvSDSFPGNERNKYCLTSKIPLGVVLAIPPFNYPVNLAVSKIAPALIAGNAVVLKPPTQGAVAALHMVHCF 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 246 HTCGLPVEDVDFINSDGKTMNKLLLEgNPRMTL--FTGSS---KVAEK-----LANDLNGR---VKLEDAGFdwkilgpd 312
Cdd:PLN00412 209 HLAGFPKGLISCVTGKGSEIGDFLTM-HPGVNCisFTGGDtgiAISKKagmvpLQMELGGKdacIVLEDADL-------- 279
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 313 vhqeDYIAWVCDQDAYACSGQKCSAQSLLFMHENWSSTsLIRKMKDlaerrKLADLTIGP 372
Cdd:PLN00412 280 ----DLAAANIIKGGFSYSGQRCTAVKVVLVMESVADA-LVEKVNA-----KVAKLTVGP 329
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
195-485 |
3.01e-05 |
|
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH aldehyde dehydrogenase (locus P39616) most closely related to the ALDHs and fatty ALDHs of families 3 and 14, and similar sequences, are included in this CD.
Pssm-ID: 143454 [Multi-domain] Cd Length: 449 Bit Score: 46.73 E-value: 3.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 195 PYGPVAIITPFNFPLEIPVLQLMGALYMGNKPVLKVD---TKVSIVMEQMlrlLHTCgLPVEDVDFINSDGKTMNKLLle 271
Cdd:cd07136 100 PYGVVLIIAPWNYPFQLALAPLIGAIAAGNTAVLKPSeltPNTSKVIAKI---IEET-FDEEYVAVVEGGVEENQELL-- 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 272 gNPRM--TLFTGSSKV--------AEKLANdlngrVKLEdagfdwkiLG---PDVHQED--------YIAWvcdqDAYAC 330
Cdd:cd07136 174 -DQKFdyIFFTGSVRVgkivmeaaAKHLTP-----VTLE--------LGgksPCIVDEDanlklaakRIVW----GKFLN 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 331 SGQKCSAQSLLFMHENWSSTsLIRKMKDLAERRKLADLTIGPvlTFTTDSMLEHTNKLLE-IPGSKLLFGGQPLENHLIp 409
Cdd:cd07136 236 AGQTCVAPDYVLVHESVKEK-FIKELKEEIKKFYGEDPLESP--DYGRIINEKHFDRLAGlLDNGKIVFGGNTDRETLY- 311
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1540552764 410 siygaIKPTavyvpieeIVKDKNYE--LVTKEIFGP-FQIITdYKSsqLSVVLDLIERMHAHLTAAVVSNDPLFLQEVI 485
Cdd:cd07136 312 -----IEPT--------ILDNVTWDdpVMQEEIFGPiLPVLT-YDT--LDEAIEIIKSRPKPLALYLFSEDKKVEKKVL 374
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
193-345 |
6.68e-05 |
|
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: 45.57 E-value: 6.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 193 RWPYGPVAIITPFNFPLEIPVLQLMGALYMGNKPVLKvDTKVS-----IVMEqmlrLLHTCGLPVEDVDFINSDGKTMNK 267
Cdd:cd07138 128 REPIGVCGLITPWNWPLNQIVLKVAPALAAGCTVVLK-PSEVAplsaiILAE----ILDEAGLPAGVFNLVNGDGPVVGE 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 268 LLLEgNPR--MTLFTGS----SKVAEKLANDLNgRVKLEDAGFDWKILGPDVHQEDYIAWVCdQDAYACSGQKCSAQSLL 341
Cdd:cd07138 203 ALSA-HPDvdMVSFTGStragKRVAEAAADTVK-RVALELGGKSANIILDDADLEKAVPRGV-AACFANSGQSCNAPTRM 279
|
....
gi 1540552764 342 FMHE 345
Cdd:cd07138 280 LVPR 283
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
195-459 |
9.02e-05 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 45.24 E-value: 9.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 195 PYGPVAIITPFNFPLeipvLQLM-GA---LYMGNKPVLKVDTKVSIVMEQMLRLLHTCGLPVEDVDFINSDGKTMNKLLl 270
Cdd:PRK13968 126 PLGTILAIMPWNFPL----WQVMrGAvpiLLAGNGYLLKHAPNVMGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMI- 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 271 eGNPRMT--LFTGSSKVAEKLANDLNGRVK---LEDAGFDWKILGPDVHQEDYI-AWVCDQdaYACSGQKCSAqSLLFMH 344
Cdd:PRK13968 201 -NDSRIAavTVTGSVRAGAAIGAQAGAALKkcvLELGGSDPFIVLNDADLELAVkAAVAGR--YQNTGQVCAA-AKRFII 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 345 ENWSSTSLIRKMKDLAERRKLADLT-----IGPVLTFTTDSMLEHTNKLLEIPGSKLLFGGQPLE---NHLIPSIYGAIK 416
Cdd:PRK13968 277 EEGIASAFTERFVAAAAALKMGDPRdeenaLGPMARFDLRDELHHQVEATLAEGARLLLGGEKIAgagNYYAPTVLANVT 356
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1540552764 417 P--TAvyvpieeivkdknyelVTKEIFGPFQIITDYKSSQLSVVL 459
Cdd:PRK13968 357 PemTA----------------FREELFGPVAAITVAKDAEHALEL 385
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
189-451 |
1.18e-04 |
|
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: 44.75 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 189 SHGFRWPYGPVAIITPFNFPLEIPVLQLMGALYMGNKPVLKV--DTKVSIvmeqmLRLLHTCG--LPVEDVDFINSDGKT 264
Cdd:cd07116 130 AYHFHEPLGVVGQIIPWNFPLLMATWKLAPALAAGNCVVLKPaeQTPASI-----LVLMELIGdlLPPGVVNVVNGFGLE 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 265 MNKLLLEgNPRMT--LFTGSSKVAEKL---ANDLNGRVKLEDAGFDWKILGPDVHQED----------YIAWVCDQdaya 329
Cdd:cd07116 205 AGKPLAS-SKRIAkvAFTGETTTGRLImqyASENIIPVTLELGGKSPNIFFADVMDADdaffdkalegFVMFALNQ---- 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 330 csGQKCSAQSLLFMHEnwsstSLIRKMKDLAERRKLADLTIGPVLTFT------TDSMLEHTNKLLEI---PGSKLLFGG 400
Cdd:cd07116 280 --GEVCTCPSRALIQE-----SIYDRFMERALERVKAIKQGNPLDTETmigaqaSLEQLEKILSYIDIgkeEGAEVLTGG 352
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1540552764 401 QplENHLIPSIYGA-IKPTAVYvpieeivKDKNYELVTKEIFGPFQIITDYK 451
Cdd:cd07116 353 E--RNELGGLLGGGyYVPTTFK-------GGNKMRIFQEEIFGPVLAVTTFK 395
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
195-492 |
1.37e-04 |
|
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: 44.44 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 195 PYGPVAIITPFNFPLEIPVLQLMGALYMGNKPVLKVDTKVSIVMEQMLRLLhTCGLPVEDVDFINSDGKTmNKLLLEGNP 274
Cdd:cd07087 100 PLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKLI-PKYFDPEAVAVVEGGVEV-ATALLAEPF 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 275 RMTLFTGSSKV--------AEKLANdlngrVKLEDAGfdwK---ILGPDVHQE---DYIAWVcdqdAYACSGQKCSAQSL 340
Cdd:cd07087 178 DHIFFTGSPAVgkivmeaaAKHLTP-----VTLELGG---KspcIVDKDANLEvaaRRIAWG----KFLNAGQTCIAPDY 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 341 LFMHENwSSTSLIRKMK---------DLAERRKLADLtigpvltfTTDsmlEHTNKLLE-IPGSKLLFGGQPLENHLips 410
Cdd:cd07087 246 VLVHES-IKDELIEELKkaikefygeDPKESPDYGRI--------INE---RHFDRLASlLDDGKVVIGGQVDKEER--- 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 411 iygAIKPTAVYVPieeivkDKNYELVTKEIFGP-FQIITdYKSsqLSVVLDLIERMHAHLTAAVVSNDPLFLQEVIGKSV 489
Cdd:cd07087 311 ---YIAPTILDDV------SPDSPLMQEEIFGPiLPILT-YDD--LDEAIEFINSRPKPLALYLFSEDKAVQERVLAETS 378
|
...
gi 1540552764 490 NGT 492
Cdd:cd07087 379 SGG 381
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
169-300 |
2.62e-03 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 40.28 E-value: 2.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540552764 169 DQVRFLA---RSfaVPGNHLGQQSHGF-----RWPYGPVAIITPFNFPLEIPVLQLMGALYMGNKPVLKVD--TKVSIVM 238
Cdd:PRK13473 106 DVFRFFAgaaRC--LEGKAAGEYLEGHtsmirRDPVGVVASIAPWNYPLMMAAWKLAPALAAGNTVVLKPSeiTPLTALK 183
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1540552764 239 eqMLRLLHTCgLPVEDVDFINSDGKTMNKLLLeGNP--RMTLFTGS----SKVAEKLANDLNgRVKLE 300
Cdd:PRK13473 184 --LAELAADI-LPPGVLNVVTGRGATVGDALV-GHPkvRMVSLTGSiatgKHVLSAAADSVK-RTHLE 246
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