|
Name |
Accession |
Description |
Interval |
E-value |
| Fe-ADH |
cd08551 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains large ... |
6-374 |
1.36e-135 |
|
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: 391.81 E-value: 1.36e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 6 STLISGAGAFTALLPLLT--GKQRILLVTDANVGKLDAARQIRTLLEDEGRQVQIVDSVPAEPSQHDMTQILRLVSANQP 83
Cdd:cd08551 2 TRIVFGAGALARLGEELKalGGKKVLLVTDPGLVKAGLLDKVLESLKAAGIEVEVFDDVEPNPTVETVEAAAELAREEGA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 84 ELIVGIGGGSVLDVAKLLSVLLHPDSPGLEALLAGEKPQQKVTSLLIPATAGTGSEATPNAILAIPEQNTKVGIISPVLL 163
Cdd:cd08551 82 DLVIAVGGGSVLDTAKAIAVLATNGGSIRDYEGIGKVPKPGLPLIAIPTTAGTGSEVTPNAVITDPETGRKMGIVSPYLL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 164 PDYVALLPELTTSMPAHIASSTGIDALCHLIECFTSTVANPVSDNAALIGLRKLVRNIELSVSEPHNLAAKLEMLWASYY 243
Cdd:cd08551 162 PDVAILDPELTLSLPPSVTAATGMDALTHAIEAYTSKKANPISDALALEAIRLIGKNLRRAVADGSDLEAREAMLLASLL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 244 GGVAINHAGTHLVHALSYPLGGKYHLPHGVANAILLAPCMKVVRPHAVAKFAQVWDLLPEADLTLSEEEKSHALVAWLAA 323
Cdd:cd08551 242 AGIAFGNAGLGAVHALAYPLGGRYHIPHGVANAILLPYVMEFNLPACPEKYAEIAEALGEDVEGLSDEEAAEAAVEAVRE 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 490214900 324 LVKRLQLPDNLAALGVPPESISELSEAALNVKRLLNNAPCSVNQDQVEAVY 374
Cdd:cd08551 322 LLRDLGIPTSLSELGVTEEDIPELAEDAMKSGRLLSNNPRPLTEEDIREIY 372
|
|
| EutG |
COG1454 |
Alcohol dehydrogenase, class IV [Energy production and conversion]; |
3-378 |
1.71e-126 |
|
Alcohol dehydrogenase, class IV [Energy production and conversion];
Pssm-ID: 441063 [Multi-domain] Cd Length: 381 Bit Score: 369.06 E-value: 1.71e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 3 TINSTLISGAGAFTALLPLLT--GKQRILLVTDANVGKLDAARQIRTLLEDEGRQVQIVDSVPAEPSQHDMTQILRLVSA 80
Cdd:COG1454 6 RLPTRIVFGAGALAELGEELKrlGAKRALIVTDPGLAKLGLLDRVLDALEAAGIEVVVFDDVEPNPTVETVEAGAAAARE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 81 NQPELIVGIGGGSVLDVAKLLSVLL-HPDSpgLEALLAGEKPQQKVTSL-LIPATAGTGSEATPNAILAIPEQNTKVGII 158
Cdd:COG1454 86 FGADVVIALGGGSAIDAAKAIALLAtNPGD--LEDYLGIKKVPGPPLPLiAIPTTAGTGSEVTPFAVITDPETGVKKGIA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 159 SPVLLPDYVALLPELTTSMPAHIASSTGIDALCHLIECFTSTVANPVSDNAALIGLRKLVRNIELSVSEPHNLAAKLEML 238
Cdd:COG1454 164 DPELLPDVAILDPELTLTLPPSLTAATGMDALTHAIEAYVSKGANPLTDALALEAIRLIARNLPRAVADGDDLEAREKMA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 239 WASYYGGVAINHAGTHLVHALSYPLGGKYHLPHGVANAILLAPCMKVVRPHAVAKFAQVWDLLpEADLTLSEEEKSHALV 318
Cdd:COG1454 244 LASLLAGMAFANAGLGAVHALAHPLGGLFHVPHGLANAILLPHVLRFNAPAAPERYAEIARAL-GLDVGLSDEEAAEALI 322
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 319 AWLAALVKRLQLPDNLAALGVPPESISELSEAALnVKRLLNNAPCSVNQDQVEAVYRTLF 378
Cdd:COG1454 323 EAIRELLRDLGIPTRLSELGVTEEDLPELAELAL-ADRCLANNPRPLTEEDIEAILRAAY 381
|
|
| Fe-ADH |
pfam00465 |
Iron-containing alcohol dehydrogenase; |
5-370 |
4.21e-110 |
|
Iron-containing alcohol dehydrogenase;
Pssm-ID: 425696 [Multi-domain] Cd Length: 362 Bit Score: 326.48 E-value: 4.21e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 5 NSTLISGAGAFTALLPLLTG-KQRILLVTDANVGKLDAARQIRTLLEDEGRQVQIVDSVPAEPSQHDMTQILRLVSANQP 83
Cdd:pfam00465 1 PTRIVFGAGALAELGEELKRlGARALIVTDPGSLKSGLLDKVLASLEEAGIEVVVFDGVEPEPTLEEVDEAAALAREAGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 84 ELIVGIGGGSVLDVAKLLSVLLHPDSPGLEALLAGEKPQQKVTSLLIPATAGTGSEATPNAILAIPEQNTKVGIISPVLL 163
Cdd:pfam00465 81 DVIIAVGGGSVIDTAKAIALLLTNPGDVWDYLGGKPLTKPALPLIAIPTTAGTGSEVTPLAVITDTETGEKLGIFSPKLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 164 PDYVALLPELTTSMPAHIASSTGIDALCHLIECFTSTVANPVSDNAALIGLRKLVRNIELSVSEPHNLAAKLEMLWASYY 243
Cdd:pfam00465 161 PDLAILDPELTLTLPPRLTAATGMDALAHAVEAYVSKGANPLTDALALEAIRLIAENLPRAVADGEDLEARENMLLASTL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 244 GGVAINHAGTHLVHALSYPLGGKYHLPHGVANAILLAPCMKVVRPHAVAKFAQVWDLLPEAdltlSEEEKSHALVAWLAA 323
Cdd:pfam00465 241 AGLAFSNAGLGAAHALAHALGGRYGIPHGLANAILLPYVLRFNAPAAPEKLAQLARALGED----SDEEAAEEAIEALRE 316
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 490214900 324 LVKRLQLPDNLAALGVPPESISELSEAALNVKRLLNNaPCSVNQDQV 370
Cdd:pfam00465 317 LLRELGLPTTLSELGVTEEDLDALAEAALRDRSLANN-PRPLTAEDI 362
|
|
| HVD |
cd08193 |
5-hydroxyvalerate dehydrogenase (HVD) catalyzes the oxidation of 5-hydroxyvalerate to ... |
6-378 |
2.89e-95 |
|
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: 289.41 E-value: 2.89e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 6 STLISGAGAFTALLPLLT--GKQRILLVTDANVGKLDAARQIRTLLEDEGRQVQIVDSVPAEPSQHDMTQILRLVSANQP 83
Cdd:cd08193 5 PRIICGAGAAARLGELLRelGARRVLLVTDPGLVKAGLADPALAALEAAGIAVTVFDDVVADPPEAVVEAAVEQAREAGA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 84 ELIVGIGGGSVLDVAKLLSVLLHPDSPgLEALLAGEKPQ-QKVTSLLIPATAGTGSEATPNAILAIPEQnTKVGIISPVL 162
Cdd:cd08193 85 DGVIGFGGGSSMDVAKLVALLAGSDQP-LDDIYGVGKATgPRLPLILVPTTAGTGSEVTPISIVTTGET-EKKGVVSPQL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 163 LPDyVALL-PELTTSMPAHIASSTGIDALCHLIECFTSTVA-NPVSDNAALIGLRKLVRNIELSVSEPHNLAAKLEMLWA 240
Cdd:cd08193 163 LPD-VALLdAELTLGLPPHVTAATGIDAMVHAIEAYTSRHKkNPISDALAREALRLLGANLRRAVEDGSDLEAREAMLLG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 241 SYYGGVAINHAGTHLVHALSYPLGGKYHLPHGVANAILLAPCMKVVRPHAVAKFAQVWDLLPEADLTLSEEEKSHALVAW 320
Cdd:cd08193 242 SMLAGQAFANAPVAAVHALAYPLGGHFHVPHGLSNALVLPHVLRFNLPAAEALYAELARALLPGLAFGSDAAAAEAFIDA 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 490214900 321 LAALVKRLQLPDNLAALGVPPESISELSEAALNVKRLLNNAPCSVNQDQVEAVYRTLF 378
Cdd:cd08193 322 LEELVEASGLPTRLRDVGVTEEDLPMLAEDAMKQTRLLVNNPREVTEEDALAIYQAAL 379
|
|
| Fe-ADH-like |
cd08194 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
6-378 |
3.93e-89 |
|
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: 273.64 E-value: 3.93e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 6 STLISGAGAFTALLPLL--TGKQRILLVTDANVGKLDAARQIRTLLEDEGRQVQIVDSVPAEPSQHDMTQILRLVSANQP 83
Cdd:cd08194 2 RTIIIGGGALEELGEEAasLGGKRALIVTDKVMVKLGLVDKVTQLLAEAGIAYAVFDDVVSEPTDEMVEEGLALYKEGGC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 84 ELIVGIGGGSVLDVAKLLSVLLHPDSPgLEALLAGEKPQQKVTSLL-IPATAGTGSEATPNAILAIPEQNTKVGIISPVL 162
Cdd:cd08194 82 DFIVALGGGSPIDTAKAIAVLATNGGP-IRDYMGPRKVDKPGLPLIaIPTTAGTGSEVTRFTVITDTETDVKMLLKGPAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 163 LPDyVALL-PELTTSMPAHIASSTGIDALCHLIECFTSTVANPVSDNAALIGLRKLVRNIELSVSEPHNLAAKLEMLWAS 241
Cdd:cd08194 161 LPA-VAIVdPELTLSMPPRVTAATGIDALTHAIEAYVSRKAQPLTDTLALSAIKLIGRNLRRAYADGDDLEAREAMMLAA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 242 YYGGVAINHAGTHLVHALSYPLGGKYHLPHGVANAILLAPCMKVVRPHAVAKFAQVWDLLPEADLTLSEEEKSHALVAWL 321
Cdd:cd08194 240 LEAGIAFSNSSVALVHGMSRPIGALFHVPHGLSNAMLLPAVTEFSLPGAPERYAEIARAMGIATEGDSDEEAAEKLVEAL 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490214900 322 AALVKRLQLPdNLAALGVPPE----SISELSEAALNVKRLLNNaPCSVNQDQVEAVYRTLF 378
Cdd:cd08194 320 ERLCADLEIP-TLREYGIDEEefeaALDKMAEDALASGSPANN-PRVPTKEEIIELYREAW 378
|
|
| Fe-ADH-like |
cd14863 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
3-378 |
4.80e-89 |
|
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: 273.26 E-value: 4.80e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 3 TINSTLISGAGAFTALLPLLT--GKQRILLVTDANVGKLDAARQIRTLLEDEGRQVQIVDSVPAEPSQHDMTQILRLVSA 80
Cdd:cd14863 3 SQLTPVIFGAGAVEQIGELLKelGCKKVLLVTDKGLKKAGIVDKIIDLLEEAGIEVVVFDDVEPDPPDEIVDEAAEIARE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 81 NQPELIVGIGGGSVLDVAKLLSVLLHPDSPGLEALLAGEKPQQK-VTSLLIPATAGTGSEATPNAILAIPEQNTKVGIIS 159
Cdd:cd14863 83 EGADGVIGIGGGSVLDTAKAIAVLLTNPGPIIDYALAGPPVPKPgIPLIAIPTTAGTGSEVTPIAVITDEENGVKKSLLG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 160 PVLLPDYVALLPELTTSMPAHIASSTGIDALCHLIECFTSTVANPVSDNAALIGLRKLVRNIELSVSEPHNLAAKLEMLW 239
Cdd:cd14863 163 PFLVPDLAILDPELTVGLPPSLTAATGMDALSHAIEAYTSKLANPMTDALALQAIRLIVKNLPRAVKDGDNLEARENMLL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 240 ASYYGGVAINHAGTHLVHALSYPLGGKYHLPHGVANAILLAPCMKVVRPHAVAKFAQVWDLLPEADLTLSEEEKSHALVA 319
Cdd:cd14863 243 ASNLAGIAFNNAGTHIGHAIAHALGALYHIPHGLACALALPVVLEFNAEAYPEKVKKIAKALGVSFPGESDEELGEAVAD 322
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 490214900 320 WLAALVKRLQLPDNLAALGVPPESISELSEAALNvKRLLNNAPCSVNQDQVEAVYRTLF 378
Cdd:cd14863 323 AIREFMKELGIPSLFEDYGIDKEDLDKIAEAVLK-DPFAMFNPRPITEEEVAEILEAIY 380
|
|
| HOT |
cd08190 |
Hydroxyacid-oxoacid transhydrogenase (HOT) involved in gamma-hydroxybutyrate metabolism; This ... |
24-375 |
4.99e-84 |
|
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: 261.33 E-value: 4.99e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 24 GKQRILLVTDANVGKLDAARQIRTLLEDEGRQVQIVDSVPAEPSQHDMTQILRLVSANQPELIVGIGGGSVLDVAKLLSV 103
Cdd:cd08190 22 GAKKVLVVTDPGLAKLGLVERVLESLEKAGIEVVVYDGVRVEPTDESFEEAIEFAKEGDFDAFVAVGGGSVIDTAKAANL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 104 LL-HPdspglEALLA--------GEKPQQKVTSLL-IPATAGTGSEATPNAILAIPEQNTKVGIISPVLLPDyVALL-PE 172
Cdd:cd08190 102 YAtHP-----GDFLDyvnapigkGKPVPGPLKPLIaIPTTAGTGSETTGVAIFDLEELKVKTGISSRYLRPT-LAIVdPL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 173 LTTSMPAHIASSTGIDALCHLIECFTSTV------------------ANPVSDNAALIGLRKLVRNIELSVSEPHNLAAK 234
Cdd:cd08190 176 LTLTLPPRVTASSGFDVLCHALESYTARPynarprpanpderpayqgSNPISDVWAEKAIELIGKYLRRAVNDGDDLEAR 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 235 LEMLWASYYGGVAINHAGTHLVHALSYPLGG-------------KYHLPHGVANAILLAPCMKVVRPHAVAKFAQVWDLL 301
Cdd:cd08190 256 SNMLLASTLAGIGFGNAGVHLPHAMAYPIAGlvkdyrppgypvdHPHVPHGLSVALTAPAVFRFTAPACPERHLEAAELL 335
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490214900 302 PEADLTLSEEEKSHALVAWLAALVKRLQLPDNLAALGVPPESISELSEAALNVKRLLNNAPCSVNQDQVEAVYR 375
Cdd:cd08190 336 GADTSGASDRDAGEVLADALIKLMRDIGIPNGLSALGYSEDDIPALVEGTLPQQRLLKLNPRPVTEEDLEEIFE 409
|
|
| Fe-ADH-like |
cd08183 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
11-373 |
8.60e-84 |
|
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: 259.74 E-value: 8.60e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 11 GAGAFtALLPLLTGK--QRILLVTDANVGKLDAARQIRTLLEDEGRQVQIVdSVPAEPSQHDMTQILRLVSANQPELIVG 88
Cdd:cd08183 7 GRGSL-QELGELAAElgKRALLVTGRSSLRSGRLARLLEALEAAGIEVALF-SVSGEPTVETVDAAVALAREAGCDVVIA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 89 IGGGSVLDVAKLLSVLL-HPDSPG--LEALLAGEKPQQKVTSLL-IPATAGTGSEATPNAILAIPEQNTKVGIISPVLLP 164
Cdd:cd08183 85 IGGGSVIDAAKAIAALLtNEGSVLdyLEVVGKGRPLTEPPLPFIaIPTTAGTGSEVTKNAVLSSPEHGVKVSLRSPSMLP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 165 DYVALLPELTTSMPAHIASSTGIDALCHLIECFTSTVANPVSDNAALIGLRKLVRNIELSVSEPHNLAAKLEMLWASYYG 244
Cdd:cd08183 165 DVALVDPELTLSLPPEVTAASGLDALTQLIEPYVSRKANPLTDALAREGLRLAARSLRRAYEDGEDLEAREDMALASLLG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 245 GVAINHAGTHLVHALSYPLGGKYHLPHGVANAILLAPCMKVVRPHAVAKF----AQVWDLLPEADLTLSEEEKSHALVAW 320
Cdd:cd08183 245 GLALANAGLGAVHGLAGPLGGMFGAPHGAICAALLPPVLEANLRALREREpdspALARYRELAGILTGDPDAAAEDGVEW 324
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 490214900 321 LAALVKRLQLPDnLAALGVPPESISELSEAALNVKRLLNNaPCSVNQDQVEAV 373
Cdd:cd08183 325 LEELCEELGIPR-LSEYGLTEEDFPEIVEKARGSSSMKGN-PIELSDEELLEI 375
|
|
| Fe-ADH-like |
cd14861 |
Iron-containing alcohol dehydrogenases-like; This family contains proteins similar to ... |
11-378 |
1.93e-82 |
|
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: 256.28 E-value: 1.93e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 11 GAGAfTALLP---LLTGKQRILLVTDANVGKLDAARQIRTLLEDEGRQVQIVDSVPAEPSQHDMTQILRLVSANQPELIV 87
Cdd:cd14861 9 GAGA-IAELPeelKALGIRRPLLVTDPGLAALGIVDRVLEALGAAGLSPAVFSDVPPNPTEADVEAGVAAYREGGCDGII 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 88 GIGGGSVLDVAKLLSVLLHPDSPgLEALLAGEKPQQKVTS-----LLIPATAGTGSEATPNAILAIPEQNTKVGIISPVL 162
Cdd:cd14861 88 ALGGGSAIDAAKAIALMATHPGP-LWDYEDGEGGPAAITPavpplIAIPTTAGTGSEVGRAAVITDDDTGRKKIIFSPKL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 163 LPDYVALLPELTTSMPAHIASSTGIDALCHLIECFTSTVANPVSDNAALIGLRKLVRNIELSVSEPHNLAAKLEMLWASY 242
Cdd:cd14861 167 LPKVAICDPELTLGLPPRLTAATGMDALTHCIEAYLSPGFHPMADGIALEGLRLISEWLPRAVADGSDLEARGEMMMAAL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 243 YGGVAInHAGTHLVHALSYPLGGKYHLPHGVANAILLAPCMKVVRPHAVAKFAQVwdllpeADLTLSEEEKSHALVAWLA 322
Cdd:cd14861 247 MGAVAF-QKGLGAVHALAHALGALYGLHHGLLNAILLPYVLRFNRPAVEDKLARL------ARALGLGLGGFDDFIAWVE 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 490214900 323 ALVKRLQLPDNLAALGVPPESISELSEAALNVKRLLNNaPCSVNQDQVEAVYRTLF 378
Cdd:cd14861 320 DLNERLGLPATLSELGVTEDDLDELAELALADPCHATN-PRPVTAEDYRALLREAL 374
|
|
| Fe-ADH-like |
cd08191 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
6-375 |
3.05e-82 |
|
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: 256.39 E-value: 3.05e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 6 STLISGAGAFTALLPLLTG-KQRILLVTDANVGKLDAARQIRTLLEDEGRQVQIVDSVPAEPSQHDMTQILRLVSANQPE 84
Cdd:cd08191 5 SRLLFGPGARRALGRVAARlGSRVLIVTDPRLASTPLVAELLAALTAAGVAVEVFDGGQPELPVSTVADAAAAARAFDPD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 85 LIVGIGGGSVLDVAKLLSVLL-HPDSPgleALLAGEK--PQQKVTSLLIPATAGTGSEATPNAILAIPEQNTKVGIISPV 161
Cdd:cd08191 85 VVIGLGGGSNMDLAKVVALLLaHGGDP---RDYYGEDrvPGPVLPLIAVPTTAGTGSEVTPVAVLTDPARGMKVGVSSPY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 162 LLPDyVALL-PELTTSMPAHIASSTGIDALCHLIECFTSTV---------------ANPVSDNAALIGLRKLVRNIELSV 225
Cdd:cd08191 162 LRPA-VAIVdPELTLTCPPGVTADSGIDALTHAIESYTARDfppfprldpdpvyvgKNPLTDLLALEAIRLIGRHLPRAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 226 SEPHNLAAKLEMLWASYYGGVAINHAGTHLVHALSYPLGGKYHLPHGVANAILLAPCMKVVRPHAVAKFAQVWDLLPEAD 305
Cdd:cd08191 241 RDGDDLEARSGMALAALLAGLAFGTAGTAAAHALQYPIGALTHTSHGVGNGLLLPYVMRFNRPARAAELAEIARALGVTT 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 306 LTLSEEEKSHAlVAWLAALVKRLQLPDNLAALGVPPESISELSEAALNVKRLLNNAPCSVNQDQVEAVYR 375
Cdd:cd08191 321 AGTSEEAADRA-IERVEELLARIGIPTTLADLGVTEADLPGLAEKALSVTRLIANNPRPPTEEDLLRILR 389
|
|
| Fe-ADH-like |
cd08189 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
7-377 |
1.61e-81 |
|
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: 253.93 E-value: 1.61e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 7 TLISGAGAFTALLPLL--TGKQRILLVTDANVGKLDAARQIRTLLEDEGRQVQIVDSVPAEPSQHDMTQILRLVSANQPE 84
Cdd:cd08189 7 ELFEGAGSLLQLPEALkkLGIKRVLIVTDKGLVKLGLLDPLLDALKKAGIEYVVFDGVVPDPTIDNVEEGLALYKENGCD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 85 LIVGIGGGSVLDVAKLLSVLLHpdspgleallAGEKPQQKVTSLL-----------IPATAGTGSEATPNAILAIPEQNT 153
Cdd:cd08189 87 AIIAIGGGSVIDCAKVIAARAA----------NPKKSVRKLKGLLkvrkklppliaVPTTAGTGSEATIAAVITDPETHE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 154 KVGIISPVLLPDYVALLPELTTSMPAHIASSTGIDALCHLIECFTSTVANPVSDNAALIGLRKLVRNIELSVSEPHNLAA 233
Cdd:cd08189 157 KYAINDPKLIPDAAVLDPELTLGLPPAITAATGMDALTHAVEAYISRSATKETDEYALEAVKLIFENLPKAYEDGSDLEA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 234 KLEMLWASYYGGVAINHAGTHLVHALSYPLGGKYHLPHGVANAILLAPCMKVVRPHAVAKFAQVWDLLPEADLTLSEEEK 313
Cdd:cd08189 237 RENMLLASYYAGLAFTRAYVGYVHAIAHQLGGLYGVPHGLANAVVLPHVLEFYGPAAEKRLAELADAAGLGDSGESDSEK 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490214900 314 SHALVAWLAALVKRLQLPDNLAALgvPPESISELSEAALNVKRLLNNAPCSVNQDQVEAVYRTL 377
Cdd:cd08189 317 AEAFIAAIRELNRRMGIPTTLEEL--KEEDIPEIAKRALKEANPLYPVPRIMDRKDCEELLRKV 378
|
|
| Fe-ADH-like |
cd14865 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
8-375 |
3.44e-79 |
|
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: 248.22 E-value: 3.44e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 8 LISGAGAFTALLPLLT--GKQRILLVTDANVGKLDAARQIRTLLEDEGRQVQIVDSVPAEPSQHDMTQILRLVSANQPEL 85
Cdd:cd14865 9 IVSGAGALENLPAELArlGARRPLIVTDKGLAAAGLLKKVEDALGDAIEIVGVFDDVPPDSSVAVVNEAAARAREAGADG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 86 IVGIGGGSVLDVAKLLSVLLhpdSPGLEAL--LAGE--KPQQKVTSLLIPATAGTGSEATPNAILAIPEQNTKVGIISPV 161
Cdd:cd14865 89 IIAVGGGSVIDTAKGVNILL---SEGGDDLddYGGAnrLTRPLKPLIAIPTTAGTGSEVTLVAVIKDEEKKVKLLFVSPF 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 162 LLPDYVALLPELTTSMPAHIASSTGIDALCHLIECFTSTVANPVSDNAALIGLRKLVRNIELSVSEPHNLAAKLEMLWAS 241
Cdd:cd14865 166 LLPDVAILDPRLTLSLPPKLTAATGMDALTHAIEAYTSLQKNPISDALALQAIRLISENLPKAVKNGKDLEARLALAIAA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 242 YYGGVAINHAGTHLVHALSYPLGGKYHLPHGVANAILLAPCMKVVRPHAVAKFAQVWDLLPEADLT--LSEEEKSHALVA 319
Cdd:cd14865 246 TMAGIAFSNSMVGLVHAIAHAVGAVAGVPHGLANSILLPHVMRYNLDAAAERYAELALALAYGVTPagRRAEEAIEAAID 325
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 490214900 320 WLAALVKRLQLPDNLAALGVPPESISELSEAALNVKRLLNNaPCSVNQDQVEAVYR 375
Cdd:cd14865 326 LVRRLHELCGLPTRLRDVGVPEEQLEAIAELALNDGAILFN-PREVDPEDILAILE 380
|
|
| Fe-ADH-like |
cd08196 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
11-374 |
9.84e-78 |
|
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: 244.03 E-value: 9.84e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 11 GAGAFTALLPLL--TGKQRILLVTDANVGKLDAARQIRTLLEdeGRQVQIVDSVPAEPSQHDMTQILRLVSANQPELIVG 88
Cdd:cd08196 12 GEGILKELPDIIkeLGGKRGLLVTDPSFIKSGLAKRIVESLK--GRIVAVFSDVEPNPTVENVDKCARLARENGADFVIA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 89 IGGGSVLDVAKLLSVLLHPDSPGLEALLAGEK-PQQKVTSLLIPATAGTGSEATPNAILAIPEQNTKVGIISPVLLPDYV 167
Cdd:cd08196 90 IGGGSVLDTAKAAACLAKTDGSIEDYLEGKKKiPKKGLPLIAIPTTAGTGSEVTPVAVLTDKEKGKKAPLVSPGFYPDIA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 168 ALLPELTTSMPAHIASSTGIDALCHLIECFTSTVANPVSDNAALIGLRKLVRNIELSVSEPHNLAAKLEMLWASYYGGVA 247
Cdd:cd08196 170 IVDPELTYSMPPKVTASTGIDALCHAIEAYWSINHQPISDALALEAAKLVLENLEKAYNNPNDKEAREKMALASLLAGLA 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 248 INHAGTHLVHALSYPLGGKYHLPHGVANAILLAPCMKVV------RPHAVAKFAQVWDllPEAdltLSEEekshalvawL 321
Cdd:cd08196 250 FSQTRTTASHACSYPLTSHFGIPHGEACALTLPSFIRLNaealpgRLDELAKQLGFKD--AEE---LADK---------I 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 490214900 322 AALVKRLQLPDNLAALGVPPESISELSEAALNVKRLLNNaPCSVNQDQVEAVY 374
Cdd:cd08196 316 EELKKRIGLRTRLSELGITEEDLEEIVEESFHPNRANNN-PVEVTKEDLEKLL 367
|
|
| NADPH_BDH |
cd08179 |
NADPH-dependent butanol dehydrogenase involved in the butanol and ethanol formation pathway in ... |
3-353 |
1.68e-76 |
|
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: 240.94 E-value: 1.68e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 3 TINSTLISGAGAFTALLPLltGKQRILLVTDANV----GKLDaarQIRTLLEDEGRQVQIVDSVPAEPSQHDMTQILRLV 78
Cdd:cd08179 3 FVPRDIYFGEGALEYLKTL--KGKRAFIVTGGGSmkrnGFLD---KVEDYLKEAGMEVKVFEGVEPDPSVETVEKGAEAM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 79 SANQPELIVGIGGGSVLDVAKLLSVLL-HPDSPGLEALLAGEKPQ--QKVTSLLIPATAGTGSEATPNAILAIPEQNTKV 155
Cdd:cd08179 78 REFEPDWIIAIGGGSVIDAAKAMWVFYeYPELTFEDALVPFPLPElrKKARFIAIPSTSGTGSEVTRASVITDTEKGIKY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 156 GIISPVLLPDYVALLPELTTSMPAHIASSTGIDALCHLIECFTSTVANPVSDNAALIGLRKLVRNIELSVSEPHNLAAKL 235
Cdd:cd08179 158 PLASFEITPDVAILDPELTMTMPPHVTANTGMDALTHAIEAYVSTLANDFTDALALGAILDIFENLPKSYNGGKDLEARE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 236 EMLWASYYGGVAINHAGTHLVHALSYPLGGKYHLPHGVANAILLAPCMKVVRPHAVAKFAQVWDLlpeadLTLSEEEKSH 315
Cdd:cd08179 238 KMHNASCLAGMAFSNSGLGIVHSMAHKGGAFFGIPHGLANAILLPYVIEFNSKDPEARARYAALL-----IGLTDEELVE 312
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 490214900 316 ALVAWLAALVKRLQLPDNLAALGVPPE----SISELSEAALN 353
Cdd:cd08179 313 DLIEAIEELNKKLGIPLSFKEAGIDEDeffaKLDEMAENAMN 354
|
|
| HEPD |
cd08182 |
Hydroxyethylphosphoate dehydrogenase (HEPD) catalyzes the reduction of phosphonoacetaldehyde ... |
8-375 |
7.47e-75 |
|
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: 236.74 E-value: 7.47e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 8 LISGAGAFTALLPLLTGK--QRILLVTD-ANVGKLDAARQIRTLLEDegRQVQIVDSVPAEPSQHDMTQILRLVSANQPE 84
Cdd:cd08182 4 IIFGPGALAELKDLLGGLgaRRVLLVTGpSAVRESGAADILDALGGR--IPVVVFSDFSPNPDLEDLERGIELFRESGPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 85 LIVGIGGGSVLDVAKLLSVLL-HPDSPGLEALLAGEKPQQKVTSL-LIPATAGTGSEATPNAILAIPEQNTKVGIISPVL 162
Cdd:cd08182 82 VIIAVGGGSVIDTAKAIAALLgSPGENLLLLRTGEKAPEENALPLiAIPTTAGTGSEVTPFATIWDEAEGKKYSLAHPSL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 163 LPDYVALLPELTTSMPAHIASSTGIDALCHLIECFTSTVANPVSDNAALIGLRKLVRNIELSVSEPHNLAAKLEMLWASY 242
Cdd:cd08182 162 YPDAAILDPELTLSLPLYLTASTGLDALSHAIESIWSVNANPESRAYALRAIRLILENLPLLLENLPNLEAREAMAEASL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 243 YGGVAINHAGTHLVHALSYPLGGKYHLPHGVANAILLAPCMKVVRPHAVAKFAqvwDLLPEADLTLSEEEKSHALVAWLA 322
Cdd:cd08182 242 LAGLAISITKTTAAHAISYPLTSRYGVPHGHACALTLPAVLRYNAGADDECDD---DPRGREILLALGASDPAEAAERLR 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 490214900 323 ALVKRLQLPDNLAALGVPPESISELSEAALNVKRLLNNaPCSVNQDQVEAVYR 375
Cdd:cd08182 319 ALLESLGLPTRLSEYGVTAEDLEALAASVNTPERLKNN-PVRLSEEDLLRLLE 370
|
|
| PDDH |
cd08188 |
1,3-Propanediol (1,3-PD) dehydrogenase; This family includes 1,3-propanediol (1,3-PD) ... |
24-375 |
3.17e-73 |
|
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: 232.40 E-value: 3.17e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 24 GKQRILLVTDANVGKLDAARQIRTLLEDEGRQVQIVDSVPAEPSQHDMTQILRLVSANQPELIVGIGGGSVLDVAKLLSV 103
Cdd:cd08188 27 GGKKALIVTDKGLVKLGLVKKVTDVLEEAGIEYVIFDGVQPNPTVTNVNEGLELFKENGCDFIISVGGGSAHDCAKAIGI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 104 LLhpDSPG-LEALLAGEKPQQKVTSLL-IPATAGTGSEATPNAILAIPEQNTKVGIISPVLLPDyVALL-PELTTSMPAH 180
Cdd:cd08188 107 LA--TNGGeIEDYEGVDKSKKPGLPLIaINTTAGTASEVTRFAVITDEERHVKMVIVDWNVTPT-IAVNdPELMLGMPPS 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 181 IASSTGIDALCHLIECFTSTVANPVSDNAALIGLRKLVRNIELSVSEPHNLAAKLEMLWASYYGGVAINHAGTHLVHALS 260
Cdd:cd08188 184 LTAATGMDALTHAIEAYVSTGATPLTDALALEAIRLIAENLPKAVANGKDLEARENMAYAQFLAGMAFNNAGLGYVHAMA 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 261 YPLGGKYHLPHGVANAILLAPCMKVVRPHAVAKFAQVWDLLPEADLTLSEEEKSHALVAWLAALVKRLQLPDNLAALGVP 340
Cdd:cd08188 264 HQLGGFYNLPHGVCNAILLPHVMEFNLPACPERFADIARALGENTEGLSDEEAAEAAIEAIRKLSRRVGIPSGLKELGVK 343
|
330 340 350
....*....|....*....|....*....|....*
gi 490214900 341 PESISELSEAALNVKRLLNNaPCSVNQDQVEAVYR 375
Cdd:cd08188 344 EEDFPLLAENALKDACGPTN-PRQATKEDVIAIYR 377
|
|
| LPO |
cd08176 |
Lactadehyde:propanediol oxidoreductase (LPO) catalyzes the interconversion between ... |
5-375 |
6.63e-73 |
|
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: 231.67 E-value: 6.63e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 5 NSTLISGAGAFTALLPLLT--GKQRILLVTDANVGKLDAARQIRTLLEDEGRQVQIVDSVPAEPSQHDMTQILRLVSANQ 82
Cdd:cd08176 6 NPTSYFGWGAIEEIGEEAKkrGFKKALIVTDKGLVKFGIVDKVTDVLKEAGIAYTVFDEVKPNPTIENVMAGVAAYKESG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 83 PELIVGIGGGSVLDVAKLLSVLL-HP--DSPGLEALLAGEKPqqKVTSLLIPATAGTGSEATPNAILAIPEQNTKVGIIS 159
Cdd:cd08176 86 ADGIIAVGGGSSIDTAKAIGIIVaNPgaDVRSLEGVAPTKNP--AVPIIAVPTTAGTGSEVTINYVITDTEKKRKFVCVD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 160 PVLLPDYVALLPELTTSMPAHIASSTGIDALCHLIECFTSTVANPVSDNAALIGLRKLVRNIELSVSEPHNLAAKLEMLW 239
Cdd:cd08176 164 PHDIPTVAIVDPDLMSSMPKGLTAATGMDALTHAIEGYITKGAWELSDMLALKAIELIAKNLRKAVANPNNVEARENMAL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 240 ASYYGGVAINHAGTHLVHALSYPLGGKYHLPHGVANAILLAPCMKVVRPHAVAKFAQVWDLLPEADLTLSEEEKSHALVA 319
Cdd:cd08176 244 AQYIAGMAFSNVGLGIVHSMAHPLSAFYDTPHGVANAILLPYVMEFNAPATGEKYRDIARAMGVDTTGMSDEEAAEAAVD 323
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 490214900 320 WLAALVKRLQLPDNLAALGVPPESISELSEAALNVKRLLNNaPCSVNQDQVEAVYR 375
Cdd:cd08176 324 AVKKLSKDVGIPQKLSELGVKEEDIEALAEDALNDVCTPGN-PREATKEDIIALYK 378
|
|
| Fe-ADH-like |
cd08185 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
8-375 |
3.05e-68 |
|
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: 219.68 E-value: 3.05e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 8 LISGAGAFTAL--LPLLTGKqRILLVTDANVGKL-DAARQIRTLLEDEGRQVQIVDSVPAEPSQHDMTQILRLVSANQPE 84
Cdd:cd08185 7 ILFGAGKLNELgeEALRPGK-KALIVTGKGSSKKtGLLDRVKKLLEKAGVEVVVFDKVEPNPLTTTVMEGAALAKEEGCD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 85 LIVGIGGGSVLDVAKLLSVLLhpDSPG-LEALLAGEKPQQKVTS-----LLIPATAGTGSEATPNAILAIPEQNTKVGII 158
Cdd:cd08185 86 FVIGLGGGSSMDAAKAIAFMA--TNPGdIWDYIFGGTGKGPPPEkalpiIAIPTTAGTGSEVDPWAVITNPETKEKKGIG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 159 SPVLLPdYVALL-PELTTSMPAHIASSTGIDALCHLIECFTSTVANPVSDNAALIGLRKLVRNIELSVSEPHNLAAKLEM 237
Cdd:cd08185 164 HPALFP-KVSIVdPELMLTVPPRVTAYTGFDALFHAFESYISKNANPFSDMLALEAIRLVAKYLPRAVKDGSDLEAREKM 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 238 LWASYYGGVAINHAGTHLVHALSYPLGGKY-HLPHGVANAILLAPCMKVVRPHAVAKFAQVWDllpEADLTLSEEEKSHA 316
Cdd:cd08185 243 AWASTLAGIVIANSGTTLPHGLEHPLSGYHpNIPHGAGLAALYPAYFEFTIEKAPEKFAFVAR---AEASGLSDAKAAED 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 317 LVAWLAALVKRLQLPDNLAALGVPPESISELSEAALNV-KRLLNNAPCSVNQDQVEAVYR 375
Cdd:cd08185 320 FIEALRKLLKDIGLDDLLSDLGVTEEDIPWLAENAMETmGGLFANNPVELTEEDIVEIYE 379
|
|
| Fe-ADH-like |
cd17814 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
24-374 |
1.84e-64 |
|
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: 209.71 E-value: 1.84e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 24 GKQRILLVTDANVGKLDAARQIRTLLEDEGRQVQIVDSVPAEPSQHDMTQILRLVSANQPELIVGIGGGSVLDVAKLLSV 103
Cdd:cd17814 25 GARKVLVVTDPGVIKAGWVDEVLDSLEAEGLEYVVFSDVTPNPRDFEVMEGAELYREEGCDGIVAVGGGSPIDCAKGIGI 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 104 L----------------LHPdSPGLeallagekpqqkvtsLLIPATAGTGSEATPNAILAIPEQNTKVGIISPVLLPDyV 167
Cdd:cd17814 105 VvsngghildyegvdkvRRP-LPPL---------------ICIPTTAGSSADVSQFAIITDTERRVKMAIISKTLVPD-V 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 168 ALL-PELTTSMPAHIASSTGIDALCHLIECFTSTVANPVSDNAALIGLRKLVRNIELSVSEPHNLAAKLEMLWASYYGGV 246
Cdd:cd17814 168 SLIdPETLTTMDPELTACTGMDALTHAIEAYVSNASSPLTDLHALEAIRLISENLPKAVADPDDLEAREKMMLASLQAGL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 247 AINHAGTHLVHALSYPLGGKYHLPHGVANAILLAPcmkVVR---PHAVAKFAQVWDLLPEADLTLSEEEKSHALVAWLAA 323
Cdd:cd17814 248 AFSNASLGAVHAMAHSLGGLLDLPHGECNALLLPH---VIRfnfPAAPERYRKIAEAMGLDVDGLDDEEVAERLIEAIRD 324
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 490214900 324 LVKRLQLPDNLAALGVPPESISELSEAALNVKRLLNNaPCSVNQDQVEAVY 374
Cdd:cd17814 325 LREDLGIPETLSELGVDEEDIPELAKRAMKDPCLVTN-PRRPTREDIEEIY 374
|
|
| PPD-like |
cd08181 |
1,3-propanediol dehydrogenase-like (PPD); This family contains proteins similar to 1, ... |
24-375 |
5.84e-63 |
|
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: 205.51 E-value: 5.84e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 24 GKqRILLVTDANVGKLDAARQIRT-LLEDEGRQVQIVDSVPAEPSQHDMTQILRLVSANQPELIVGIGGGSVLDVAKLLS 102
Cdd:cd08181 25 GK-KALIVTGKHSAKKNGSLDDVTeALEENGIEYFIFDEVEENPSIETVEKGAELARKEGADFVIGIGGGSPLDAAKAIA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 103 VLL-HPDSPglEALLAGEKPQQKVTSLLIPATAGTGSEATPNAILAIPEQNTKVGIISPVLLPDYvALL-PELTTSMPAH 180
Cdd:cd08181 104 LLAaNKDGD--EDLFQNGKYNPPLPIVAIPTTAGTGSEVTPYSILTDHEKGTKKSFGNPLIFPKL-ALLdPKYTLSLPEE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 181 IASSTGIDALCHLIECFTSTVANPVSDNAALIGLRKLVRNIELSVSEPHNLAAKLEMLWASYYGGVAINHAGTHLVHALS 260
Cdd:cd08181 181 LTIDTAVDALSHAIEGYLSVKATPLSDALALEALRLIGECLPNLLGDELDEEDREKLMYASTLAGMVIAQTGTTLPHGLG 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 261 YPLGGKYHLPHGVANAILLAPCMKVVRPHAVAKFAQVWDLLPEADLtlsEEekshalvawLAALVKRLqLPDNLAalgVP 340
Cdd:cd08181 261 YPLTYFKGIPHGRANGILLPAYLKLCEKQEPEKVDKILKLLGFGSI---EE---------FQKFLNRL-LGKKEE---LS 324
|
330 340 350
....*....|....*....|....*....|....*
gi 490214900 341 PESISELSEAALNVKRLLNNAPcSVNQDQVEAVYR 375
Cdd:cd08181 325 EEELEKYADEAMKAKNKKNTPG-NVTKEDILRIYR 358
|
|
| Fe-ADH-like |
cd14862 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
27-353 |
1.06e-59 |
|
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: 197.45 E-value: 1.06e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 27 RILLVTDANVGKLDAARQIRTLLEDEGRQVQIVDSVPAEPSQHDMTQILRLVSANQPELIVGIGGGSVLDVAKLLSVLLH 106
Cdd:cd14862 26 RALIVTDKVLVKLGLLKKVLKRLLQAGFEVEVFDEVEPEPPLETVLKGAEAMREFEPDLIIALGGGSVMDAAKAAWVLYE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 107 PDSPGLEALLAGEK--PQQKVTSLLIPATAGTGSEATPNAILAIPEQNTKVGIISPVLLPDYVALLPELTTSMPAHIASS 184
Cdd:cd14862 106 RPDLDPEDISPLDLlgLRKKAKLIAIPTTSGTGSEATWAIVLTDTEEPRKIAVANPELVPDVAILDPEFVLGMPPKLTAG 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 185 TGIDALCHLIECFTSTVANPVSDNAALIGLRKLVRNIELSVSEPHNLAAKLEMLWASYYGGVAINHAGTHLVHALSYPLG 264
Cdd:cd14862 186 TGLDALAHAVEAYLSTWSNDFSDALALKAIELIFKYLPRAYKDGDDLEAREKMHNAATIAGLAFGNSQAGLAHALGHSLG 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 265 GKYHLPHGVANAILLapcmkvvrPHAVAKFAQV----WDLLPEADL-TLSEEEKSHALVAWLAALVKRLQLPDNLAALGV 339
Cdd:cd14862 266 AVFHVPHGIAVGLFL--------PYVIEFYAKVtderYDLLKLLGIeARDEEEALKKLVEAIRELYKEVGQPLSIKDLGI 337
|
330
....*....|....*...
gi 490214900 340 PPES----ISELSEAALN 353
Cdd:cd14862 338 SEEEfeekLDELVEYAME 355
|
|
| AAD_C |
cd08178 |
C-terminal alcohol dehydrogenase domain of the acetaldehyde dehydrogenase-alcohol ... |
13-353 |
6.46e-59 |
|
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: 196.25 E-value: 6.46e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 13 GAFTALLPLLTGKQRILLVTDANVGKLDAARQIRTLLEDEGRQVQIVDSVPAEPSQHDMTQILRLVSANQPELIVGIGGG 92
Cdd:cd08178 11 GCLPYLLLELPGVKRAFIVTDRVLYKLGYVDKVLDVLEARGVETEVFSDVEPDPTLSTVRKGLEAMNAFKPDVIIALGGG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 93 SVLDVAKLLSVLL-HPDSPgLEALlAGE------------KPQQKVTSLLIPATAGTGSEATPNAILAIPEQNTKVGIIS 159
Cdd:cd08178 91 SAMDAAKIMWLFYeHPETK-FEDL-AQRfmdirkrvykfpKLGKKAKLVAIPTTSGTGSEVTPFAVITDDKTGKKYPLAD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 160 PVLLPDyVALL-PELTTSMPAHIASSTGIDALCHLIECFTSTVANPVSDNAALIGLRKLVRNIELSVSEPHNLAAKLEML 238
Cdd:cd08178 169 YALTPD-MAIVdPELVMTMPKRLTADTGIDALTHAIEAYVSVMASDYTDGLALQAIKLIFEYLPRSYNNGNDIEAREKMH 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 239 WASYYGGVAINHAGTHLVHALSYPLGGKYHLPHGVANAILL---------------APCMKVVRPHAVAKFAQVWDLLpe 303
Cdd:cd08178 248 NAATIAGMAFANAFLGICHSLAHKLGAAFHIPHGRANAILLphvirynatdpptkqAAFPQYKYYVAKERYAEIADLL-- 325
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 490214900 304 ADLTLSEEEKSHALVAWLAALVKRLQLPDNLAALGVPPE----SISELSEAALN 353
Cdd:cd08178 326 GLGGKTPEEKVESLIKAIEDLKKDLGIPTSIREAGIDEAdflaAVDKLAEDAFD 379
|
|
| 4HBD_NAD |
cd14860 |
4-hydroxybutyrate dehydrogenase, also called gamma-hydroxybutyrate dehydrogenase, catalyzes ... |
65-378 |
2.90e-57 |
|
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: 190.89 E-value: 2.90e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 65 EPSQHDMTQILRLVSANQPELIVGIGGGSVLDVAKLLSvlLHPDSPgLEALLAGEKPQQKVTSL-LIPATAGTGSEATPN 143
Cdd:cd14860 61 EPSDEMVEAIYKDIKKYGYKRVIAIGGGTVIDIAKLLA--LKGISP-VLDLFDGKIPLIKEKELiIVPTTCGTGSEVTNI 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 144 AILAIPEQNTKVGIISPVLLPDYVALLPELTTSMPAHIASSTGIDALCHLIECFTSTVANPVSDNAALIGLRKLVRNIEL 223
Cdd:cd14860 138 SIVELTSLGTKKGLAVDELYADKAVLIPELLKGLPYKVFATSSIDALIHAIESYLSPKATPYTEMFSYKAIEMILEGYQE 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 224 SVSEPHNLAAKL--EMLWASYYGGVAINHAGTHLVHALSYPLGGKYHLPHGVANAILLAPCMKVVRPH----AVAKFAQV 297
Cdd:cd14860 218 IAEKGEEARFPLlgDFLIASNYAGIAFGNAGCAAVHALSYPLGGKYHVPHGEANYAVFTGVLKNYQEKnpdgEIKKLNEF 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 298 WDLLPEADltlseeeKSHALVAWLAALVKRLQLPDnLAALGVPPESISELSEAAL-NVKRLLNNAPCSVNQDQVEAVYRT 376
Cdd:cd14860 298 LAKILGCD-------EEDVYDELEELLNKILPKKP-LHEYGMKEEEIDEFADSVMeNQQRLLANNYVPLDREDVAEIYKE 369
|
..
gi 490214900 377 LF 378
Cdd:cd14860 370 LY 371
|
|
| PDD |
cd08180 |
1,3-propanediol dehydrogenase (PPD) catalyzes the reduction of 3-hydroxypropionaldehyde (3-HPA) ... |
4-375 |
4.37e-55 |
|
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: 184.23 E-value: 4.37e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 4 INSTLISGAGAFTALLPLltGKQRILLVTDANVGKLDAARQIRTLLeDEGRQVQIVDSVPAEPSQHDMTQILRLVSANQP 83
Cdd:cd08180 3 LKTKIYSGEDSLERLKEL--KGKRVFIVTDPFMVKSGMVDKVTDEL-DKSNEVEIFSDVVPDPSIEVVAKGLAKILEFKP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 84 ELIVGIGGGSVLDVAK-----LLSVLLHPDSPGLEAllagekpqqkvtsllIPATAGTGSEATPNAILAIPEQNTKVGII 158
Cdd:cd08180 80 DTIIALGGGSAIDAAKaiiyfALKQKGNIKKPLFIA---------------IPTTSGTGSEVTSFAVITDPEKGIKYPLV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 159 SPVLLPDyVALL-PELTTSMPAHIASSTGIDALCHLIECFTSTVANPVSDNAALIGLRKLVRNIELSVSEPHNLAAKLEM 237
Cdd:cd08180 145 DDSMLPD-IAILdPELVKSVPPKVTADTGMDVLTHALEAYVSTNANDFTDALAEKAIKLVFENLPRAYRDGDDLEAREKM 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 238 LWASYYGGVAINHAGTHLVHALSYPLGGKYHLPHGVANAILLapcmkvvrPHAVAkfaqvwdllpeadltlseeekshAL 317
Cdd:cd08180 224 HNASCMAGIAFNNAGLGINHSLAHALGGRFHIPHGRANAILL--------PYVIE-----------------------FL 272
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490214900 318 VAWLAALVKRLQLPDNLAALGVPPE----SISELSEAALNVKRLLNNaPCSVNQDQVEAVYR 375
Cdd:cd08180 273 IAAIRRLNKKLGIPSTLKELGIDEEefekAIDEMAEAALADRCTATN-PRKPTAEDLIELLR 333
|
|
| Fe-ADH-like |
cd08186 |
Iron-containing alcohol dehydrogenase; This family contains iron-containing alcohol ... |
24-375 |
7.49e-50 |
|
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: 171.68 E-value: 7.49e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 24 GKQRILLVTDANVGKLDAARQ-IRTLLEDEGRQVQIVDSVPAEPSQHDMTQILRLVSANQPELIVGIGGGSVLDVAKLLS 102
Cdd:cd08186 22 GIDKVIIVTGRSSYKKSGAWDdVEKALEENGIEYVVYDKVTPNPTVDQADEAAKLARDFGADAVIAIGGGSPIDTAKSVA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 103 VLL-HPDSPGlEALLAGEKPQQKVTSLL-IPATAGTGSEATPNAILAIPEQNTKVGIISPVLLPDYVALLPELTTSMPAH 180
Cdd:cd08186 102 VLLaYGGKTA-RDLYGFRFAPERALPLVaINLTHGTGSEVDRFAVATIPEKGYKPGIAYDCIYPLYAIDDPRLTLTLPKE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 181 IASSTGIDALCHLIECFTSTVANPVSDNAALIGLRKLVRNIELSVSEPHNLAAKLEMLWASYYGGVAINHAGTHLVHALS 260
Cdd:cd08186 181 QTLYTSIDAFNHVYEAATTKVSSPYVITLAKEAIRLIAEYLPRALANPKDLEARYWLLYASMIAGIAIDNGLLHLTHALE 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 261 YPLGG-KYHLPHGVANAILLAPCMKVVRPHAVAKFAQVWD-LLPEADLTLSEEEKSHALV-AWLaalvKRLQLPDNLAAL 337
Cdd:cd08186 261 HPLSGlKPELPHGLGLALLGPAVVKYIYKAVPETLADILRpIVPGLKGTPDEAEKAARGVeEFL----FSVGFTEKLSDY 336
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 490214900 338 GVPPESISELSEAALN---VKRLLNNAPCSVNQDQVEAVYR 375
Cdd:cd08186 337 GFTEDDVDRLVELAFTtpsLDLLLSLAPVEVTEEVVREIYE 377
|
|
| BDH |
cd08187 |
Butanol dehydrogenase catalyzes the conversion of butyraldehyde to butanol with the cofactor ... |
44-375 |
7.79e-50 |
|
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: 171.85 E-value: 7.79e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 44 QIRTLLEDEGRQVQIVDSVPAEPSQHDMTQILRLVSANQPELIVGIGGGSVLDVAKLLSV-LLHPDSPglEALLAGEKPQ 122
Cdd:cd08187 48 RVVASLKEAGIEVVEFGGVEPNPRLETVREGIELAREENVDFILAVGGGSVIDAAKAIAAgAKYDGDV--WDFFTGKAPP 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 123 QKVTSLL-IPATAGTGSEATPNAILAIPEQNTKVGIISPVLLPDyVALL-PELTTSMPAHIASSTGIDALCHLIEC-FTS 199
Cdd:cd08187 126 EKALPVGtVLTLAATGSEMNGGAVITNEETKEKLGFGSPLLRPK-FSILdPELTYTLPKYQTAAGIVDIFSHVLEQyFTG 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 200 TVANPVSDNAALIGLRKLVRNIELSVSEPHNLAAKLEMLWASYyggVAINH---AGTHL---VHALSYPLGGKYHLPHGV 273
Cdd:cd08187 205 TEDAPLQDRLAEGLLRTVIENGPKALKDPDDYEARANLMWAAT---LALNGllgAGRGGdwaTHAIEHELSALYDITHGA 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 274 ANAILLAPCMKVVRPHAVAKFAQ----VWDLLPEADltlsEEEKSHALVAWLAALVKRLQLPDNLAALGVPPESISELSE 349
Cdd:cd08187 282 GLAIVFPAWMRYVLKKKPERFAQfarrVFGIDPGGD----DEETALEGIEALEEFFKSIGLPTTLSELGIDEEDIEEMAE 357
|
330 340
....*....|....*....|....*.
gi 490214900 350 AALNVKRLLNNAPcSVNQDQVEAVYR 375
Cdd:cd08187 358 KAVRGGGLGGGFK-PLTREDIEEILK 382
|
|
| PRK09860 |
PRK09860 |
putative alcohol dehydrogenase; Provisional |
4-375 |
2.11e-49 |
|
putative alcohol dehydrogenase; Provisional
Pssm-ID: 182118 [Multi-domain] Cd Length: 383 Bit Score: 170.91 E-value: 2.11e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 4 INSTLISGAGAFTALLPLLT--GKQRILLVTDANVGKLDAARQIRTLLEDEGRQVQIVDSVPAEPSQHDMTQILRLVSAN 81
Cdd:PRK09860 8 IPSVNVIGADSLTDAMNMMAdyGFTRTLIVTDNMLTKLGMAGDVQKALEERNIFSVIYDGTQPNPTTENVAAGLKLLKEN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 82 QPELIVGIGGGSVLDVAKLLSVLLHP--DSPGLEALLAGEKPQqkVTSLLIPATAGTGSEATPNAILAIPEQNTKVGIIS 159
Cdd:PRK09860 88 NCDSVISLGGGSPHDCAKGIALVAANggDIRDYEGVDRSAKPQ--LPMIAINTTAGTASEMTRFCIITDEARHIKMAIVD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 160 PVLLPDYVALLPELTTSMPAHIASSTGIDALCHLIECFTSTVANPVSDNAALIGLRKLVRNIELSVSEPHNLAAKLEMLW 239
Cdd:PRK09860 166 KHVTPLLSVNDSSLMIGMPKSLTAATGMDALTHAIEAYVSIAATPITDACALKAVTMIAENLPLAVEDGSNAKAREAMAY 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 240 ASYYGGVAINHAGTHLVHALSYPLGGKYHLPHGVANAILLaPCMKVVRPHAVAKFAQVWDLLPEADLT-LSEEEKSHALV 318
Cdd:PRK09860 246 AQFLAGMAFNNASLGYVHAMAHQLGGFYNLPHGVCNAVLL-PHVQVFNSKVAAARLRDCAAAMGVNVTgKNDAEGAEACI 324
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 490214900 319 AWLAALVKRLQLPDNLAALGVPPESISELSEAALNVKRLLNNaPCSVNQDQVEAVYR 375
Cdd:PRK09860 325 NAIRELAKKVDIPAGLRDLNVKEEDFAVLATNALKDACGFTN-PIQATHEEIVAIYR 380
|
|
| PRK13805 |
PRK13805 |
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional |
13-353 |
3.46e-48 |
|
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional
Pssm-ID: 237515 [Multi-domain] Cd Length: 862 Bit Score: 174.60 E-value: 3.46e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 13 GAFTALLPLLTGKQRILLVTDANVGKLDAARQIRTLLE--DEGRQVQIVDSVPAEPSQHDMTQILRLVSANQPELIVGIG 90
Cdd:PRK13805 468 GSLPYLLDELDGKKRAFIVTDRFMVELGYVDKVTDVLKkrENGVEYEVFSEVEPDPTLSTVRKGAELMRSFKPDTIIALG 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 91 GGSVLDVAKLLSVLL-HPdspglEALLAG---------------EKPQQKVTSLLIPATAGTGSEATPNAILAIPEQNTK 154
Cdd:PRK13805 548 GGSPMDAAKIMWLFYeHP-----ETDFEDlaqkfmdirkriykfPKLGKKAKLVAIPTTSGTGSEVTPFAVITDDKTGVK 622
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 155 VGIISPVLLPDyVALL-PELTTSMPAHIASSTGIDALCHLIECFTSTVANPVSDNAALIGLRKLVRNIELSVSE-PHNLA 232
Cdd:PRK13805 623 YPLADYELTPD-VAIVdPNLVMTMPKSLTADTGIDALTHALEAYVSVMASDYTDGLALQAIKLVFEYLPRSYKNgAKDPE 701
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 233 AKLEMLWASYYGGVAINHAGTHLVHALSYPLGGKYHLPHGVANAILL--------------APCMKVVRPHAVAKFAQVW 298
Cdd:PRK13805 702 AREKMHNASTIAGMAFANAFLGICHSMAHKLGAEFHIPHGRANAILLphvirynatdppkqAAFPQYEYPRADERYAEIA 781
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490214900 299 DL--LPEAdltlSEEEKSHALVAWLAALVKRLQLPDNLAALGVPPE----SISELSEAALN 353
Cdd:PRK13805 782 RHlgLPGS----TTEEKVESLIKAIEELKAELGIPMSIKEAGVDEAdflaKLDELAELAFD 838
|
|
| PRK10624 |
PRK10624 |
L-1,2-propanediol oxidoreductase; Provisional |
4-378 |
4.77e-48 |
|
L-1,2-propanediol oxidoreductase; Provisional
Pssm-ID: 182595 [Multi-domain] Cd Length: 382 Bit Score: 167.10 E-value: 4.77e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 4 INSTLISGAGAFTALLPLLT--GKQRILLVTDANVGKLDAARQIRTLLEDEGRQVQIVDSVPAEPSQHDMTQILRLVSAN 81
Cdd:PRK10624 7 LNETAYFGRGAIGALTDEVKrrGFKKALIVTDKTLVKCGVVAKVTDVLDAAGLAYEIYDGVKPNPTIEVVKEGVEVFKAS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 82 QPELIVGIGGGSVLDVAKLLSVLL-HP---DSPGLEALLAGEKPQqkVTSLLIPATAGTGSEATPNAILAIPEQNTKVGI 157
Cdd:PRK10624 87 GADYLIAIGGGSPQDTCKAIGIISnNPefaDVRSLEGVAPTKKPS--VPIIAIPTTAGTAAEVTINYVITDEEKRRKFVC 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 158 ISPVLLPDYVALLPELTTSMPAHIASSTGIDALCHLIECFTSTVANPVSDNAALIGLRKLVRNIELSVSEPhnLAAKLEM 237
Cdd:PRK10624 165 VDPHDIPQVAFVDADMMDSMPPGLKAATGVDALTHAIEGYITRGAWALTDMLHLKAIEIIAGALRGAVAGD--KEAGEGM 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 238 LWASYYGGVAINHAGTHLVHALSYPLGGKYHLPHGVANAILLAPCMKVVRPHAVAKFAQVWDLLPEADLTLSEEEKSHAL 317
Cdd:PRK10624 243 ALGQYIAGMGFSNVGLGLVHGMAHPLGAFYNTPHGVANAILLPHVMEYNADFTGEKYRDIARAMGVKVEGMSLEEARNAA 322
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490214900 318 VAWLAALVKRLQLPDNLAALGVPPESISELSEAALN-VKRLLNNAPCSVnqDQVEAVYRTLF 378
Cdd:PRK10624 323 VEAVKALNRDVGIPPHLRDVGVKEEDIPALAQAAFDdVCTGGNPREATL--EDIVELYKKAW 382
|
|
| MAR-like |
cd08192 |
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic ... |
8-373 |
5.59e-45 |
|
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: 158.95 E-value: 5.59e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 8 LISGAGAFTALLPLL--TGKQRILLVTDANV-GKLDAARQIRTLLEDegRQVQIVDSVPaepsQH----DMTQILRLVSA 80
Cdd:cd08192 4 VSYGPGAVEALLHELatLGASRVFIVTSKSLaTKTDVIKRLEEALGD--RHVGVFSGVR----QHtpreDVLEAARAVRE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 81 NQPELIVGIGGGSVLDVAKLLSVLLH---PDSPGLEALLAGEKPQQKVTSLLIPATAG----TGSEATPNAILAIPEQNT 153
Cdd:cd08192 78 AGADLLVSLGGGSPIDAAKAVALALAedvTDVDQLDALEDGKRIDPNVTGPTLPHIAIpttlSGAEFTAGAGATDDDTGH 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 154 KVGIISPVLLPDYVALLPELTTSMPAHIASSTGIDALCHLIECFTSTVANPVSDNAALIGLRKLVRNIELSVSEPHNLAA 233
Cdd:cd08192 158 KQGFAHPELGPDAVILDPELTLHTPERLWLSTGIRAVDHAVETLCSPQATPFVDALALKALRLLFEGLPRSKADPEDLEA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 234 KLEMLWASYY-GGVAINHAGTHLVHALSYPLGGKYHLPHGVANAILLAPCMKVVRPHAVAKFAQVWDLLPEADLTLSEEE 312
Cdd:cd08192 238 RLKCQLAAWLsLFGLGSGVPMGASHAIGHQLGPLYGVPHGITSCIMLPAVLRFNAPVNAERQRLIARALGLVTGGLGREA 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490214900 313 ksHALVAWLAALVKRLQLPDNLAALGVPPESISELSEAALNVKRLLNNAPCSVNQDQVEAV 373
Cdd:cd08192 318 --ADAADAIDALIRELGLPRTLRDVGVGRDQLEKIAENALTDVWCRTNPRPITDKDDVLEI 376
|
|
| YqdH |
COG1979 |
Alcohol dehydrogenase YqhD, Fe-dependent ADH family [Energy production and conversion]; |
44-351 |
3.25e-39 |
|
Alcohol dehydrogenase YqhD, Fe-dependent ADH family [Energy production and conversion];
Pssm-ID: 441582 [Multi-domain] Cd Length: 387 Bit Score: 143.67 E-value: 3.25e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 44 QIRTLLEDEGRQVQIVDSVPAEPSQHDMTQILRLVSANQPELIVGIGGGSVLDVAKLLSVLLHPDSPGLEALLAGEKPQQ 123
Cdd:COG1979 50 QVKAALKEAGIEVVEFGGVEPNPRLETVRKGVELCKEEGIDFILAVGGGSVIDGAKAIAAGAKYDGDPWDILTGKAPVEK 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 124 KV---TSLLIPATagtGSEATPNAILAIPEQNTKVGIISPVLLPDyVALL-PELTTSMPA-HIASstGI-DALCHLIEC- 196
Cdd:COG1979 130 ALplgTVLTLPAT---GSEMNSGSVITNEETKEKLGFGSPLVFPK-FSILdPELTYTLPKrQTAN--GIvDIFSHVMEQy 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 197 FTSTVANPVSDNAALIGLRKLVRNIELSVSEPHNLAAKLEMLWASYyggVAIN---HAGTH---LVHALSYPLGGKYHLP 270
Cdd:COG1979 204 FTYPVDAPLQDRFAEGLLRTLIEEGPKALKDPEDYDARANLMWAAT---LALNgliGAGVPqdwATHMIEHELSALYDID 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 271 HGVANAILLAPCMKVVRPHAVAKFAQ----VWDLLPEadltlSEEEKSHALVAWLAALVKRLQLPDNLAALGVPPESISE 346
Cdd:COG1979 281 HGAGLAIVLPAWMRYVLEEKPEKFAQyaerVWGITEG-----DDEERALEGIEATEEFFESLGLPTRLSEYGIDEEDIEE 355
|
....*
gi 490214900 347 LSEAA 351
Cdd:COG1979 356 MAEKA 360
|
|
| PRK15454 |
PRK15454 |
ethanolamine utilization ethanol dehydrogenase EutG; |
63-374 |
1.75e-36 |
|
ethanolamine utilization ethanol dehydrogenase EutG;
Pssm-ID: 185351 [Multi-domain] Cd Length: 395 Bit Score: 136.70 E-value: 1.75e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 63 PAEPSQHDMTQILRLVSANQPELIVGIGGGSVLDVAKLLSVLLHPDSPGLEALLAGEKPQQKVTSLLIPATAGTGSEATP 142
Cdd:PRK15454 87 VGEPCITDVCAAVAQLRESGCDGVIAFGGGSVLDAAKAVALLVTNPDSTLAEMSETSVLQPRLPLIAIPTTAGTGSETTN 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 143 NAILAIPEQNTKVGIISPVLLPDYVALLPELTTSMPAHIASSTGIDALCHLIECFTSTVANPVSDNAALIGLRKLVRNIE 222
Cdd:PRK15454 167 VTVIIDAVSGRKQVLAHASLMPDVAILDAALTEGVPSHVTAMTGIDALTHAIEAYSALNATPFTDSLAIGAIAMIGKSLP 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 223 LSVSEPHNLAAKLEMLWASYYGGVAINHAGTHLVHALSYPLGGKYHLPHGVANAILLAPCMKVVRPHAVAKFAQVWDLLp 302
Cdd:PRK15454 247 KAVGYGHDLAARESMLLASCMAGMAFSSAGLGLCHAMAHQPGAALHIPHGLANAMLLPTVMEFNRMVCRERFSQIGRAL- 325
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490214900 303 eadltLSEEEKSHALVAWLAALVKRLQLPDNLAALGVPPESISELSEAALNVKRLLNNaPCSVNQDQVEAVY 374
Cdd:PRK15454 326 -----RTKKSDDRDAINAVSELIAEVGIGKRLGDVGATSAHYGAWAQAALEDICLRSN-PRTASLEQIVGLY 391
|
|
| Fe-ADH-like |
cd14864 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
26-373 |
2.35e-36 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341486 [Multi-domain] Cd Length: 376 Bit Score: 135.89 E-value: 2.35e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 26 QRILLVTDANVGKLDAARQIRTLLEDEGRQVQIVDSVPAEPSQHDMTQILRLVSANQPELIVGIGGGSVLDVAKLLSVLL 105
Cdd:cd14864 26 SRFLLITDPVLKESGLADKIVSSLEKAGISVIVFDEIPASATSDTIDEAAELARKAGADGIIAVGGGKVLDTAKAVAILA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 106 HPDSpGLEALLAGEKPQQKVTSL-LIPATAGTGSEATPNAILaIPEQNTKVGII-SPVLLPDYVALLPELTTSMPAHIAS 183
Cdd:cd14864 106 NNDG-GAYDFLEGAKPKKKPLPLiAVPTTPRSGFEFSDRFPV-VDSRSREVKLLkAQPGLPKAVIVDPNLMASLTGNQTA 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 184 STGIDALCHLIECFTSTVANPVSDNAALIGLRKLVRNIELSVSEPHNLAAKLEMLWASYYGGVAINHAGTHLVHALSYPL 263
Cdd:cd14864 184 AMALAALALAVEAYLSKKSNFFSDALALKAIELVSENLDGALADPKNTPAEELLAQAGCLAGLAASSSSPGLATALALAV 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 264 GGKYHLPHGVANAILLAPCMKVVRPHAVAKFAQVWDLLPEADLTLSEEEKSHALVAWLAALVKRLQLPDNLAALGVpPES 343
Cdd:cd14864 264 NSRYKVSKSLVASILLPHVIEYAATSAPDKYAKIARALGEDVEGASPEEAAIAAVEGVRRLIAQLNLPTRLKDLDL-ASS 342
|
330 340 350
....*....|....*....|....*....|
gi 490214900 344 ISELSEAALNVKRlLNNAPCSVNQDQVEAV 373
Cdd:cd14864 343 LEQLAAIAEDAPK-LNGLPRSMSSDDIFDI 371
|
|
| Fe-ADH-like |
cd14866 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
7-376 |
9.27e-35 |
|
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: 131.58 E-value: 9.27e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 7 TLISGAGAFTALLPLL--TGKQRILLVTDANVGKLDAARQ-IRTLLEDegRQVQIVDSVPAEPSQHDMTQILRLVSANQP 83
Cdd:cd14866 7 RLFSGRGALARLGRELdrLGARRALVVCGSSVGANPDLMDpVRAALGD--RLAGVFDGVRPHSPLETVEAAAEALREADA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 84 ELIVGIGGGSVLDVAKLLSVLLHPDSPGLEALLAGEKPQQKVTSLL---------IPATAGTGSEATPNAILAiPEQNTK 154
Cdd:cd14866 85 DAVVAVGGGSAIVTARAASILLAEDRDVRELCTRRAEDGLMVSPRLdapklpifvVPTTPTTADVKAGSAVTD-PPAGQR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 155 VGIISPVLLPDYVALLPELTTSMPAHIASSTGIDALCHLIECFTSTVANPVSDNAALIGLRKLVRNIELSVSEPhNLAAK 234
Cdd:cd14866 164 LALFDPKTRPAAVFYDPELLATAPASLVAGAAMNGFDMAVEGLYSRHADPLADATLMHALRLLADGLPRLADDD-DPAAR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 235 LEMLWASYYGGVAINHAGTHLVHALSYPLGGKYHLPHGVANAILLAPCMKVVRPHA---VAKFAQVWDLLPEADltlseE 311
Cdd:cd14866 243 ADLVLAAVLAGYGTDHTGGGVIHALGHAIGARYGVQNGVVHAILLPHVLRFNAPATdgrLDRLAEALGVADAGD-----E 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490214900 312 EKSHALVAWLAALVKRLQLPDNLAALGVPPESISELSEAALNVKRLLNNAPCSVNQDQVEAVYRT 376
Cdd:cd14866 318 ASAAAVVDAVEALLDALGVPTRLRDLGVSREDLPAIAEAAMDDWFMDNNPRPVPTAEELEALLEA 382
|
|
| Fe-ADH_KdnB-like |
cd08184 |
Iron-containing alcohol dehydrogenase similar to Shewanella oneidensis KdnB required for Kdo8N ... |
9-361 |
7.74e-33 |
|
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: 125.84 E-value: 7.74e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 9 ISGAGAFTALLPLLtgKQRILLVTDANVGKLDAARQIRTLLED----EGRQVQIVDsVPAEPSQHD---MTQILRLVSAN 81
Cdd:cd08184 5 LFGRGSFDQLGELL--AERRKSNNDYVVFFIDDVFKGKPLLDRlplqNGDLLIFVD-TTDEPKTDQidaLRAQIRAENDK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 82 QPELIVGIGGGSVLDVAKLLSVLLhpDSPGLEAL-----LAGEKPQQKVTsllIPATAGTGSEATPNAILAIPEQntKVG 156
Cdd:cd08184 82 LPAAVVGIGGGSTMDIAKAVSNML--TNPGSAADyqgwdLVKNPGIYKIG---VPTLSGTGAEASRTAVLTGPEK--KLG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 157 IISPVLLPDYVALLPELTTSMPAHIASSTGIDALCHLIECFTSTVANPVSDNAALIGLrKLVRNIELS-VSEPHNLAAKL 235
Cdd:cd08184 155 INSDYTVFDQVILDPELIATVPRDQYFYTGMDCYIHCVESLNGTYRNAFGDAYAEKAL-ELCRDVFLSdDMMSPENREKL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 236 EMlwASYYGGVAINHAGTHLVHALSYPLGGKYHLPHGVANAILlapcmkvvrphavakFAQVWDLLPEADLTLSEEEKSH 315
Cdd:cd08184 234 MV--ASYLGGSSIANSQVGVCHALSYGLSVVLGTHHGVANCIV---------------FNVLEEFYPEGVKEFREMLEKQ 296
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 490214900 316 alvawlaalvkRLQLPDNLAAlGVPPESISELSEAALNVKRLLNNA 361
Cdd:cd08184 297 -----------NITLPKGICK-DLTDEQYEKMVAVTLIHEKPLTNA 330
|
|
| MAR |
cd08177 |
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic ... |
11-352 |
2.41e-31 |
|
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: 121.46 E-value: 2.41e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 11 GAGAFTALLPLLT--GKQRILLVTDAnvGKLDAARQIRTLLEDEGRQV--QIVDSVPAEpsqhDMTQILRLVSANQPELI 86
Cdd:cd08177 7 GAGTLAELAEELErlGARRALVLSTP--RQRALAERVAALLGDRVAGVfdGAVMHVPVE----VAERALAAAREAGADGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 87 VGIGGGSVLDVAKLLSvlLHPDSPgleaLLAgekpqqkvtsllIPATAgTGSEATPnaILAIPEQNTKVGIISPVLLPDY 166
Cdd:cd08177 81 VAIGGGSAIGLAKAIA--LRTGLP----IVA------------VPTTY-AGSEMTP--IWGETEDGVKTTGRDPRVLPRT 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 167 VALLPELTTSMPAHIASSTGIDALCHLIECFTSTVANPVSDNAALIGLRKLVRNIELSVSEPHNLAAKLEMLWASYYGGV 246
Cdd:cd08177 140 VIYDPDLTLGLPAALSVASGLNALAHAVEALYAPDANPITSLLAEEGIRALARALPRLVADPSDLEARSDALYGAWLAGV 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 247 AINHAGTHLVHALSYPLGGKYHLPHGVANAILLapcmkvvrPHAVakfAQVWDLLPEADLTLSEEEKSHALVAWLAALVK 326
Cdd:cd08177 220 VLGSVGMGLHHKLCHVLGGTFDLPHAETHAVVL--------PHVL---AYNAPAAPDAMARLARALGGGDAAGGLYDLAR 288
|
330 340
....*....|....*....|....*.
gi 490214900 327 RLQLPDNLAALGVPPESISELSEAAL 352
Cdd:cd08177 289 RLGAPTSLRDLGMPEDDIDRAADLAL 314
|
|
| DHQ_Fe-ADH |
cd07766 |
Dehydroquinate synthase-like (DHQ-like) and iron-containing alcohol dehydrogenases (Fe-ADH); ... |
26-352 |
5.24e-22 |
|
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: 94.35 E-value: 5.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 26 QRILLVTDANVGKLDAArQIRTLLeDEGRQVQIVDSVPAEPSQHDMTQILRLVSANQPELIVGIGGGSVLDVAKLLSVLL 105
Cdd:cd07766 23 DRALVVSDEGVVKGVGE-KVADSL-KKGLAVAIFDFVGENPTFEEVKNAVERARAAEADAVIAVGGGSTLDTAKAVAALL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 106 HPDSPGLEallagekpqqkvtsllIPATAGTGSEATPNAILAIPEQNTKVgiISPVLLPDYVALLPELTTSMPAHIASST 185
Cdd:cd07766 101 NRGIPFII----------------VPTTASTDSEVSPKSVITDKGGKNKQ--VGPHYNPDVVFVDTDITKGLPPRQVASG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 186 GIDALCHLIEcftstvanpvsdnaaligLRKLVrnielsvsephnlaaklemlWASYY-GGVAINHAGTHLVHALSYPLG 264
Cdd:cd07766 163 GVDALAHAVE------------------LEKVV--------------------EAATLaGMGLFESPGLGLAHAIGHALT 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 265 GKYHLPHGVANAILLAPCMKVVRphavakfaqvwDLLPEadltlseeekSHALVAWLAALVKRLQLPDNLAALGVPPESI 344
Cdd:cd07766 205 AFEGIPHGEAVAVGLPYVLKVAN-----------DMNPE----------PEAAIEAVFKFLEDLGLPTHLADLGVSKEDI 263
|
....*...
gi 490214900 345 SELSEAAL 352
Cdd:cd07766 264 PKLAEKAL 271
|
|
| PRK15138 |
PRK15138 |
alcohol dehydrogenase; |
11-347 |
2.41e-12 |
|
alcohol dehydrogenase;
Pssm-ID: 185092 [Multi-domain] Cd Length: 387 Bit Score: 67.51 E-value: 2.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 11 GAGAFTALLPLLTGKQRILLV-TDANVGKLDAARQIRTLLEdeGRQVQIVDSVPAEPSQHDMTQILRLVSANQPELIVGI 89
Cdd:PRK15138 15 GKGAIAGLREQIPADARVLITyGGGSVKKTGVLDQVLDALK--GMDVLEFGGIEPNPTYETLMKAVKLVREEKITFLLAV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 90 GGGSVLDVAKLLSVLLHPDSpGLEALLAGEKPQQKVTS-------LLIPAtagTGSEATPNAILAIPEQNTKVGIISPVL 162
Cdd:PRK15138 93 GGGSVLDGTKFIAAAANYPE-NIDPWHILETGGKEIKSaipmgsvLTLPA---TGSESNAGAVISRKTTGDKQAFHSPHV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 163 LPDYVALLPELTTSMPAHIASSTGIDALCHLIECF-TSTVANPVSDNAALIGLRKLVRNIELSVSEPHNLAAKLEMLWAS 241
Cdd:PRK15138 169 QPVFAVLDPVYTYTLPPRQVANGVVDAFVHTVEQYvTYPVDAKIQDRFAEGILLTLIEEGPKALKEPENYDVRANVMWAA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 242 YYGGVAINHAGTH---LVHALSYPLGGKYHLPHGVANAILLAPCMKVVRPHAVAKFAQ----VWDLLPEadltlSEEEKS 314
Cdd:PRK15138 249 TQALNGLIGAGVPqdwATHMLGHELTAMHGLDHAQTLAIVLPALWNEKRDTKRAKLLQyaerVWNITEG-----SDDERI 323
|
330 340 350
....*....|....*....|....*....|...
gi 490214900 315 HALVAWLAALVKRLQLPDNLAALGVPPESISEL 347
Cdd:PRK15138 324 DAAIAATRNFFEQMGVPTRLSDYGLDGSSIPAL 356
|
|
| GldA |
COG0371 |
Glycerol dehydrogenase or related enzyme, iron-containing ADH family [Energy production and ... |
6-106 |
2.28e-11 |
|
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: 64.42 E-value: 2.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 6 STLISGAGAFTALLPLLTG-KQRILLVTDANVGKLdAARQIRTLLEDEGRQVQIVdSVPAEPSQHDMTQILRLVSANQPE 84
Cdd:COG0371 7 RRYVQGEGALDELGEYLADlGKRALIITGPTALKA-AGDRLEESLEDAGIEVEVE-VFGGECSEEEIERLAEEAKEQGAD 84
|
90 100
....*....|....*....|..
gi 490214900 85 LIVGIGGGSVLDVAKLLSVLLH 106
Cdd:COG0371 85 VIIGVGGGKALDTAKAVAYRLG 106
|
|
| G1PDH-like |
cd08174 |
Glycerol-1-phosphate dehydrogenase-like; These glycerol-1-phosphate dehydrogenase-like ... |
11-99 |
7.52e-09 |
|
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: 56.76 E-value: 7.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 11 GAGAFTALLPLLT----GKQRILLVTDANVGKLdAARQIRTLLEDEGRQVQIVDSVPAEpsqhDMTQILRLVSANQPELI 86
Cdd:cd08174 7 EEGALEHLGKYLAdrnqGFGKVAIVTGEGIDEL-LGEDILESLEEAGEIVTVEENTDNS----AEELAEKAFSLPKVDAI 81
|
90
....*....|...
gi 490214900 87 VGIGGGSVLDVAK 99
Cdd:cd08174 82 VGIGGGKVLDVAK 94
|
|
| Gro1PDH |
cd08173 |
Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) catalyzes the reversible conversion between ... |
18-102 |
4.09e-07 |
|
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: 51.40 E-value: 4.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 18 LLPLLTGKQRILLVTDANVGKLdAARQIRTLLEDEGRQVQIVDSVPAEPSQhDMTQILRLVSANQPELIVGIGGGSVLDV 97
Cdd:cd08173 18 VLKKLLLGKRALIITGPNTYKI-AGKRVEDLLESSGVEVVIVDIATIEEAA-EVEKVKKLIKESKADFIIGVGGGKVIDV 95
|
....*
gi 490214900 98 AKLLS 102
Cdd:cd08173 96 AKYAA 100
|
|
| GlyDH-like |
cd08550 |
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins. ... |
26-106 |
3.74e-06 |
|
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: 48.30 E-value: 3.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 26 QRILLVTDANVgkLDAARQ-IRTLLEDEGRQVQIVdSVPAEPSQHDMTQILRLVSANQPELIVGIGGGSVLDVAKLLSVL 104
Cdd:cd08550 23 KKALIIGGKTA--LEAVGEkLEKSLEEAGIDYEVE-VFGGECTEENIERLAEKAKEEGADVIIGIGGGKVLDTAKAVADR 99
|
..
gi 490214900 105 LH 106
Cdd:cd08550 100 LG 101
|
|
| GlyDH |
cd08170 |
Glycerol dehydrogenases (GlyDH) catalyzes oxidation of glycerol to dihydroxyacetone in ... |
9-99 |
2.58e-05 |
|
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: 45.87 E-value: 2.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 9 ISGAGAFTALLplltGKqRILLVTDANVGKLdAARQIRTLLEDEGRQVQIVDsVPAEPSQHDMTQILRLVSANQPELIVG 88
Cdd:cd08170 11 LDRLGEYLAPL----GK-KALVIADPFVLDL-VGERLEESLEKAGLEVVFEV-FGGECSREEIERLAAIARANGADVVIG 83
|
90
....*....|.
gi 490214900 89 IGGGSVLDVAK 99
Cdd:cd08170 84 IGGGKTIDTAK 94
|
|
| egsA |
PRK00843 |
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed |
22-102 |
5.36e-05 |
|
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed
Pssm-ID: 179139 Cd Length: 350 Bit Score: 44.88 E-value: 5.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 22 LTGKQRILLVTDANVGKLdAARQIRTLLEDEGR-QVQIVDSVPAEpsqhDMTQILRLVSANQPELIVGIGGGSVLDVAKL 100
Cdd:PRK00843 31 LKLTGRALIVTGPTTKKI-AGDRVEENLEDAGDvEVVIVDEATME----EVEKVEEKAKDVNAGFLIGVGGGKVIDVAKL 105
|
..
gi 490214900 101 LS 102
Cdd:PRK00843 106 AA 107
|
|
| GlyDH-like |
cd08172 |
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins ... |
9-106 |
1.53e-04 |
|
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: 43.28 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 9 ISGAGAFTALLPLLT--GKQRILLVTDANVgkLDAARQIRTLLEDEGRQVQIVDsvpAEPSQHDMTQILRLVSANQPELI 86
Cdd:cd08172 5 ICEEGALKELPELLSefGIKRPLIIHGEKS--WQAAKPYLPKLFEIEYPVLRYD---GECSYEEIDRLAEEAKEHQADVI 79
|
90 100
....*....|....*....|
gi 490214900 87 VGIGGGSVLDVAKLLSVLLH 106
Cdd:cd08172 80 IGIGGGKVLDTAKAVADKLN 99
|
|
| gldA |
PRK09423 |
glycerol dehydrogenase; Provisional |
9-99 |
3.97e-03 |
|
glycerol dehydrogenase; Provisional
Pssm-ID: 181843 Cd Length: 366 Bit Score: 39.03 E-value: 3.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 9 ISGAGAFTALLPLLT--GKqRILLVTDANVGKLdAARQIRTLLEDEGrqVQIVDSV-PAEPSQHDMTQILRLVSANQPEL 85
Cdd:PRK09423 12 VQGKGALARLGEYLKplGK-RALVIADEFVLGI-VGDRVEASLKEAG--LTVVFEVfNGECSDNEIDRLVAIAEENGCDV 87
|
90
....*....|....
gi 490214900 86 IVGIGGGSVLDVAK 99
Cdd:PRK09423 88 VIGIGGGKTLDTAK 101
|
|
| DHQS |
cd08195 |
Dehydroquinate synthase (DHQS) catalyzes the conversion of DAHP to DHQ in shikimate pathway ... |
10-98 |
6.37e-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: 38.19 E-value: 6.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 10 SGAGAFTALLPLLTGKQRILLVTDANVGKLdAARQIRTLLEDEGRQVQIVdSVPA-EPSQhDMTQILRLVS------ANQ 82
Cdd:cd08195 8 SGLLDKLGELLELKKGSKVVIVTDENVAKL-YGELLLKSLEAAGFKVEVI-VIPAgEKSK-SLETVERIYDflleagLDR 84
|
90
....*....|....*.
gi 490214900 83 PELIVGIGGGSVLDVA 98
Cdd:cd08195 85 DSLLIALGGGVVGDLA 100
|
|
| EEVS |
cd08199 |
2-epi-5-epi-valiolone synthase (EEVS); 2-epi-5-epi-valiolone synthase catalyzes the ... |
5-106 |
6.81e-03 |
|
2-epi-5-epi-valiolone synthase (EEVS); 2-epi-5-epi-valiolone synthase catalyzes the cyclization of sedoheptulose 7-phosphate to 2-epi-5-epi-valiolone in the biosynthesis of C(7)N-aminocyclitol-containing products. The cyclization product, 2-epi-5-epi-valiolone ((2S,3S,4S,5R)-5-(hydroxymethyl)cyclohexanon-2,3,4,5-tetrol), is a precursor of the valienamine moiety. The valienamine unit is responsible for their biological activities as various glycosidic hydrolases inhibitors. Two important microbial secondary metabolites, validamycin and acarbose, are used in agricultural and biomedical applications. Validamycin A is an antifungal antibiotic which has a strong trehalase inhibitory activity and has been used to control sheath blight disease in rice caused by Rhizoctonia solani. Acarbose is an alpha-glucosidase inhibitor used for the treatment of type II insulin-independent diabetes. Salbostatin produced by Streptomyces albus also belongs to this family. It exhibits strong trehalase inhibitory activity.
Pssm-ID: 341478 Cd Length: 349 Bit Score: 38.28 E-value: 6.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490214900 5 NSTLISGAGaftallpllTGKQRILLVTDANVGKLDAARqIRTLLEDEGRQVQIVdsvPAEPSQH--DMTQILRLVSA-- 80
Cdd:cd08199 15 NPTLADAYG---------RPGRRRLVVVDENVDRLYGAR-IRAYFAAHGIEATIL---VLPGGEAnkTMETVLRIVDAld 81
|
90 100 110
....*....|....*....|....*....|
gi 490214900 81 ----NQPELIVGIGGGSVLDVAKLLSVLLH 106
Cdd:cd08199 82 dfglDRREPVIAIGGGVLLDVVGFAASLYR 111
|
|
| |
