|
Name |
Accession |
Description |
Interval |
E-value |
| Fe-ADH-like |
cd08183 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
8-378 |
2.80e-147 |
|
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: 423.45 E-value: 2.80e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 8 TKIIFGDGALSASLSLFNQYGYSVLLVTGNTLERTSV---VTDYLDAQSMRYQHIAVSGEPNIKMVEEAAISARRFKPDM 84
Cdd:cd08183 2 PRIVFGRGSLQELGELAAELGKRALLVTGRSSLRSGRlarLLEALEAAGIEVALFSVSGEPTVETVDAAVALAREAGCDV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 85 VVAMGGGSAIDMGKALAAVLPNQGNLYDYVEVVGRNVPLKTKPLPFIAIPTTASTGAEVTKNAVLKSGQDQVKVSLRSPD 164
Cdd:cd08183 82 VIAIGGGSVIDAAKAIAALLTNEGSVLDYLEVVGKGRPLTEPPLPFIAIPTTAGTGSEVTKNAVLSSPEHGVKVSLRSPS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 165 MLADVAIVDPTLTHGTNLYLSGRGAMDAFTHLMEAYVCGEPNPLTDMICEEGLRKLSSSVVRAC-VYDEPQARSDLAFAS 243
Cdd:cd08183 162 MLPDVALVDPELTLSLPPEVTAASGLDALTQLIEPYVSRKANPLTDALAREGLRLAARSLRRAYeDGEDLEAREDMALAS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 244 MLGGMAITNAKLGAAHGLASALGGKISAPHSVITARLAPFVMLENIAVAREEK-RLDILARYQRIAQIVIGNSEAKEEEA 322
Cdd:cd08183 242 LLGGLALANAGLGAVHGLAGPLGGMFGAPHGAICAALLPPVLEANLRALREREpDSPALARYRELAGILTGDPDAAAEDG 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1515916685 323 ISWLSEVLDTLKLPNLQEFGVCEAQFDEVSADALKSVAIKGNPLPLNQERLVHILK 378
Cdd:cd08183 322 VEWLEELCEELGIPRLSEYGLTEEDFPEIVEKARGSSSMKGNPIELSDEELLEILE 377
|
|
| EutG |
COG1454 |
Alcohol dehydrogenase, class IV [Energy production and conversion]; |
1-380 |
6.09e-115 |
|
Alcohol dehydrogenase, class IV [Energy production and conversion];
Pssm-ID: 441063 [Multi-domain] Cd Length: 381 Bit Score: 341.33 E-value: 6.09e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 1 MFQFMTSTKIIFGDGALSASLSLFNQYGYS-VLLVTGNTLERTSV---VTDYLDAQSMRYQHIA-VSGEPNIKMVEEAAI 75
Cdd:COG1454 2 MFTFRLPTRIVFGAGALAELGEELKRLGAKrALIVTDPGLAKLGLldrVLDALEAAGIEVVVFDdVEPNPTVETVEAGAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 76 SARRFKPDMVVAMGGGSAIDMGKALAAVLPNQGNLYDYVEVVgrnvPLKTKPLPFIAIPTTASTGAEVTKNAVLKSGQDQ 155
Cdd:COG1454 82 AAREFGADVVIALGGGSAIDAAKAIALLATNPGDLEDYLGIK----KVPGPPLPLIAIPTTAGTGSEVTPFAVITDPETG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 156 VKVSLRSPDMLADVAIVDPTLTHGTNLYLSGRGAMDAFTHLMEAYVCGEPNPLTDMICEEGLRKLSSSVVRACVY-DEPQ 234
Cdd:COG1454 158 VKKGIADPELLPDVAILDPELTLTLPPSLTAATGMDALTHAIEAYVSKGANPLTDALALEAIRLIARNLPRAVADgDDLE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 235 ARSDLAFASMLGGMAITNAKLGAAHGLASALGGKISAPHSVITARLAPFVMLENIAVAREekrldilaRYQRIAQI---- 310
Cdd:COG1454 238 AREKMALASLLAGMAFANAGLGAVHALAHPLGGLFHVPHGLANAILLPHVLRFNAPAAPE--------RYAEIARAlgld 309
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1515916685 311 VIGNSEAKEEEAISWLSEVLDTLKLP-NLQEFGVCEAQFDEVSADALKSVAIKGNPLPLNQERLVHILKQV 380
Cdd:COG1454 310 VGLSDEEAAEALIEAIRELLRDLGIPtRLSELGVTEEDLPELAELALADRCLANNPRPLTEEDIEAILRAA 380
|
|
| Fe-ADH |
pfam00465 |
Iron-containing alcohol dehydrogenase; |
8-373 |
8.78e-104 |
|
Iron-containing alcohol dehydrogenase;
Pssm-ID: 425696 [Multi-domain] Cd Length: 362 Bit Score: 312.23 E-value: 8.78e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 8 TKIIFGDGALSASLSLFNQYGYSVLLVTGNTLERTSV---VTDYLDAQSMRYQHIA-VSGEPNIKMVEEAAISARRFKPD 83
Cdd:pfam00465 2 TRIVFGAGALAELGEELKRLGARALIVTDPGSLKSGLldkVLASLEEAGIEVVVFDgVEPEPTLEEVDEAAALAREAGAD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 84 MVVAMGGGSAIDMGKALAAVLPNQGNLYDYVEVVgrnvPLKTKPLPFIAIPTTASTGAEVTKNAVLKSGQDQVKVSLRSP 163
Cdd:pfam00465 82 VIIAVGGGSVIDTAKAIALLLTNPGDVWDYLGGK----PLTKPALPLIAIPTTAGTGSEVTPLAVITDTETGEKLGIFSP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 164 DMLADVAIVDPTLTHGTNLYLSGRGAMDAFTHLMEAYVCGEPNPLTDMICEEGLRKLSSSVVRAcvYDEP---QARSDLA 240
Cdd:pfam00465 158 KLLPDLAILDPELTLTLPPRLTAATGMDALAHAVEAYVSKGANPLTDALALEAIRLIAENLPRA--VADGedlEARENML 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 241 FASMLGGMAITNAKLGAAHGLASALGGKISAPHSVITARLAPFVMLENIAVAREekrldilaRYQRIAQIVIGNS-EAKE 319
Cdd:pfam00465 236 LASTLAGLAFSNAGLGAAHALAHALGGRYGIPHGLANAILLPYVLRFNAPAAPE--------KLAQLARALGEDSdEEAA 307
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1515916685 320 EEAISWLSEVLDTLKLP-NLQEFGVCEAQFDEVSADALKSVAIKGNPLPLNQERL 373
Cdd:pfam00465 308 EEAIEALRELLRELGLPtTLSELGVTEEDLDALAEAALRDRSLANNPRPLTAEDI 362
|
|
| Fe-ADH |
cd08551 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains large ... |
8-377 |
6.42e-96 |
|
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: 292.43 E-value: 6.42e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 8 TKIIFGDGALSASLSLFNQYGYS-VLLVTGNTLERTSV---VTDYLDAQSMRYQHIA-VSGEPNIKMVEEAAISARRFKP 82
Cdd:cd08551 2 TRIVFGAGALARLGEELKALGGKkVLLVTDPGLVKAGLldkVLESLKAAGIEVEVFDdVEPNPTVETVEAAAELAREEGA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 83 DMVVAMGGGSAIDMGKALAAVLPNQGNLYDYVEVVgrnvPLKTKPLPFIAIPTTASTGAEVTKNAVLKSGQDQVKVSLRS 162
Cdd:cd08551 82 DLVIAVGGGSVLDTAKAIAVLATNGGSIRDYEGIG----KVPKPGLPLIAIPTTAGTGSEVTPNAVITDPETGRKMGIVS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 163 PDMLADVAIVDPTLTHG--------TnlylsgrgAMDAFTHLMEAYVCGEPNPLTDMICEEGLRKLSSSVVRAcvYDEP- 233
Cdd:cd08551 158 PYLLPDVAILDPELTLSlppsvtaaT--------GMDALTHAIEAYTSKKANPISDALALEAIRLIGKNLRRA--VADGs 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 234 --QARSDLAFASMLGGMAITNAKLGAAHGLASALGGKISAPHSVITARLAPFVMLENIAVAREekrldilaRYQRIAQIV 311
Cdd:cd08551 228 dlEAREAMLLASLLAGIAFGNAGLGAVHALAYPLGGRYHIPHGVANAILLPYVMEFNLPACPE--------KYAEIAEAL 299
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1515916685 312 IGNSEAKEEE-----AISWLSEVLDTLKLP-NLQEFGVCEAQFDEVSADALKSVAIKGN-PLPLNQERLVHIL 377
Cdd:cd08551 300 GEDVEGLSDEeaaeaAVEAVRELLRDLGIPtSLSELGVTEEDIPELAEDAMKSGRLLSNnPRPLTEEDIREIY 372
|
|
| Fe-ADH-like |
cd08191 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
10-378 |
1.35e-78 |
|
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: 248.68 E-value: 1.35e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 10 IIFGDGALSASLSLFNQYGYSVLLVTGNTLERTSVVTDYLdaQSMRYQHIAVS----GEPNI--KMVEEAAISARRFKPD 83
Cdd:cd08191 7 LLFGPGARRALGRVAARLGSRVLIVTDPRLASTPLVAELL--AALTAAGVAVEvfdgGQPELpvSTVADAAAAARAFDPD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 84 MVVAMGGGSAIDMGKALAAVLPNQGNLYDYVevvGRN-VPlkTKPLPFIAIPTTASTGAEVTKNAVLKSGQDQVKVSLRS 162
Cdd:cd08191 85 VVIGLGGGSNMDLAKVVALLLAHGGDPRDYY---GEDrVP--GPVLPLIAVPTTAGTGSEVTPVAVLTDPARGMKVGVSS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 163 PDMLADVAIVDPTLTHGTNLYLSGRGAMDAFTHLMEAYVC----------GEP-----NPLTDMICEEGLRKLSSSVVRA 227
Cdd:cd08191 160 PYLRPAVAIVDPELTLTCPPGVTADSGIDALTHAIESYTArdfppfprldPDPvyvgkNPLTDLLALEAIRLIGRHLPRA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 228 cvYDEP---QARSDLAFASMLGGMAITNAKLGAAHGLASALGGKISAPHSVITARLAPFVMLENiavareekRLDILARY 304
Cdd:cd08191 240 --VRDGddlEARSGMALAALLAGLAFGTAGTAAAHALQYPIGALTHTSHGVGNGLLLPYVMRFN--------RPARAAEL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 305 QRIAQI----VIGNSEAKEEEAISWLSEVLDTLKLP-NLQEFGVCEAQFDEVSADALKSVA-IKGNPLPLNQERLVHILK 378
Cdd:cd08191 310 AEIARAlgvtTAGTSEEAADRAIERVEELLARIGIPtTLADLGVTEADLPGLAEKALSVTRlIANNPRPPTEEDLLRILR 389
|
|
| Fe-ADH-like |
cd14863 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
3-381 |
1.84e-76 |
|
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: 242.83 E-value: 1.84e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 3 QFMTSTKIIFGDGALSASLSLFNQYGYS-VLLVTGNTLERTSV---VTDYLDAQSMRY-QHIAVSGEPNIKMVEEAAISA 77
Cdd:cd14863 1 TYSQLTPVIFGAGAVEQIGELLKELGCKkVLLVTDKGLKKAGIvdkIIDLLEEAGIEVvVFDDVEPDPPDEIVDEAAEIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 78 RRFKPDMVVAMGGGSAIDMGKALAAVLPNQGNLYDYVevvGRNVPLKTKPLPFIAIPTTASTGAEVTKNAVLKSGQDQVK 157
Cdd:cd14863 81 REEGADGVIGIGGGSVLDTAKAIAVLLTNPGPIIDYA---LAGPPVPKPGIPLIAIPTTAGTGSEVTPIAVITDEENGVK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 158 VSLRSPDMLADVAIVDPTLTHGTNLYLSGRGAMDAFTHLMEAYVCGEPNPLTDMICEEGLRKLSSSVVRAcvYDEPQ--- 234
Cdd:cd14863 158 KSLLGPFLVPDLAILDPELTVGLPPSLTAATGMDALSHAIEAYTSKLANPMTDALALQAIRLIVKNLPRA--VKDGDnle 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 235 ARSDLAFASMLGGMAITNAKLGAAHGLASALGGKISAPHSVITARLAPFVMLENIAVAREekrldilaRYQRIAQIVIGN 314
Cdd:cd14863 236 ARENMLLASNLAGIAFNNAGTHIGHAIAHALGALYHIPHGLACALALPVVLEFNAEAYPE--------KVKKIAKALGVS 307
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1515916685 315 SEAKEEEAIS-----WLSEVLDTLKLP-NLQEFGVCEAQFDEVSADALKSVAIKGNPLPLNQERLVHILKQVC 381
Cdd:cd14863 308 FPGESDEELGeavadAIREFMKELGIPsLFEDYGIDKEDLDKIAEAVLKDPFAMFNPRPITEEEVAEILEAIY 380
|
|
| Fe-ADH-like |
cd08185 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
8-378 |
8.43e-76 |
|
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: 240.86 E-value: 8.43e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 8 TKIIFGDGALSASLSLFNQYGYSVLLVTGNT-------LERtsvVTDYLDAQSMRYQHIA-VSGEPNIKMVEEAAISARR 79
Cdd:cd08185 5 TRILFGAGKLNELGEEALRPGKKALIVTGKGsskktglLDR---VKKLLEKAGVEVVVFDkVEPNPLTTTVMEGAALAKE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 80 FKPDMVVAMGGGSAIDMGKALAAVLPNQGNLYDYVEVVGRNVPLKTKPLPFIAIPTTASTGAEVTKNAVLKSGQDQVKVS 159
Cdd:cd08185 82 EGCDFVIGLGGGSSMDAAKAIAFMATNPGDIWDYIFGGTGKGPPPEKALPIIAIPTTAGTGSEVDPWAVITNPETKEKKG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 160 LRSPDMLADVAIVDPTLT-----HGTnlylSGRGaMDAFTHLMEAYVCGEPNPLTDMICEEGLRKLSSSVVRAcvYDEPQ 234
Cdd:cd08185 162 IGHPALFPKVSIVDPELMltvppRVT----AYTG-FDALFHAFESYISKNANPFSDMLALEAIRLVAKYLPRA--VKDGS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 235 ---ARSDLAFASMLGGMAITNAKLGAAHGLASALGG-KISAPHSVITARLAPFVMLENIAVAREekrldilaRYQRIAQI 310
Cdd:cd08185 235 dleAREKMAWASTLAGIVIANSGTTLPHGLEHPLSGyHPNIPHGAGLAALYPAYFEFTIEKAPE--------KFAFVARA 306
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1515916685 311 -VIGNSEAKEEEA-ISWLSEVLDTLKLPN-LQEFGVCEAQFDEVSADALKSVA--IKGNPLPLNQERLVHILK 378
Cdd:cd08185 307 eASGLSDAKAAEDfIEALRKLLKDIGLDDlLSDLGVTEEDIPWLAENAMETMGglFANNPVELTEEDIVEIYE 379
|
|
| Fe-ADH-like |
cd14865 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
2-380 |
1.31e-69 |
|
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: 225.11 E-value: 1.31e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 2 FQFMTSTKIIFGDGALSASLSLFNQYGYS-VLLVTGNTLERTSVVTDYLDAQSMRYQHIAVSGE--PN--IKMVEEAAIS 76
Cdd:cd14865 1 FEFFNPTKIVSGAGALENLPAELARLGARrPLIVTDKGLAAAGLLKKVEDALGDAIEIVGVFDDvpPDssVAVVNEAAAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 77 ARRFKPDMVVAMGGGSAIDMGKALAAVLPNQGNLYDYVEVVGRnvpLKTKPLPFIAIPTTASTGAEVTKNAVLKSGQDQV 156
Cdd:cd14865 81 AREAGADGIIAVGGGSVIDTAKGVNILLSEGGDDLDDYGGANR---LTRPLKPLIAIPTTAGTGSEVTLVAVIKDEEKKV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 157 KVSLRSPDMLADVAIVDPTLTHGTNLYLSGRGAMDAFTHLMEAYVCGEPNPLTDMICEEGLRKLSSSVVRACvyDEPQ-- 234
Cdd:cd14865 158 KLLFVSPFLLPDVAILDPRLTLSLPPKLTAATGMDALTHAIEAYTSLQKNPISDALALQAIRLISENLPKAV--KNGKdl 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 235 -ARSDLAFASMLGGMAITNAKLGAAHGLASALGGKISAPHSVITARLAPFVMLENIAVAREEKRLdiLARYQRIAQIVIG 313
Cdd:cd14865 236 eARLALAIAATMAGIAFSNSMVGLVHAIAHAVGAVAGVPHGLANSILLPHVMRYNLDAAAERYAE--LALALAYGVTPAG 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1515916685 314 NSEAKEEEAISWLSEVL-DTLKLP-NLQEFGVCEAQFDEVSADALKSVAIKGNPLPLNQERLVHILKQV 380
Cdd:cd14865 314 RRAEEAIEAAIDLVRRLhELCGLPtRLRDVGVPEEQLEAIAELALNDGAILFNPREVDPEDILAILEAA 382
|
|
| NADPH_BDH |
cd08179 |
NADPH-dependent butanol dehydrogenase involved in the butanol and ethanol formation pathway in ... |
8-380 |
1.70e-69 |
|
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: 224.76 E-value: 1.70e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 8 TKIIFGDGALSAslsLFNQYGYSVLLVTG-NTLERTSV---VTDYLDAQSMRYQHIA-VSGEPNIKMVEEAAISARRFKP 82
Cdd:cd08179 6 RDIYFGEGALEY---LKTLKGKRAFIVTGgGSMKRNGFldkVEDYLKEAGMEVKVFEgVEPDPSVETVEKGAEAMREFEP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 83 DMVVAMGGGSAIDMGKALAAvlpnqgnLYDYVEVVGRNVpLKTKPLP-------FIAIPTTASTGAEVTKNAVLKSGQDQ 155
Cdd:cd08179 83 DWIIAIGGGSVIDAAKAMWV-------FYEYPELTFEDA-LVPFPLPelrkkarFIAIPSTSGTGSEVTRASVITDTEKG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 156 VKVSLRSPDMLADVAIVDPTLT-----HGT-NlylSGrgaMDAFTHLMEAYVCGEPNPLTDMICEEGLRKLSSSVVRACV 229
Cdd:cd08179 155 IKYPLASFEITPDVAILDPELTmtmppHVTaN---TG---MDALTHAIEAYVSTLANDFTDALALGAILDIFENLPKSYN 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 230 YDE-PQARSDLAFASMLGGMAITNAKLGAAHGLASALGGKISAPHSVITARLAPFVMLENIAVAReekrldilARYQRIA 308
Cdd:cd08179 229 GGKdLEAREKMHNASCLAGMAFSNSGLGIVHSMAHKGGAFFGIPHGLANAILLPYVIEFNSKDPE--------ARARYAA 300
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1515916685 309 QIVIGNSEAKEEEAISWLSEVLDTLKLP-NLQEFGVCE----AQFDEVSADALKSVAIKGNPLPLNQERLVHILKQV 380
Cdd:cd08179 301 LLIGLTDEELVEDLIEAIEELNKKLGIPlSFKEAGIDEdeffAKLDEMAENAMNDACTGTNPRKPTVEEMKELLKAA 377
|
|
| Fe-ADH-like |
cd08194 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
9-379 |
1.03e-68 |
|
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: 222.41 E-value: 1.03e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 9 KIIFGDGALSASLSLFNQYGYS-VLLVTGNTLERTSV---VTDYLDAQSMRYQ-HIAVSGEPNIKMVEEAAISARRFKPD 83
Cdd:cd08194 3 TIIIGGGALEELGEEAASLGGKrALIVTDKVMVKLGLvdkVTQLLAEAGIAYAvFDDVVSEPTDEMVEEGLALYKEGGCD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 84 MVVAMGGGSAIDMGKALAAVLPNQGNLYDYVevvGRNVPLKtKPLPFIAIPTTASTGAEVTKNAVLKSGQDQVKVSLRSP 163
Cdd:cd08194 83 FIVALGGGSPIDTAKAIAVLATNGGPIRDYM---GPRKVDK-PGLPLIAIPTTAGTGSEVTRFTVITDTETDVKMLLKGP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 164 DMLADVAIVDPTLTHGTNLYLSGRGAMDAFTHLMEAYVCGEPNPLTDMICEEGLRKLSSSVVRAcvYDEP---QARSDLA 240
Cdd:cd08194 159 ALLPAVAIVDPELTLSMPPRVTAATGIDALTHAIEAYVSRKAQPLTDTLALSAIKLIGRNLRRA--YADGddlEAREAMM 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 241 FASMLGGMAITNAKLGAAHGLASALGGKISAPHSVITARLAPFVMLENIAVAreekrldiLARYQRIAQIV-IGNSEAKE 319
Cdd:cd08194 237 LAALEAGIAFSNSSVALVHGMSRPIGALFHVPHGLSNAMLLPAVTEFSLPGA--------PERYAEIARAMgIATEGDSD 308
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1515916685 320 EEA----ISWLSEVLDTLKLPNLQEFGVCEAQFDEV----SADALKSVAIKGNPLPLNQERLVHILKQ 379
Cdd:cd08194 309 EEAaeklVEALERLCADLEIPTLREYGIDEEEFEAAldkmAEDALASGSPANNPRVPTKEEIIELYRE 376
|
|
| Fe-ADH-like |
cd14861 |
Iron-containing alcohol dehydrogenases-like; This family contains proteins similar to ... |
8-371 |
2.22e-67 |
|
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: 218.92 E-value: 2.22e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 8 TKIIFGDGALSASLSLFNQYGYS-VLLVTGNTLERTSVVTDYLDAqsMRYQHIA------VSGEPNIKMVEEAAISARRF 80
Cdd:cd14861 4 TRIRFGAGAIAELPEELKALGIRrPLLVTDPGLAALGIVDRVLEA--LGAAGLSpavfsdVPPNPTEADVEAGVAAYREG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 81 KPDMVVAMGGGSAIDMGKALAAVLPNQGNLYDYvEVVGRNVPLKTKPL-PFIAIPTTASTGAEVTKNAVLKSGQDQVKVS 159
Cdd:cd14861 82 GCDGIIALGGGSAIDAAKAIALMATHPGPLWDY-EDGEGGPAAITPAVpPLIAIPTTAGTGSEVGRAAVITDDDTGRKKI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 160 LRSPDMLADVAIVDPTLTHGTNLYLSGRGAMDAFTHLMEAYVCGEPNPLTDMICEEGLRKLSSSVVRAcvYDEPQ---AR 236
Cdd:cd14861 161 IFSPKLLPKVAICDPELTLGLPPRLTAATGMDALTHCIEAYLSPGFHPMADGIALEGLRLISEWLPRA--VADGSdleAR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 237 SDLAFASMLGGMAItnAK-LGAAHGLASALGGKISAPHSVITARLAPFVMLENIAVareekrldILARYQRIAQiVIGNS 315
Cdd:cd14861 239 GEMMMAALMGAVAF--QKgLGAVHALAHALGALYGLHHGLLNAILLPYVLRFNRPA--------VEDKLARLAR-ALGLG 307
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1515916685 316 EAKEEEAISWLSEVLDTLKLP-NLQEFGVCEAQFDEVSADALKSVAIKGNPLPLNQE 371
Cdd:cd14861 308 LGGFDDFIAWVEDLNERLGLPaTLSELGVTEDDLDELAELALADPCHATNPRPVTAE 364
|
|
| PDDH |
cd08188 |
1,3-Propanediol (1,3-PD) dehydrogenase; This family includes 1,3-propanediol (1,3-PD) ... |
11-378 |
3.56e-64 |
|
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: 210.83 E-value: 3.56e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 11 IFGDGALSASLSLFNQYGY-SVLLVTGNTLERTSV---VTDYLDAQSMRYqHI--AVSGEPNIKMVEEAAISARRFKPDM 84
Cdd:cd08188 10 LFGPGCLKEIGDELKKLGGkKALIVTDKGLVKLGLvkkVTDVLEEAGIEY-VIfdGVQPNPTVTNVNEGLELFKENGCDF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 85 VVAMGGGSAIDMGKALAAVLPNQGNLYDYvEVVGRnvpLKTKPLPFIAIPTTASTGAEVTKNAVLKSGQDQVKVSLRSPD 164
Cdd:cd08188 89 IISVGGGSAHDCAKAIGILATNGGEIEDY-EGVDK---SKKPGLPLIAINTTAGTASEVTRFAVITDEERHVKMVIVDWN 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 165 MLADVAIVDPTLTHGTNLYLSGRGAMDAFTHLMEAYVCGEPNPLTDMICEEGLRKLSSSVVRACVY-DEPQARSDLAFAS 243
Cdd:cd08188 165 VTPTIAVNDPELMLGMPPSLTAATGMDALTHAIEAYVSTGATPLTDALALEAIRLIAENLPKAVANgKDLEARENMAYAQ 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 244 MLGGMAITNAKLGAAHGLASALGGKISAPHSVITARLAPFVMLENIAVAREekrldilaRYQRIAQIVIGNSEAKE---- 319
Cdd:cd08188 245 FLAGMAFNNAGLGYVHAMAHQLGGFYNLPHGVCNAILLPHVMEFNLPACPE--------RFADIARALGENTEGLSdeea 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1515916685 320 -EEAISWLSEVLDTLKLP-NLQEFGVCEAQFDEVSADALKSVAIKGNPLPLNQERLVHILK 378
Cdd:cd08188 317 aEAAIEAIRKLSRRVGIPsGLKELGVKEEDFPLLAENALKDACGPTNPRQATKEDVIAIYR 377
|
|
| Fe-ADH-like |
cd08196 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
2-377 |
6.97e-63 |
|
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: 207.05 E-value: 6.97e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 2 FQFMTSTKIIFGDGALSASLSLFNQYGYS-VLLVTGNTLERTSVVTDYLDAQSMRYQHI--AVSGEPNIKMVEEAAISAR 78
Cdd:cd08196 1 WSYYQPVKIIFGEGILKELPDIIKELGGKrGLLVTDPSFIKSGLAKRIVESLKGRIVAVfsDVEPNPTVENVDKCARLAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 79 RFKPDMVVAMGGGSAIDMGKALAAVLPNQGNLYDYVEvvGRNvPLKTKPLPFIAIPTTASTGAEVTKNAVLKSGQDQVKV 158
Cdd:cd08196 81 ENGADFVIAIGGGSVLDTAKAAACLAKTDGSIEDYLE--GKK-KIPKKGLPLIAIPTTAGTGSEVTPVAVLTDKEKGKKA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 159 SLRSPDMLADVAIVDPTLTHGTNLYLSGRGAMDAFTHLMEAYVCGEPNPLTDMICEEGLRKLSSSVVRAcvYDEPQ---A 235
Cdd:cd08196 158 PLVSPGFYPDIAIVDPELTYSMPPKVTASTGIDALCHAIEAYWSINHQPISDALALEAAKLVLENLEKA--YNNPNdkeA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 236 RSDLAFASMLGGMAITNAKLGAAHGLASALGGKISAPHSVITARLAPFVMLENIAVarEEKRLDILARYqriaqivIGNS 315
Cdd:cd08196 236 REKMALASLLAGLAFSQTRTTASHACSYPLTSHFGIPHGEACALTLPSFIRLNAEA--LPGRLDELAKQ-------LGFK 306
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1515916685 316 EAKEeeaiswLSEVLDTLK----LP-NLQEFGVCEAQFDEVSADALKSVAIKGNPLPLNQERLVHIL 377
Cdd:cd08196 307 DAEE------LADKIEELKkrigLRtRLSELGITEEDLEEIVEESFHPNRANNNPVEVTKEDLEKLL 367
|
|
| Fe-ADH-like |
cd17814 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
10-371 |
1.50e-61 |
|
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: 203.93 E-value: 1.50e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 10 IIFGDGALS-ASLSLFNQYGYSVLLVTGNTLER---TSVVTDYLDAQSMRYQ-HIAVSgePNIKM--VEEAAISARRFKP 82
Cdd:cd17814 7 FIFGVGARKlAGRYAKNLGARKVLVVTDPGVIKagwVDEVLDSLEAEGLEYVvFSDVT--PNPRDfeVMEGAELYREEGC 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 83 DMVVAMGGGSAIDMGKALAAVLPNQGNLYDY--VEVVGRNVPlktkplPFIAIPTTASTGAEVTKNAVLKSGQDQVKVSL 160
Cdd:cd17814 85 DGIVAVGGGSPIDCAKGIGIVVSNGGHILDYegVDKVRRPLP------PLICIPTTAGSSADVSQFAIITDTERRVKMAI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 161 RSPDMLADVAIVDPTLTHGTNLYLSGRGAMDAFTHLMEAYVCGEPNPLTDMICEEGLRKLSSSVVRACVY-DEPQARSDL 239
Cdd:cd17814 159 ISKTLVPDVSLIDPETLTTMDPELTACTGMDALTHAIEAYVSNASSPLTDLHALEAIRLISENLPKAVADpDDLEAREKM 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 240 AFASMLGGMAITNAKLGAAHGLASALGGKISAPHSVITARLAPFVMLENIAVAREekrldilaRYQRIAQiVIG------ 313
Cdd:cd17814 239 MLASLQAGLAFSNASLGAVHAMAHSLGGLLDLPHGECNALLLPHVIRFNFPAAPE--------RYRKIAE-AMGldvdgl 309
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1515916685 314 NSEAKEEEAISWLSEVLDTLKLPN-LQEFGVCEAQFDEVSADALKSVAIKGNPLPLNQE 371
Cdd:cd17814 310 DDEEVAERLIEAIRDLREDLGIPEtLSELGVDEEDIPELAKRAMKDPCLVTNPRRPTRE 368
|
|
| HOT |
cd08190 |
Hydroxyacid-oxoacid transhydrogenase (HOT) involved in gamma-hydroxybutyrate metabolism; This ... |
7-379 |
2.39e-61 |
|
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: 204.32 E-value: 2.39e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 7 STKIIFGDGALSASLSLFNQYGYS-VLLVTGNTLERTSVVTDYLDaqSMRYQHIA------VSGEPNIKMVEEAAISARR 79
Cdd:cd08190 1 ASNIRFGPGATRELGMDLKRLGAKkVLVVTDPGLAKLGLVERVLE--SLEKAGIEvvvydgVRVEPTDESFEEAIEFAKE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 80 FKPDMVVAMGGGSAIDMGKALAAVLPNQGNLYDYV--EV-VGRNVPLKTKPLpfIAIPTTASTGAEVTKNAVLKSGQDQV 156
Cdd:cd08190 79 GDFDAFVAVGGGSVIDTAKAANLYATHPGDFLDYVnaPIgKGKPVPGPLKPL--IAIPTTAGTGSETTGVAIFDLEELKV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 157 KVSLRSPDMLADVAIVDPTLTHGTNLYLSGRGAMDAFTHLMEAYVC-------------GEP-----NPLTDMICEEGLR 218
Cdd:cd08190 157 KTGISSRYLRPTLAIVDPLLTLTLPPRVTASSGFDVLCHALESYTArpynarprpanpdERPayqgsNPISDVWAEKAIE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 219 KLSSSVVRAcVYDEP--QARSDLAFASMLGGMAITNAKLGAAHGLASALGGKIS-------------APHSVITARLAPF 283
Cdd:cd08190 237 LIGKYLRRA-VNDGDdlEARSNMLLASTLAGIGFGNAGVHLPHAMAYPIAGLVKdyrppgypvdhphVPHGLSVALTAPA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 284 VMLENIAVAREekrldilaRYQRIAQIVIGN-SEAKEEEAISWLSEVL----DTLKLPN-LQEFGVCEAQFDEVSADALK 357
Cdd:cd08190 316 VFRFTAPACPE--------RHLEAAELLGADtSGASDRDAGEVLADALiklmRDIGIPNgLSALGYSEDDIPALVEGTLP 387
|
410 420
....*....|....*....|...
gi 1515916685 358 SVA-IKGNPLPLNQERLVHILKQ 379
Cdd:cd08190 388 QQRlLKLNPRPVTEEDLEEIFED 410
|
|
| BDH |
cd08187 |
Butanol dehydrogenase catalyzes the conversion of butyraldehyde to butanol with the cofactor ... |
2-378 |
9.53e-60 |
|
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: 199.20 E-value: 9.53e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 2 FQFMTSTKIIFGDGALSASLSLFNQYGYSVLLVTG-NTLERTSV---VTDYLDAQSmrYQHIAVSG-EPN--IKMVEEAA 74
Cdd:cd08187 2 FTFYNPTKIIFGKGAIEELGEEIKKYGKKVLLVYGgGSIKKNGLydrVVASLKEAG--IEVVEFGGvEPNprLETVREGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 75 ISARRFKPDMVVAMGGGSAIDMGKALAAVLPNQGNLYDYVEvvGRNVPlkTKPLPFIAIPTTASTGAEVTKNAVLKSGQD 154
Cdd:cd08187 80 ELAREENVDFILAVGGGSVIDAAKAIAAGAKYDGDVWDFFT--GKAPP--EKALPVGTVLTLAATGSEMNGGAVITNEET 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 155 QVKVSLRSPDMLADVAIVDPTLTHGTNLYLSGRGAMDAFTHLMEAYVCGEPN-PLTDMICEEGLRklssSVVRAC--VYD 231
Cdd:cd08187 156 KEKLGFGSPLLRPKFSILDPELTYTLPKYQTAAGIVDIFSHVLEQYFTGTEDaPLQDRLAEGLLR----TVIENGpkALK 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 232 EPQ---ARSDLAFASMLG--GMaITNAKLG--AAHGLASALGGKISAPH----SVITARLAPFVMleniavareEKRLDI 300
Cdd:cd08187 232 DPDdyeARANLMWAATLAlnGL-LGAGRGGdwATHAIEHELSALYDITHgaglAIVFPAWMRYVL---------KKKPER 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 301 LARY-QRIAQIVIGNSEAKE-EEAISWLSEVLDTLKLP-NLQEFGVCEAQFDEVSADALKSVAIKGNPLPLNQERLVHIL 377
Cdd:cd08187 302 FAQFaRRVFGIDPGGDDEETaLEGIEALEEFFKSIGLPtTLSELGIDEEDIEEMAEKAVRGGGLGGGFKPLTREDIEEIL 381
|
.
gi 1515916685 378 K 378
Cdd:cd08187 382 K 382
|
|
| HEPD |
cd08182 |
Hydroxyethylphosphoate dehydrogenase (HEPD) catalyzes the reduction of phosphonoacetaldehyde ... |
8-377 |
2.58e-59 |
|
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: 197.83 E-value: 2.58e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 8 TKIIFGDGALSASLSLFNQYGYS-VLLVTGNTLERTSVVTDYLDAQSMRYQHIAVSG-EPN--IKMVEEAAISARRFKPD 83
Cdd:cd08182 2 VKIIFGPGALAELKDLLGGLGARrVLLVTGPSAVRESGAADILDALGGRIPVVVFSDfSPNpdLEDLERGIELFRESGPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 84 MVVAMGGGSAIDMGKALAAVLPNQGNlyDYVEVVGRNVPLKTKPLPFIAIPTTASTGAEVTKNAVLKSGQDQVKVSLRSP 163
Cdd:cd08182 82 VIIAVGGGSVIDTAKAIAALLGSPGE--NLLLLRTGEKAPEENALPLIAIPTTAGTGSEVTPFATIWDEAEGKKYSLAHP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 164 DMLADVAIVDPTLTHGTNLYLSGRGAMDAFTHLMEAYVCGEPNPLTDMICEEGLRKLSSSVVraCVYDEP---QARSDLA 240
Cdd:cd08182 160 SLYPDAAILDPELTLSLPLYLTASTGLDALSHAIESIWSVNANPESRAYALRAIRLILENLP--LLLENLpnlEAREAMA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 241 FASMLGGMAITNAKLGAAHGLASALGGKISAPHSVITARLAPFVMLENIAVAREEkrlDILARYQRIAQIVIGNSEAkee 320
Cdd:cd08182 238 EASLLAGLAISITKTTAAHAISYPLTSRYGVPHGHACALTLPAVLRYNAGADDEC---DDDPRGREILLALGASDPA--- 311
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1515916685 321 EAISWLSEVLDTLKLP-NLQEFGVCEAQFDEVSADALKSVAIKGNPLPLNQERLVHIL 377
Cdd:cd08182 312 EAAERLRALLESLGLPtRLSEYGVTAEDLEALAASVNTPERLKNNPVRLSEEDLLRLL 369
|
|
| LPO |
cd08176 |
Lactadehyde:propanediol oxidoreductase (LPO) catalyzes the interconversion between ... |
2-378 |
1.95e-54 |
|
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: 185.06 E-value: 1.95e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 2 FQFMTSTKIIFGDGALSASLSLFNQYGYS-VLLVTGNTLERTSV---VTDYLDAQSMRYqHIAVSGEPN--IKMVEEAAI 75
Cdd:cd08176 1 NRFVLNPTSYFGWGAIEEIGEEAKKRGFKkALIVTDKGLVKFGIvdkVTDVLKEAGIAY-TVFDEVKPNptIENVMAGVA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 76 SARRFKPDMVVAMGGGSAIDMGKALAAVLPNQGNLYDYVEVVGrnvPLKTKPLPFIAIPTTASTGAEVTKNAVLKSGQDQ 155
Cdd:cd08176 80 AYKESGADGIIAVGGGSSIDTAKAIGIIVANPGADVRSLEGVA---PTKNPAVPIIAVPTTAGTGSEVTINYVITDTEKK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 156 VKVSLRSPDMLADVAIVDPTLTHGTNLYLSGRGAMDAFTHLMEAYVCGEPNPLTDMICEEGLRKLSSSvVRACVYDE--P 233
Cdd:cd08176 157 RKFVCVDPHDIPTVAIVDPDLMSSMPKGLTAATGMDALTHAIEGYITKGAWELSDMLALKAIELIAKN-LRKAVANPnnV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 234 QARSDLAFASMLGGMAITNAKLGAAHGLASALGGKISAPHSVITARLAPFVMLENIAVAREekrldilaRYQRIAQI--V 311
Cdd:cd08176 236 EARENMALAQYIAGMAFSNVGLGIVHSMAHPLSAFYDTPHGVANAILLPYVMEFNAPATGE--------KYRDIARAmgV 307
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1515916685 312 IGNSEAKEEEAISWLSEV---LDTLKLP-NLQEFGVCEAQFDEVSADALKSVAIKGNPLPLNQERLVHILK 378
Cdd:cd08176 308 DTTGMSDEEAAEAAVDAVkklSKDVGIPqKLSELGVKEEDIEALAEDALNDVCTPGNPREATKEDIIALYK 378
|
|
| PDD |
cd08180 |
1,3-propanediol dehydrogenase (PPD) catalyzes the reduction of 3-hydroxypropionaldehyde (3-HPA) ... |
2-378 |
2.09e-52 |
|
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: 178.46 E-value: 2.09e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 2 FQFmtSTKIIFGDGALSAsLSLFNqyGYSVLLVTGNTLERTSV---VTDYLDAQSmRYqHI--AVSGEPNIKMVEEAAIS 76
Cdd:cd08180 1 FSL--KTKIYSGEDSLER-LKELK--GKRVFIVTDPFMVKSGMvdkVTDELDKSN-EV-EIfsDVVPDPSIEVVAKGLAK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 77 ARRFKPDMVVAMGGGSAIDMGKALaavlpnqgnLYDYVEVVGRNvplktKPLPFIAIPTTASTGAEVTKNAVLKSGQDQV 156
Cdd:cd08180 74 ILEFKPDTIIALGGGSAIDAAKAI---------IYFALKQKGNI-----KKPLFIAIPTTSGTGSEVTSFAVITDPEKGI 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 157 KVSLRSPDMLADVAIVDPTLThgtnlyLS---------GrgaMDAFTHLMEAYVCGEPNPLTDMICEEGLRKLSSSVVRA 227
Cdd:cd08180 140 KYPLVDDSMLPDIAILDPELV------KSvppkvtadtG---MDVLTHALEAYVSTNANDFTDALAEKAIKLVFENLPRA 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 228 cvYDEPQ---ARSDLAFASMLGGMAITNAKLGAAHGLASALGGKISAPHSVITARLAPFVMLENIAvareekrldilary 304
Cdd:cd08180 211 --YRDGDdleAREKMHNASCMAGIAFNNAGLGINHSLAHALGGRFHIPHGRANAILLPYVIEFLIA-------------- 274
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1515916685 305 qriaqivignseakeeeAISWLSEvldTLKLP-NLQEFGVCEAQF----DEVSADALKSVAIKGNPLPLNQERLVHILK 378
Cdd:cd08180 275 -----------------AIRRLNK---KLGIPsTLKELGIDEEEFekaiDEMAEAALADRCTATNPRKPTAEDLIELLR 333
|
|
| AAD_C |
cd08178 |
C-terminal alcohol dehydrogenase domain of the acetaldehyde dehydrogenase-alcohol ... |
31-377 |
7.17e-52 |
|
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: 178.92 E-value: 7.17e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 31 VLLVTGNTLERTSV---VTDYLDAQSMRYQ-HIAVSGEPNIKMVEEAAISARRFKPDMVVAMGGGSAIDMGKALaavlpn 106
Cdd:cd08178 26 AFIVTDRVLYKLGYvdkVLDVLEARGVETEvFSDVEPDPTLSTVRKGLEAMNAFKPDVIIALGGGSAMDAAKIM------ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 107 qGNLYDYVEV-----VGR---------NVP---LKTKplpFIAIPTTASTGAEVTKNAVLKSGQDQVKVSLRSPDMLADV 169
Cdd:cd08178 100 -WLFYEHPETkfedlAQRfmdirkrvyKFPklgKKAK---LVAIPTTSGTGSEVTPFAVITDDKTGKKYPLADYALTPDM 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 170 AIVDPTLTHGTNLYLSGRGAMDAFTHLMEAYVCGEPNPLTDMICEEGLRKLSSSVVRACVYDE-PQARSDLAFASMLGGM 248
Cdd:cd08178 176 AIVDPELVMTMPKRLTADTGIDALTHAIEAYVSVMASDYTDGLALQAIKLIFEYLPRSYNNGNdIEAREKMHNAATIAGM 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 249 AITNAKLGAAHGLASALGGKISAPHSVITARLAPFVMLENIAVAREE-------KRLDILARYQRIAQIV---IGNSEAK 318
Cdd:cd08178 256 AFANAFLGICHSLAHKLGAAFHIPHGRANAILLPHVIRYNATDPPTKqaafpqyKYYVAKERYAEIADLLglgGKTPEEK 335
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1515916685 319 EEEAISWLSEVLDTLKLP-NLQEFGVCEAQF----DEVSADALKSVAIKGNP-LPLNQErLVHIL 377
Cdd:cd08178 336 VESLIKAIEDLKKDLGIPtSIREAGIDEADFlaavDKLAEDAFDDQCTGANPrYPLISE-LKEIL 399
|
|
| Fe-ADH-like |
cd14862 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
7-377 |
4.36e-51 |
|
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: 176.26 E-value: 4.36e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 7 STKIIFGDGALSAslslFNQY-GYSVLLVTGNTLERTSV---VTDYLDAQSMRYQHIA-VSGEPNIKMVEEAAISARRFK 81
Cdd:cd14862 6 SPKIVFGEDALSH----LEQLsGKRALIVTDKVLVKLGLlkkVLKRLLQAGFEVEVFDeVEPEPPLETVLKGAEAMREFE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 82 PDMVVAMGGGSAIDMGKALAAvlpnqgnLYDYVEVVGRNVP------LKTKPLpFIAIPTTASTGAEVTKNAVLKSGQDQ 155
Cdd:cd14862 82 PDLIIALGGGSVMDAAKAAWV-------LYERPDLDPEDISpldllgLRKKAK-LIAIPTTSGTGSEATWAIVLTDTEEP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 156 VKVSLRSPDMLADVAIVDPTLTHG--TNLYLSgrGAMDAFTHLMEAYVCGEPNPLTDMICEEGLRKLSSSVVRACVY-DE 232
Cdd:cd14862 154 RKIAVANPELVPDVAILDPEFVLGmpPKLTAG--TGLDALAHAVEAYLSTWSNDFSDALALKAIELIFKYLPRAYKDgDD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 233 PQARSDLAFASMLGGMAITNAKLGAAHGLASALGGKISAPHSVITARLAPFVMLENIAVAREEKRLDILAryqriaqivI 312
Cdd:cd14862 232 LEAREKMHNAATIAGLAFGNSQAGLAHALGHSLGAVFHVPHGIAVGLFLPYVIEFYAKVTDERYDLLKLL---------G 302
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1515916685 313 GNSEAKEEEAISWLSEVLDTLK---LP-NLQEFGVCEAQF----DEVSADALKSVAIKGNPLPLNQERLVHIL 377
Cdd:cd14862 303 IEARDEEEALKKLVEAIRELYKevgQPlSIKDLGISEEEFeeklDELVEYAMEDSCTITSPRPPSEEDLKKLF 375
|
|
| PPD-like |
cd08181 |
1,3-propanediol dehydrogenase-like (PPD); This family contains proteins similar to 1, ... |
4-261 |
5.05e-51 |
|
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: 175.85 E-value: 5.05e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 4 FMTSTKIIFGDGALSASLSLFNQYGYSVLLVTGntleRTSV--------VTDYLDAQSMRYQ-HIAVSGEPNIKMVEEAA 74
Cdd:cd08181 1 FYMPTKVYFGKNCVEKHADELAALGKKALIVTG----KHSAkkngslddVTEALEENGIEYFiFDEVEENPSIETVEKGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 75 ISARRFKPDMVVAMGGGSAIDMGKALAAVLPNQGNLYDYVEVvgrnvPLKTKPLPFIAIPTTASTGAEVTKNAVLKSGQD 154
Cdd:cd08181 77 ELARKEGADFVIGIGGGSPLDAAKAIALLAANKDGDEDLFQN-----GKYNPPLPIVAIPTTAGTGSEVTPYSILTDHEK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 155 QVKVSLRSPDMLADVAIVDPTLTHGTNLYLSGRGAMDAFTHLMEAYVCGEPNPLTDMICEEGLRKLSSS--VVRACVYDe 232
Cdd:cd08181 152 GTKKSFGNPLIFPKLALLDPKYTLSLPEELTIDTAVDALSHAIEGYLSVKATPLSDALALEALRLIGEClpNLLGDELD- 230
|
250 260
....*....|....*....|....*....
gi 1515916685 233 PQARSDLAFASMLGGMAITNAKLGAAHGL 261
Cdd:cd08181 231 EEDREKLMYASTLAGMVIAQTGTTLPHGL 259
|
|
| HVD |
cd08193 |
5-hydroxyvalerate dehydrogenase (HVD) catalyzes the oxidation of 5-hydroxyvalerate to ... |
4-374 |
1.27e-49 |
|
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: 172.70 E-value: 1.27e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 4 FMTSTKIIFGDGALSASLSLFNQYGYS-VLLVTGNTLERTSVVTDYLDAqsMRYQHIAVS------GEPNIKMVEEAAIS 76
Cdd:cd08193 1 FQTVPRIICGAGAAARLGELLRELGARrVLLVTDPGLVKAGLADPALAA--LEAAGIAVTvfddvvADPPEAVVEAAVEQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 77 ARRFKPDMVVAMGGGSAIDMGKALAAVLPNQGNLYDYVEVvGRnvpLKTKPLPFIAIPTTASTGAEVTKNAVLKSGQDQv 156
Cdd:cd08193 79 AREAGADGVIGFGGGSSMDVAKLVALLAGSDQPLDDIYGV-GK---ATGPRLPLILVPTTAGTGSEVTPISIVTTGETE- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 157 KVSLRSPDMLADVAIVDPTLTHGTNLYLSGRGAMDAFTHLMEAYVCG-EPNPLTDMICEEGLRKLSSSVVRAC-VYDEPQ 234
Cdd:cd08193 154 KKGVVSPQLLPDVALLDAELTLGLPPHVTAATGIDAMVHAIEAYTSRhKKNPISDALAREALRLLGANLRRAVeDGSDLE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 235 ARSDLAFASMLGGMAITNAKLGAAHGLASALGGKISAPHSVITARLAPFVMLENIAVAREEkrldilarYQRIAQIVI-G 313
Cdd:cd08193 234 AREAMLLGSMLAGQAFANAPVAAVHALAYPLGGHFHVPHGLSNALVLPHVLRFNLPAAEAL--------YAELARALLpG 305
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1515916685 314 NSEAKEEEA----ISWLSEVLDTLKLP-NLQEFGVCEAQFDEVSADALKsvaikgnplplnQERLV 374
Cdd:cd08193 306 LAFGSDAAAaeafIDALEELVEASGLPtRLRDVGVTEEDLPMLAEDAMK------------QTRLL 359
|
|
| Fe-ADH-like |
cd08189 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
9-380 |
1.39e-49 |
|
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: 172.27 E-value: 1.39e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 9 KIIFGDGALSASLSLFNQYGYS-VLLVTGNTLERTSVV---TDYLDAQSMRYqHI--AVSGEPNIKMVEEAAISARRFKP 82
Cdd:cd08189 7 ELFEGAGSLLQLPEALKKLGIKrVLIVTDKGLVKLGLLdplLDALKKAGIEY-VVfdGVVPDPTIDNVEEGLALYKENGC 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 83 DMVVAMGGGSAIDMGKALAAVLPNQGNlyDYVEVVGRNvPLKTKPLPFIAIPTTASTGAEVTKNAVLKSGQDQVKVSLRS 162
Cdd:cd08189 86 DAIIAIGGGSVIDCAKVIAARAANPKK--SVRKLKGLL-KVRKKLPPLIAVPTTAGTGSEATIAAVITDPETHEKYAIND 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 163 PDMLADVAIVDPTLTHGTNLYLSGRGAMDAFTHLMEAYVCGEPNPLTDMICEEGLRKLSSSVVRAcvYDEPQ---ARSDL 239
Cdd:cd08189 163 PKLIPDAAVLDPELTLGLPPAITAATGMDALTHAVEAYISRSATKETDEYALEAVKLIFENLPKA--YEDGSdleARENM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 240 AFASMLGGMAITNAKLGAAHGLASALGGKISAPHSVITARLAPFVMLENIAVAreEKRLDILARYQRIAQIVIGNSEaKE 319
Cdd:cd08189 241 LLASYYAGLAFTRAYVGYVHAIAHQLGGLYGVPHGLANAVVLPHVLEFYGPAA--EKRLAELADAAGLGDSGESDSE-KA 317
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 320 EEAISWLSEVLDTL----KLPNLQefgvcEAQFDEVSADALKsvaiKGNPL---P--LNQERLVHILKQV 380
Cdd:cd08189 318 EAFIAAIRELNRRMgiptTLEELK-----EEDIPEIAKRALK----EANPLypvPriMDRKDCEELLRKV 378
|
|
| MAR-like |
cd08192 |
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic ... |
8-380 |
1.41e-46 |
|
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: 164.73 E-value: 1.41e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 8 TKIIFGDGALSASLSLFNQYGYS-VLLVTGNTL-ERTSVVTDYLDAQSMRY--------QHIAVSGepnikmVEEAAISA 77
Cdd:cd08192 2 ERVSYGPGAVEALLHELATLGASrVFIVTSKSLaTKTDVIKRLEEALGDRHvgvfsgvrQHTPRED------VLEAARAV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 78 RRFKPDMVVAMGGGSAIDMGKALAAVLPNQ----GNLYDYVEVVGRNVPLKTKPLPFIAIPTTAStGAEVTKNAVLKSGQ 153
Cdd:cd08192 76 REAGADLLVSLGGGSPIDAAKAVALALAEDvtdvDQLDALEDGKRIDPNVTGPTLPHIAIPTTLS-GAEFTAGAGATDDD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 154 DQVKVSLRSPDMLADVAIVDPTLTHGT--NLYLS-GRGAMDaftHLMEAYVCGEPNPLTDMICEEGLRKLSSSVVRA-CV 229
Cdd:cd08192 155 TGHKQGFAHPELGPDAVILDPELTLHTpeRLWLStGIRAVD---HAVETLCSPQATPFVDALALKALRLLFEGLPRSkAD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 230 YDEPQARSDL---AFASMLGGMAitNAKLGAAHGLASALGGKISAPHSVITARLAPFVMLENIAVAREEKRldilaryqR 306
Cdd:cd08192 232 PEDLEARLKCqlaAWLSLFGLGS--GVPMGASHAIGHQLGPLYGVPHGITSCIMLPAVLRFNAPVNAERQR--------L 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 307 IAQIVIGNSEAKEEEAISwLSEVLDT----LKLPN-LQEFGVCEAQFDEVSADALKSVAIKGNPLPLNQ-ERLVHILKQV 380
Cdd:cd08192 302 IARALGLVTGGLGREAAD-AADAIDAlireLGLPRtLRDVGVGRDQLEKIAENALTDVWCRTNPRPITDkDDVLEILESA 380
|
|
| YqdH |
COG1979 |
Alcohol dehydrogenase YqhD, Fe-dependent ADH family [Energy production and conversion]; |
2-378 |
1.54e-44 |
|
Alcohol dehydrogenase YqhD, Fe-dependent ADH family [Energy production and conversion];
Pssm-ID: 441582 [Multi-domain] Cd Length: 387 Bit Score: 159.08 E-value: 1.54e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 2 FQFMTSTKIIFGDGALSASLSLFNQYGYSVLLVTGN-------TLERtsvVTDYLDAQSMRYqhIAVSG-EPN--IKMVE 71
Cdd:COG1979 4 FTFYNPTKIIFGKGQIAKLGEEIPKYGKKVLLVYGGgsikkngLYDQ---VKAALKEAGIEV--VEFGGvEPNprLETVR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 72 EAAISARRFKPDMVVAMGGGSAIDMGKALAAVLPNQGNLYDYVEvvGRNVPlkTKPLPFIAIPTTASTGAEVTKNAVLKS 151
Cdd:COG1979 79 KGVELCKEEGIDFILAVGGGSVIDGAKAIAAGAKYDGDPWDILT--GKAPV--EKALPLGTVLTLPATGSEMNSGSVITN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 152 GQDQVKVSLRSPDMLADVAIVDPTLThgtnlY-LSGR----GAMDAFTHLMEAYVCGEPN-PLTDMICEEGLRklssSVV 225
Cdd:COG1979 155 EETKEKLGFGSPLVFPKFSILDPELT-----YtLPKRqtanGIVDIFSHVMEQYFTYPVDaPLQDRFAEGLLR----TLI 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 226 RAC--VYDEPQ---ARSDLAFASMlggMAItNAKLG-------AAHGLASALGGKISAPH----SVITARLAPFVMleni 289
Cdd:COG1979 226 EEGpkALKDPEdydARANLMWAAT---LAL-NGLIGagvpqdwATHMIEHELSALYDIDHgaglAIVLPAWMRYVL---- 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 290 avareEKRLDILARY-QRIAQIVIGNSEAKEEEAISWLSEVLDTLKLP-NLQEFGVCEAQFDEV--SADALKSVAIkGNP 365
Cdd:COG1979 298 -----EEKPEKFAQYaERVWGITEGDDEERALEGIEATEEFFESLGLPtRLSEYGIDEEDIEEMaeKATAHGMTAL-GEF 371
|
410
....*....|...
gi 1515916685 366 LPLNQERLVHILK 378
Cdd:COG1979 372 KDLTPEDVREILE 384
|
|
| PRK13805 |
PRK13805 |
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional |
31-380 |
2.61e-42 |
|
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional
Pssm-ID: 237515 [Multi-domain] Cd Length: 862 Bit Score: 159.19 E-value: 2.61e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 31 VLLVTGNTLER---TSVVTDYLDAQSMRYQH---IAVSGEPNIKMVEEAAISARRFKPDMVVAMGGGSAIDMGKALAAvl 104
Cdd:PRK13805 483 AFIVTDRFMVElgyVDKVTDVLKKRENGVEYevfSEVEPDPTLSTVRKGAELMRSFKPDTIIALGGGSPMDAAKIMWL-- 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 105 pnqgnLYDYVEVVGRNVPLK-------TKPLP-------FIAIPTTASTGAEVTKNAVLKSGQDQVKVSLRSPDMLADVA 170
Cdd:PRK13805 561 -----FYEHPETDFEDLAQKfmdirkrIYKFPklgkkakLVAIPTTSGTGSEVTPFAVITDDKTGVKYPLADYELTPDVA 635
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 171 IVDPTLTHGTNLYLSGRGAMDAFTHLMEAYVCGEPNPLTDMICEEGLRKLSSSVVRAcvYDE----PQARSDLAFASMLG 246
Cdd:PRK13805 636 IVDPNLVMTMPKSLTADTGIDALTHALEAYVSVMASDYTDGLALQAIKLVFEYLPRS--YKNgakdPEAREKMHNASTIA 713
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 247 GMAITNAKLGAAHGLASALGGKISAPHSVITARLAPFVMLENIAVAREE------KRLDILARYQRIAQI--VIGNS-EA 317
Cdd:PRK13805 714 GMAFANAFLGICHSMAHKLGAEFHIPHGRANAILLPHVIRYNATDPPKQaafpqyEYPRADERYAEIARHlgLPGSTtEE 793
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1515916685 318 KEEEAISWLSEVLDTLKLP-NLQEFGVCEAQF----DEVSADALKSVAIKGNP-LPLNQErlvhiLKQV 380
Cdd:PRK13805 794 KVESLIKAIEELKAELGIPmSIKEAGVDEADFlaklDELAELAFDDQCTGANPrYPLISE-----LKEI 857
|
|
| PRK10624 |
PRK10624 |
L-1,2-propanediol oxidoreductase; Provisional |
12-379 |
8.68e-42 |
|
L-1,2-propanediol oxidoreductase; Provisional
Pssm-ID: 182595 [Multi-domain] Cd Length: 382 Bit Score: 151.69 E-value: 8.68e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 12 FGDGALSASLSLFNQYGYS-VLLVTGNTLERTSV---VTDYLDAQSMRYQ-HIAVSGEPNIKMVEEAAISARRFKPDMVV 86
Cdd:PRK10624 13 FGRGAIGALTDEVKRRGFKkALIVTDKTLVKCGVvakVTDVLDAAGLAYEiYDGVKPNPTIEVVKEGVEVFKASGADYLI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 87 AMGGGSAIDMGKALAAVLPNQgnlyDYVEVVGRN--VPLKTKPLPFIAIPTTASTGAEVTKNAVLKSGQDQVKVSLRSPD 164
Cdd:PRK10624 93 AIGGGSPQDTCKAIGIISNNP----EFADVRSLEgvAPTKKPSVPIIAIPTTAGTAAEVTINYVITDEEKRRKFVCVDPH 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 165 MLADVAIVDPTLTHGTNLYLSGRGAMDAFTHLMEAYVCGEPNPLTDMICEEGLRKLSSSVvRACVYDEPQARSDLAFASM 244
Cdd:PRK10624 169 DIPQVAFVDADMMDSMPPGLKAATGVDALTHAIEGYITRGAWALTDMLHLKAIEIIAGAL-RGAVAGDKEAGEGMALGQY 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 245 LGGMAITNAKLGAAHGLASALGGKISAPHSVITARLAPFVMLENiAVAREEKRLDIlARYQRIAQIVIGNSEAKEE--EA 322
Cdd:PRK10624 248 IAGMGFSNVGLGLVHGMAHPLGAFYNTPHGVANAILLPHVMEYN-ADFTGEKYRDI-ARAMGVKVEGMSLEEARNAavEA 325
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1515916685 323 ISWLSEvldTLKLP-NLQEFGVCEAQFDEVSADALKSVAIKGNPLPLNQERLVHILKQ 379
Cdd:PRK10624 326 VKALNR---DVGIPpHLRDVGVKEEDIPALAQAAFDDVCTGGNPREATLEDIVELYKK 380
|
|
| Fe-ADH-like |
cd14864 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
4-380 |
8.13e-41 |
|
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: 148.99 E-value: 8.13e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 4 FMTSTKIIFGDGALSASLSLFNQYGYSVLLVTG---NTLERTSVVTDYL-DAQS--MRYQHIavSGEPNIKMVEEAAISA 77
Cdd:cd14864 1 FKIPPNIVFGADSLERIGEEVKEYGSRFLLITDpvlKESGLADKIVSSLeKAGIsvIVFDEI--PASATSDTIDEAAELA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 78 RRFKPDMVVAMGGGSAIDMGKALAAVLPNQGNLYDYVEvvgrNVPLKTKPLPFIAIPTTASTGAEVT-KNAVLKSGQDQV 156
Cdd:cd14864 79 RKAGADGIIAVGGGKVLDTAKAVAILANNDGGAYDFLE----GAKPKKKPLPLIAVPTTPRSGFEFSdRFPVVDSRSREV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 157 KVsLRSPDMLADVAIVDPTLTHGTNLYLSGRGAMDAFTHLMEAYVCGEPNPLTDMICEEGLRKLSSSVVRACVyDEP--Q 234
Cdd:cd14864 155 KL-LKAQPGLPKAVIVDPNLMASLTGNQTAAMALAALALAVEAYLSKKSNFFSDALALKAIELVSENLDGALA-DPKntP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 235 ARSDLAFASMLGGMAITNAKLGAAHGLASALGGKISAPHSVITARLAPFVMLENIAVAREEkrldiLARYQRIAQIVIGN 314
Cdd:cd14864 233 AEELLAQAGCLAGLAASSSSPGLATALALAVNSRYKVSKSLVASILLPHVIEYAATSAPDK-----YAKIARALGEDVEG 307
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1515916685 315 --SEAKEEEAISWLSEVLDTLKLPN-LQEFGVcEAQFDEVSADALKSVAIKGNPLPLNQERLVHILKQV 380
Cdd:cd14864 308 asPEEAAIAAVEGVRRLIAQLNLPTrLKDLDL-ASSLEQLAAIAEDAPKLNGLPRSMSSDDIFDILKAA 375
|
|
| PRK15454 |
PRK15454 |
ethanolamine utilization ethanol dehydrogenase EutG; |
13-376 |
2.84e-39 |
|
ethanolamine utilization ethanol dehydrogenase EutG;
Pssm-ID: 185351 [Multi-domain] Cd Length: 395 Bit Score: 145.56 E-value: 2.84e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 13 GDGALSASLSLFNQYGYSVLLVTGNTLERTSVVTDYLdAQSMRYQHIAVS------GEPNIKMVEEAAISARRFKPDMVV 86
Cdd:PRK15454 33 GPGAVSSCGQQAQTRGLKHLFVMADSFLHQAGMTAGL-TRSLAVKGIAMTlwpcpvGEPCITDVCAAVAQLRESGCDGVI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 87 AMGGGSAIDMGKALAAVLPNQGNlyDYVEVVGRNVpLKTKpLPFIAIPTTASTGAEVTKNAVL---KSGQDQVkvsLRSP 163
Cdd:PRK15454 112 AFGGGSVLDAAKAVALLVTNPDS--TLAEMSETSV-LQPR-LPLIAIPTTAGTGSETTNVTVIidaVSGRKQV---LAHA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 164 DMLADVAIVDPTLTHGTNLYLSGRGAMDAFTHLMEAYVCGEPNPLTDMICEEGLRKLSSSVVRACVY-DEPQARSDLAFA 242
Cdd:PRK15454 185 SLMPDVAILDAALTEGVPSHVTAMTGIDALTHAIEAYSALNATPFTDSLAIGAIAMIGKSLPKAVGYgHDLAARESMLLA 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 243 SMLGGMAITNAKLGAAHGLASALGGKISAPHSVITARLAPFVMLENIAVAREekrldilaRYQRIAQiVIGNSEAKEEEA 322
Cdd:PRK15454 265 SCMAGMAFSSAGLGLCHAMAHQPGAALHIPHGLANAMLLPTVMEFNRMVCRE--------RFSQIGR-ALRTKKSDDRDA 335
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1515916685 323 ISWLSEVLDTLKLP-NLQEFGVCEAQFDEVSADALKSVAIKGNPLPLNQERLVHI 376
Cdd:PRK15454 336 INAVSELIAEVGIGkRLGDVGATSAHYGAWAQAALEDICLRSNPRTASLEQIVGL 390
|
|
| PRK09860 |
PRK09860 |
putative alcohol dehydrogenase; Provisional |
4-376 |
6.12e-38 |
|
putative alcohol dehydrogenase; Provisional
Pssm-ID: 182118 [Multi-domain] Cd Length: 383 Bit Score: 141.63 E-value: 6.12e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 4 FMTSTKIIfGDGALSASLSLFNQYGY-SVLLVTGNTLERTSVVTDYLDAQSMR-YQHIAVSG---EPNIKMVEEAAISAR 78
Cdd:PRK09860 7 FIPSVNVI-GADSLTDAMNMMADYGFtRTLIVTDNMLTKLGMAGDVQKALEERnIFSVIYDGtqpNPTTENVAAGLKLLK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 79 RFKPDMVVAMGGGSAIDMGKALAAVLPNQGNLYDYvEVVGRNvplkTKP-LPFIAIPTTASTGAEVTKNAVLKSGQDQVK 157
Cdd:PRK09860 86 ENNCDSVISLGGGSPHDCAKGIALVAANGGDIRDY-EGVDRS----AKPqLPMIAINTTAGTASEMTRFCIITDEARHIK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 158 VSLRSPDMLADVAIVDPTLTHGTNLYLSGRGAMDAFTHLMEAYVCGEPNPLTDMICEEGLRKLSSSVVRACVY-DEPQAR 236
Cdd:PRK09860 161 MAIVDKHVTPLLSVNDSSLMIGMPKSLTAATGMDALTHAIEAYVSIAATPITDACALKAVTMIAENLPLAVEDgSNAKAR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 237 SDLAFASMLGGMAITNAKLGAAHGLASALGGKISAPHSVITARLAPFVMLENIAVAreEKRLDILAryQRIAQIVIGNSE 316
Cdd:PRK09860 241 EAMAYAQFLAGMAFNNASLGYVHAMAHQLGGFYNLPHGVCNAVLLPHVQVFNSKVA--AARLRDCA--AAMGVNVTGKND 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1515916685 317 AKEEEA-ISWLSEVLDTLKLP-NLQEFGVCEAQFDEVSADALKSVAIKGNPLPLNQERLVHI 376
Cdd:PRK09860 317 AEGAEAcINAIRELAKKVDIPaGLRDLNVKEEDFAVLATNALKDACGFTNPIQATHEEIVAI 378
|
|
| MAR |
cd08177 |
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic ... |
7-377 |
1.12e-35 |
|
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: 134.17 E-value: 1.12e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 7 STKIIFGDGALSASLSLFNQYGYSVLLV--TGNTLERTSVVTDYLDAQSMRYQHIAVSGEPnIKMVEEAAISARRFKPDM 84
Cdd:cd08177 1 PQRVVFGAGTLAELAEELERLGARRALVlsTPRQRALAERVAALLGDRVAGVFDGAVMHVP-VEVAERALAAAREAGADG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 85 VVAMGGGSAIDMGKALAavlpnqgnlydyvevvgrnvpLKTKpLPFIAIPTTAStGAEVTknAVLKSGQDQVKVSLRSPD 164
Cdd:cd08177 80 LVAIGGGSAIGLAKAIA---------------------LRTG-LPIVAVPTTYA-GSEMT--PIWGETEDGVKTTGRDPR 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 165 MLADVAIVDPTLTHGTNLYLSGRGAMDAFTHLMEAYVCGEPNPLTDMICEEGLRKLSSSVVRacVYDEPQ---ARSDLAF 241
Cdd:cd08177 135 VLPRTVIYDPDLTLGLPAALSVASGLNALAHAVEALYAPDANPITSLLAEEGIRALARALPR--LVADPSdleARSDALY 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 242 ASMLGGMAITNAKLGAAHGLASALGGKISAPHSVITARLAPFVMLENIAVAREEkrldilarYQRIAQIVIGNSeakeee 321
Cdd:cd08177 213 GAWLAGVVLGSVGMGLHHKLCHVLGGTFDLPHAETHAVVLPHVLAYNAPAAPDA--------MARLARALGGGD------ 278
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1515916685 322 AISWLSEVLDTLKLPN-LQEFGVCEAQFDEVSADALKSVAikGNPLPLNQERLVHIL 377
Cdd:cd08177 279 AAGGLYDLARRLGAPTsLRDLGMPEDDIDRAADLALANPY--PNPRPVERDALRALL 333
|
|
| Fe-ADH-like |
cd14866 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
10-367 |
3.22e-34 |
|
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: 131.20 E-value: 3.22e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 10 IIFGDGALSASLSLFNQYGYS-VLLVTGNTLERTSVVTDYL-DAQSMRYQHI--AVSGEPNIKMVEEAAISARRFKPDMV 85
Cdd:cd14866 8 LFSGRGALARLGRELDRLGARrALVVCGSSVGANPDLMDPVrAALGDRLAGVfdGVRPHSPLETVEAAAEALREADADAV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 86 VAMGGGSAIDMGKALAAVLPNQGNLYDYVEVV---GRNV--PLKTKPLPFIAIPTTASTGAEVTKNAVLKSGQDQvKVSL 160
Cdd:cd14866 88 VAVGGGSAIVTARAASILLAEDRDVRELCTRRaedGLMVspRLDAPKLPIFVVPTTPTTADVKAGSAVTDPPAGQ-RLAL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 161 RSPDMLADVAIVDPTLTHGTNLYLSGRGAMDAFTHLMEAYVCGEPNPLTDMICEEGLRKLSSSVVRACVYDEPQARSDLA 240
Cdd:cd14866 167 FDPKTRPAAVFYDPELLATAPASLVAGAAMNGFDMAVEGLYSRHADPLADATLMHALRLLADGLPRLADDDDPAARADLV 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 241 FASMLGGMAITNAKLGAAHGLASALGGKISAPHSVITARLAPFVMLENIAVAREekRLDILARYQRIAQiviGNSEAKEE 320
Cdd:cd14866 247 LAAVLAGYGTDHTGGGVIHALGHAIGARYGVQNGVVHAILLPHVLRFNAPATDG--RLDRLAEALGVAD---AGDEASAA 321
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1515916685 321 EAISWLSEVLDTLKLPN-LQEFGVCEAQFDEVSADALKSVAIKGNPLP 367
Cdd:cd14866 322 AVVDAVEALLDALGVPTrLRDLGVSREDLPAIAEAAMDDWFMDNNPRP 369
|
|
| 4HBD_NAD |
cd14860 |
4-hydroxybutyrate dehydrogenase, also called gamma-hydroxybutyrate dehydrogenase, catalyzes ... |
49-378 |
1.09e-30 |
|
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: 121.17 E-value: 1.09e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 49 LDAQSMrYQHIAVSGEPNIKMVEEAAISARRFKPDMVVAMGGGSAIDMGKALAavLPNQGNLYDYVEvvgRNVPL-KTKP 127
Cdd:cd14860 47 LDCAVI-FQEKYGTGEPSDEMVEAIYKDIKKYGYKRVIAIGGGTVIDIAKLLA--LKGISPVLDLFD---GKIPLiKEKE 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 128 LpfIAIPTTASTGAEVTKNAVLKSGQDQVKVSLRSPDMLADVAIVDPTLTHGTNLYLSGRGAMDAFTHLMEAYVCGEPNP 207
Cdd:cd14860 121 L--IIVPTTCGTGSEVTNISIVELTSLGTKKGLAVDELYADKAVLIPELLKGLPYKVFATSSIDALIHAIESYLSPKATP 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 208 LTDM-------ICEEGLRKLSSsvvracvyDEPQARS----DLAFASMLGGMAITNAKLGAAHGLASALGGKISAPH--- 273
Cdd:cd14860 199 YTEMfsykaieMILEGYQEIAE--------KGEEARFpllgDFLIASNYAGIAFGNAGCAAVHALSYPLGGKYHVPHgea 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 274 --SVITArlapfvMLENIAVAREEKRLDILARYqrIAQIVignsEAKEEEAISWLSEVLDT-LKLPNLQEFGVCEAQFDE 350
Cdd:cd14860 271 nyAVFTG------VLKNYQEKNPDGEIKKLNEF--LAKIL----GCDEEDVYDELEELLNKiLPKKPLHEYGMKEEEIDE 338
|
330 340 350
....*....|....*....|....*....|
gi 1515916685 351 VSADALKSVA--IKGNPLPLNQERLVHILK 378
Cdd:cd14860 339 FADSVMENQQrlLANNYVPLDREDVAEIYK 368
|
|
| Fe-ADH-like |
cd08186 |
Iron-containing alcohol dehydrogenase; This family contains iron-containing alcohol ... |
8-378 |
6.27e-29 |
|
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: 116.60 E-value: 6.27e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 8 TKIIFGDGALSASLSLFNQYGYS-VLLVTGNTLERTS----VVTDYLDAQSMRYQHIA-VSGEPNIKMVEEAAISARRFK 81
Cdd:cd08186 2 TTLYFGVGAIAKIKDILKDLGIDkVIIVTGRSSYKKSgawdDVEKALEENGIEYVVYDkVTPNPTVDQADEAAKLARDFG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 82 PDMVVAMGGGSAIDMGKALAAVLPNQGNLYDYVeVVGRNVPlkTKPLPFIAIPTTASTGAEVTKNAVLKSGQDQVKVSLR 161
Cdd:cd08186 82 ADAVIAIGGGSPIDTAKSVAVLLAYGGKTARDL-YGFRFAP--ERALPLVAINLTHGTGSEVDRFAVATIPEKGYKPGIA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 162 SPDMLADVAIVDPTLTHG----TNLYLSgrgaMDAFTHLMEAYVCGEPNPLTDMICEEGLRKLSSSVVRACvyDEP---Q 234
Cdd:cd08186 159 YDCIYPLYAIDDPRLTLTlpkeQTLYTS----IDAFNHVYEAATTKVSSPYVITLAKEAIRLIAEYLPRAL--ANPkdlE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 235 ARSDLAFASMLGGMAITNAKLGAAHGLASALGG-KISAPHSVITARLAPFVmLENIAVAREEkrldILAR-YQRIAQIVI 312
Cdd:cd08186 233 ARYWLLYASMIAGIAIDNGLLHLTHALEHPLSGlKPELPHGLGLALLGPAV-VKYIYKAVPE----TLADiLRPIVPGLK 307
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1515916685 313 GNSEAKEEEA---ISWLSEVLDTLKLPNLQeFG------VCEAQFDEVSADALKSVAikgnPLPLNQERLVHILK 378
Cdd:cd08186 308 GTPDEAEKAArgvEEFLFSVGFTEKLSDYG-FTeddvdrLVELAFTTPSLDLLLSLA----PVEVTEEVVREIYE 377
|
|
| Fe-ADH_KdnB-like |
cd08184 |
Iron-containing alcohol dehydrogenase similar to Shewanella oneidensis KdnB required for Kdo8N ... |
8-275 |
4.00e-26 |
|
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: 108.12 E-value: 4.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 8 TKIIFGDGALSASLSLFNQY-----GYSVLLVTGNTLERTSVvtDYLDAQSMRYQH-IAVSGEPNIKMVEE--AAISARR 79
Cdd:cd08184 2 PKYLFGRGSFDQLGELLAERrksnnDYVVFFIDDVFKGKPLL--DRLPLQNGDLLIfVDTTDEPKTDQIDAlrAQIRAEN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 80 FK-PDMVVAMGGGSAIDMGKALAAVLPNQGNLYDYvevVGRNVpLKTKPLPFIAIPTTASTGAEVTKNAVLKSgqDQVKV 158
Cdd:cd08184 80 DKlPAAVVGIGGGSTMDIAKAVSNMLTNPGSAADY---QGWDL-VKNPGIYKIGVPTLSGTGAEASRTAVLTG--PEKKL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 159 SLRSPDMLADVAIVDPTLTHGT---NLYLSGrgaMDAFTHLMEAYVCGEPNPLTDMICEEGLrKLSSSVVRACVYDEPQA 235
Cdd:cd08184 154 GINSDYTVFDQVILDPELIATVprdQYFYTG---MDCYIHCVESLNGTYRNAFGDAYAEKAL-ELCRDVFLSDDMMSPEN 229
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1515916685 236 RSDLAFASMLGGMAITNAKLGAAHGLASALGGKISAPHSV 275
Cdd:cd08184 230 REKLMVASYLGGSSIANSQVGVCHALSYGLSVVLGTHHGV 269
|
|
| DHQ_Fe-ADH |
cd07766 |
Dehydroquinate synthase-like (DHQ-like) and iron-containing alcohol dehydrogenases (Fe-ADH); ... |
8-297 |
1.70e-17 |
|
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: 82.03 E-value: 1.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 8 TKIIFGDGALSASLSLFNQYGYSVLLVTGNTLERTSV--VTDYLDAQSMRYQHIAVSGEPNIKMVEEAAISARRFKPDMV 85
Cdd:cd07766 2 TRIVFGEGAIAKLGEIKRRGFDRALVVSDEGVVKGVGekVADSLKKGLAVAIFDFVGENPTFEEVKNAVERARAAEADAV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 86 VAMGGGSAIDMGKALAAVLPNQgnlydyvevvgrnvplktkpLPFIAIPTTASTGAEVTKNAVLKSgqDQVKVSLRSPDM 165
Cdd:cd07766 82 IAVGGGSTLDTAKAVAALLNRG--------------------IPFIIVPTTASTDSEVSPKSVITD--KGGKNKQVGPHY 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 166 LADVAIVDPTLTHGTNLYLSGRGAMDAFTHLMEayvcgepnpltdmiceeglrklsssvvracvydepqaRSDLAFASML 245
Cdd:cd07766 140 NPDVVFVDTDITKGLPPRQVASGGVDALAHAVE-------------------------------------LEKVVEAATL 182
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1515916685 246 GGMAITNAK-LGAAHGLASALGGKISAPHSVITARLAPFVmlenIAVAREEKR 297
Cdd:cd07766 183 AGMGLFESPgLGLAHAIGHALTAFEGIPHGEAVAVGLPYV----LKVANDMNP 231
|
|
| GldA |
COG0371 |
Glycerol dehydrogenase or related enzyme, iron-containing ADH family [Energy production and ... |
9-172 |
1.91e-16 |
|
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: 80.21 E-value: 1.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 9 KIIFGDGALSASLSLFNQYGYSVLLVTG-NTLERTS-VVTDYLDAQSMRYQHIAVSGEPNIKMVEEAAISARRFKPDMVV 86
Cdd:COG0371 8 RYVQGEGALDELGEYLADLGKRALIITGpTALKAAGdRLEESLEDAGIEVEVEVFGGECSEEEIERLAEEAKEQGADVII 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 87 AMGGGSAIDMGKALAAvlpnqgnlydyvevvgrnvplKTKpLPFIAIPTTASTGAEVTKNAVLKSGQDQVKVSL---RSP 163
Cdd:COG0371 88 GVGGGKALDTAKAVAY---------------------RLG-LPVVSVPTIASTDAPASPLSVIYTEDGAFDGYSflaKNP 145
|
170
....*....|
gi 1515916685 164 DM-LADVAIV 172
Cdd:COG0371 146 DLvLVDTDII 155
|
|
| PRK15138 |
PRK15138 |
alcohol dehydrogenase; |
2-343 |
1.95e-13 |
|
alcohol dehydrogenase;
Pssm-ID: 185092 [Multi-domain] Cd Length: 387 Bit Score: 71.36 E-value: 1.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 2 FQFMTSTKIIFGDGALSASLSLFNQYGYSVLLVTGNTLERTSVVTDYLDAQSMRYQHIAVSGEPN------IKMVEeaai 75
Cdd:PRK15138 4 FNLHTPTRILFGKGAIAGLREQIPADARVLITYGGGSVKKTGVLDQVLDALKGMDVLEFGGIEPNptyetlMKAVK---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 76 SARRFKPDMVVAMGGGSAIDMGK--ALAAVLPNQGNLYDYVEVVGRNVplkTKPLPFIAIPTTASTGAEVTKNAVLKSGQ 153
Cdd:PRK15138 80 LVREEKITFLLAVGGGSVLDGTKfiAAAANYPENIDPWHILETGGKEI---KSAIPMGSVLTLPATGSESNAGAVISRKT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 154 DQVKVSLRSPDMLADVAIVDPTLTHGTNLYLSGRGAMDAFTHLMEAYVCGEPN-PLTDMICEEGLRKLSSSVVRACVydE 232
Cdd:PRK15138 157 TGDKQAFHSPHVQPVFAVLDPVYTYTLPPRQVANGVVDAFVHTVEQYVTYPVDaKIQDRFAEGILLTLIEEGPKALK--E 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 233 PQ---ARSDLAFASMlggMAItNAKLGAA-------HglasALGGKISAPHSVITARLAPFVMLENIAVAREEKRLDILA 302
Cdd:PRK15138 235 PEnydVRANVMWAAT---QAL-NGLIGAGvpqdwatH----MLGHELTAMHGLDHAQTLAIVLPALWNEKRDTKRAKLLQ 306
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1515916685 303 RYQRIAQIVIGNSEAKEEEAISWLSEVLDTLKLPN-LQEFGV 343
Cdd:PRK15138 307 YAERVWNITEGSDDERIDAAIAATRNFFEQMGVPTrLSDYGL 348
|
|
| GlyDH |
cd08170 |
Glycerol dehydrogenases (GlyDH) catalyzes oxidation of glycerol to dihydroxyacetone in ... |
13-172 |
1.07e-11 |
|
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: 65.90 E-value: 1.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 13 GDGALSASLSLFNQYGYSVLLVTGNTLERT--SVVTDYLDAQSMRYQHIAVSGEPNIKMVEEAAISARRFKPDMVVAMGG 90
Cdd:cd08170 7 GPGALDRLGEYLAPLGKKALVIADPFVLDLvgERLEESLEKAGLEVVFEVFGGECSREEIERLAAIARANGADVVIGIGG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 91 GSAIDMGKALAavlpnqgnlyDYVEvvgrnvplktkpLPFIAIPTTASTGAEVTKNAVLKS--GQ-DQVKVSLRSPDM-L 166
Cdd:cd08170 87 GKTIDTAKAVA----------DYLG------------LPVVIVPTIASTDAPCSALSVIYTedGEfDEYLFLPRNPDLvL 144
|
....*.
gi 1515916685 167 ADVAIV 172
Cdd:cd08170 145 VDTEII 150
|
|
| GlyDH-like |
cd08550 |
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins. ... |
8-172 |
1.15e-10 |
|
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: 62.55 E-value: 1.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 8 TKIIFGDGALSASLSLFNQYGYSVLLVTGNT-LERTS-VVTDYLDAQSMRYQHIAVSGEPNIKMVEEAAISARRFKPDMV 85
Cdd:cd08550 2 GRYIQEPGILAKAGEYIAPLGKKALIIGGKTaLEAVGeKLEKSLEEAGIDYEVEVFGGECTEENIERLAEKAKEEGADVI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 86 VAMGGGSAIDMGKALAAVLpnqgnlydyvevvgrnvplktkPLPFIAIPTTASTGAEVTKNAVLKS---GQDQVKVSLRS 162
Cdd:cd08550 82 IGIGGGKVLDTAKAVADRL----------------------GLPVVTVPTIAATCAAWSALSVLYDeegEFLGYSLLKRS 139
|
170
....*....|.
gi 1515916685 163 PDM-LADVAIV 172
Cdd:cd08550 140 PDLvLVDTDII 150
|
|
| Gro1PDH |
cd08173 |
Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) catalyzes the reversible conversion between ... |
9-172 |
2.66e-10 |
|
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: 61.41 E-value: 2.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 9 KIIFGDGALSASLSLFNQ--YGYSVLLVTGNTLERT--SVVTDYLDAQSMRYQHIAVSGEPNIKMVEEAAISARRFKPDM 84
Cdd:cd08173 4 NVVVGHGAINKIGEVLKKllLGKRALIITGPNTYKIagKRVEDLLESSGVEVVIVDIATIEEAAEVEKVKKLIKESKADF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 85 VVAMGGGSAIDMGKALAAvlpnqgnlydyvevvgrnvplKTKpLPFIAIPTTASTGAEVTKNAVLKSGQDQVKVSLRSP- 163
Cdd:cd08173 84 IIGVGGGKVIDVAKYAAY---------------------KLN-LPFISIPTSASHDGIASPFASIKGGDKPYSIKAKAPi 141
|
....*....
gi 1515916685 164 DMLADVAIV 172
Cdd:cd08173 142 AIIADTEII 150
|
|
| Fe-ADH_2 |
pfam13685 |
Iron-containing alcohol dehydrogenase; |
11-265 |
1.31e-09 |
|
Iron-containing alcohol dehydrogenase;
Pssm-ID: 404557 [Multi-domain] Cd Length: 251 Bit Score: 58.47 E-value: 1.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 11 IFGDGALSASLSLFNQYGYS-VLLVTGNTLERT--SVVTDYLDAQSMRYQHIA-VSGEPNIKMVEEAAISARRFKPDMVV 86
Cdd:pfam13685 1 VIGPGALGRLGEYLAELGFRrVALVADANTYAAagRKVAESLKRAGIEVETRLeVAGNADMETAEKLVGALRERDADAVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 87 AMGGGSAIDMGKALAAVLPnqgnlydyvevvgrnvplktkpLPFIAIPTTASTGAEVTKNAVLKSGQDQVKVSLRSP-DM 165
Cdd:pfam13685 81 GVGGGTVIDLAKYAAFKLG----------------------KPFISVPTAASNDGFASPGASLTVDGKKRSIPAAAPfGV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 166 LADVAIVdptLTHGTNLYLSGRGAMDA-FTHLM--EAYVCGEPN----PLTDMICEEGLRKLSSSVvracvyDEPQARSD 238
Cdd:pfam13685 139 IADTDVI---AAAPRRLLASGVGDLLAkITAVAdwELAHAEEVAaplaLLSAAMVMNFADRPLRDP------GDIEALAE 209
|
250 260
....*....|....*....|....*..
gi 1515916685 239 LAFASMLGGMAITNAKLGAAHGLASAL 265
Cdd:pfam13685 210 LLSALAMGGAGSSRPASGSEHLISHAL 236
|
|
| egsA |
PRK00843 |
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed |
1-172 |
2.52e-05 |
|
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed
Pssm-ID: 179139 Cd Length: 350 Bit Score: 46.04 E-value: 2.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 1 MFQFMTST----KIIFGDGALSASLSLFNQY--GYSVLLVTGNTLERTSV--VTDYLDAQSMryQHIAVSGEPNIKMVEE 72
Cdd:PRK00843 1 MFEKSHWIqlprDVVVGHGVLDDIGDVCSDLklTGRALIVTGPTTKKIAGdrVEENLEDAGD--VEVVIVDEATMEEVEK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 73 AAISARRFKPDMVVAMGGGSAIDMGKaLAAVLPNqgnlydyvevvgrnvplktkpLPFIAIPTTASTGAEVTKNAVLKSG 152
Cdd:PRK00843 79 VEEKAKDVNAGFLIGVGGGKVIDVAK-LAAYRLG---------------------IPFISVPTAASHDGIASPRASIKGG 136
|
170 180
....*....|....*....|.
gi 1515916685 153 QDQVKVSLRSP-DMLADVAIV 172
Cdd:PRK00843 137 GKPVSVKAKPPlAVIADTEII 157
|
|
| GlyDH-like |
cd08172 |
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins ... |
13-176 |
2.57e-05 |
|
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins that have yet to be characterized, but show sequence homology with glycerol dehydrogenase. 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: 341451 [Multi-domain] Cd Length: 346 Bit Score: 45.97 E-value: 2.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 13 GDGALSASLSLFNQYGYS-VLLVTGNT-LErtsVVTDYLDA-QSMRYQHIAVSGEPNIKMVEEAAISARRFKPDMVVAMG 89
Cdd:cd08172 7 EEGALKELPELLSEFGIKrPLIIHGEKsWQ---AAKPYLPKlFEIEYPVLRYDGECSYEEIDRLAEEAKEHQADVIIGIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 90 GGSAIDMGKALAAVLPnqgnlydyvevvgrnvplktkpLPFIAIPTTASTGAEVTKNAVL--KSGQ-DQVKVSLRSPDML 166
Cdd:cd08172 84 GGKVLDTAKAVADKLN----------------------IPLILIPTLASNCAAWTPLSVIydEDGEfIGYDYFPRSAYLV 141
|
170
....*....|
gi 1515916685 167 advaIVDPTL 176
Cdd:cd08172 142 ----LVDPRL 147
|
|
| G1PDH-like |
cd08174 |
Glycerol-1-phosphate dehydrogenase-like; These glycerol-1-phosphate dehydrogenase-like ... |
31-150 |
4.19e-05 |
|
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: 45.20 E-value: 4.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 31 VLLVTGNTLER--TSVVTDYLDAQSMRYQhiaVSGEPNIKMVEEAAISARRFKPDMVVAMGGGSAIDMGKALAAVLpnqg 108
Cdd:cd08174 28 VAIVTGEGIDEllGEDILESLEEAGEIVT---VEENTDNSAEELAEKAFSLPKVDAIVGIGGGKVLDVAKYAAFLS---- 100
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1515916685 109 nlydyvevvgrnvplktkPLPFIAIPTTASTGAEVTKNAVLK 150
Cdd:cd08174 101 ------------------KLPFISVPTSLSNDGIASPVAVLK 124
|
|
| GlyDH-like |
cd08171 |
Glycerol dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins ... |
83-149 |
2.08e-03 |
|
Glycerol dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins that have yet to be characterized, but show sequence homology with glycerol dehydrogenase. 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: 341450 Cd Length: 345 Bit Score: 40.20 E-value: 2.08e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1515916685 83 DMVVAMGGGSAIDMGKALAAVLpnqgnlydyvevvgrNVPLKTkplpfiaIPTTASTGAEVTKNAVL 149
Cdd:cd08171 80 DMIFAVGGGKAIDTVKVLADRL---------------NKPVFT-------FPTIASNCAAVTAVSVM 124
|
|
| AroB |
COG0337 |
3-dehydroquinate synthetase [Amino acid transport and metabolism]; 3-dehydroquinate synthetase ... |
7-148 |
2.18e-03 |
|
3-dehydroquinate synthetase [Amino acid transport and metabolism]; 3-dehydroquinate synthetase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis
Pssm-ID: 440106 Cd Length: 355 Bit Score: 40.07 E-value: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 7 STKIIFGDGALSASLSLFNQY--GYSVLLVTGNTLERT--SVVTDYLDAQSMRYQHIAV-SGEP--NIKMVE---EAAIS 76
Cdd:COG0337 12 SYDIRIGRGLLDELGELLAELlkGRRVLVVTDENVAPLygERLRAALEAAGFEVHLLVLpDGEAskTLETLErilDALLE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 77 A---RRfkpDMVVAMGGGSAIDMGKALAAVLpnqgnlydyvevvGRNVplktkplPFIAIPTT------ASTGAevtKNA 147
Cdd:COG0337 92 AgldRD---DLVVALGGGVVGDLAGFAAATY-------------LRGV-------PFIQVPTTllaqvdSSVGG---KTG 145
|
.
gi 1515916685 148 V 148
Cdd:COG0337 146 V 146
|
|
| DHQS |
cd08195 |
Dehydroquinate synthase (DHQS) catalyzes the conversion of DAHP to DHQ in shikimate pathway ... |
7-136 |
4.84e-03 |
|
Dehydroquinate synthase (DHQS) catalyzes the conversion of DAHP to DHQ in shikimate pathway for aromatic compounds synthesis; 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, which involves seven sequential enzymatic steps in the conversion of erythrose 4-phosphate and phosphoenolpyruvate into chorismate for subsequent synthesis of aromatic compounds, is found in bacteria, microbial eukaryotes, and plants, but not in mammals. Therefore, enzymes of this pathway are attractive targets for the development of non-toxic antimicrobial compounds, herbicides and anti-parasitic agents. The activity of DHQS requires nicotinamide adenine dinucleotide (NAD) as cofactor. A single active site in DHQS catalyzes five sequential reactions involving alcohol oxidation, phosphate elimination, carbonyl reduction, ring opening, and intramolecular aldol condensation. The binding of substrates and ligands induces domain conformational changes. In some fungi and protozoa, this domain is fused with the other four domains in shikimate pathway and forms a penta-domain AROM protein, which catalyzes steps 2-6 in the shikimate pathway.
Pssm-ID: 341474 Cd Length: 343 Bit Score: 38.96 E-value: 4.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 7 STKIIFGDGALSASLSLFNQYGYS-VLLVTGNTLERT--SVVTDYLDAQSMRYQHIAV-SGEP--NIKMVE---EAAISA 77
Cdd:cd08195 1 SYPILIGSGLLDKLGELLELKKGSkVVIVTDENVAKLygELLLKSLEAAGFKVEVIVIpAGEKskSLETVEriyDFLLEA 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1515916685 78 RRFKPDMVVAMGGGSAIDMGKALAAVLpNQGnlydyvevvgrnvplktkpLPFIAIPTT 136
Cdd:cd08195 81 GLDRDSLLIALGGGVVGDLAGFVASTY-MRG-------------------IPFIQVPTT 119
|
|
| G1PDH_related |
cd08549 |
Glycerol-1-phosphate dehydrogenase and related proteins; This family contains bacterial and ... |
83-172 |
8.03e-03 |
|
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: 38.31 E-value: 8.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 83 DMVVAMGGGSAIDMGKALAAVLpnqgnlydyvevvgrnvplktkPLPFIAIPTTASTGAEVTKNAVLKSGQDQVKVSLRS 162
Cdd:cd08549 72 DCVIGIGGGRSIDTGKYLAYKL----------------------KIPFISVPTSASNDGIASPIVSLRIPGVKKTFMADA 129
|
90
....*....|.
gi 1515916685 163 PD-MLADVAIV 172
Cdd:cd08549 130 PIaIIADTEII 140
|
|
| gldA |
PRK09423 |
glycerol dehydrogenase; Provisional |
9-172 |
8.61e-03 |
|
glycerol dehydrogenase; Provisional
Pssm-ID: 181843 Cd Length: 366 Bit Score: 38.26 E-value: 8.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 9 KIIFGDGALSASLSLFNQYGYSVLLVTGNT-LERT-SVVTDYLDAQSMRYQHIAVSGEPNIKMVEEAAISARRFKPDMVV 86
Cdd:PRK09423 10 KYVQGKGALARLGEYLKPLGKRALVIADEFvLGIVgDRVEASLKEAGLTVVFEVFNGECSDNEIDRLVAIAEENGCDVVI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1515916685 87 AMGGGSAIDMGKALAavlpnqgnlyDYVEVvgrnvplktkplPFIAIPTTASTGAEVTKNAVLKSGQDQVKVSL---RSP 163
Cdd:PRK09423 90 GIGGGKTLDTAKAVA----------DYLGV------------PVVIVPTIASTDAPTSALSVIYTEEGEFERYLflpKNP 147
|
170
....*....|
gi 1515916685 164 DM-LADVAIV 172
Cdd:PRK09423 148 DLvLVDTAII 157
|
|
| |
