|
Name |
Accession |
Description |
Interval |
E-value |
| MAR |
cd08177 |
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic ... |
9-349 |
1.23e-155 |
|
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic microbes; Maleylacetate reductase (MAR) plays an important role in the degradation of aromatic compounds in aerobic microbes. In fungi and yeasts, the enzyme is involved in the catabolism of compounds such as phenol, tyrosine, benzoate, 4-hydroxybenzoate and resorcinol. In bacteria, the enzyme contributes to the degradation of resorcinol, 2,4-dihydroxybenzoate ([beta]-resorcylate) and 2,6-dihydroxybenzoate ([gamma]-resorcylate) via hydroxyquinol and maleylacetate. Maleylacetate reductase catalyzes NADH- or NADPH-dependent reduction, at the carbon-carbon double bond, of maleylacetate or 2-chloromaleylacetate to 3-oxoadipate. In the case of 2-chloromaleylacetate, MAR initially catalyzes the NAD(P)H-dependent dechlorination to maleylacetate, which is then reduced to 3-oxoadipate. This enzyme is a homodimer and is inhibited by thiol-blocking reagents such as p-chloromercuribenzoate and Hg++, indicating that the cysteine residue is probably necessary for the catalytic activity of maleylacetate reductase.
Pssm-ID: 341456 [Multi-domain] Cd Length: 337 Bit Score: 440.02 E-value: 1.23e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 9 PNQVYFGAGQIQKLPSILKnylHNPTDKVLVLAEARVQAHVERLETSLGKEVVHHFDKIIQHVPQTLVEEGLKVTNKLQP 88
Cdd:cd08177 1 PQRVVFGAGTLAELAEELE---RLGARRALVLSTPRQRALAERVAALLGDRVAGVFDGAVMHVPVEVAERALAAAREAGA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 89 KVMLSIGGGSAVGLAKALALKNHLPIIAVPTTFAGSEQTNIWGISNEEGKTTGRDDVVLPQVVVYDPELTQTMPQRLAVM 168
Cdd:cd08177 78 DGLVAIGGGSAIGLAKAIALRTGLPIVAVPTTYAGSEMTPIWGETEDGVKTTGRDPRVLPRTVIYDPDLTLGLPAALSVA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 169 SAMNAMAHLMEAVYSPTGNPITRNQALLGMQQLKKGLENIAQQKAfTTEANEQILLGAYLAGRALCEVTMALHHKAAHVL 248
Cdd:cd08177 158 SGLNALAHAVEALYAPDANPITSLLAEEGIRALARALPRLVADPS-DLEARSDALYGAWLAGVVLGSVGMGLHHKLCHVL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 249 GGSFGMQHAEVHTVLQTYVLAYQWPHLSTEIQQDFKLTLGNNPPLALKMLAENAGAPTTLEEIGFDQADIGKAVRIMLAN 328
Cdd:cd08177 237 GGTFDLPHAETHAVVLPHVLAYNAPAAPDAMARLARALGGGDAAGGLYDLARRLGAPTSLRDLGMPEDDIDRAADLALAN 316
|
330 340
....*....|....*....|.
gi 1111735350 329 PYPNPAPLVESQLLVMLERAF 349
Cdd:cd08177 317 PYPNPRPVERDALRALLERAW 337
|
|
| EutG |
COG1454 |
Alcohol dehydrogenase, class IV [Energy production and conversion]; |
1-349 |
2.11e-75 |
|
Alcohol dehydrogenase, class IV [Energy production and conversion];
Pssm-ID: 441063 [Multi-domain] Cd Length: 381 Bit Score: 237.33 E-value: 2.11e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 1 MNFTYKsFPNQVYFGAGQIQKLPSILKNYlhnPTDKVLVLAEARVQA--HVERLETSLGKE--VVHHFDKIIQHVPQTLV 76
Cdd:COG1454 1 MMFTFR-LPTRIVFGAGALAELGEELKRL---GAKRALIVTDPGLAKlgLLDRVLDALEAAgiEVVVFDDVEPNPTVETV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 77 EEGLKVTNKLQPKVMLSIGGGSAVGLAKALAL------------------KNHLPIIAVPTTF-AGSEQTNIWGISNEEG 137
Cdd:COG1454 77 EAGAAAAREFGADVVIALGGGSAIDAAKAIALlatnpgdledylgikkvpGPPLPLIAIPTTAgTGSEVTPFAVITDPET 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 138 --KTTGRDDVVLPQVVVYDPELTQTMPQRLAVMSAMNAMAHLMEAVYSPTGNPITRNQALLGMQQLKKGLENIAQQKAfT 215
Cdd:COG1454 157 gvKKGIADPELLPDVAILDPELTLTLPPSLTAATGMDALTHAIEAYVSKGANPLTDALALEAIRLIARNLPRAVADGD-D 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 216 TEANEQILLGAYLAGRALCEVTMALHHKAAHVLGGSFGMQHAEVHTVLQTYVLAYQWPHLST---EIQQDFKLTLGNNPP 292
Cdd:COG1454 236 LEAREKMALASLLAGMAFANAGLGAVHALAHPLGGLFHVPHGLANAILLPHVLRFNAPAAPEryaEIARALGLDVGLSDE 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1111735350 293 L-------ALKMLAENAGAPTTLEEIGFDQADIGKAVRIMLANP--YPNPAPLVESQLLVMLERAF 349
Cdd:COG1454 316 EaaealieAIRELLRDLGIPTRLSELGVTEEDLPELAELALADRclANNPRPLTEEDIEAILRAAY 381
|
|
| Fe-ADH |
pfam00465 |
Iron-containing alcohol dehydrogenase; |
9-341 |
5.41e-66 |
|
Iron-containing alcohol dehydrogenase;
Pssm-ID: 425696 [Multi-domain] Cd Length: 362 Bit Score: 212.46 E-value: 5.41e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 9 PNQVYFGAGQIQKLPSILKNYlhnpTDKVLVLAEARVQA--HVERLETSLGKE--VVHHFDKIIQHVPQTLVEEGLKVTN 84
Cdd:pfam00465 1 PTRIVFGAGALAELGEELKRL----GARALIVTDPGSLKsgLLDKVLASLEEAgiEVVVFDGVEPEPTLEEVDEAAALAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 85 KLQPKVMLSIGGGSAVGLAKALAL------------------KNHLPIIAVPTTFA-GSEQTNIWGISNEEG--KTTGRD 143
Cdd:pfam00465 77 EAGADVIIAVGGGSVIDTAKAIALlltnpgdvwdylggkpltKPALPLIAIPTTAGtGSEVTPLAVITDTETgeKLGIFS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 144 DVVLPQVVVYDPELTQTMPQRLAVMSAMNAMAHLMEAVYSPTGNPITRNQALLGMQQLKKGLEnIAQQKAFTTEANEQIL 223
Cdd:pfam00465 157 PKLLPDLAILDPELTLTLPPRLTAATGMDALAHAVEAYVSKGANPLTDALALEAIRLIAENLP-RAVADGEDLEARENML 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 224 LGAYLAGRALCEVTMALHHKAAHVLGGSFGMQHAEVHTVLQTYVLAYQWPHlSTEIQQDFKLTLGNNPPL--------AL 295
Cdd:pfam00465 236 LASTLAGLAFSNAGLGAAHALAHALGGRYGIPHGLANAILLPYVLRFNAPA-APEKLAQLARALGEDSDEeaaeeaieAL 314
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1111735350 296 KMLAENAGAPTTLEEIGFDQADIGKAVRIMLANP--YPNPAPLVESQL 341
Cdd:pfam00465 315 RELLRELGLPTTLSELGVTEEDLDALAEAALRDRslANNPRPLTAEDI 362
|
|
| Fe-ADH |
cd08551 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains large ... |
9-342 |
1.97e-50 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains large metal-containing alcohol dehydrogenases (ADH), known as iron-containing alcohol dehydrogenases. They contain a dehydroquinate synthase-like protein structural fold and mostly contain iron. They are distinct from other alcohol dehydrogenases which contains different protein domains. There are several distinct families of alcohol dehydrogenases: Zinc-containing long-chain alcohol dehydrogenases, insect-type, or short-chain alcohol dehydrogenases, iron-containing alcohol dehydrogenases, among others. The iron-containing family has a Rossmann fold-like topology that resembles the fold of the zinc-dependent alcohol dehydrogenases, but lacks sequence homology, and differs in strand arrangement. ADH catalyzes the reversible oxidation of alcohol to acetaldehyde with the simultaneous reduction of NAD(P)+ to NAD(P)H.
Pssm-ID: 341481 [Multi-domain] Cd Length: 372 Bit Score: 172.25 E-value: 1.97e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 9 PNQVYFGAGQIQKLPSILKNYLHNptdKVLVLAEARVQA--HVERLETSLGKE--VVHHFDKIIQHVPQTLVEEGLKVTN 84
Cdd:cd08551 1 PTRIVFGAGALARLGEELKALGGK---KVLLVTDPGLVKagLLDKVLESLKAAgiEVEVFDDVEPNPTVETVEAAAELAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 85 KLQPKVMLSIGGGSAVGLAKALAL------------------KNHLPIIAVPTTFA-GSEQTNIWGISNEEG--KTTGRD 143
Cdd:cd08551 78 EEGADLVIAVGGGSVLDTAKAIAVlatnggsirdyegigkvpKPGLPLIAIPTTAGtGSEVTPNAVITDPETgrKMGIVS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 144 DVVLPQVVVYDPELTQTMPQRLAVMSAMNAMAHLMEAVYSPTGNPITRNQALLGMQQLKKGLEnIAQQKAFTTEANEQIL 223
Cdd:cd08551 158 PYLLPDVAILDPELTLSLPPSVTAATGMDALTHAIEAYTSKKANPISDALALEAIRLIGKNLR-RAVADGSDLEAREAML 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 224 LGAYLAGRALCEVTMALHHKAAHVLGGSFGMQHAEVHTVLQTYVLAYQWPHLST---EIQQDFKLTLGNNPPL------- 293
Cdd:cd08551 237 LASLLAGIAFGNAGLGAVHALAYPLGGRYHIPHGVANAILLPYVMEFNLPACPEkyaEIAEALGEDVEGLSDEeaaeaav 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1111735350 294 -ALKMLAENAGAPTTLEEIGFDQADIGKAVRIMLANPYP---NPAPLVESQLL 342
Cdd:cd08551 317 eAVRELLRDLGIPTSLSELGVTEEDIPELAEDAMKSGRLlsnNPRPLTEEDIR 369
|
|
| MAR-like |
cd08192 |
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic ... |
11-348 |
3.99e-41 |
|
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic microbes; Maleylacetate reductase (MAR) plays an important role in the degradation of aromatic compounds in aerobic microbes. In fungi and yeasts, the enzyme is involved in the catabolism of compounds such as phenol, tyrosine, benzoate, 4-hydroxybenzoate and resorcinol. In bacteria, the enzyme contributes to the degradation of resorcinol, 2,4-dihydroxybenzoate ([beta]-resorcylate) and 2,6-dihydroxybenzoate ([gamma]-resorcylate) via hydroxyquinol and maleylacetate. Maleylacetate reductase (MAR) catalyzes NADH- or NADPH-dependent reduction, at the carbon-carbon double bond, of maleylacetate or 2-chloromaleylacetate to 3-oxoadipate. In the case of 2-chloromaleylacetate, MAR initially catalyzes the NAD(P)H-dependent dechlorination to maleylacetate, which is then reduced to 3-oxoadipate. This enzyme is a homodimer. It is inhibited by thiol-blocking reagents such as p-chloromercuribenzoate and Hg++, indicating that the cysteine residue is probably necessary for the catalytic activity of maleylacetate reductase.
Pssm-ID: 341471 [Multi-domain] Cd Length: 380 Bit Score: 147.78 E-value: 3.99e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 11 QVYFGAGQIQKLPSILKNYlhnPTDKVLVLAE---ARVQAHVERLETSLGKEVVHHFDKIIQHVPQTLVEEGLKVTNKLQ 87
Cdd:cd08192 3 RVSYGPGAVEALLHELATL---GASRVFIVTSkslATKTDVIKRLEEALGDRHVGVFSGVRQHTPREDVLEAARAVREAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 88 PKVMLSIGGGSAVGLAKA--LALKNH------------------------LPIIAVPTTFAGSEQTNIWGISNEEG--KT 139
Cdd:cd08192 80 ADLLVSLGGGSPIDAAKAvaLALAEDvtdvdqldaledgkridpnvtgptLPHIAIPTTLSGAEFTAGAGATDDDTghKQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 140 TGRDDVVLPQVVVYDPELTQTMPQRLAVMSAMNAMAHLMEAVYSPTGNPITRNQALLGMQQLKKGLEnIAQQKAFTTEAN 219
Cdd:cd08192 160 GFAHPELGPDAVILDPELTLHTPERLWLSTGIRAVDHAVETLCSPQATPFVDALALKALRLLFEGLP-RSKADPEDLEAR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 220 EQILLGAYLAGRAL-CEVTMALHHKAAHVLGGSFGMQHAEVHTVLQTYVLAYQWPHLSTEIQQ----DFKLTLGNNPPL- 293
Cdd:cd08192 239 LKCQLAAWLSLFGLgSGVPMGASHAIGHQLGPLYGVPHGITSCIMLPAVLRFNAPVNAERQRLiaraLGLVTGGLGREAa 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1111735350 294 ----ALKMLAENAGAPTTLEEIGFDQADIGK-AVRIMLA-----NPYPNPAPlveSQLLVMLERA 348
Cdd:cd08192 319 daadAIDALIRELGLPRTLRDVGVGRDQLEKiAENALTDvwcrtNPRPITDK---DDVLEILESA 380
|
|
| Fe-ADH-like |
cd08185 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
9-336 |
1.92e-39 |
|
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol dehydrogenase-like (ADH) proteins. Alcohol dehydrogenase catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase fold and is a member of the iron-containing alcohol dehydrogenase-like family. They are distinct from other alcohol dehydrogenases which contain different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341464 [Multi-domain] Cd Length: 379 Bit Score: 143.41 E-value: 1.92e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 9 PNQVYFGAGQIQKLPSILKNYlhnpTDKVLVLAE---ARVQAHVERLETSL---GKEVVHhFDKIIQHVPQTLVEEGLKV 82
Cdd:cd08185 4 PTRILFGAGKLNELGEEALRP----GKKALIVTGkgsSKKTGLLDRVKKLLekaGVEVVV-FDKVEPNPLTTTVMEGAAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 83 TNKLQPKVMLSIGGGSAVGLAKALAL----------------------KNHLPIIAVPTTFA-GSEqTNIWG-ISNEE-- 136
Cdd:cd08185 79 AKEEGCDFVIGLGGGSSMDAAKAIAFmatnpgdiwdyifggtgkgpppEKALPIIAIPTTAGtGSE-VDPWAvITNPEtk 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 137 GKTTGRDDVVLPQVVVYDPELTQTMPQRLAVMSAMNAMAHLMEAVYSPTGNPITRNQALLGMQQLKKGLEnIAQQKAFTT 216
Cdd:cd08185 158 EKKGIGHPALFPKVSIVDPELMLTVPPRVTAYTGFDALFHAFESYISKNANPFSDMLALEAIRLVAKYLP-RAVKDGSDL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 217 EANEQILLGAYLAGRALCEVTMALHHKAAHVLGGSFG-MQHAEVHTVLQTYVLAYQWPHLsteiQQDF---------KLT 286
Cdd:cd08185 237 EAREKMAWASTLAGIVIANSGTTLPHGLEHPLSGYHPnIPHGAGLAALYPAYFEFTIEKA----PEKFafvaraeasGLS 312
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1111735350 287 LGNNP---PLALKMLAENAGAPTTLEEIGFDQADIGK----AVRIMLANPYPNPAPL 336
Cdd:cd08185 313 DAKAAedfIEALRKLLKDIGLDDLLSDLGVTEEDIPWlaenAMETMGGLFANNPVEL 369
|
|
| Fe-ADH-like |
cd14863 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
7-349 |
3.78e-39 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341485 [Multi-domain] Cd Length: 380 Bit Score: 142.67 E-value: 3.78e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 7 SFPNQVYFGAGQIQKLPSILKNYlhnPTDKVLVLAEARVQA--HVERLETSL---GKEVVHhFDKIIQHVPQTLVEEGLK 81
Cdd:cd14863 3 SQLTPVIFGAGAVEQIGELLKEL---GCKKVLLVTDKGLKKagIVDKIIDLLeeaGIEVVV-FDDVEPDPPDEIVDEAAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 82 VTNKLQPKVMLSIGGGSAVGLAKALALKNH-------------------LPIIAVPTTfAG--SEQTNIWGISNEE--GK 138
Cdd:cd14863 79 IAREEGADGVIGIGGGSVLDTAKAIAVLLTnpgpiidyalagppvpkpgIPLIAIPTT-AGtgSEVTPIAVITDEEngVK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 139 TTGRDDVVLPQVVVYDPELTQTMPQRLAVMSAMNAMAHLMEAVYSPTGNPITrnqALLGMQQLKKGLENIaqQKAFTT-- 216
Cdd:cd14863 158 KSLLGPFLVPDLAILDPELTVGLPPSLTAATGMDALSHAIEAYTSKLANPMT---DALALQAIRLIVKNL--PRAVKDgd 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 217 --EANEQILLGAYLAGRALCEVTMALHHKAAHVLGGSFGMQHAEVHTVLQTYVLAYQWPHLSTEIQQ--------DFKLT 286
Cdd:cd14863 233 nlEARENMLLASNLAGIAFNNAGTHIGHAIAHALGALYHIPHGLACALALPVVLEFNAEAYPEKVKKiakalgvsFPGES 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1111735350 287 ---LGNNPPLALKMLAENAGAPTTLEEIGFDQADIGKAVRIMLANP--YPNPAPLVESQLLVMLERAF 349
Cdd:cd14863 313 deeLGEAVADAIREFMKELGIPSLFEDYGIDKEDLDKIAEAVLKDPfaMFNPRPITEEEVAEILEAIY 380
|
|
| Fe-ADH-like |
cd14861 |
Iron-containing alcohol dehydrogenases-like; This family contains proteins similar to ... |
7-349 |
9.92e-38 |
|
Iron-containing alcohol dehydrogenases-like; This family contains proteins similar to iron-containing alcohol dehydrogenase (Fe-ADH), most of which have not been characterized. Their specific function is unknown. The protein structure represents a dehydroquinate synthase-like fold and belongs to the alcohol dehydrogenase-like superfamily. It is distinct from other alcohol dehydrogenases which contain different protein domains. Alcohol dehydrogenase catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions.
Pssm-ID: 341483 [Multi-domain] Cd Length: 374 Bit Score: 138.80 E-value: 9.92e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 7 SFPNQVYFGAGQIQKLPSILKNY-LHNP---TDKVLVLAEarvqaHVERLETSLGKEV--VHHFDkiiqHVP----QTLV 76
Cdd:cd14861 1 NYPTRIRFGAGAIAELPEELKALgIRRPllvTDPGLAALG-----IVDRVLEALGAAGlsPAVFS----DVPpnptEADV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 77 EEGLKVTNKLQPKVMLSIGGGSAVGLAKALALK-NH---------------------LPIIAVPTTfAG--SEQTNIWGI 132
Cdd:cd14861 72 EAGVAAYREGGCDGIIALGGGSAIDAAKAIALMaTHpgplwdyedgeggpaaitpavPPLIAIPTT-AGtgSEVGRAAVI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 133 SNEEgktTGRDDVV-----LPQVVVYDPELTQTMPQRLAVMSAMNAMAHLMEAVYSPTGNPITRNQALLGMQQLKKGLEN 207
Cdd:cd14861 151 TDDD---TGRKKIIfspklLPKVAICDPELTLGLPPRLTAATGMDALTHCIEAYLSPGFHPMADGIALEGLRLISEWLPR 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 208 IAQQKAfTTEANEQILLGAYLAGralcevtMALH------HKAAHVLGGSFGMQHAEVHTVLQTYVLAYQWPHLSTEIQQ 281
Cdd:cd14861 228 AVADGS-DLEARGEMMMAALMGA-------VAFQkglgavHALAHALGALYGLHHGLLNAILLPYVLRFNRPAVEDKLAR 299
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1111735350 282 -----DFKLTLGNNPPLALKMLAENAGAPTTLEEIGFDQADIGKAVRIMLANPY--PNPAPLVESQLLVMLERAF 349
Cdd:cd14861 300 laralGLGLGGFDDFIAWVEDLNERLGLPATLSELGVTEDDLDELAELALADPChaTNPRPVTAEDYRALLREAL 374
|
|
| Fe-ADH-like |
cd14865 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
3-349 |
1.64e-36 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341487 [Multi-domain] Cd Length: 383 Bit Score: 135.75 E-value: 1.64e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 3 FTYKSfPNQVYFGAGQIQKLPSILKNYlhnPTDKVLVLAEARVQAH--VERLETSLGK--EVVHHFDKIIQHVPQTLVEE 78
Cdd:cd14865 1 FEFFN-PTKIVSGAGALENLPAELARL---GARRPLIVTDKGLAAAglLKKVEDALGDaiEIVGVFDDVPPDSSVAVVNE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 79 GLKVTNKLQPKVMLSIGGGSAVGLAKALAL-------------------KNHLPIIAVPTTF-AGSEQTNIWGISNEEG- 137
Cdd:cd14865 77 AAARAREAGADGIIAVGGGSVIDTAKGVNIllseggddlddygganrltRPLKPLIAIPTTAgTGSEVTLVAVIKDEEKk 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 138 -KTTGRDDVVLPQVVVYDPELTQTMPQRLAVMSAMNAMAHLMEAVYSPTGNPITRNQALLGMQQLKKGLENIAQQKAfTT 216
Cdd:cd14865 157 vKLLFVSPFLLPDVAILDPRLTLSLPPKLTAATGMDALTHAIEAYTSLQKNPISDALALQAIRLISENLPKAVKNGK-DL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 217 EANEQILLGAYLAGRALCEVTMALHHKAAHVLGGSFGMQHAEVHTVLQTYVLAYQWPHLSTEI-QQDFKLTLGNNPP--- 292
Cdd:cd14865 236 EARLALAIAATMAGIAFSNSMVGLVHAIAHAVGAVAGVPHGLANSILLPHVMRYNLDAAAERYaELALALAYGVTPAgrr 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1111735350 293 ---------LALKMLAENAGAPTTLEEIGFDQADIGKAVRIMLANP--YPNPAPLVESQLLVMLERAF 349
Cdd:cd14865 316 aeeaieaaiDLVRRLHELCGLPTRLRDVGVPEEQLEAIAELALNDGaiLFNPREVDPEDILAILEAAY 383
|
|
| Fe-ADH-like |
cd08183 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
9-346 |
2.59e-35 |
|
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contain different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341462 [Multi-domain] Cd Length: 377 Bit Score: 132.24 E-value: 2.59e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 9 PNQVYFGAGQIQKLPSILKNYlhnpTDKVLVL--AEARVQAHVERLETSL---GKEVVHHfdkIIQHVPQT-LVEEGLKV 82
Cdd:cd08183 1 PPRIVFGRGSLQELGELAAEL----GKRALLVtgRSSLRSGRLARLLEALeaaGIEVALF---SVSGEPTVeTVDAAVAL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 83 TNKLQPKVMLSIGGGSAVGLAKALA--LKNH--------------------LPIIAVPTTfAG--SEQTNIWGISNEEG- 137
Cdd:cd08183 74 AREAGCDVVIAIGGGSVIDAAKAIAalLTNEgsvldylevvgkgrplteppLPFIAIPTT-AGtgSEVTKNAVLSSPEHg 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 138 -KTTGRDDVVLPQVVVYDPELTQTMPQRLAVMSAMNAMAHLMEAVYSPTGNPITRNQALLGMQQLKKGLENIAQQKAfTT 216
Cdd:cd08183 153 vKVSLRSPSMLPDVALVDPELTLSLPPEVTAASGLDALTQLIEPYVSRKANPLTDALAREGLRLAARSLRRAYEDGE-DL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 217 EANEQILLGAYLAGRALCEVTMALHHKAAHVLGGSFGMQHAEVHTVLQTYVLAYQWPHLSTEIQQDFKLT--------LG 288
Cdd:cd08183 232 EAREDMALASLLGGLALANAGLGAVHGLAGPLGGMFGAPHGAICAALLPPVLEANLRALREREPDSPALAryrelagiLT 311
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1111735350 289 NNPPLA-------LKMLAENAGAPtTLEEIGFDQADIGKAVR------IMLAnpypNPAPLVESQLLVMLE 346
Cdd:cd08183 312 GDPDAAaedgvewLEELCEELGIP-RLSEYGLTEEDFPEIVEkargssSMKG----NPIELSDEELLEILE 377
|
|
| Fe-ADH-like |
cd14866 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
12-348 |
3.83e-33 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341488 [Multi-domain] Cd Length: 384 Bit Score: 126.58 E-value: 3.83e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 12 VYFGAGQIQKLPSILKNYlhnPTDKVLVLAEARVQAH---VERLETSLGKEVVHHFDKIIQHVPQTLVEEGLKVTNKLQP 88
Cdd:cd14866 8 LFSGRGALARLGRELDRL---GARRALVVCGSSVGANpdlMDPVRAALGDRLAGVFDGVRPHSPLETVEAAAEALREADA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 89 KVMLSIGGGSAVGLAKALAL---------------------------KNHLPIIAVPTTFAGSEQTNIWGISNEEgkTTG 141
Cdd:cd14866 85 DAVVAVGGGSAIVTARAASIllaedrdvrelctrraedglmvsprldAPKLPIFVVPTTPTTADVKAGSAVTDPP--AGQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 142 R----DDVVLPQVVVYDPELTQTMPQRLAVMSAMNAMAHLMEAVYSPTGNPITRNQALLGMQQLKKGLENIAQqkAFTTE 217
Cdd:cd14866 163 RlalfDPKTRPAAVFYDPELLATAPASLVAGAAMNGFDMAVEGLYSRHADPLADATLMHALRLLADGLPRLAD--DDDPA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 218 ANEQILLGAYLAGRALCEVTMALHHKAAHVLGGSFGMQHAEVHTVLQTYVLAYQWPHlsTEIQQD-----FKLTLGNNP- 291
Cdd:cd14866 241 ARADLVLAAVLAGYGTDHTGGGVIHALGHAIGARYGVQNGVVHAILLPHVLRFNAPA--TDGRLDrlaeaLGVADAGDEa 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1111735350 292 -----PLALKMLAENAGAPTTLEEIGFDQADIGKAVRIMLANPY--PNPAPLVE-SQLLVMLERA 348
Cdd:cd14866 319 saaavVDAVEALLDALGVPTRLRDLGVSREDLPAIAEAAMDDWFmdNNPRPVPTaEELEALLEAA 383
|
|
| Fe-ADH-like |
cd08196 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
3-345 |
3.08e-32 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341475 [Multi-domain] Cd Length: 367 Bit Score: 123.84 E-value: 3.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 3 FTYKSfPNQVYFGAGQIQKLPSILKNY-LHNP---TDKVLVLAEarvqaHVERLETSLGKEVVHHFDKIIQHVPQTLVEE 78
Cdd:cd08196 1 WSYYQ-PVKIIFGEGILKELPDIIKELgGKRGllvTDPSFIKSG-----LAKRIVESLKGRIVAVFSDVEPNPTVENVDK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 79 GLKVTNKLQPKVMLSIGGGSAVGLAKALAL-------------------KNHLPIIAVPTTfAG--SEQTNIWGISNEEG 137
Cdd:cd08196 75 CARLARENGADFVIAIGGGSVLDTAKAAAClaktdgsiedylegkkkipKKGLPLIAIPTT-AGtgSEVTPVAVLTDKEK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 138 --KTTGRDDVVLPQVVVYDPELTQTMPQRLAVMSAMNAMAHLMEAVYSPTGNPITRnqaLLGMQQLKKGLENIaqQKAFT 215
Cdd:cd08196 154 gkKAPLVSPGFYPDIAIVDPELTYSMPPKVTASTGIDALCHAIEAYWSINHQPISD---ALALEAAKLVLENL--EKAYN 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 216 ----TEANEQILLGAYLAGRALCEVTMALHHKAAHVLGGSFGMQHAEVHTVLQTYVLAYQWPHLSTEIQQDFKLtLGNNP 291
Cdd:cd08196 229 npndKEAREKMALASLLAGLAFSQTRTTASHACSYPLTSHFGIPHGEACALTLPSFIRLNAEALPGRLDELAKQ-LGFKD 307
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 292 PLALK----MLAENAGAPTTLEEIGFDQADIGKAVRI-MLANPYP-NPAPLVESQLLVML 345
Cdd:cd08196 308 AEELAdkieELKKRIGLRTRLSELGITEEDLEEIVEEsFHPNRANnNPVEVTKEDLEKLL 367
|
|
| HEPD |
cd08182 |
Hydroxyethylphosphoate dehydrogenase (HEPD) catalyzes the reduction of phosphonoacetaldehyde ... |
9-232 |
6.36e-32 |
|
Hydroxyethylphosphoate dehydrogenase (HEPD) catalyzes the reduction of phosphonoacetaldehyde (PnAA) to hydroxyethylphosphoate (HEP); Hydroxyethylphosphoate dehydrogenase (HEPD) catalyzes the reduction of phosphonoacetaldehyde (PnAA) to hydroxyethylphosphoate (HEP) with either NADH or NADPH as a cofactor, although NADH is the preferred cofactor. PnAA is a biosynthetic intermediate for several phosphonates such as the antibiotic fosfomycin, phosphinothricin tripeptide (PTT), and 2-aminoethylphosphonate (AEP). This enzyme is named PhpC in PTT biosynthesis pathway in Streptomyces hygroscopicus and S. viridochromogenes.
Pssm-ID: 341461 [Multi-domain] Cd Length: 370 Bit Score: 123.10 E-value: 6.36e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 9 PNQVYFGAGQIQKLPSILKNYlhnPTDKVLVLA--EARVQAHVERLETSLGKEV-VHHFDKIIQHVPQTLVEEGLKVTNK 85
Cdd:cd08182 1 PVKIIFGPGALAELKDLLGGL---GARRVLLVTgpSAVRESGAADILDALGGRIpVVVFSDFSPNPDLEDLERGIELFRE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 86 LQPKVMLSIGGGSAVGLAKALAL--------------------KNHLPIIAVPTTfAG--SEQTN---IWgiSNEEG-KT 139
Cdd:cd08182 78 SGPDVIIAVGGGSVIDTAKAIAAllgspgenllllrtgekapeENALPLIAIPTT-AGtgSEVTPfatIW--DEAEGkKY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 140 TGRDDVVLPQVVVYDPELTQTMPQRLAVMSAMNAMAHLMEAVYSPTGNPITRNQAL----LGMQQLKKGLENIAqqkafT 215
Cdd:cd08182 155 SLAHPSLYPDAAILDPELTLSLPLYLTASTGLDALSHAIESIWSVNANPESRAYALrairLILENLPLLLENLP-----N 229
|
250
....*....|....*..
gi 1111735350 216 TEANEQILLGAYLAGRA 232
Cdd:cd08182 230 LEAREAMAEASLLAGLA 246
|
|
| LPO |
cd08176 |
Lactadehyde:propanediol oxidoreductase (LPO) catalyzes the interconversion between ... |
8-318 |
3.79e-31 |
|
Lactadehyde:propanediol oxidoreductase (LPO) catalyzes the interconversion between L-lactaldehyde and L-1,2-propanediol in Escherichia coli and other enterobacteria; Lactadehyde:propanediol oxidoreductase (LPO) is a member of the group III iron-activated dehydrogenases which catalyze the interconversion between L-lactaldehyde and L-1,2-propanediol in Escherichia coli and other enterobacteria. L-fucose and L-rhamnose are used by Escherichia coli through an inducible pathway mediated by the fucose regulon comprising four linked operons fucO, fucA, fucPIK, and fucR. The fucA-encoded aldolase catalyzes the formation of dihydroxyacetone phosphate and L-lactaldehyde. Under anaerobic conditions, with NADH as a cofactor, lactaldehyde is converted by a fucO-encoded lactadehyde:propanediol oxidoreductase (LPO) to L-1,2-propanediol, which is excreted as a fermentation product. In mutant strains, E. coli adapted to grow on L-1,2-propanediol, FucO catalyzes the oxidation of the polyol to L-lactaldehyde. FucO is induced regardless of the respiratory conditions of the culture, remains fully active in the absence of oxygen. In the presence of oxygen, this enzyme becomes oxidatively inactivated by a metal-catalyzed oxidation mechanism. FucO is an iron-dependent metalloenzyme that is inactivated by other metals, such as zinc, copper, or cadmium. This enzyme can also reduce glycol aldehyde with similar efficiency. Beside L-1,2-propanediol, the enzyme is also able to oxidize methanol as an alternative substrate.
Pssm-ID: 341455 [Multi-domain] Cd Length: 378 Bit Score: 121.11 E-value: 3.79e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 8 FPNQVYFGAGQIQKLP-SILKNYLHNP---TDKVLVlaEARVqahVERLETSLGKEVV--HHFDKIIQHVPQTLVEEGLK 81
Cdd:cd08176 5 LNPTSYFGWGAIEEIGeEAKKRGFKKAlivTDKGLV--KFGI---VDKVTDVLKEAGIayTVFDEVKPNPTIENVMAGVA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 82 VTNKLQPKVMLSIGGGSAVGLAKALAL------------------KNHL-PIIAVPTTfAG--SEQTNIWGISNEEG--K 138
Cdd:cd08176 80 AYKESGADGIIAVGGGSSIDTAKAIGIivanpgadvrslegvaptKNPAvPIIAVPTT-AGtgSEVTINYVITDTEKkrK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 139 TTGRDDVVLPQVVVYDPELTQTMPQRLAVMSAMNAMAHLMEAVYSPTGNPITRNQALLGMQQLKKGLENiAQQKAFTTEA 218
Cdd:cd08176 159 FVCVDPHDIPTVAIVDPDLMSSMPKGLTAATGMDALTHAIEGYITKGAWELSDMLALKAIELIAKNLRK-AVANPNNVEA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 219 NEQILLGAYLAGRALCEVTMALHHKAAHVLGGSFGMQHAEVHTVLQTYVLAYQWPHLST---EIQQDFKLTLGNNPP--- 292
Cdd:cd08176 238 RENMALAQYIAGMAFSNVGLGIVHSMAHPLSAFYDTPHGVANAILLPYVMEFNAPATGEkyrDIARAMGVDTTGMSDeea 317
|
330 340 350
....*....|....*....|....*....|.
gi 1111735350 293 -----LALKMLAENAGAPTTLEEIGFDQADI 318
Cdd:cd08176 318 aeaavDAVKKLSKDVGIPQKLSELGVKEEDI 348
|
|
| Fe-ADH-like |
cd08194 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
9-273 |
3.26e-30 |
|
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) most of which have not been characterized. Their specific function is unknown. The protein structure represents a dehydroquinate synthase-like fold and belongs to the alcohol dehydrogenase-like superfamily. It is distinct from other alcohol dehydrogenases which contain different protein domains. Alcohol dehydrogenase catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions.
Pssm-ID: 341473 [Multi-domain] Cd Length: 378 Bit Score: 118.40 E-value: 3.26e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 9 PNQVYFGAGQIQKLPSILKNYL-HNP---TDKVLVlaearVQAHVERLETSLGKEVVHH--FDKIIQHVPQTLVEEGLKV 82
Cdd:cd08194 1 PRTIIIGGGALEELGEEAASLGgKRAlivTDKVMV-----KLGLVDKVTQLLAEAGIAYavFDDVVSEPTDEMVEEGLAL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 83 TNKLQPKVMLSIGGGSAVGLAKALAL------------------KNHLPIIAVPTTfA--GSEQTNIWGISNEEG--KTT 140
Cdd:cd08194 76 YKEGGCDFIVALGGGSPIDTAKAIAVlatnggpirdymgprkvdKPGLPLIAIPTT-AgtGSEVTRFTVITDTETdvKML 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 141 GRDDVVLPQVVVYDPELTQTMPQRLAVMSAMNAMAHLMEAVYSPTGNPITRNQALLGMQQLKKGLEniaqqKAFT----T 216
Cdd:cd08194 155 LKGPALLPAVAIVDPELTLSMPPRVTAATGIDALTHAIEAYVSRKAQPLTDTLALSAIKLIGRNLR-----RAYAdgddL 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1111735350 217 EANEQILLGAYLAGRALCEVTMALHHKAAHVLGGSFGMQHAEVHTVLQTYVLAYQWP 273
Cdd:cd08194 230 EAREAMMLAALEAGIAFSNSSVALVHGMSRPIGALFHVPHGLSNAMLLPAVTEFSLP 286
|
|
| Fe-ADH-like |
cd08191 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
9-349 |
1.34e-28 |
|
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contain different protein domain. Proteins of this family have not been characterized.
Pssm-ID: 341470 [Multi-domain] Cd Length: 392 Bit Score: 114.25 E-value: 1.34e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 9 PNQVYFGAGQIQKLPSILKNYlhnpTDKVLVLAEARV--QAHVERLETSLGK--EVVHHFDKIIQHVPQTLVEEGLKVTN 84
Cdd:cd08191 4 PSRLLFGPGARRALGRVAARL----GSRVLIVTDPRLasTPLVAELLAALTAagVAVEVFDGGQPELPVSTVADAAAAAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 85 KLQPKVMLSIGGGSAVGLAKALALK-NH-----------------LPIIAVPTTFA-GSEQTNIWGISNEE-GKTTGRDD 144
Cdd:cd08191 80 AFDPDVVIGLGGGSNMDLAKVVALLlAHggdprdyygedrvpgpvLPLIAVPTTAGtGSEVTPVAVLTDPArGMKVGVSS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 145 VVL-PQVVVYDPELTQTMPQRLAVMSAMNAMAHLMEA----------------VYSptG-NPITRNQALLGMQQLKKGLE 206
Cdd:cd08191 160 PYLrPAVAIVDPELTLTCPPGVTADSGIDALTHAIESytardfppfprldpdpVYV--GkNPLTDLLALEAIRLIGRHLP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 207 NIAQQKAfTTEANEQILLGAYLAGRALCEVTMALHHKAAHVLGGSFGMQHAEVHTVLQTYVLAYQWPHlsteIQQDFK-- 284
Cdd:cd08191 238 RAVRDGD-DLEARSGMALAALLAGLAFGTAGTAAAHALQYPIGALTHTSHGVGNGLLLPYVMRFNRPA----RAAELAei 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 285 -LTLGNNPPLALKMLAENA-----------GAPTTLEEIGFDQADIG----KAVRI--MLANpypNPAPLVESQLLVMLE 346
Cdd:cd08191 313 aRALGVTTAGTSEEAADRAierveellariGIPTTLADLGVTEADLPglaeKALSVtrLIAN---NPRPPTEEDLLRILR 389
|
...
gi 1111735350 347 RAF 349
Cdd:cd08191 390 AAF 392
|
|
| NADPH_BDH |
cd08179 |
NADPH-dependent butanol dehydrogenase involved in the butanol and ethanol formation pathway in ... |
9-350 |
5.06e-28 |
|
NADPH-dependent butanol dehydrogenase involved in the butanol and ethanol formation pathway in bacteria; NADPH-dependent butanol dehydrogenase (BDH) is involved in the butanol and ethanol formation pathway of some bacteria. The fermentation process is characterized by an acid producing growth phase, followed by a solvent producing phase. The latter phase is associated with the induction of solventogenic enzymes such as butanol dehydrogenase. The activity of the enzyme requires NADPH as cofactor, as well as divalent ions zinc or iron. This family is a member of the iron-containing alcohol dehydrogenase superfamily. Protein structure has a dehydroquinate synthase-like fold.
Pssm-ID: 341458 [Multi-domain] Cd Length: 379 Bit Score: 112.67 E-value: 5.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 9 PNQVYFGAGQIQKLpsilKNYLHNptdKVLVLAEARVQAH---VERLETSL---GKEVvhhfdKIIQHVPQ----TLVEE 78
Cdd:cd08179 5 PRDIYFGEGALEYL----KTLKGK---RAFIVTGGGSMKRngfLDKVEDYLkeaGMEV-----KVFEGVEPdpsvETVEK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 79 GLKVTNKLQPKVMLSIGGGSAVGLAKALAL--------------KNHLP-------IIAVPTTF-AGSEQTNIWGISNEE 136
Cdd:cd08179 73 GAEAMREFEPDWIIAIGGGSVIDAAKAMWVfyeypeltfedalvPFPLPelrkkarFIAIPSTSgTGSEVTRASVITDTE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 137 GKTTG--RDDVVLPQVVVYDPELTQTMPQRLAVMSAMNAMAHLMEAVYSPTGNPITRNQALLGMQQLKKGLEnIAQQKAF 214
Cdd:cd08179 153 KGIKYplASFEITPDVAILDPELTMTMPPHVTANTGMDALTHAIEAYVSTLANDFTDALALGAILDIFENLP-KSYNGGK 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 215 TTEANEQILLGAYLAGRALCEVTMALHHKAAHVLGGSFGMQHAEVHTVLQTYVLAYQWPHLSTEIQQDFKLTLGNNPPL- 293
Cdd:cd08179 232 DLEAREKMHNASCLAGMAFSNSGLGIVHSMAHKGGAFFGIPHGLANAILLPYVIEFNSKDPEARARYAALLIGLTDEELv 311
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1111735350 294 -----ALKMLAENAGAPTTLEEIGFDQADIGKAVRIMLANPYP------NPAPLVESQLLVMLERAFE 350
Cdd:cd08179 312 edlieAIEELNKKLGIPLSFKEAGIDEDEFFAKLDEMAENAMNdactgtNPRKPTVEEMKELLKAAYY 379
|
|
| DHQ_Fe-ADH |
cd07766 |
Dehydroquinate synthase-like (DHQ-like) and iron-containing alcohol dehydrogenases (Fe-ADH); ... |
9-326 |
5.66e-28 |
|
Dehydroquinate synthase-like (DHQ-like) and iron-containing alcohol dehydrogenases (Fe-ADH); This superfamily consists of two subgroups: the dehydroquinate synthase (DHQS)-like, and a large metal-containing alcohol dehydrogenases (ADH), known as iron-containing alcohol dehydrogenases. Dehydroquinate synthase (DHQS) catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate-7-phosphate (DAHP) to dehydroquinate (DHQ) in the second step of the shikimate pathway. This pathway involves seven sequential enzymatic steps in the conversion of erythrose 4-phosphate and phosphoenolpyruvate into chorismate for subsequent synthesis of aromatic compounds. Dehydroquinate synthase-like group includes dehydroquinate synthase, 2-deoxy-scyllo-inosose synthase, and 2-epi-5-epi-valiolone synthase. The alcohol dehydrogenases (ADHs) in this superfamily contain a dehydroquinate synthase-like protein structural fold and mostly contain iron. They are distinct from other alcohol dehydrogenases which contains different protein domains. There are several distinct families of alcohol dehydrogenases: Zinc-containing long-chain alcohol dehydrogenases; insect-type, or short-chain alcohol dehydrogenases; iron-containing alcohol dehydrogenases, and others. The iron-containing family has a Rossmann fold-like topology that resembles the fold of the zinc-dependent alcohol dehydrogenases, but lacks sequence homology, and differs in strand arrangement. ADH catalyzes the reversible oxidation of alcohol to acetaldehyde with the simultaneous reduction of NAD(P)+ to NAD(P)H.
Pssm-ID: 341447 [Multi-domain] Cd Length: 271 Bit Score: 110.15 E-value: 5.66e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 9 PNQVYFGAGQIQKLPSILKNYLhnptDKVLVLA-EARVQAHVERLETSLGKEV-VHHFDKIIQHVPQTLVEEGLKVTNKL 86
Cdd:cd07766 1 PTRIVFGEGAIAKLGEIKRRGF----DRALVVSdEGVVKGVGEKVADSLKKGLaVAIFDFVGENPTFEEVKNAVERARAA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 87 QPKVMLSIGGGSAVGLAKALA--LKNHLPIIAVPTTFA-GSEQTNIWGISNEEGKTTGRDDVVLPQVVVYDPELTQTMPQ 163
Cdd:cd07766 77 EADAVIAVGGGSTLDTAKAVAalLNRGIPFIIVPTTAStDSEVSPKSVITDKGGKNKQVGPHYNPDVVFVDTDITKGLPP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 164 RLAVMSAMNAMAHLMEAvysptgnpitrnqallgmqqlkkgleniaqqkaftteanEQILLGAYLAGRALCEVT-MALHH 242
Cdd:cd07766 157 RQVASGGVDALAHAVEL---------------------------------------EKVVEAATLAGMGLFESPgLGLAH 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 243 KAAHVLGGSFGMQHAEVHTVLQTYVLAYQwPHLSTEIQQDFKltlgnnpplALKMLAENAGAPTTLEEIGFDQADIGKAV 322
Cdd:cd07766 198 AIGHALTAFEGIPHGEAVAVGLPYVLKVA-NDMNPEPEAAIE---------AVFKFLEDLGLPTHLADLGVSKEDIPKLA 267
|
....
gi 1111735350 323 RIML 326
Cdd:cd07766 268 EKAL 271
|
|
| PDDH |
cd08188 |
1,3-Propanediol (1,3-PD) dehydrogenase; This family includes 1,3-propanediol (1,3-PD) ... |
8-331 |
1.50e-27 |
|
1,3-Propanediol (1,3-PD) dehydrogenase; This family includes 1,3-propanediol (1,3-PD) dehydrogenase, a key enzyme in the microbial production of 1,3-PD that has been previously characterized as the product of dhaT gene in Klebsiella pneumoniae. 1,3-PD dehydrogenase is a member of the family III metal-dependent polyol dehydrogenases, which are shown to require a divalent metal ion for catalysis. However, some members of this family showed a dependence on Fe(2+) or Zn(2+) for activity.
Pssm-ID: 341467 [Multi-domain] Cd Length: 377 Bit Score: 111.07 E-value: 1.50e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 8 FPNQVYFGAGQIQKLPSILKNY-LHNP---TDKVLVLAearvqAHVERLETSL---GKEVVHhFDKIiqhVPQ---TLVE 77
Cdd:cd08188 5 IPPVNLFGPGCLKEIGDELKKLgGKKAlivTDKGLVKL-----GLVKKVTDVLeeaGIEYVI-FDGV---QPNptvTNVN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 78 EGLKVTNKLQPKVMLSIGGGSAVGLAKALAL------------------KNHLPIIAVPTTfAG--SEQTNIWGISNEEG 137
Cdd:cd08188 76 EGLELFKENGCDFIISVGGGSAHDCAKAIGIlatnggeiedyegvdkskKPGLPLIAINTT-AGtaSEVTRFAVITDEER 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 138 --KTTGRDDVVLPQVVVYDPELTQTMPQRLAVMSAMNAMAHLMEAVYSPTGNPITRNQALLGMQQLKKGLENiAQQKAFT 215
Cdd:cd08188 155 hvKMVIVDWNVTPTIAVNDPELMLGMPPSLTAATGMDALTHAIEAYVSTGATPLTDALALEAIRLIAENLPK-AVANGKD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 216 TEANEQILLGAYLAGRALCEVTMALHHKAAHVLGGSFGMQHAEVHTVLQTYVLAY---QWPHLSTEIQQDFKLTLGNNPP 292
Cdd:cd08188 234 LEARENMAYAQFLAGMAFNNAGLGYVHAMAHQLGGFYNLPHGVCNAILLPHVMEFnlpACPERFADIARALGENTEGLSD 313
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1111735350 293 --------LALKMLAENAGAPTTLEEIGFDQADIGKAVR------IMLANPYP 331
Cdd:cd08188 314 eeaaeaaiEAIRKLSRRVGIPSGLKELGVKEEDFPLLAEnalkdaCGPTNPRQ 366
|
|
| BDH |
cd08187 |
Butanol dehydrogenase catalyzes the conversion of butyraldehyde to butanol with the cofactor ... |
2-328 |
6.31e-27 |
|
Butanol dehydrogenase catalyzes the conversion of butyraldehyde to butanol with the cofactor NAD(P)H being oxidized in the process; The butanol dehydrogenase (BDH) is involved in the final step of the butanol formation pathway in anaerobic micro-organism. Butanol dehydrogenase catalyzes the conversion of butyraldehyde to butanol with the cofactor NAD(P)H being oxidized in the process. Activity in the reverse direction is 50-fold lower than that in the forward direction. The NADH-BDH has higher activity with longer chained aldehydes and is inhibited by metabolites containing an adenine moiety. This protein family belongs to the so-called iron-containing alcohol dehydrogenase superfamily. Since members of this superfamily use different divalent ions, preferentially iron or zinc, it has been suggested to be renamed to family III metal-dependent polyol dehydrogenases. This family also includes E. coli YqhD enzyme, an NADP-dependent dehydrogenase whose activity measurements with several alcohols demonstrate preference for alcohols longer than C3. The active site of YqhD contains a Zn metal, and a modified NADPH cofactor bearing OH groups on the saturated C5 and C6 atoms, possibly due to oxygen stress on the enzyme, which would functionally work under anaerobic conditions.
Pssm-ID: 341466 [Multi-domain] Cd Length: 382 Bit Score: 109.45 E-value: 6.31e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 2 NFTYKSfPNQVYFGAGQIQKLPSILKNYLHnptdKVLVLA-EARVQAH--VERLETSL---GKEVVHhFDKIiqhVPQ-- 73
Cdd:cd08187 1 NFTFYN-PTKIIFGKGAIEELGEEIKKYGK----KVLLVYgGGSIKKNglYDRVVASLkeaGIEVVE-FGGV---EPNpr 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 74 -TLVEEGLKVTNKLQPKVMLSIGGGSAVGLAKALAL------------------KNHLPIIAVPTTFA-GSEQTNIWGIS 133
Cdd:cd08187 72 lETVREGIELAREENVDFILAVGGGSVIDAAKAIAAgakydgdvwdfftgkappEKALPVGTVLTLAAtGSEMNGGAVIT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 134 NEEG--KTTGRDDVVLPQVVVYDPELTQTMPQRLAVMSAMNAMAHLMEAVYSPT-GNPITRNQALLGMQQLkkgLEN--I 208
Cdd:cd08187 152 NEETkeKLGFGSPLLRPKFSILDPELTYTLPKYQTAAGIVDIFSHVLEQYFTGTeDAPLQDRLAEGLLRTV---IENgpK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 209 AQQKAFTTEANEQILLGAYLA-------GRALCEVTmalhHKAAHVLGGSFGMQHAEVHTVLQTYVLAYQWPH------- 274
Cdd:cd08187 229 ALKDPDDYEARANLMWAATLAlngllgaGRGGDWAT----HAIEHELSALYDITHGAGLAIVFPAWMRYVLKKkperfaq 304
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1111735350 275 LSTEIqqdFKLTLGNNPPLALKMLAE-------NAGAPTTLEEIGFDQADIGKAVRIMLAN 328
Cdd:cd08187 305 FARRV---FGIDPGGDDEETALEGIEaleeffkSIGLPTTLSELGIDEEDIEEMAEKAVRG 362
|
|
| Fe-ADH-like |
cd14862 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
8-325 |
1.13e-26 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341484 [Multi-domain] Cd Length: 375 Bit Score: 108.85 E-value: 1.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 8 FPNQVYFGAGQIQKLPSILKNYLHNPTDKVLVLAEArVQAHVERLEtSLGKEVVHhFDKIIQHVPQTLVEEGLKVTNKLQ 87
Cdd:cd14862 5 SSPKIVFGEDALSHLEQLSGKRALIVTDKVLVKLGL-LKKVLKRLL-QAGFEVEV-FDEVEPEPPLETVLKGAEAMREFE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 88 PKVMLSIGGGSAVGLAKALALKNHLP--------------------IIAVPTTFA-GSEQTNIWGISNEEGK---TTGRD 143
Cdd:cd14862 82 PDLIIALGGGSVMDAAKAAWVLYERPdldpedispldllglrkkakLIAIPTTSGtGSEATWAIVLTDTEEPrkiAVANP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 144 DVVlPQVVVYDPELTQTMPQRLAVMSAMNAMAHLMEAVYSPTGNPITRNQALLGMQQLKKGLEniaqqKAFTT----EAN 219
Cdd:cd14862 162 ELV-PDVAILDPEFVLGMPPKLTAGTGLDALAHAVEAYLSTWSNDFSDALALKAIELIFKYLP-----RAYKDgddlEAR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 220 EQILLGAYLAGRALCEVTMALHHKAAHVLGGSFGMQHAEVHTVLQTYVLAYQWPHLSTEIQQDFKLTLGNNPPL-ALKML 298
Cdd:cd14862 236 EKMHNAATIAGLAFGNSQAGLAHALGHSLGAVFHVPHGIAVGLFLPYVIEFYAKVTDERYDLLKLLGIEARDEEeALKKL 315
|
330 340 350
....*....|....*....|....*....|....
gi 1111735350 299 AEN-------AGAPTTLEEIGFDQADIGKAVRIM 325
Cdd:cd14862 316 VEAirelykeVGQPLSIKDLGISEEEFEEKLDEL 349
|
|
| PRK10624 |
PRK10624 |
L-1,2-propanediol oxidoreductase; Provisional |
10-318 |
2.11e-26 |
|
L-1,2-propanediol oxidoreductase; Provisional
Pssm-ID: 182595 [Multi-domain] Cd Length: 382 Bit Score: 108.16 E-value: 2.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 10 NQV-YFGAGQIQKLPSILKNY-LHNP---TDKVLVlaEARVQAHVERL--ETSLGKEVvhhFDKIIQHVPQTLVEEGLKV 82
Cdd:PRK10624 8 NETaYFGRGAIGALTDEVKRRgFKKAlivTDKTLV--KCGVVAKVTDVldAAGLAYEI---YDGVKPNPTIEVVKEGVEV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 83 TNKLQPKVMLSIGGGSAVGLAKALAL-------------------KNH-LPIIAVPTTfAG--SEQTNIWGISNEEGKtt 140
Cdd:PRK10624 83 FKASGADYLIAIGGGSPQDTCKAIGIisnnpefadvrslegvaptKKPsVPIIAIPTT-AGtaAEVTINYVITDEEKR-- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 141 gRDDVV-----LPQVVVYDPELTQTMPQRLAVMSAMNAMAHLMEAVysptgnpITRNQ-ALLGMQQLkKGLENIAQQ--- 211
Cdd:PRK10624 160 -RKFVCvdphdIPQVAFVDADMMDSMPPGLKAATGVDALTHAIEGY-------ITRGAwALTDMLHL-KAIEIIAGAlrg 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 212 -KAFTTEANEQILLGAYLAGRALCEVTMALHHKAAHVLGGSFGMQHAEVHTVLQTYVLAYQWPHlSTEIQQDFKLTLG-- 288
Cdd:PRK10624 231 aVAGDKEAGEGMALGQYIAGMGFSNVGLGLVHGMAHPLGAFYNTPHGVANAILLPHVMEYNADF-TGEKYRDIARAMGvk 309
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1111735350 289 -NNPPL---------ALKMLAENAGAPTTLEEIGFDQADI 318
Cdd:PRK10624 310 vEGMSLeearnaaveAVKALNRDVGIPPHLRDVGVKEEDI 349
|
|
| Fe-ADH-like |
cd17814 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
36-331 |
1.64e-25 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341489 [Multi-domain] Cd Length: 374 Bit Score: 105.32 E-value: 1.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 36 KVLVLAEARVQAH--VERLETSLGKEVVHH--FDKIIQHVPQTLVEEGLKVTNKLQPKVMLSIGGGSAVGLAKALAL--- 108
Cdd:cd17814 28 KVLVVTDPGVIKAgwVDEVLDSLEAEGLEYvvFSDVTPNPRDFEVMEGAELYREEGCDGIVAVGGGSPIDCAKGIGIvvs 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 109 -KNHL--------------PIIAVPTTfAGSE----QTNIwgISNEE--------GKTtgrddvVLPQVVVYDPELTQTM 161
Cdd:cd17814 108 nGGHIldyegvdkvrrplpPLICIPTT-AGSSadvsQFAI--ITDTErrvkmaiiSKT------LVPDVSLIDPETLTTM 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 162 PQRLAVMSAMNAMAHLMEAVYSPTGNPITRNQALLGMQQLKKGLENIAQQKAfTTEANEQILLGAYLAGRALCEVTMALH 241
Cdd:cd17814 179 DPELTACTGMDALTHAIEAYVSNASSPLTDLHALEAIRLISENLPKAVADPD-DLEAREKMMLASLQAGLAFSNASLGAV 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 242 HKAAHVLGGSFGMQHAEVHTVLQTYVLAYQWP---------------HLSTEIQQDFKLTLGNnpplALKMLAENAGAPT 306
Cdd:cd17814 258 HAMAHSLGGLLDLPHGECNALLLPHVIRFNFPaaperyrkiaeamglDVDGLDDEEVAERLIE----AIRDLREDLGIPE 333
|
330 340 350
....*....|....*....|....*....|.
gi 1111735350 307 TLEEIGFDQADI----GKAVR--IMLANPYP 331
Cdd:cd17814 334 TLSELGVDEEDIpelaKRAMKdpCLVTNPRR 364
|
|
| AAD_C |
cd08178 |
C-terminal alcohol dehydrogenase domain of the acetaldehyde dehydrogenase-alcohol ... |
9-331 |
1.81e-25 |
|
C-terminal alcohol dehydrogenase domain of the acetaldehyde dehydrogenase-alcohol dehydrogenase bifunctional two-domain protein (AAD); This alcohol dehydrogenase domain is located on the C-terminal of a bifunctional two-domain protein. The N-terminal of the protein contains an acetaldehyde-CoA dehydrogenase domain. This protein is involved in pyruvate metabolism whereby pyruvate is converted to acetyl-CoA and formate by pyruvate formate-lysase (PFL). Under anaerobic condition, acetyl-CoA is reduced to acetaldehyde and ethanol by this two-domain protein. Acetyl-CoA is first converted into an enzyme-bound thiohemiacetal by the N-terminal acetaldehyde dehydrogenase domain. The enzyme-bound thiohemiacetal is subsequently reduced by the C-terminal NAD+-dependent alcohol dehydrogenase domain. In E. coli, this protein is called AdhE and has been shown to have pyruvate formate-lyase (PFL) deactivase activity, which leads to the inactivation of PFL, a key enzyme in anaerobic metabolism. In Escherichia coli and Entamoeba histolytica, this enzyme forms homopolymeric peptides composed of more than 20 protomers associated in a helical rod-like structure.
Pssm-ID: 341457 [Multi-domain] Cd Length: 400 Bit Score: 105.73 E-value: 1.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 9 PNQVYFGAGQIQKLPSILKNylHNP----TDKVLVlaearVQAHVERLETSLGKEVVHH--FDKIIQHVPQTLVEEGLKV 82
Cdd:cd08178 3 PPKIYFEPGCLPYLLLELPG--VKRafivTDRVLY-----KLGYVDKVLDVLEARGVETevFSDVEPDPTLSTVRKGLEA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 83 TNKLQPKVMLSIGGGSAVGLAKALALK-NH---------------------LPI-------IAVPTTF-AGSEQTNIWGI 132
Cdd:cd08178 76 MNAFKPDVIIALGGGSAMDAAKIMWLFyEHpetkfedlaqrfmdirkrvykFPKlgkkaklVAIPTTSgTGSEVTPFAVI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 133 SNEEgktTGR-----DDVVLPQVVVYDPELTQTMPQRLAVMSAMNAMAHLMEAVYSPTGNPITRNQALLGMQQLKKGLEN 207
Cdd:cd08178 156 TDDK---TGKkyplaDYALTPDMAIVDPELVMTMPKRLTADTGIDALTHAIEAYVSVMASDYTDGLALQAIKLIFEYLPR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 208 iAQQKAFTTEANEQILLGAYLAGRALCEVTMALHHKAAHVLGGSFGMQHAEVHTVLQTYVLAYQ----------WPHLST 277
Cdd:cd08178 233 -SYNNGNDIEAREKMHNAATIAGMAFANAFLGICHSLAHKLGAAFHIPHGRANAILLPHVIRYNatdpptkqaaFPQYKY 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 278 --------EIQQDFKLTlGNNPPLALKMLAE-------NAGAPTTLEEIGFDQADIGKAVRIM----------LANP-YP 331
Cdd:cd08178 312 yvakeryaEIADLLGLG-GKTPEEKVESLIKaiedlkkDLGIPTSIREAGIDEADFLAAVDKLaedafddqctGANPrYP 390
|
|
| Fe-ADH-like |
cd08189 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
11-333 |
1.04e-24 |
|
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and belongs to the alcohol dehydrogenase-like superfamily. It is distinct from other alcohol dehydrogenases which contain different protein domain. Proteins of this family have not been characterized.
Pssm-ID: 341468 [Multi-domain] Cd Length: 378 Bit Score: 103.32 E-value: 1.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 11 QVYFGAGQIQKLPSILKNY-LHNP---TDKVLVLAEarvqaHVERLETSLGKE--VVHHFDKIiqhVPQ---TLVEEGLK 81
Cdd:cd08189 7 ELFEGAGSLLQLPEALKKLgIKRVlivTDKGLVKLG-----LLDPLLDALKKAgiEYVVFDGV---VPDptiDNVEEGLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 82 VTNKLQPKVMLSIGGGSAVGLAKALALK--NH-----------------LPIIAVPTTfAG--SEQTNIWGISNEEG--K 138
Cdd:cd08189 79 LYKENGCDAIIAIGGGSVIDCAKVIAARaaNPkksvrklkgllkvrkklPPLIAVPTT-AGtgSEATIAAVITDPETheK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 139 TTGRDDVVLPQVVVYDPELTQTMPQRLAVMSAMNAMAHLMEAVYSPTGNPITRNQALLGMQQLkkgLENIaqQKAFT--- 215
Cdd:cd08189 158 YAINDPKLIPDAAVLDPELTLGLPPAITAATGMDALTHAVEAYISRSATKETDEYALEAVKLI---FENL--PKAYEdgs 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 216 -TEANEQILLGAYLAGRALcevTMAL---HHKAAHVLGGSFGMQHAEVHTVLQTYVL-AYQ---WPHLStEIQQDFKLTL 287
Cdd:cd08189 233 dLEARENMLLASYYAGLAF---TRAYvgyVHAIAHQLGGLYGVPHGLANAVVLPHVLeFYGpaaEKRLA-ELADAAGLGD 308
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1111735350 288 GNNPP--LALKM------LAENAGAPTTLEEIgfDQADIGK-AVRIML-ANP-YPNP 333
Cdd:cd08189 309 SGESDseKAEAFiaaireLNRRMGIPTTLEEL--KEEDIPEiAKRALKeANPlYPVP 363
|
|
| HVD |
cd08193 |
5-hydroxyvalerate dehydrogenase (HVD) catalyzes the oxidation of 5-hydroxyvalerate to ... |
14-349 |
3.82e-23 |
|
5-hydroxyvalerate dehydrogenase (HVD) catalyzes the oxidation of 5-hydroxyvalerate to 5-oxovalerate with NAD+ as cofactor; 5-hydroxyvalerate dehydrogenase (HVD) is an iron-containing (type III) NAD-dependent alcohol dehydrogenase. It plays a role in the cyclopentanol metabolism biochemical pathway. It catalyzes the oxidation of 5-hydroxyvalerate to 5-oxovalerate with NAD+ as cofactor. This cyclopentanol (cpn) degradation pathway is present in some bacteria which can use cyclopentanol as sole carbon source. In Comamonas sp. strain NCIMB 9872, this enzyme is encoded by the CpnD gene.
Pssm-ID: 341472 [Multi-domain] Cd Length: 379 Bit Score: 98.74 E-value: 3.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 14 FGAGQIQKLPSILKNYLHNptdKVLVLAEARVQAH--VERLETSLGKE--VVHHFDKIIQHVPQTLVEEGLKVTNKLQPK 89
Cdd:cd08193 9 CGAGAAARLGELLRELGAR---RVLLVTDPGLVKAglADPALAALEAAgiAVTVFDDVVADPPEAVVEAAVEQAREAGAD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 90 VMLSIGGGSAVGLAK--ALALKN----------------HLPIIAVPTTfAG--SEQTNIWGISNEEGKTTG-RDDVVLP 148
Cdd:cd08193 86 GVIGFGGGSSMDVAKlvALLAGSdqplddiygvgkatgpRLPLILVPTT-AGtgSEVTPISIVTTGETEKKGvVSPQLLP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 149 QVVVYDPELTQTMPQRLAVMSAMNAMAHLMEAVYSPTG-NPITRNQALLGMQQLKKGLEniaqqKAFTT----EANEQIL 223
Cdd:cd08193 165 DVALLDAELTLGLPPHVTAATGIDAMVHAIEAYTSRHKkNPISDALAREALRLLGANLR-----RAVEDgsdlEAREAML 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 224 LGAYLAGRALCEVTMALHHKAAHVLGGSFGMQHAEVHTVLQTYVLAYQWPH-----------LSTEIQQDFKLTLGNNPP 292
Cdd:cd08193 240 LGSMLAGQAFANAPVAAVHALAYPLGGHFHVPHGLSNALVLPHVLRFNLPAaealyaelaraLLPGLAFGSDAAAAEAFI 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1111735350 293 LALKMLAENAGAPTTLEEIGFDQADIGKA------VRIMLANpypNPAPLVESQLLVMLERAF 349
Cdd:cd08193 320 DALEELVEASGLPTRLRDVGVTEEDLPMLaedamkQTRLLVN---NPREVTEEDALAIYQAAL 379
|
|
| PDD |
cd08180 |
1,3-propanediol dehydrogenase (PPD) catalyzes the reduction of 3-hydroxypropionaldehyde (3-HPA) ... |
7-328 |
1.09e-20 |
|
1,3-propanediol dehydrogenase (PPD) catalyzes the reduction of 3-hydroxypropionaldehyde (3-HPA) to 1,3-propanediol in glycerol metabolism; 1,3-propanediol dehydrogenase (PPD) plays a role in glycerol metabolism of some bacteria in anaerobic conditions. In this degradation pathway, glycerol is converted in a two-step process to 1,3-propanediol (1,3-PD) which is then excreted into the extracellular medium. The first reaction involves the transformation of glycerol into 3-hydroxypropionaldehyde (3-HPA) by a coenzyme B-12-dependent dehydratase. The second reaction involves the dismutation of the 3-hydroxypropionaldehyde (3-HPA) to 1,3-propanediol by the NADH-linked 1,3-propanediol dehydrogenase (PPD). The enzyme requires iron ion for its function. Because many genes in this pathway are present in the propanediol utilization (pdu) operon, they are also named pdu genes. PPD is a member of the iron-containing alcohol dehydrogenase superfamily. The PPD structure has a dehydroquinate synthase-like fold.
Pssm-ID: 341459 [Multi-domain] Cd Length: 333 Bit Score: 91.40 E-value: 1.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 7 SFPNQVYFGAGQIQKLPSILKNYLHNPTDKVLVLAEarvqaHVERLETSLGKEV-VHHFDKIIQHVPQTLVEEGLKVTNK 85
Cdd:cd08180 2 SLKTKIYSGEDSLERLKELKGKRVFIVTDPFMVKSG-----MVDKVTDELDKSNeVEIFSDVVPDPSIEVVAKGLAKILE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 86 LQPKVMLSIGGGSAVGLAKALAL--------KNHLPIIAVPTTFA-GSEQTNIWGISNEEG--KTTGRDDVVLPQVVVYD 154
Cdd:cd08180 77 FKPDTIIALGGGSAIDAAKAIIYfalkqkgnIKKPLFIAIPTTSGtGSEVTSFAVITDPEKgiKYPLVDDSMLPDIAILD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 155 PELTQTMPQRLAVMSAMNAMAHLMEAVYSPTGNPITRNQAllgmqqlKKGLENIAQ--QKAF----TTEANEQILLGAYL 228
Cdd:cd08180 157 PELVKSVPPKVTADTGMDVLTHALEAYVSTNANDFTDALA-------EKAIKLVFEnlPRAYrdgdDLEAREKMHNASCM 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 229 AGRALCEVTMALHHKAAHVLGGSFGMQHAEVHTVLQTYVLAYqwphLSTEIQQdfkltlgnnpplalkmLAENAGAPTTL 308
Cdd:cd08180 230 AGIAFNNAGLGINHSLAHALGGRFHIPHGRANAILLPYVIEF----LIAAIRR----------------LNKKLGIPSTL 289
|
330 340
....*....|....*....|
gi 1111735350 309 EEIGFDQADIGKAVRIMLAN 328
Cdd:cd08180 290 KELGIDEEEFEKAIDEMAEA 309
|
|
| HOT |
cd08190 |
Hydroxyacid-oxoacid transhydrogenase (HOT) involved in gamma-hydroxybutyrate metabolism; This ... |
11-331 |
3.73e-19 |
|
Hydroxyacid-oxoacid transhydrogenase (HOT) involved in gamma-hydroxybutyrate metabolism; This family contains hydroxyacid-oxoacid transhydrogenase (HOT), also known as D-2-hydroxyglutarate transhydrogenase. It catalyzes the conversion of gamma-hydroxybutyrate (GHB) to succinic semialdehyde (SSA), coupled to the stoichiometric conversion of alpha-ketoglutarate to D-2-hydroxyglutarate in gamma-Hydroxybutyrate catabolism. Unlike many other alcohols, which are oxidized by NAD-linked dehydrogenases, gamma-hydroxybutyrate is metabolized to succinate semialdehyde by hydroxyacid-oxoacid transhydrogenase which does not require free NAD or NADP; instead, it uses alpha-ketoglutarate as an acceptor, converting it to d-2-hydroxyglutarate. Alpha-ketoglutarate serves as an intermediate acceptor to regenerate NAD(P) required for the oxidation of GHB. HOT also catalyzes the reversible oxidation of a hydroxyacid obligatorily coupled to the reduction of an oxoacid, and requires no cofactor. In mammals, the HOT enzyme is located in mitochondria, and is expressed with an N-terminal mitochondrial targeting sequence. HOT enzyme is member of the metal-containing alcohol dehydrogenase family. It typically contains an iron although other metal ions may be used.
Pssm-ID: 341469 [Multi-domain] Cd Length: 412 Bit Score: 87.60 E-value: 3.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 11 QVYFGAGQIQKLPSILKNYlhnPTDKVLVLAEARVQ--AHVERLETSLGKE----VVhhFDKIiqHVPQTL--VEEGLKV 82
Cdd:cd08190 3 NIRFGPGATRELGMDLKRL---GAKKVLVVTDPGLAklGLVERVLESLEKAgievVV--YDGV--RVEPTDesFEEAIEF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 83 TNKLQPKVMLSIGGGSAVGLAKALAL-KNH----------------------LPIIAVPTTFA-GSEQTN--IWGISNEE 136
Cdd:cd08190 76 AKEGDFDAFVAVGGGSVIDTAKAANLyATHpgdfldyvnapigkgkpvpgplKPLIAIPTTAGtGSETTGvaIFDLEELK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 137 GKTTGRDDVVLPQVVVYDPELTQTMPQRLAVMSAMNAMAHLMEA-------------------VYSptG-NPITRNQALL 196
Cdd:cd08190 156 VKTGISSRYLRPTLAIVDPLLTLTLPPRVTASSGFDVLCHALESytarpynarprpanpderpAYQ--GsNPISDVWAEK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 197 GMQQLKKGLENIAQQKAfTTEANEQILLGAYLAGRALCEVTMALHHKAAHVLGG------SFGMQHAEVHT-------VL 263
Cdd:cd08190 234 AIELIGKYLRRAVNDGD-DLEARSNMLLASTLAGIGFGNAGVHLPHAMAYPIAGlvkdyrPPGYPVDHPHVphglsvaLT 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 264 QTYVLAYQWP-----HLstEIQQDFKLTLGNNPPL--------ALKMLAENAGAPTTLEEIGFDQADIGKAV-------R 323
Cdd:cd08190 313 APAVFRFTAPacperHL--EAAELLGADTSGASDRdagevladALIKLMRDIGIPNGLSALGYSEDDIPALVegtlpqqR 390
|
....*...
gi 1111735350 324 IMLANPYP 331
Cdd:cd08190 391 LLKLNPRP 398
|
|
| PRK13805 |
PRK13805 |
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional |
76-349 |
7.97e-19 |
|
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional
Pssm-ID: 237515 [Multi-domain] Cd Length: 862 Bit Score: 87.93 E-value: 7.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 76 VEEGLKVTNKLQPKVMLSIGGGSAVGLAKA--------------LALK---------------NHLPIIAVPTTFA-GSE 125
Cdd:PRK13805 528 VRKGAELMRSFKPDTIIALGGGSPMDAAKImwlfyehpetdfedLAQKfmdirkriykfpklgKKAKLVAIPTTSGtGSE 607
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 126 QTNIWGISNEEgktTGR-----DDVVLPQVVVYDPELTQTMPQRLAVMSAMNAMAHLMEAVYSPTGNPITRNQALLGMQQ 200
Cdd:PRK13805 608 VTPFAVITDDK---TGVkyplaDYELTPDVAIVDPNLVMTMPKSLTADTGIDALTHALEAYVSVMASDYTDGLALQAIKL 684
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 201 LKKGLENIAQQKAFTTEANEQILLGAYLAGRALCEVTMALHHKAAHVLGGSFGMQHAEVHTVLQTYVLAYQ--------- 271
Cdd:PRK13805 685 VFEYLPRSYKNGAKDPEAREKMHNASTIAGMAFANAFLGICHSMAHKLGAEFHIPHGRANAILLPHVIRYNatdppkqaa 764
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 272 WPHLST--------EIQQDFKLTlGNNPP-------LALKMLAENAGAPTTLEEIGFDQADIGKAVRIM----------L 326
Cdd:PRK13805 765 FPQYEYpraderyaEIARHLGLP-GSTTEekvesliKAIEELKAELGIPMSIKEAGVDEADFLAKLDELaelafddqctG 843
|
330 340
....*....|....*....|...
gi 1111735350 327 ANPYpnpAPLVeSQLLVMLERAF 349
Cdd:PRK13805 844 ANPR---YPLI-SELKEILLDAY 862
|
|
| PPD-like |
cd08181 |
1,3-propanediol dehydrogenase-like (PPD); This family contains proteins similar to 1, ... |
94-249 |
7.55e-18 |
|
1,3-propanediol dehydrogenase-like (PPD); This family contains proteins similar to 1,3-propanediol dehydrogenase (PPD) which is a member of the iron-containing alcohol dehydrogenase superfamily, and exhibits a dehydroquinate synthase-like fold. Protein sequence similarity search and other biochemical evidences suggest that they are close to the iron-containing 1,3-propanediol dehydrogenase (EC 1.1.1.202). 1,3-propanediol dehydrogenase catalyzes the oxidation of propane-1,3-diol to 3-hydroxypropanal with the simultaneous reduction of NADP+ to NADPH. The protein structure of Thermotoga maritima TM0920 gene contains one NADP+ and one iron ion.
Pssm-ID: 341460 [Multi-domain] Cd Length: 358 Bit Score: 83.40 E-value: 7.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 94 IGGGSAVGLAKALAL-----------------KNHLPIIAVPTTfAG--SEQTNIWGISNEEGKTTG--RDDVVLPQVVV 152
Cdd:cd08181 90 IGGGSPLDAAKAIALlaankdgdedlfqngkyNPPLPIVAIPTT-AGtgSEVTPYSILTDHEKGTKKsfGNPLIFPKLAL 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 153 YDPELTQTMPQRLAVMSAMNAMAHLMEAVYSPTGNPITRNQALLGMQQLKKGLENIAQQkAFTTEANEQILLGAYLAGra 232
Cdd:cd08181 169 LDPKYTLSLPEELTIDTAVDALSHAIEGYLSVKATPLSDALALEALRLIGECLPNLLGD-ELDEEDREKLMYASTLAG-- 245
|
170 180
....*....|....*....|
gi 1111735350 233 lcevtMALHH---KAAHVLG 249
Cdd:cd08181 246 -----MVIAQtgtTLPHGLG 260
|
|
| PRK09860 |
PRK09860 |
putative alcohol dehydrogenase; Provisional |
76-267 |
1.07e-17 |
|
putative alcohol dehydrogenase; Provisional
Pssm-ID: 182118 [Multi-domain] Cd Length: 383 Bit Score: 83.46 E-value: 1.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 76 VEEGLKVTNKLQPKVMLSIGGGSAVGLAKALAL------------------KNHLPIIAVPTTfAG--SEQTNIWGISNE 135
Cdd:PRK09860 77 VAAGLKLLKENNCDSVISLGGGSPHDCAKGIALvaanggdirdyegvdrsaKPQLPMIAINTT-AGtaSEMTRFCIITDE 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 136 EG--KTTGRDDVVLPQVVVYDPELTQTMPQRLAVMSAMNAMAHLMEAVYSPTGNPITRNQALLGMQQLKKGLEnIAQQKA 213
Cdd:PRK09860 156 ARhiKMAIVDKHVTPLLSVNDSSLMIGMPKSLTAATGMDALTHAIEAYVSIAATPITDACALKAVTMIAENLP-LAVEDG 234
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1111735350 214 FTTEANEQILLGAYLAGRALCEVTMALHHKAAHVLGGSFGMQHAEVHTVLQTYV 267
Cdd:PRK09860 235 SNAKAREAMAYAQFLAGMAFNNASLGYVHAMAHQLGGFYNLPHGVCNAVLLPHV 288
|
|
| Fe-ADH-like |
cd14864 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
7-349 |
1.31e-16 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341486 [Multi-domain] Cd Length: 376 Bit Score: 80.04 E-value: 1.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 7 SFPNQVYFGAGQIQKLPSILKNYLHNP---TDKVLVLAEArvqahVERLETSL--GKEVVHHFDKIIQHVPQTLVEEGLK 81
Cdd:cd14864 2 KIPPNIVFGADSLERIGEEVKEYGSRFlliTDPVLKESGL-----ADKIVSSLekAGISVIVFDEIPASATSDTIDEAAE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 82 VTNKLQPKVMLSIGGGSAVGLAKALAL------------------KNHLPIIAVPTTF-AGSEQTNIWGIsneEGKTTGR 142
Cdd:cd14864 77 LARKAGADGIIAVGGGKVLDTAKAVAIlanndggaydflegakpkKKPLPLIAVPTTPrSGFEFSDRFPV---VDSRSRE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 143 DDVV-----LPQVVVYDPELTQTMPQRLAVMSAMNAMAHLMEAVYSPTGNPITRNQALLGMQQLKKGLEniAQQKAFTTE 217
Cdd:cd14864 154 VKLLkaqpgLPKAVIVDPNLMASLTGNQTAAMALAALALAVEAYLSKKSNFFSDALALKAIELVSENLD--GALADPKNT 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 218 -ANEQILLGAYLAGRALCEVTMALHHKAAHVLGGSFGMQHAEVHTVLQTYVLAYqwpHLSTEIQQDFKL-------TLGN 289
Cdd:cd14864 232 pAEELLAQAGCLAGLAASSSSPGLATALALAVNSRYKVSKSLVASILLPHVIEY---AATSAPDKYAKIaralgedVEGA 308
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1111735350 290 NPPLALKMLAEN-------AGAPTTLEEIGFDqADIGKAVRI--MLANPYPNPAPLVESQLLVMLERAF 349
Cdd:cd14864 309 SPEEAAIAAVEGvrrliaqLNLPTRLKDLDLA-SSLEQLAAIaeDAPKLNGLPRSMSSDDIFDILKAAF 376
|
|
| 4HBD_NAD |
cd14860 |
4-hydroxybutyrate dehydrogenase, also called gamma-hydroxybutyrate dehydrogenase, catalyzes ... |
65-286 |
9.95e-16 |
|
4-hydroxybutyrate dehydrogenase, also called gamma-hydroxybutyrate dehydrogenase, catalyzes the reduction of succinic simialdehyde to 4-hydroxybutyrate in the succinic degradation pathway; 4-hydroxybutyrate dehydrogenase (4HBD) is an iron-containing (type III) NAD-dependent alcohol dehydrogenase. It plays a role in the succinate metabolism biochemical pathway. It catalyzes the reduction of succinic simialdehide to 4-hydroxybutyrate in the succinate degradation pathway This succinate degradation pathway is present in some bacteria which can use succinate as sole carbon source.
Pssm-ID: 341482 Cd Length: 371 Bit Score: 77.26 E-value: 9.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 65 DKIIQHVP-QTLVEEGLKVTNKLQPKVMLSIGGGSAVGLAKALALKNHLPI----------------IAVPTTF-AGSEQ 126
Cdd:cd14860 55 EKYGTGEPsDEMVEAIYKDIKKYGYKRVIAIGGGTVIDIAKLLALKGISPVldlfdgkiplikekelIIVPTTCgTGSEV 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 127 TNI--WGISNEEGKTTGRDDVVLPQVVVYDPELTQTMPQRLAVMSAMNAMAHLMEAVYSPTGNPITRNQALLGMQQLKKG 204
Cdd:cd14860 135 TNIsiVELTSLGTKKGLAVDELYADKAVLIPELLKGLPYKVFATSSIDALIHAIESYLSPKATPYTEMFSYKAIEMILEG 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 205 LENIAQQ-KAFTTEANEQILLGAYLAGRALCEVTMALHHKAAHVLGGSFGMQHAEVHTVLQTYVL-AYQwphlstEIQQD 282
Cdd:cd14860 215 YQEIAEKgEEARFPLLGDFLIASNYAGIAFGNAGCAAVHALSYPLGGKYHVPHGEANYAVFTGVLkNYQ------EKNPD 288
|
....
gi 1111735350 283 FKLT 286
Cdd:cd14860 289 GEIK 292
|
|
| PRK15454 |
PRK15454 |
ethanolamine utilization ethanol dehydrogenase EutG; |
91-270 |
1.08e-15 |
|
ethanolamine utilization ethanol dehydrogenase EutG;
Pssm-ID: 185351 [Multi-domain] Cd Length: 395 Bit Score: 77.38 E-value: 1.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 91 MLSIGGGSAVGLAKALAL------------------KNHLPIIAVPTTFA-GSEQTNIWGISNeegKTTGRDDV-----V 146
Cdd:PRK15454 110 VIAFGGGSVLDAAKAVALlvtnpdstlaemsetsvlQPRLPLIAIPTTAGtGSETTNVTVIID---AVSGRKQVlahasL 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 147 LPQVVVYDPELTQTMPQRLAVMSAMNAMAHLMEAVYSPTGNPITRNQALLGMQQLKKGLENiAQQKAFTTEANEQILLGA 226
Cdd:PRK15454 187 MPDVAILDAALTEGVPSHVTAMTGIDALTHAIEAYSALNATPFTDSLAIGAIAMIGKSLPK-AVGYGHDLAARESMLLAS 265
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1111735350 227 YLAGRALCEVTMALHHKAAHVLGGSFGMQHAEVHTVLQTYVLAY 270
Cdd:PRK15454 266 CMAGMAFSSAGLGLCHAMAHQPGAALHIPHGLANAMLLPTVMEF 309
|
|
| Fe-ADH_KdnB-like |
cd08184 |
Iron-containing alcohol dehydrogenase similar to Shewanella oneidensis KdnB required for Kdo8N ... |
11-256 |
4.99e-11 |
|
Iron-containing alcohol dehydrogenase similar to Shewanella oneidensis KdnB required for Kdo8N biosynthesis; This family contains iron-containing alcohol dehydrogenase-like proteins, many of which have not been characterized. Their specific function is unknown. The protein structure represents a dehydroquinate synthase-like fold and belongs to the iron-containing alcohol dehydrogenase-like superfamily. It is distinct from other alcohol dehydrogenases which contain different protein domains. Alcohol dehydrogenase catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron or zinc ions. This family also includes Shewanella oneidensis KdnB which is required for biosynthesis of 8-Amino-3,8-dideoxy-D-manno-octulosonic acid (Kdo8N), a unique amino sugar that has thus far only been observed on the lipopolysaccharides of marine bacteria belonging to the genus Shewanella, and thought to be important for the integrity of the bacterial cell outer membrane. KdnB requires NAD(P) and zinc ion for activity.
Pssm-ID: 341463 [Multi-domain] Cd Length: 348 Bit Score: 63.06 E-value: 4.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 11 QVYFGAGQIQKLPSILKNYLHNPTDKVLVLAEarvqaHVERLETSLGKEVVHHFDKII----QHVPQT-----LVEEgLK 81
Cdd:cd08184 3 KYLFGRGSFDQLGELLAERRKSNNDYVVFFID-----DVFKGKPLLDRLPLQNGDLLIfvdtTDEPKTdqidaLRAQ-IR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 82 VTNKLQPKVMLSIGGGSAVGLAKALAL-----------------KNH-LPIIAVPT-TFAGSEQTNIWGISNEEGKTTGR 142
Cdd:cd08184 77 AENDKLPAAVVGIGGGSTMDIAKAVSNmltnpgsaadyqgwdlvKNPgIYKIGVPTlSGTGAEASRTAVLTGPEKKLGIN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 143 DDVVLPQVVVYDPELTQTMPQRLAVMSAMNAMAHLMEAVYSPTGNPITRNQAllgmqqlKKGLENIAQ----QKAFTTEA 218
Cdd:cd08184 157 SDYTVFDQVILDPELIATVPRDQYFYTGMDCYIHCVESLNGTYRNAFGDAYA-------EKALELCRDvflsDDMMSPEN 229
|
250 260 270
....*....|....*....|....*....|....*...
gi 1111735350 219 NEQILLGAYLAGRALCEVTMALHHKAAHVLGGSFGMQH 256
Cdd:cd08184 230 REKLMVASYLGGSSIANSQVGVCHALSYGLSVVLGTHH 267
|
|
| G1PDH_related |
cd08549 |
Glycerol-1-phosphate dehydrogenase and related proteins; This family contains bacterial and ... |
9-323 |
6.11e-11 |
|
Glycerol-1-phosphate dehydrogenase and related proteins; This family contains bacterial and archeal glycerol-1-phosphate dehydrogenase-like oxidoreductases. These proteins have similarity with glycerol-1-phosphate dehydrogenase (G1PDH) which plays a role in the synthesis of phosphoglycerolipids in gram-positive bacterial species. It catalyzes the reversibly reduction of dihydroxyacetone phosphate (DHAP) to glycerol-1-phosphate (G1P) in a NADH-dependent manner. Its activity requires Ni++ ion. It also contains archaeal Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) that plays an important role in the formation of the enantiomeric configuration of the glycerophosphate backbone (sn-glycerol-1-phosphate) of archaeal ether lipids.
Pssm-ID: 341479 [Multi-domain] Cd Length: 331 Bit Score: 62.58 E-value: 6.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 9 PNQVYFGAGQIQKLPSILKnylHNPTDKVLVLAEARVQAHVERLETSLGKEVvhhfdKIIQHVPQTLVEEGLKVTNKLQp 88
Cdd:cd08549 1 PRYTIVGDGAINKIEEILK---KLNLKRVLIITGKNTKAKYCRFFYDQLKTV-----CDIVYYDNIDNLEDELKKYTFY- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 89 KVMLSIGGGSAVGLAKALALKNHLPIIAVPTTfagseqTNIWGISN------EEGKTTGRdDVVLPQVVVYDPELTQTMP 162
Cdd:cd08549 72 DCVIGIGGGRSIDTGKYLAYKLKIPFISVPTS------ASNDGIASpivslrIPGVKKTF-MADAPIAIIADTEIIKKSP 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 163 QRLaVMSAMNAMAHLMEAVYS------PTGNPITRNQALLGMQQLKKGLENIaqQKAFTTEANEQILLGAYLAgralCEV 236
Cdd:cd08549 145 RRL-LSAGIGDLVSNITAVLDwklahkEKGEKYSEFAAILSKTSAKELVSYV--LKASDLEEYHRVLVKALVG----SGI 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 237 TMALHHKAAHVLGGSFGMQHA---EVHTVLQTYVLAYQWPHLSTEI-----QQDFKLTLGNnpPLALKMLAENAGAPTTL 308
Cdd:cd08549 218 AMAIAGSSRPASGSEHLFSHAldkLKEEYLNINVLHGEQVGVGTIImsylhEKENKKLSGL--HERIKMILKKVGAPTTA 295
|
330
....*....|....*
gi 1111735350 309 EEIGFDQADIGKAVR 323
Cdd:cd08549 296 KQLGIDEDLIIEALT 310
|
|
| GldA |
COG0371 |
Glycerol dehydrogenase or related enzyme, iron-containing ADH family [Energy production and ... |
8-324 |
1.14e-10 |
|
Glycerol dehydrogenase or related enzyme, iron-containing ADH family [Energy production and conversion]; Glycerol dehydrogenase or related enzyme, iron-containing ADH family is part of the Pathway/BioSystem: Isoprenoid biosynthesis
Pssm-ID: 440140 [Multi-domain] Cd Length: 355 Bit Score: 62.11 E-value: 1.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 8 FPNQVYFGAGQIQKLPSILKNYlhnpTDKVLVLAEARVQAHV-ERLETSLGKE----VVHHFDKiiqHVPQTLVEEGLKV 82
Cdd:COG0371 5 LPRRYVQGEGALDELGEYLADL----GKRALIITGPTALKAAgDRLEESLEDAgievEVEVFGG---ECSEEEIERLAEE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 83 TNKLQPKVMLSIGGGSAVGLAKALALKNHLPIIAVPTTFA----GSEQTNIWgisNEEGKTtgRDDVVLPQ---VVVYDP 155
Cdd:COG0371 78 AKEQGADVIIGVGGGKALDTAKAVAYRLGLPVVSVPTIAStdapASPLSVIY---TEDGAF--DGYSFLAKnpdLVLVDT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 156 ELTQTMPQRL-------------AVMSAMNAMAHLMEAVYSPTGnpitRNQALLGMQQL-KKGLENI-AQQKAFTTEANE 220
Cdd:COG0371 153 DIIAKAPVRLlaagigdalakwyEARDWSLAHRDLAGEYYTEAA----VALARLCAETLlEYGEAAIkAVEAGVVTPALE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 221 QILLGA-YLAGralceVTMALHHK-----AAH-------VLGGSFGMQHAE---VHTVLQTYVlaYQWPhlsTEIQQdfk 284
Cdd:COG0371 229 RVVEANlLLSG-----LAMGIGSSrpgsgAAHaihngltALPETHHALHGEkvaFGTLVQLVL--EGRP---EEIEE--- 295
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1111735350 285 ltlgnnpplaLKMLAENAGAPTTLEEIGFDQADIGKAVRI 324
Cdd:COG0371 296 ----------LLDFLRSVGLPTTLADLGLDDETEEELLTV 325
|
|
| Fe-ADH-like |
cd08186 |
Iron-containing alcohol dehydrogenase; This family contains iron-containing alcohol ... |
12-329 |
8.10e-10 |
|
Iron-containing alcohol dehydrogenase; This family contains iron-containing alcohol dehydrogenase (ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. The ADH of hyperthermophilic archaeon Thermococcus hydrothermalis oxidizes a series of primary aliphatic and aromatic alcohols, preferentially from C2 to C8, but is also active towards methanol and glycerol, and is stereospecific for monoterpenes. It has been suggested that the type III ADHs in microorganisms are involved in acetaldehyde detoxication rather than in alcohol turnover.
Pssm-ID: 341465 [Multi-domain] Cd Length: 380 Bit Score: 59.59 E-value: 8.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 12 VYFGAGQIQKLPSILKNYlhnPTDKVLVLA---EARVQ---AHVERLETSLGKEVVHhFDKIIQHVPQTLVEEGLKVTNK 85
Cdd:cd08186 4 LYFGVGAIAKIKDILKDL---GIDKVIIVTgrsSYKKSgawDDVEKALEENGIEYVV-YDKVTPNPTVDQADEAAKLARD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 86 LQPKVMLSIGGGSAVGLAKALAL-------------------KNHLPIIAVPTTFA-GSEqTNIWGISNEEGKTTGRD-- 143
Cdd:cd08186 80 FGADAVIAIGGGSPIDTAKSVAVllayggktardlygfrfapERALPLVAINLTHGtGSE-VDRFAVATIPEKGYKPGia 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 144 -DVVLPQVVVYDPELTQTMPQRLAVMSAMNAMAHLMEAVYSPTGNPITRNQALLGMQQLKKGL-ENIAQQKAFttEANEQ 221
Cdd:cd08186 159 yDCIYPLYAIDDPRLTLTLPKEQTLYTSIDAFNHVYEAATTKVSSPYVITLAKEAIRLIAEYLpRALANPKDL--EARYW 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 222 ILLGAYLAGRA----LCEVTMALHH-------KAAHVLGgsFGMqhaevhtvLQTYVLAYQWPHLSTEIQQDFKLTLGNN 290
Cdd:cd08186 237 LLYASMIAGIAidngLLHLTHALEHplsglkpELPHGLG--LAL--------LGPAVVKYIYKAVPETLADILRPIVPGL 306
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1111735350 291 PPLA---------LKMLAENAGAPTTLEEIGFDQADIGKAVRIMLANP 329
Cdd:cd08186 307 KGTPdeaekaargVEEFLFSVGFTEKLSDYGFTEDDVDRLVELAFTTP 354
|
|
| Gro1PDH |
cd08173 |
Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) catalyzes the reversible conversion between ... |
8-120 |
1.13e-09 |
|
Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) catalyzes the reversible conversion between dihydroxyacetone phosphate and glycerol-1-phosphate using either NADH or NADPH as a coenzyme; Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH, EC 1.1.1.261) plays an important role in the formation of the enantiomeric configuration of the glycerophosphate backbone (sn-glycerol-1-phosphate) of archaeal ether lipids. It catalyzes the reversible conversion between dihydroxyacetone phosphate and glycerol-1-phosphate using either NADH or NADPH as a coenzyme. The activity is zinc-dependent. One characteristic feature of archaea is that their cellular membrane has an ether linkage between the glycerol backbone and the hydrocarbon residues. The polar lipids of the members of Archaea consist of di- and tetra-ethers of glycerol with isoprenoid alcohols bound at the sn-2 and sn-3 positions of the glycerol moiety. The archaeal polar lipids have the enantiomeric configuration of a glycerophosphate backbone [sn-glycerol-1-phosphate (G-1-P)] that is the mirror image structure of the bacterial or eukaryal counterpart [sn-glycerol- 3-phosphate (G-3-P)]. The absolute stereochemistry of the glycerol moiety in all archaeal polar lipids is opposite to that of glycerol ester lipids in bacteria and eukarya.
Pssm-ID: 341452 Cd Length: 343 Bit Score: 59.10 E-value: 1.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 8 FPNQVYFGAGQIQKLPSILKNyLHNPTDKVLVLAEARVQAHVERLETSLGKEVVHHFD-KIIQHVPQTLVEEGLKVTNKL 86
Cdd:cd08173 1 LPRNVVVGHGAINKIGEVLKK-LLLGKRALIITGPNTYKIAGKRVEDLLESSGVEVVIvDIATIEEAAEVEKVKKLIKES 79
|
90 100 110
....*....|....*....|....*....|....
gi 1111735350 87 QPKVMLSIGGGSAVGLAKALALKNHLPIIAVPTT 120
Cdd:cd08173 80 KADFIIGVGGGKVIDVAKYAAYKLNLPFISIPTS 113
|
|
| GlyDH |
cd08170 |
Glycerol dehydrogenases (GlyDH) catalyzes oxidation of glycerol to dihydroxyacetone in ... |
15-120 |
5.56e-07 |
|
Glycerol dehydrogenases (GlyDH) catalyzes oxidation of glycerol to dihydroxyacetone in glycerol dissmilation; Glycerol dehydrogenases (GlyDH) is a key enzyme in the glycerol dissimilation pathway. In anaerobic conditions, many microorganisms utilize glycerol as a source of carbon through coupled oxidative and reductive pathways. One of the pathways involves the oxidation of glycerol to dihydroxyacetone with the reduction of NAD+ to NADH catalyzed by glycerol dehydrogenases. Dihydroxyacetone is then phosphorylated by dihydroxyacetone kinase and enters the glycolytic pathway for further degradation. The activity of GlyDH is zinc-dependent; the zinc ion plays a role in stabilizing an alkoxide intermediate at the active site.
Pssm-ID: 341449 [Multi-domain] Cd Length: 351 Bit Score: 50.87 E-value: 5.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 15 GAGQIQKLPSILKNYlhnpTDKVLVLAEARVQAHV-ERLETSLGKE-VVHHFDKIIQHVPQTLVEEGLKVTNKLQPKVML 92
Cdd:cd08170 7 GPGALDRLGEYLAPL----GKKALVIADPFVLDLVgERLEESLEKAgLEVVFEVFGGECSREEIERLAAIARANGADVVI 82
|
90 100
....*....|....*....|....*...
gi 1111735350 93 SIGGGSAVGLAKALALKNHLPIIAVPTT 120
Cdd:cd08170 83 GIGGGKTIDTAKAVADYLGLPVVIVPTI 110
|
|
| GlyDH-like |
cd08550 |
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins. ... |
9-230 |
9.79e-07 |
|
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins. Glycerol dehydrogenases (GlyDH) is a key enzyme in the glycerol dissimilation pathway. In anaerobic conditions, many microorganisms utilize glycerol as a source of carbon through coupled oxidative and reductive pathways. One of the pathways involves the oxidation of glycerol to dihydroxyacetone with the reduction of NAD+ to NADH catalyzed by glycerol dehydrogenases. Dihydroxyacetone is then phosphorylated by dihydroxyacetone kinase and enters the glycolytic pathway for further degradation. The activity of GlyDH is zinc-dependent; the zinc ion plays a role in stabilizing an alkoxide intermediate at the active site. Some subfamilies have yet to be characterized.
Pssm-ID: 341480 [Multi-domain] Cd Length: 347 Bit Score: 49.84 E-value: 9.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 9 PNQVYFGAGQIQKLPSILKNYLHnptdKVLVLAEARV-QAHVERLETSLGKE----VVHHF-----DKIIQHVPQTLVEE 78
Cdd:cd08550 1 PGRYIQEPGILAKAGEYIAPLGK----KALIIGGKTAlEAVGEKLEKSLEEAgidyEVEVFggectEENIERLAEKAKEE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 79 GlkvtnklqPKVMLSIGGGSAVGLAKALALKNHLPIIAVPT---TFAG-SEQTNIWgisNEEGKTtgRDDVVL---PQVV 151
Cdd:cd08550 77 G--------ADVIIGIGGGKVLDTAKAVADRLGLPVVTVPTiaaTCAAwSALSVLY---DEEGEF--LGYSLLkrsPDLV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 152 VYDPELTQTMPQRLAVMSAMNAMAHLMEAVYSPTGNP------ITRNQALLGMQQLK----KGLENIAQQKAftTEANEQ 221
Cdd:cd08550 144 LVDTDIIAAAPVRYLAAGIGDTLAKWYEARPSSRGGPddlalqAAVQLAKLAYDLLLeygvQAVEDVRQGKV--TPALED 221
|
250
....*....|
gi 1111735350 222 ILLGA-YLAG 230
Cdd:cd08550 222 VVDAIiLLAG 231
|
|
| Fe-ADH_2 |
pfam13685 |
Iron-containing alcohol dehydrogenase; |
13-120 |
1.18e-05 |
|
Iron-containing alcohol dehydrogenase;
Pssm-ID: 404557 [Multi-domain] Cd Length: 251 Bit Score: 46.14 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 13 YFGAGQIQKLPSILknyLHNPTDKVLVLAEARVQAHV-ERLETSL-GKEV-VHHFDKIIQHVPQTLVEEGLKVTNKLQPK 89
Cdd:pfam13685 1 VIGPGALGRLGEYL---AELGFRRVALVADANTYAAAgRKVAESLkRAGIeVETRLEVAGNADMETAEKLVGALRERDAD 77
|
90 100 110
....*....|....*....|....*....|.
gi 1111735350 90 VMLSIGGGSAVGLAKALALKNHLPIIAVPTT 120
Cdd:pfam13685 78 AVVGVGGGTVIDLAKYAAFKLGKPFISVPTA 108
|
|
| egsA |
PRK00843 |
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed |
8-120 |
3.53e-05 |
|
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed
Pssm-ID: 179139 Cd Length: 350 Bit Score: 45.27 E-value: 3.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 8 FPNQVYFGAGQIQKLPSILKNyLHnPTDKVLV--------LAEARVQAHverLETSLGKEVVhhfdkIIQHVPQTLVEEG 79
Cdd:PRK00843 10 LPRDVVVGHGVLDDIGDVCSD-LK-LTGRALIvtgpttkkIAGDRVEEN---LEDAGDVEVV-----IVDEATMEEVEKV 79
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1111735350 80 LKVTNKLQPKVMLSIGGGSAVGLAKALALKNHLPIIAVPTT 120
Cdd:PRK00843 80 EEKAKDVNAGFLIGVGGGKVIDVAKLAAYRLGIPFISVPTA 120
|
|
| G1PDH-like |
cd08174 |
Glycerol-1-phosphate dehydrogenase-like; These glycerol-1-phosphate dehydrogenase-like ... |
9-120 |
1.11e-04 |
|
Glycerol-1-phosphate dehydrogenase-like; These glycerol-1-phosphate dehydrogenase-like proteins have not been characterized. The protein sequences have high similarity with that of glycerol-1-phosphate dehydrogenase (G1PDH) which plays a role in the synthesis of phosphoglycerolipids in Gram-positive bacterial species. It catalyzes the reversibly reduction of dihydroxyacetone phosphate (DHAP) to glycerol-1-phosphate (G1P) in a NADH-dependent manner. Its activity requires Ni++ ion.
Pssm-ID: 341453 [Multi-domain] Cd Length: 332 Bit Score: 43.66 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 9 PNQVYFGAGQIQKLPSILKnYLHNPTDKVLVLAEARVQAHV-ERLETSL-GKEVVHHFDkiiQHVPQTLVEEGLKVTNKL 86
Cdd:cd08174 1 PLILKIEEGALEHLGKYLA-DRNQGFGKVAIVTGEGIDELLgEDILESLeEAGEIVTVE---ENTDNSAEELAEKAFSLP 76
|
90 100 110
....*....|....*....|....*....|....
gi 1111735350 87 QPKVMLSIGGGSAVGLAKALALKNHLPIIAVPTT 120
Cdd:cd08174 77 KVDAIVGIGGGKVLDVAKYAAFLSKLPFISVPTS 110
|
|
| gldA |
PRK09423 |
glycerol dehydrogenase; Provisional |
15-119 |
1.41e-03 |
|
glycerol dehydrogenase; Provisional
Pssm-ID: 181843 Cd Length: 366 Bit Score: 40.18 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111735350 15 GAGQIQKLPSILKNYlhnpTDKVLVLAEARVQAHV-ERLETSLGKEVVH-HFDKIIQHVPQTLVEEGLKVTNKLQPKVML 92
Cdd:PRK09423 14 GKGALARLGEYLKPL----GKRALVIADEFVLGIVgDRVEASLKEAGLTvVFEVFNGECSDNEIDRLVAIAEENGCDVVI 89
|
90 100
....*....|....*....|....*..
gi 1111735350 93 SIGGGSAVGLAKALALKNHLPIIAVPT 119
Cdd:PRK09423 90 GIGGGKTLDTAKAVADYLGVPVVIVPT 116
|
|
| |
