|
Name |
Accession |
Description |
Interval |
E-value |
| YqdH |
COG1979 |
Alcohol dehydrogenase YqhD, Fe-dependent ADH family [Energy production and conversion]; |
1-389 |
0e+00 |
|
Alcohol dehydrogenase YqhD, Fe-dependent ADH family [Energy production and conversion];
Pssm-ID: 441582 [Multi-domain] Cd Length: 387 Bit Score: 619.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 1 MNIFLQHNPTKLYFGENQITKLSQELASYHKqvNVLLVYGGGSIKRNGVYDEVKAELQSINAVVHELSGVEPNPRLTTVA 80
Cdd:COG1979 1 MNNFTFYNPTKIIFGKGQIAKLGEEIPKYGK--KVLLVYGGGSIKKNGLYDQVKAALKEAGIEVVEFGGVEPNPRLETVR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 81 KGVDICKKENIGFLLAVGGGSVIDCTKAIAAGAVYEGNTWDLITRKKEITDALPFGTVLTLAATGSEMNSTSVITNWETK 160
Cdd:COG1979 79 KGVELCKEEGIDFILAVGGGSVIDGAKAIAAGAKYDGDPWDILTGKAPVEKALPLGTVLTLPATGSEMNSGSVITNEETK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 161 EKLGWTSSHVFPVFSILDPAYTFSVPRDQTVYGIVDSMSHALEHYFHRTENTPMIDGFIESLLRTAVQEGPKLLKDLTSY 240
Cdd:COG1979 159 EKLGFGSPLVFPKFSILDPELTYTLPKRQTANGIVDIFSHVMEQYFTYPVDAPLQDRFAEGLLRTLIEEGPKALKDPEDY 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 241 KYRETMMYISTTAFNGSLANGTdGGDWATHRIEHALSAVYDIPHGGGLAILFPNWLEHVLKEDPSRVKQLAVNVFGIDPa 320
Cdd:COG1979 239 DARANLMWAATLALNGLIGAGV-PQDWATHMIEHELSALYDIDHGAGLAIVLPAWMRYVLEEKPEKFAQYAERVWGITE- 316
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1265435555 321 gKSDEETAMEGAKALRTFWNDLGAPNSLRDYDIDDSEFDAIVEKTFV--KPGVGTYKELDYASVRDILERS 389
Cdd:COG1979 317 -GDDEERALEGIEATEEFFESLGLPTRLSEYGIDEEDIEEMAEKATAhgMTALGEFKDLTPEDVREILELA 386
|
|
| BDH |
cd08187 |
Butanol dehydrogenase catalyzes the conversion of butyraldehyde to butanol with the cofactor ... |
4-387 |
0e+00 |
|
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: 580.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 4 FLQHNPTKLYFGENQITKLSQELASYHKqvNVLLVYGGGSIKRNGVYDEVKAELQSINAVVHELSGVEPNPRLTTVAKGV 83
Cdd:cd08187 2 FTFYNPTKIIFGKGAIEELGEEIKKYGK--KVLLVYGGGSIKKNGLYDRVVASLKEAGIEVVEFGGVEPNPRLETVREGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 84 DICKKENIGFLLAVGGGSVIDCTKAIAAGAVYEGNTWDLITRKKEITDALPFGTVLTLAATGSEMNSTSVITNWETKEKL 163
Cdd:cd08187 80 ELAREENVDFILAVGGGSVIDAAKAIAAGAKYDGDVWDFFTGKAPPEKALPVGTVLTLAATGSEMNGGAVITNEETKEKL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 164 GWTSSHVFPVFSILDPAYTFSVPRDQTVYGIVDSMSHALEHYFHRTENTPMIDGFIESLLRTAVQEGPKLLKDLTSYKYR 243
Cdd:cd08187 160 GFGSPLLRPKFSILDPELTYTLPKYQTAAGIVDIFSHVLEQYFTGTEDAPLQDRLAEGLLRTVIENGPKALKDPDDYEAR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 244 ETMMYISTTAFNGSLANGTdGGDWATHRIEHALSAVYDIPHGGGLAILFPNWLEHVLKEDPSRVKQLAVNVFGIDPaGKS 323
Cdd:cd08187 240 ANLMWAATLALNGLLGAGR-GGDWATHAIEHELSALYDITHGAGLAIVFPAWMRYVLKKKPERFAQFARRVFGIDP-GGD 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1265435555 324 DEETAMEGAKALRTFWNDLGAPNSLRDYDIDDSEFDAIVEKTFVKPGVGT-YKELDYASVRDILE 387
Cdd:cd08187 318 DEETALEGIEALEEFFKSIGLPTTLSELGIDEEDIEEMAEKAVRGGGLGGgFKPLTREDIEEILK 382
|
|
| Fe-ADH |
pfam00465 |
Iron-containing alcohol dehydrogenase; |
9-366 |
7.17e-114 |
|
Iron-containing alcohol dehydrogenase;
Pssm-ID: 425696 [Multi-domain] Cd Length: 362 Bit Score: 336.50 E-value: 7.17e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 9 PTKLYFGENQITKLSQELASYHKqvNVLLVYGGGSIKrNGVYDEVKAELQSINAVVHELSGVEPNPRLTTVAKGVDICKK 88
Cdd:pfam00465 1 PTRIVFGAGALAELGEELKRLGA--RALIVTDPGSLK-SGLLDKVLASLEEAGIEVVVFDGVEPEPTLEEVDEAAALARE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 89 ENIGFLLAVGGGSVIDCTKAIAAGAVYEGNTWDLITRKKEITDALPFGTVLTLAATGSEMNSTSVITNWETKEKLGWTSS 168
Cdd:pfam00465 78 AGADVIIAVGGGSVIDTAKAIALLLTNPGDVWDYLGGKPLTKPALPLIAIPTTAGTGSEVTPLAVITDTETGEKLGIFSP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 169 HVFPVFSILDPAYTFSVPRDQTVYGIVDSMSHALEHYFHRTENtPMIDGFIESLLRTAVQEGPKLLKDLTSYKYRETMMY 248
Cdd:pfam00465 158 KLLPDLAILDPELTLTLPPRLTAATGMDALAHAVEAYVSKGAN-PLTDALALEAIRLIAENLPRAVADGEDLEARENMLL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 249 IST---TAF-NGSLAngtdggdwATHRIEHALSAVYDIPHGGGLAILFPNWLEHVLKEDPSRVKQLAVNVFGIdpagkSD 324
Cdd:pfam00465 237 ASTlagLAFsNAGLG--------AAHALAHALGGRYGIPHGLANAILLPYVLRFNAPAAPEKLAQLARALGED-----SD 303
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1265435555 325 EETAMEGAKALRTFWNDLGAPNSLRDYDIDDSEFDAIVEKTF 366
Cdd:pfam00465 304 EEAAEEAIEALRELLRELGLPTTLSELGVTEEDLDALAEAAL 345
|
|
| PRK15138 |
PRK15138 |
alcohol dehydrogenase; |
1-364 |
1.25e-102 |
|
alcohol dehydrogenase;
Pssm-ID: 185092 [Multi-domain] Cd Length: 387 Bit Score: 308.65 E-value: 1.25e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 1 MNIFLQHNPTKLYFGENQITKLSQELASyhkQVNVLLVYGGGSIKRNGVYDEVKAELQSINavVHELSGVEPNPRLTTVA 80
Cdd:PRK15138 1 MNNFNLHTPTRILFGKGAIAGLREQIPA---DARVLITYGGGSVKKTGVLDQVLDALKGMD--VLEFGGIEPNPTYETLM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 81 KGVDICKKENIGFLLAVGGGSVIDCTKAIAAGAVYEGNT--WDLI-TRKKEITDALPFGTVLTLAATGSEMNSTSVITNW 157
Cdd:PRK15138 76 KAVKLVREEKITFLLAVGGGSVLDGTKFIAAAANYPENIdpWHILeTGGKEIKSAIPMGSVLTLPATGSESNAGAVISRK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 158 ETKEKLGWTSSHVFPVFSILDPAYTFSVPRDQTVYGIVDSMSHALEHYFHRTENTPMIDGFIESLLRTAVQEGPKLLKDL 237
Cdd:PRK15138 156 TTGDKQAFHSPHVQPVFAVLDPVYTYTLPPRQVANGVVDAFVHTVEQYVTYPVDAKIQDRFAEGILLTLIEEGPKALKEP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 238 TSYKYRETMMYISTTAFNGSLANGTDgGDWATHRIEHALSAVYDIPHGGGLAILFPNWLehVLKEDPSRVK--QLAVNVF 315
Cdd:PRK15138 236 ENYDVRANVMWAATQALNGLIGAGVP-QDWATHMLGHELTAMHGLDHAQTLAIVLPALW--NEKRDTKRAKllQYAERVW 312
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1265435555 316 GIdpAGKSDEETAMEGAKALRTFWNDLGAPNSLRDYDIDDSEFDAIVEK 364
Cdd:PRK15138 313 NI--TEGSDDERIDAAIAATRNFFEQMGVPTRLSDYGLDGSSIPALLKK 359
|
|
| EutG |
COG1454 |
Alcohol dehydrogenase, class IV [Energy production and conversion]; |
1-389 |
6.64e-90 |
|
Alcohol dehydrogenase, class IV [Energy production and conversion];
Pssm-ID: 441063 [Multi-domain] Cd Length: 381 Bit Score: 275.85 E-value: 6.64e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 1 MNIFlqHNPTKLYFGENQITKLSQELASYHKQvNVLLVyGGGSIKRNGVYDEVKAELQSINAVVHELSGVEPNPRLTTVA 80
Cdd:COG1454 2 MFTF--RLPTRIVFGAGALAELGEELKRLGAK-RALIV-TDPGLAKLGLLDRVLDALEAAGIEVVVFDDVEPNPTVETVE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 81 KGVDICKKENIGFLLAVGGGSVIDCTKAIAAGAVYEGNTWDLITRKKEITDALPFGTVLTLAATGSEMNSTSVITNWETK 160
Cdd:COG1454 78 AGAAAAREFGADVVIALGGGSAIDAAKAIALLATNPGDLEDYLGIKKVPGPPLPLIAIPTTAGTGSEVTPFAVITDPETG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 161 EKLGWTSSHVFPVFSILDPAYTFSVPRDQTVYGIVDSMSHALEHYFHRTeNTPMIDGF-IESL------LRTAVQEGpkl 233
Cdd:COG1454 158 VKKGIADPELLPDVAILDPELTLTLPPSLTAATGMDALTHAIEAYVSKG-ANPLTDALaLEAIrliarnLPRAVADG--- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 234 lKDLtsyKYRETMMYIST---TAF-NGSLAngtdggdwATHRIEHALSAVYDIPHGGGLAILFPNWLEHVLKEDPSRVKQ 309
Cdd:COG1454 234 -DDL---EAREKMALASLlagMAFaNAGLG--------AVHALAHPLGGLFHVPHGLANAILLPHVLRFNAPAAPERYAE 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 310 LAvNVFGIDpAGKSDEETAMEGAKALRTFWNDLGAPNSLRDYDIDDSEFDAIVEKTFVKPGVGT-YKELDYASVRDILER 388
Cdd:COG1454 302 IA-RALGLD-VGLSDEEAAEALIEAIRELLRDLGIPTRLSELGVTEEDLPELAELALADRCLANnPRPLTEEDIEAILRA 379
|
.
gi 1265435555 389 S 389
Cdd:COG1454 380 A 380
|
|
| Fe-ADH-like |
cd08185 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
7-387 |
1.44e-88 |
|
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: 272.45 E-value: 1.44e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 7 HNPTKLYFGENQITKLSQELASYHKqvNVLLVYGGGSIKRNGVYDEVKAELQS--INAVVheLSGVEPNPRLTTVAKGVD 84
Cdd:cd08185 2 YQPTRILFGAGKLNELGEEALRPGK--KALIVTGKGSSKKTGLLDRVKKLLEKagVEVVV--FDKVEPNPLTTTVMEGAA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 85 ICKKENIGFLLAVGGGSVIDCTKAIAAGAVYEGNTWDLI---TRKKEITD-ALPFGTVLTLAATGSEMNSTSVITNWETK 160
Cdd:cd08185 78 LAKEEGCDFVIGLGGGSSMDAAKAIAFMATNPGDIWDYIfggTGKGPPPEkALPIIAIPTTAGTGSEVDPWAVITNPETK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 161 EKLGWTSSHVFPVFSILDPAYTFSVPRDQTVYGIVDSMSHALEHYFHrTENTPMIDGFIESLLRTAVQEGPKLLKDLTSY 240
Cdd:cd08185 158 EKKGIGHPALFPKVSIVDPELMLTVPPRVTAYTGFDALFHAFESYIS-KNANPFSDMLALEAIRLVAKYLPRAVKDGSDL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 241 KYRETMMYISTTAfnG-SLANgtdGGDWATHRIEHALSAVY-DIPHGGGLAILFPNWLEHVLKEDPSRVKQLAVnvfgID 318
Cdd:cd08185 237 EAREKMAWASTLA--GiVIAN---SGTTLPHGLEHPLSGYHpNIPHGAGLAALYPAYFEFTIEKAPEKFAFVAR----AE 307
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1265435555 319 PAGKSDEETAMEGAKALRTFWNDLGAPNSLRDYDIDDSEFDAIVEKTFVKPGV---GTYKELDYASVRDILE 387
Cdd:cd08185 308 ASGLSDAKAAEDFIEALRKLLKDIGLDDLLSDLGVTEEDIPWLAENAMETMGGlfaNNPVELTEEDIVEIYE 379
|
|
| Fe-ADH |
cd08551 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains large ... |
9-366 |
5.40e-85 |
|
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: 263.15 E-value: 5.40e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 9 PTKLYFGENQITKLSQELASYHKQvNVLLVYGGGsIKRNGVYDEVKAELQSINAVVHELSGVEPNPRLTTVAKGVDICKK 88
Cdd:cd08551 1 PTRIVFGAGALARLGEELKALGGK-KVLLVTDPG-LVKAGLLDKVLESLKAAGIEVEVFDDVEPNPTVETVEAAAELARE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 89 ENIGFLLAVGGGSVIDCTKAIAAGAVYEGNTWDLITRKKEITDALPFGTVLTLAATGSEMNSTSVITNWETKEKLGWTSS 168
Cdd:cd08551 79 EGADLVIAVGGGSVLDTAKAIAVLATNGGSIRDYEGIGKVPKPGLPLIAIPTTAGTGSEVTPNAVITDPETGRKMGIVSP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 169 HVFPVFSILDPAYTFSVPRDQTVYGIVDSMSHALEHYFHRTENtPMIDGF-IESL------LRTAVQEGpkllKDLTSyk 241
Cdd:cd08551 159 YLLPDVAILDPELTLSLPPSVTAATGMDALTHAIEAYTSKKAN-PISDALaLEAIrligknLRRAVADG----SDLEA-- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 242 yRETMMYIST---TAFNGSlangtdgGDWATHRIEHALSAVYDIPHGGGLAILFPNWLEHVLKEDPSRVKQLAvNVFGID 318
Cdd:cd08551 232 -REAMLLASLlagIAFGNA-------GLGAVHALAYPLGGRYHIPHGVANAILLPYVMEFNLPACPEKYAEIA-EALGED 302
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1265435555 319 PAGKSDEETAMEGAKALRTFWNDLGAPNSLRDYDIDDSEFDAIVEKTF 366
Cdd:cd08551 303 VEGLSDEEAAEAAVEAVRELLRDLGIPTSLSELGVTEEDIPELAEDAM 350
|
|
| Fe-ADH-like |
cd14863 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
9-388 |
3.08e-71 |
|
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: 227.80 E-value: 3.08e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 9 PTKLYFGENQITKLSQELASYHKQvNVLLVYGGGsIKRNGVYDEVKAELQSINAVVHELSGVEPNPRLTTVAKGVDICKK 88
Cdd:cd14863 5 LTPVIFGAGAVEQIGELLKELGCK-KVLLVTDKG-LKKAGIVDKIIDLLEEAGIEVVVFDDVEPDPPDEIVDEAAEIARE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 89 ENIGFLLAVGGGSVIDCTKAIAAGAVYEGNTWD-LITRKKEITDALPFGTVLTLAATGSEMNSTSVITNWETKEKLGWTS 167
Cdd:cd14863 83 EGADGVIGIGGGSVLDTAKAIAVLLTNPGPIIDyALAGPPVPKPGIPLIAIPTTAGTGSEVTPIAVITDEENGVKKSLLG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 168 SHVFPVFSILDPAYTFSVPRDQTVYGIVDSMSHALEHYFHrTENTPMIDGF-------IESLLRTAVQEGpkllKDLTSy 240
Cdd:cd14863 163 PFLVPDLAILDPELTVGLPPSLTAATGMDALSHAIEAYTS-KLANPMTDALalqairlIVKNLPRAVKDG----DNLEA- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 241 kyRETMMYIST---TAFNgslangtDGGDWATHRIEHALSAVYDIPHGGGLAILFPNWLEHVLKEDPSRVKQLAvNVFGI 317
Cdd:cd14863 237 --RENMLLASNlagIAFN-------NAGTHIGHAIAHALGALYHIPHGLACALALPVVLEFNAEAYPEKVKKIA-KALGV 306
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1265435555 318 DPAGKSDEETAMEGAKALRTFWNDLGAPNSLRDYDIDDSEFDAIVEKTFVKP-GVGTYKELDYASVRDILER 388
Cdd:cd14863 307 SFPGESDEELGEAVADAIREFMKELGIPSLFEDYGIDKEDLDKIAEAVLKDPfAMFNPRPITEEEVAEILEA 378
|
|
| Fe-ADH-like |
cd08196 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
7-366 |
1.12e-60 |
|
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: 200.11 E-value: 1.12e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 7 HNPTKLYFGENQITKLSQELASYHKQvNVLLVyGGGSIKRNGVYDEVKAELQSINAVVHelSGVEPNPRLTTVAKGVDIC 86
Cdd:cd08196 4 YQPVKIIFGEGILKELPDIIKELGGK-RGLLV-TDPSFIKSGLAKRIVESLKGRIVAVF--SDVEPNPTVENVDKCARLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 87 KKENIGFLLAVGGGSVIDCTKAIAAGAVYEGNTWDLITRKKEITD-ALPFGTVLTLAATGSEMNSTSVITNWETKEKLGW 165
Cdd:cd08196 80 RENGADFVIAIGGGSVLDTAKAAACLAKTDGSIEDYLEGKKKIPKkGLPLIAIPTTAGTGSEVTPVAVLTDKEKGKKAPL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 166 TSSHVFPVFSILDPAYTFSVPRDQTV-YGIvDSMSHALEHYFHRTENtPMIDGF-IESL------LRTAVQEGPKLlkdl 237
Cdd:cd08196 160 VSPGFYPDIAIVDPELTYSMPPKVTAsTGI-DALCHAIEAYWSINHQ-PISDALaLEAAklvlenLEKAYNNPNDK---- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 238 tsyKYRETMMYISTT---AFNgslANGTDggdwATHRIEHALSAVYDIPHGGGLAILFPNWLEHVLKEDPSRVKQLAvNV 314
Cdd:cd08196 234 ---EAREKMALASLLaglAFS---QTRTT----ASHACSYPLTSHFGIPHGEACALTLPSFIRLNAEALPGRLDELA-KQ 302
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1265435555 315 FGIdpagksdeETAMEGAKALRTFWNDLGAPNSLRDYDIDDSEFDAIVEKTF 366
Cdd:cd08196 303 LGF--------KDAEELADKIEELKKRIGLRTRLSELGITEEDLEEIVEESF 346
|
|
| Fe-ADH-like |
cd08186 |
Iron-containing alcohol dehydrogenase; This family contains iron-containing alcohol ... |
10-389 |
2.77e-58 |
|
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: 194.41 E-value: 2.77e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 10 TKLYFGENQITKLSQELASYHKQvNVLLVYGGGSIKRNGVYDEVKAELQSiNAVVHEL-SGVEPNPRLTTVAKGVDICKK 88
Cdd:cd08186 2 TTLYFGVGAIAKIKDILKDLGID-KVIIVTGRSSYKKSGAWDDVEKALEE-NGIEYVVyDKVTPNPTVDQADEAAKLARD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 89 ENIGFLLAVGGGSVIDCTKAIAAGAVYEGNTW-DLITRKKEITDALPFGTVLTLAATGSEMNSTSVITNWETKEKLGWTS 167
Cdd:cd08186 80 FGADAVIAIGGGSPIDTAKSVAVLLAYGGKTArDLYGFRFAPERALPLVAINLTHGTGSEVDRFAVATIPEKGYKPGIAY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 168 SHVFPVFSILDPAYTFSVPRDQTVYGIVDSMSHALEHYFHRTENtPMIDGFIESLLRTAVQEGPKLLKDLTSYKYRETMM 247
Cdd:cd08186 160 DCIYPLYAIDDPRLTLTLPKEQTLYTSIDAFNHVYEAATTKVSS-PYVITLAKEAIRLIAEYLPRALANPKDLEARYWLL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 248 Y---ISTTAFNGSLANgtdggdwATHRIEHALSAVY-DIPHGGGLAILFPNWLEHVLkedPSRVKQLAVNVFGIDPAGKS 323
Cdd:cd08186 239 YasmIAGIAIDNGLLH-------LTHALEHPLSGLKpELPHGLGLALLGPAVVKYIY---KAVPETLADILRPIVPGLKG 308
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1265435555 324 DEETAMEGAKALRTFWNDLGAPNSLRDYDIDDSEFDAIVEKTFVKPGVGTYK-----ELDYASVRDILERS 389
Cdd:cd08186 309 TPDEAEKAARGVEEFLFSVGFTEKLSDYGFTEDDVDRLVELAFTTPSLDLLLslapvEVTEEVVREIYEES 379
|
|
| PPD-like |
cd08181 |
1,3-propanediol dehydrogenase-like (PPD); This family contains proteins similar to 1, ... |
9-387 |
4.28e-57 |
|
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: 190.49 E-value: 4.28e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 9 PTKLYFGENQITKLSQELASYHKqvNVLLVYGGGSIKRNGVYDEVKAELQSiNAVVHEL-SGVEPNPRLTTVAKGVDICK 87
Cdd:cd08181 4 PTKVYFGKNCVEKHADELAALGK--KALIVTGKHSAKKNGSLDDVTEALEE-NGIEYFIfDEVEENPSIETVEKGAELAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 88 KENIGFLLAVGGGSVIDCTKAIAAGAVYEGNTWDLITRKKEiTDALPFGTVLTLAATGSEMNSTSVITNWETKEKLGWTS 167
Cdd:cd08181 81 KEGADFVIGIGGGSPLDAAKAIALLAANKDGDEDLFQNGKY-NPPLPIVAIPTTAGTGSEVTPYSILTDHEKGTKKSFGN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 168 SHVFPVFSILDPAYTFSVPRDQTVYGIVDSMSHALEHYFHRtENTPMIDGFIESLLRTAVQEGPKLLKDLTSYKYRETMM 247
Cdd:cd08181 160 PLIFPKLALLDPKYTLSLPEELTIDTAVDALSHAIEGYLSV-KATPLSDALALEALRLIGECLPNLLGDELDEEDREKLM 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 248 YISTTAfnGSLANGTdgGDWATHRIEHALSAVYDIPHGGGLAILFPNWLEHVLKEDPSRVKQLAvnvfgidpagksdEET 327
Cdd:cd08181 239 YASTLA--GMVIAQT--GTTLPHGLGYPLTYFKGIPHGRANGILLPAYLKLCEKQEPEKVDKIL-------------KLL 301
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1265435555 328 AMEGAKALRTFWNDLGAPNSlrdyDIDDSEFDAIVEKTFVKPGV-GTYKELDYASVRDILE 387
Cdd:cd08181 302 GFGSIEEFQKFLNRLLGKKE----ELSEEELEKYADEAMKAKNKkNTPGNVTKEDILRIYR 358
|
|
| Fe-ADH-like |
cd14865 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
7-389 |
7.92e-54 |
|
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: 182.74 E-value: 7.92e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 7 HNPTKLYFGENQITKLSQELASYHKQvNVLLVYGGGsIKRNGVYDEVKAELQSINAVVHELSGVEPNPRLTTVAKGVDIC 86
Cdd:cd14865 4 FNPTKIVSGAGALENLPAELARLGAR-RPLIVTDKG-LAAAGLLKKVEDALGDAIEIVGVFDDVPPDSSVAVVNEAAARA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 87 KKENIGFLLAVGGGSVIDCTKAIAAGAVYEGNTWD------LITRKKeitdaLPFGTVLTLAATGSEMNSTSVITNWETK 160
Cdd:cd14865 82 REAGADGIIAVGGGSVIDTAKGVNILLSEGGDDLDdygganRLTRPL-----KPLIAIPTTAGTGSEVTLVAVIKDEEKK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 161 EKLGWTSSHVFPVFSILDPAYTFSVPRDQTVYGIVDSMSHALEHYfHRTENTPMIDGF-------IESLLRTAVQEGpkl 233
Cdd:cd14865 157 VKLLFVSPFLLPDVAILDPRLTLSLPPKLTAATGMDALTHAIEAY-TSLQKNPISDALalqairlISENLPKAVKNG--- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 234 lKDLtsyKYRETMMYIST---TAFNGSLANgtdggdwATHRIEHALSAVYDIPHGGGLAILFPNWLEHVLKEDPSRVKQL 310
Cdd:cd14865 233 -KDL---EARLALAIAATmagIAFSNSMVG-------LVHAIAHAVGAVAGVPHGLANSILLPHVMRYNLDAAAERYAEL 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 311 AVN-VFGIDPAGKSDEETAMEGAKALRTFWNDLGAPNSLRDYDIDDSEFDAIVEKTFVKpGVGTY--KELDYASVRDILE 387
Cdd:cd14865 302 ALAlAYGVTPAGRRAEEAIEAAIDLVRRLHELCGLPTRLRDVGVPEEQLEAIAELALND-GAILFnpREVDPEDILAILE 380
|
..
gi 1265435555 388 RS 389
Cdd:cd14865 381 AA 382
|
|
| PDDH |
cd08188 |
1,3-Propanediol (1,3-PD) dehydrogenase; This family includes 1,3-propanediol (1,3-PD) ... |
7-366 |
2.07e-52 |
|
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: 178.86 E-value: 2.07e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 7 HNPTKLYFGENQITKLSQELAS--YHKqvnVLLVYGGGSIKrNGVYDEVKAEL--QSINAVVHelSGVEPNPRLTTVAKG 82
Cdd:cd08188 4 YIPPVNLFGPGCLKEIGDELKKlgGKK---ALIVTDKGLVK-LGLVKKVTDVLeeAGIEYVIF--DGVQPNPTVTNVNEG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 83 VDICKKENIGFLLAVGGGSVIDCTKAIAAGAVYEGNTWDLITRKKEITDALPFGTVLTLAATGSEMNSTSVITNWETKEK 162
Cdd:cd08188 78 LELFKENGCDFIISVGGGSAHDCAKAIGILATNGGEIEDYEGVDKSKKPGLPLIAINTTAGTASEVTRFAVITDEERHVK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 163 LGWTSSHVFPVFSILDPAYTFSVPRDQTVYGIVDSMSHALEHYFhRTENTPMIDGF-------IESLLRTAVQEGpkllK 235
Cdd:cd08188 158 MVIVDWNVTPTIAVNDPELMLGMPPSLTAATGMDALTHAIEAYV-STGATPLTDALaleairlIAENLPKAVANG----K 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 236 DLtsyKYRETMMY---ISTTAF-NGSLANgtdggdwaTHRIEHALSAVYDIPHGGGLAILFPNWLEHVLKEDPSRVKQLA 311
Cdd:cd08188 233 DL---EARENMAYaqfLAGMAFnNAGLGY--------VHAMAHQLGGFYNLPHGVCNAILLPHVMEFNLPACPERFADIA 301
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1265435555 312 vNVFGIDPAGKSDEETAMEGAKALRTFWNDLGAPNSLRDYDIDDSEFDAIVEKTF 366
Cdd:cd08188 302 -RALGENTEGLSDEEAAEAAIEAIRKLSRRVGIPSGLKELGVKEEDFPLLAENAL 355
|
|
| LPO |
cd08176 |
Lactadehyde:propanediol oxidoreductase (LPO) catalyzes the interconversion between ... |
7-363 |
2.10e-52 |
|
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: 178.89 E-value: 2.10e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 7 HNPTKLYFGENQITKLSQELASYHKQvNVLLVYGGGSIKrNGVYDEVKAELQSINAVVHELSGVEPNPRLTTVAKGVDIC 86
Cdd:cd08176 4 VLNPTSYFGWGAIEEIGEEAKKRGFK-KALIVTDKGLVK-FGIVDKVTDVLKEAGIAYTVFDEVKPNPTIENVMAGVAAY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 87 KKENIGFLLAVGGGSVIDCTKAIAA-----GAV---YEGntWDLITRKKEITDALPfgtvlTLAATGSEMNSTSVITNWE 158
Cdd:cd08176 82 KESGADGIIAVGGGSSIDTAKAIGIivanpGADvrsLEG--VAPTKNPAVPIIAVP-----TTAGTGSEVTINYVITDTE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 159 TKEKLGWTSSHVFPVFSILDPAYTFSVPRDQTVYGIVDSMSHALEHYFHRtENTPMIDGF----IESL---LRTAVQEGp 231
Cdd:cd08176 155 KKRKFVCVDPHDIPTVAIVDPDLMSSMPKGLTAATGMDALTHAIEGYITK-GAWELSDMLalkaIELIaknLRKAVANP- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 232 kllkdlTSYKYRETMM---YISTTAFNGslangtdGGDWATHRIEHALSAVYDIPHGGGLAILFPNWLEHVLKEDPSRVK 308
Cdd:cd08176 233 ------NNVEARENMAlaqYIAGMAFSN-------VGLGIVHSMAHPLSAFYDTPHGVANAILLPYVMEFNAPATGEKYR 299
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1265435555 309 QLAVnVFGIDPAGKSDEETAMEGAKALRTFWNDLGAPNSLRDYDIDDSEFDAIVE 363
Cdd:cd08176 300 DIAR-AMGVDTTGMSDEEAAEAAVDAVKKLSKDVGIPQKLSELGVKEEDIEALAE 353
|
|
| Fe-ADH-like |
cd08194 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
9-364 |
4.76e-51 |
|
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: 175.03 E-value: 4.76e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 9 PTKLYFGENQITKLSQELASYHKQvNVLLVyGGGSIKRNGVYDEVKAEL--QSINAVVHelSGVEPNPRLTTVAKGVDIC 86
Cdd:cd08194 1 PRTIIIGGGALEELGEEAASLGGK-RALIV-TDKVMVKLGLVDKVTQLLaeAGIAYAVF--DDVVSEPTDEMVEEGLALY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 87 KKENIGFLLAVGGGSVIDCTKAIAAGAVYEGNTWDLITRKKEITDALPFGTVLTLAATGSEMNSTSVITNWETKEKLGWT 166
Cdd:cd08194 77 KEGGCDFIVALGGGSPIDTAKAIAVLATNGGPIRDYMGPRKVDKPGLPLIAIPTTAGTGSEVTRFTVITDTETDVKMLLK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 167 SSHVFPVFSILDPAYTFSVPRDQTVYGIVDSMSHALEHYFHRTENtPMIDGF-------IESLLRTAVQEGpkllKDLTS 239
Cdd:cd08194 157 GPALLPAVAIVDPELTLSMPPRVTAATGIDALTHAIEAYVSRKAQ-PLTDTLalsaiklIGRNLRRAYADG----DDLEA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 240 ykyRETMMYIST---TAF-NGSLAngtdggdwathrIEHALS----AVYDIPHGGGLAILFPNWLEHVLKEDPSRVKQLA 311
Cdd:cd08194 232 ---REAMMLAALeagIAFsNSSVA------------LVHGMSrpigALFHVPHGLSNAMLLPAVTEFSLPGAPERYAEIA 296
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1265435555 312 VnVFGIDPAGKSDEETAMEGAKALRTFWNDLGAPnSLRDYDIDDSEFDAIVEK 364
Cdd:cd08194 297 R-AMGIATEGDSDEEAAEKLVEALERLCADLEIP-TLREYGIDEEEFEAALDK 347
|
|
| NADPH_BDH |
cd08179 |
NADPH-dependent butanol dehydrogenase involved in the butanol and ethanol formation pathway in ... |
8-388 |
1.27e-47 |
|
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: 166.21 E-value: 1.27e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 8 NPTKLYFGENQITKLSQelASYHKqvnVLLVYGGGSIKRNGVYDEVKAELQSINAVVHELSGVEPNPRLTTVAKGVDICK 87
Cdd:cd08179 4 VPRDIYFGEGALEYLKT--LKGKR---AFIVTGGGSMKRNGFLDKVEDYLKEAGMEVKVFEGVEPDPSVETVEKGAEAMR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 88 KENIGFLLAVGGGSVIDCTKAIAagAVYE--GNTWDLIT--------RKKEITDALPfgtvlTLAATGSEMNSTSVITNW 157
Cdd:cd08179 79 EFEPDWIIAIGGGSVIDAAKAMW--VFYEypELTFEDALvpfplpelRKKARFIAIP-----STSGTGSEVTRASVITDT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 158 ETKEKLGWTSSHVFPVFSILDPAYTFSVPRDQTVYGIVDSMSHALEHYFhrtenTPMIDGFIESLLRTAVQEGPKLLKdl 237
Cdd:cd08179 152 EKGIKYPLASFEITPDVAILDPELTMTMPPHVTANTGMDALTHAIEAYV-----STLANDFTDALALGAILDIFENLP-- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 238 TSY------KYRETMMYISTTA---F-NGSLANgtdggdwaTHRIEHALSAVYDIPHGGGLAILFPNWLEHvLKEDPSRV 307
Cdd:cd08179 225 KSYnggkdlEAREKMHNASCLAgmaFsNSGLGI--------VHSMAHKGGAFFGIPHGLANAILLPYVIEF-NSKDPEAR 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 308 KQLAVnvfgiDPAGKSDEETAMEGAKALRTFWNDLGAPNSLRDYDIDDSEF----DAIVEKTFVKPGVGTY-KELDYASV 382
Cdd:cd08179 296 ARYAA-----LLIGLTDEELVEDLIEAIEELNKKLGIPLSFKEAGIDEDEFfaklDEMAENAMNDACTGTNpRKPTVEEM 370
|
....*.
gi 1265435555 383 RDILER 388
Cdd:cd08179 371 KELLKA 376
|
|
| HEPD |
cd08182 |
Hydroxyethylphosphoate dehydrogenase (HEPD) catalyzes the reduction of phosphonoacetaldehyde ... |
9-387 |
1.65e-47 |
|
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: 165.86 E-value: 1.65e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 9 PTKLYFGENQITKLSQELASYHKQvNVLLVYGGGSIKRNGVYDEVKAELQSINAVVHelSGVEPNPRLTTVAKGVDICKK 88
Cdd:cd08182 1 PVKIIFGPGALAELKDLLGGLGAR-RVLLVTGPSAVRESGAADILDALGGRIPVVVF--SDFSPNPDLEDLERGIELFRE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 89 ENIGFLLAVGGGSVIDCTKAIAAGAVYEGNTWDLI--TRKKEITDALPFGTVLTLAATGSEMNSTSVItnW--ETKEKLG 164
Cdd:cd08182 78 SGPDVIIAVGGGSVIDTAKAIAALLGSPGENLLLLrtGEKAPEENALPLIAIPTTAGTGSEVTPFATI--WdeAEGKKYS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 165 WTSSHVFPVFSILDPAYTFSVPRDQTVYGIVDSMSHALEHYFHRteN-TPMIDGFIESLLRTAVQEGPKLLKDLTSYKYR 243
Cdd:cd08182 156 LAHPSLYPDAAILDPELTLSLPLYLTASTGLDALSHAIESIWSV--NaNPESRAYALRAIRLILENLPLLLENLPNLEAR 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 244 ETMMYISTT---AFNGSlanGTDggdwATHRIEHALSAVYDIPHGGGLAILFPNWLEHVL-----KEDPSRVKQLAVNVF 315
Cdd:cd08182 234 EAMAEASLLaglAISIT---KTT----AAHAISYPLTSRYGVPHGHACALTLPAVLRYNAgaddeCDDDPRGREILLALG 306
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1265435555 316 GIDPAgksdeetamEGAKALRTFWNDLGAPNSLRDYDIDDSEFDAIVEKTFVKP-GVGTYKELDYASVRDILE 387
Cdd:cd08182 307 ASDPA---------EAAERLRALLESLGLPTRLSEYGVTAEDLEALAASVNTPErLKNNPVRLSEEDLLRLLE 370
|
|
| Fe-ADH-like |
cd14861 |
Iron-containing alcohol dehydrogenases-like; This family contains proteins similar to ... |
7-366 |
8.17e-45 |
|
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: 158.44 E-value: 8.17e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 7 HNPTKLYFGENQITKLSQELASyHKQVNVLLVYGGGsIKRNGVYDEVKAELQSINAVVHELSGVEPNPRLTTVAKGVDIC 86
Cdd:cd14861 1 NYPTRIRFGAGAIAELPEELKA-LGIRRPLLVTDPG-LAALGIVDRVLEALGAAGLSPAVFSDVPPNPTEADVEAGVAAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 87 KKENIGFLLAVGGGSVIDCTKAIAAGAVYEGNTWD---LITRKKEITDAL-PFGTVLTLAATGSEMNSTSVITNWETKEK 162
Cdd:cd14861 79 REGGCDGIIALGGGSAIDAAKAIALMATHPGPLWDyedGEGGPAAITPAVpPLIAIPTTAGTGSEVGRAAVITDDDTGRK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 163 LGWTSSHVFPVFSILDPAYTFSVPRDQTVYGIVDSMSHALEHY----FHrtentPMIDGF-IESL------LRTAVQEGp 231
Cdd:cd14861 159 KIIFSPKLLPKVAICDPELTLGLPPRLTAATGMDALTHCIEAYlspgFH-----PMADGIaLEGLrlisewLPRAVADG- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 232 kllKDLTSykyRETMMyisTTAFNGSLANGTDGGdwATHRIEHALSAVYDIPHGGGLAILFPNWLEHVLKEDPSRVKQLA 311
Cdd:cd14861 233 ---SDLEA---RGEMM---MAALMGAVAFQKGLG--AVHALAHALGALYGLHHGLLNAILLPYVLRFNRPAVEDKLARLA 301
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1265435555 312 VNVFGIDPAGksdeETAMEGAKALRtfwNDLGAPNSLRDYDIDDSEFDAIVEKTF 366
Cdd:cd14861 302 RALGLGLGGF----DDFIAWVEDLN---ERLGLPATLSELGVTEDDLDELAELAL 349
|
|
| Fe-ADH-like |
cd08189 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
11-388 |
1.83e-44 |
|
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: 157.63 E-value: 1.83e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 11 KLYFGENQITKLSQELASYHKQvNVLLVYGGGSIKRnGVYDEVKAELQSINAVVHELSGVEPNPRLTTVAKGVDICKKEN 90
Cdd:cd08189 7 ELFEGAGSLLQLPEALKKLGIK-RVLIVTDKGLVKL-GLLDPLLDALKKAGIEYVVFDGVVPDPTIDNVEEGLALYKENG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 91 IGFLLAVGGGSVIDCTKAIAAGAVyegNTWDLIT--------RKKeitdALPFGTVLTLAATGSEMNSTSVITNWETKEK 162
Cdd:cd08189 85 CDAIIAIGGGSVIDCAKVIAARAA---NPKKSVRklkgllkvRKK----LPPLIAVPTTAGTGSEATIAAVITDPETHEK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 163 LGWTSSHVFPVFSILDPAYTFSVPRDQTVYGIVDSMSHALEHY--FHRTENTpmidgfiESLLRTAVQEG----PKLLKD 236
Cdd:cd08189 158 YAINDPKLIPDAAVLDPELTLGLPPAITAATGMDALTHAVEAYisRSATKET-------DEYALEAVKLIfenlPKAYED 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 237 LTSYKYRETMmyiSTTAFNGSLANgTDGGDWATHRIEHALSAVYDIPHGGGLAILFPNWLEHVLKEDPSRVKQLAVNVfG 316
Cdd:cd08189 231 GSDLEARENM---LLASYYAGLAF-TRAYVGYVHAIAHQLGGLYGVPHGLANAVVLPHVLEFYGPAAEKRLAELADAA-G 305
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1265435555 317 IDPAGKSDEETAMEGAKALRTFWNDLGAPNSLrdYDIDDSEFDAIVEKTFvKPGVGTY---KELDYASVRDILER 388
Cdd:cd08189 306 LGDSGESDSEKAEAFIAAIRELNRRMGIPTTL--EELKEEDIPEIAKRAL-KEANPLYpvpRIMDRKDCEELLRK 377
|
|
| Fe-ADH-like |
cd08183 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
9-387 |
7.43e-42 |
|
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: 150.73 E-value: 7.43e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 9 PTKLYFGENQITKLSQELASYHKqvNVLLVYGGGSIkRNGVYDEVKAELQSINAVVHELSGVEpNPRLTTVAKGVDICKK 88
Cdd:cd08183 1 PPRIVFGRGSLQELGELAAELGK--RALLVTGRSSL-RSGRLARLLEALEAAGIEVALFSVSG-EPTVETVDAAVALARE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 89 ENIGFLLAVGGGSVIDCTKAIAAGAVYEGNT---WDLITRKKEIT-DALPFGTVLTLAATGSEMNSTSVITNWETKEKLG 164
Cdd:cd08183 77 AGCDVVIAIGGGSVIDAAKAIAALLTNEGSVldyLEVVGKGRPLTePPLPFIAIPTTAGTGSEVTKNAVLSSPEHGVKVS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 165 WTSSHVFPVFSILDPAYTFSVPRDQTVYGIVDSMSHALEHYFHRTENtPMIDGFIESLLRTAVQEGPKLLKDLTSYKYRE 244
Cdd:cd08183 157 LRSPSMLPDVALVDPELTLSLPPEVTAASGLDALTQLIEPYVSRKAN-PLTDALAREGLRLAARSLRRAYEDGEDLEARE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 245 TMMYISttAFNG-SLAN---GtdggdwATHRIEHALSAVYDIPHGGGLAILFPNWLE---HVLKEDPSRVKQLAVNVFGI 317
Cdd:cd08183 236 DMALAS--LLGGlALANaglG------AVHGLAGPLGGMFGAPHGAICAALLPPVLEanlRALREREPDSPALARYRELA 307
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1265435555 318 DPAGKSDEETAMEGAKALRTFWNDLGAPnSLRDYDIDDSEFDAIVEKTFVKPGV-GTYKELDYASVRDILE 387
Cdd:cd08183 308 GILTGDPDAAAEDGVEWLEELCEELGIP-RLSEYGLTEEDFPEIVEKARGSSSMkGNPIELSDEELLEILE 377
|
|
| DHQ_Fe-ADH |
cd07766 |
Dehydroquinate synthase-like (DHQ-like) and iron-containing alcohol dehydrogenases (Fe-ADH); ... |
9-364 |
7.61e-39 |
|
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: 140.19 E-value: 7.61e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 9 PTKLYFGENQITKLSQELASYHKQVnvLLVYGGGSIKrnGVYDEVKAELQSINAVvHELSGVEPNPRLTTVAKGVDICKK 88
Cdd:cd07766 1 PTRIVFGEGAIAKLGEIKRRGFDRA--LVVSDEGVVK--GVGEKVADSLKKGLAV-AIFDFVGENPTFEEVKNAVERARA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 89 ENIGFLLAVGGGSVIDCTKAIAAgavyegntwdlitrkkEITDALPFGTVLTLAATGSEMNSTSVITNWETKEKLGwtSS 168
Cdd:cd07766 76 AEADAVIAVGGGSTLDTAKAVAA----------------LLNRGIPFIIVPTTASTDSEVSPKSVITDKGGKNKQV--GP 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 169 HVFPVFSILDPAYTFSVPRDQTVYGIVDSMSHALEhyfhrtentpmidgfiesllrtavqegpkllkdltsykyRETMMY 248
Cdd:cd07766 138 HYNPDVVFVDTDITKGLPPRQVASGGVDALAHAVE---------------------------------------LEKVVE 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 249 ISTTAFNGSLANgtdGGDWATHRIEHALSAVYDIPHGGGLAILFPnwleHVLKEdpsrVKQLAvnvfgidPAGKSDEEta 328
Cdd:cd07766 179 AATLAGMGLFES---PGLGLAHAIGHALTAFEGIPHGEAVAVGLP----YVLKV----ANDMN-------PEPEAAIE-- 238
|
330 340 350
....*....|....*....|....*....|....*.
gi 1265435555 329 megakALRTFWNDLGAPNSLRDYDIDDSEFDAIVEK 364
Cdd:cd07766 239 -----AVFKFLEDLGLPTHLADLGVSKEDIPKLAEK 269
|
|
| Fe-ADH-like |
cd14862 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
1-366 |
2.43e-38 |
|
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: 141.21 E-value: 2.43e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 1 MNIFLqhnPTKLYFGENQITKLSQelasyHKQVNVLLVYGGGsIKRNGVYDEVKAELQSINAVVHELSGVEPNPRLTTVA 80
Cdd:cd14862 1 MWYFS---SPKIVFGEDALSHLEQ-----LSGKRALIVTDKV-LVKLGLLKKVLKRLLQAGFEVEVFDEVEPEPPLETVL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 81 KGVDICKKENIGFLLAVGGGSVIDCTKaiAAGAVYE---------GNTWDLITRKKEITDALPfgtvlTLAATGSEMNST 151
Cdd:cd14862 72 KGAEAMREFEPDLIIALGGGSVMDAAK--AAWVLYErpdldpediSPLDLLGLRKKAKLIAIP-----TTSGTGSEATWA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 152 SVITNWETKEKLGWTSSHVFPVFSILDPAYTFSVPRDQTVYGIVDSMSHALEHYFHRTENtPMIDGFIESLLRTAVQEGP 231
Cdd:cd14862 145 IVLTDTEEPRKIAVANPELVPDVAILDPEFVLGMPPKLTAGTGLDALAHAVEAYLSTWSN-DFSDALALKAIELIFKYLP 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 232 KLLKDLTSYKYRETMM---YISTTAFNGSLAnGTdggdwaTHRIEHALSAVYDIPHGGGLAILFPNWLEHVLKEDPSRVK 308
Cdd:cd14862 224 RAYKDGDDLEAREKMHnaaTIAGLAFGNSQA-GL------AHALGHSLGAVFHVPHGIAVGLFLPYVIEFYAKVTDERYD 296
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1265435555 309 QLAVnvfgIDPAGKSDEETAMEGAKALRTFWNDLGAPNSLRDYDIDDSEF----DAIVEKTF 366
Cdd:cd14862 297 LLKL----LGIEARDEEEALKKLVEAIRELYKEVGQPLSIKDLGISEEEFeeklDELVEYAM 354
|
|
| Fe-ADH-like |
cd17814 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
34-369 |
4.44e-38 |
|
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: 140.76 E-value: 4.44e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 34 NVLLVYGGGSIKrNGVYDEVKAELQSINAVVHELSGVEPNPRLTTVAKGVDICKKENIGFLLAVGGGSVIDCTKAIAAGA 113
Cdd:cd17814 28 KVLVVTDPGVIK-AGWVDEVLDSLEAEGLEYVVFSDVTPNPRDFEVMEGAELYREEGCDGIVAVGGGSPIDCAKGIGIVV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 114 V-------YEGntWDLITRKkeitdALPFGTVLTLAATGSEMNSTSVITNWETKEKLGWTSSHVFPVFSILDPAYTFSVP 186
Cdd:cd17814 107 SngghildYEG--VDKVRRP-----LPPLICIPTTAGSSADVSQFAIITDTERRVKMAIISKTLVPDVSLIDPETLTTMD 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 187 RDQTVYGIVDSMSHALEHYFhRTENTPMIDGFIESLLRTAVQEGPKLLKDLTSYKYRETMMYISTT---AF-NGSLAngt 262
Cdd:cd17814 180 PELTACTGMDALTHAIEAYV-SNASSPLTDLHALEAIRLISENLPKAVADPDDLEAREKMMLASLQaglAFsNASLG--- 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 263 dggdwATHRIEHALSAVYDIPHGGGLAILfpnwLEHV----LKEDPSRVKQLAvNVFGIDPAGKSDEETAMEGAKALRTF 338
Cdd:cd17814 256 -----AVHAMAHSLGGLLDLPHGECNALL----LPHVirfnFPAAPERYRKIA-EAMGLDVDGLDDEEVAERLIEAIRDL 325
|
330 340 350
....*....|....*....|....*....|.
gi 1265435555 339 WNDLGAPNSLRDYDIDDSEFDAIVEKTFVKP 369
Cdd:cd17814 326 REDLGIPETLSELGVDEEDIPELAKRAMKDP 356
|
|
| Fe-ADH-like |
cd08191 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
7-389 |
2.18e-35 |
|
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contain different protein domain. Proteins of this family have not been characterized.
Pssm-ID: 341470 [Multi-domain] Cd Length: 392 Bit Score: 133.89 E-value: 2.18e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 7 HNPTKLYFGENQITKLSQELASYHKQVnvlLVYGGGSIKRNGVYDEVKAELQSINAVVHELSGVEPNPRLTTVAKGVDIC 86
Cdd:cd08191 2 RSPSRLLFGPGARRALGRVAARLGSRV---LIVTDPRLASTPLVAELLAALTAAGVAVEVFDGGQPELPVSTVADAAAAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 87 KKENIGFLLAVGGGSVIDCTKAIAAGAVYEGNTWDLITRKKEITDALPFGTVLTLAATGSEMNSTSVITNWETKEKLGWT 166
Cdd:cd08191 79 RAFDPDVVIGLGGGSNMDLAKVVALLLAHGGDPRDYYGEDRVPGPVLPLIAVPTTAGTGSEVTPVAVLTDPARGMKVGVS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 167 SSHVFPVFSILDPAYTFSVPRDQTVYGIVDSMSHALEHYFHRTEN--------------TPMIDGFIESLLRTAVQEGPK 232
Cdd:cd08191 159 SPYLRPAVAIVDPELTLTCPPGVTADSGIDALTHAIESYTARDFPpfprldpdpvyvgkNPLTDLLALEAIRLIGRHLPR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 233 LLKDLTSYKYRETMMYISTTAfngSLANGTDGGDwATHRIEHALSAVYDIPHGGGLAILFPNWLEHVLKEDPSRVKQLAV 312
Cdd:cd08191 239 AVRDGDDLEARSGMALAALLA---GLAFGTAGTA-AAHALQYPIGALTHTSHGVGNGLLLPYVMRFNRPARAAELAEIAR 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 313 nVFGIDPAGKSdEETAMEGAKALRTFWNDLGAPNSLRDYDIDDSEFDAIVEKTF-------VKPGvgtykELDYASVRDI 385
Cdd:cd08191 315 -ALGVTTAGTS-EEAADRAIERVEELLARIGIPTTLADLGVTEADLPGLAEKALsvtrliaNNPR-----PPTEEDLLRI 387
|
....
gi 1265435555 386 LERS 389
Cdd:cd08191 388 LRAA 391
|
|
| HOT |
cd08190 |
Hydroxyacid-oxoacid transhydrogenase (HOT) involved in gamma-hydroxybutyrate metabolism; This ... |
10-365 |
2.62e-35 |
|
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: 133.82 E-value: 2.62e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 10 TKLYFGENQITKLSQELASYhKQVNVLLVYGGGsIKRNGVYDEVKAEL--QSINAVVHelSGVEPNPRLTTVAKGVDICK 87
Cdd:cd08190 2 SNIRFGPGATRELGMDLKRL-GAKKVLVVTDPG-LAKLGLVERVLESLekAGIEVVVY--DGVRVEPTDESFEEAIEFAK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 88 KENIGFLLAVGGGSVIDCTKAIAAGAVYEGNTWDL----ITRKKEITDAL-PFGTVLTLAATGSEMNSTSVITNWETKEK 162
Cdd:cd08190 78 EGDFDAFVAVGGGSVIDTAKAANLYATHPGDFLDYvnapIGKGKPVPGPLkPLIAIPTTAGTGSETTGVAIFDLEELKVK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 163 LGWTSSHVFPVFSILDPAYTFSVPRDQTVYGIVDSMSHALEHY-------FHRTEN----------TPMIDGF----IES 221
Cdd:cd08190 158 TGISSRYLRPTLAIVDPLLTLTLPPRVTASSGFDVLCHALESYtarpynaRPRPANpderpayqgsNPISDVWaekaIEL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 222 L---LRTAVQEGpkllKDLTSykyRETMMYISTTAfngSLANGTDGgdwaTHrIEHALS-----------------AVYD 281
Cdd:cd08190 238 IgkyLRRAVNDG----DDLEA---RSNMLLASTLA---GIGFGNAG----VH-LPHAMAypiaglvkdyrppgypvDHPH 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 282 IPHGGGLAILFPNWLEHVLKEDPSRVKQLAvNVFGIDPAGKSDEETAMEGAKALRTFWNDLGAPNSLRDYDIDDSEFDAI 361
Cdd:cd08190 303 VPHGLSVALTAPAVFRFTAPACPERHLEAA-ELLGADTSGASDRDAGEVLADALIKLMRDIGIPNGLSALGYSEDDIPAL 381
|
....
gi 1265435555 362 VEKT 365
Cdd:cd08190 382 VEGT 385
|
|
| PRK09860 |
PRK09860 |
putative alcohol dehydrogenase; Provisional |
37-358 |
6.75e-33 |
|
putative alcohol dehydrogenase; Provisional
Pssm-ID: 182118 [Multi-domain] Cd Length: 383 Bit Score: 126.99 E-value: 6.75e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 37 LVYGGGSIKRNGVYDEVKAELQS--INAVVHElsGVEPNPRLTTVAKGVDICKKENIGFLLAVGGGSVIDCTKAIAAGAV 114
Cdd:PRK09860 35 LIVTDNMLTKLGMAGDVQKALEErnIFSVIYD--GTQPNPTTENVAAGLKLLKENNCDSVISLGGGSPHDCAKGIALVAA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 115 YEGNTWDLITRKKEITDALPFGTVLTLAATGSEMNSTSVITNWETKEKLGWTSSHVFPVFSILDPAYTFSVPRDQTVYGI 194
Cdd:PRK09860 113 NGGDIRDYEGVDRSAKPQLPMIAINTTAGTASEMTRFCIITDEARHIKMAIVDKHVTPLLSVNDSSLMIGMPKSLTAATG 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 195 VDSMSHALEHYFhRTENTPMIDG-------FIESLLRTAVQEGpkllkdlTSYKYRETMMY---ISTTAFNgslaNGTDG 264
Cdd:PRK09860 193 MDALTHAIEAYV-SIAATPITDAcalkavtMIAENLPLAVEDG-------SNAKAREAMAYaqfLAGMAFN----NASLG 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 265 gdwATHRIEHALSAVYDIPHGGGLAILFPNWLEHVLKEDPSRVKQLAvNVFGIDPAGKSDEETAMEGAKALRTFWNDLGA 344
Cdd:PRK09860 261 ---YVHAMAHQLGGFYNLPHGVCNAVLLPHVQVFNSKVAAARLRDCA-AAMGVNVTGKNDAEGAEACINAIRELAKKVDI 336
|
330
....*....|....
gi 1265435555 345 PNSLRDYDIDDSEF 358
Cdd:PRK09860 337 PAGLRDLNVKEEDF 350
|
|
| PDD |
cd08180 |
1,3-propanediol dehydrogenase (PPD) catalyzes the reduction of 3-hydroxypropionaldehyde (3-HPA) ... |
9-363 |
6.57e-32 |
|
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: 122.99 E-value: 6.57e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 9 PTKLYFGENQITKLSQelasYHKQvNVLLVyGGGSIKRNGVYDEVKAELQSINAVvHELSGVEPNPRLTTVAKGVDICKK 88
Cdd:cd08180 4 KTKIYSGEDSLERLKE----LKGK-RVFIV-TDPFMVKSGMVDKVTDELDKSNEV-EIFSDVVPDPSIEVVAKGLAKILE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 89 ENIGFLLAVGGGSVIDCTKAIAAgavyegntwdLITRKKEITDALPFGTVLTLAATGSEMNSTSVITNWETKEKLGWTSS 168
Cdd:cd08180 77 FKPDTIIALGGGSAIDAAKAIIY----------FALKQKGNIKKPLFIAIPTTSGTGSEVTSFAVITDPEKGIKYPLVDD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 169 HVFPVFSILDPAYTFSVPRDQTVYGIVDSMSHALEHYFhRTENTPMIDGFIESLLRTAVQEGPKLLKDLTSYKYRETMMY 248
Cdd:cd08180 147 SMLPDIAILDPELVKSVPPKVTADTGMDVLTHALEAYV-STNANDFTDALAEKAIKLVFENLPRAYRDGDDLEAREKMHN 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 249 IST---TAFNGSlangtdgGDWATHRIEHALSAVYDIPHGGGLAILFPnwleHVLKedpsrvkqlavnvFGIdpagksde 325
Cdd:cd08180 226 ASCmagIAFNNA-------GLGINHSLAHALGGRFHIPHGRANAILLP----YVIE-------------FLI-------- 273
|
330 340 350
....*....|....*....|....*....|....*...
gi 1265435555 326 etamegaKALRTFWNDLGAPNSLRDYDIDDSEFDAIVE 363
Cdd:cd08180 274 -------AAIRRLNKKLGIPSTLKELGIDEEEFEKAID 304
|
|
| PRK10624 |
PRK10624 |
L-1,2-propanediol oxidoreductase; Provisional |
8-387 |
8.20e-32 |
|
L-1,2-propanediol oxidoreductase; Provisional
Pssm-ID: 182595 [Multi-domain] Cd Length: 382 Bit Score: 123.95 E-value: 8.20e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 8 NPTKlYFGENQITKLSQELAS--YHKqvnVLLVYGGGSIKrNGVYDEVKAELQSiNAVVHEL-SGVEPNPRLTTVAKGVD 84
Cdd:PRK10624 8 NETA-YFGRGAIGALTDEVKRrgFKK---ALIVTDKTLVK-CGVVAKVTDVLDA-AGLAYEIyDGVKPNPTIEVVKEGVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 85 ICKKENIGFLLAVGGGSVIDCTKAIAagavyegntwdLITRKKEITD-------------ALPFGTVLTLAATGSEMNST 151
Cdd:PRK10624 82 VFKASGADYLIAIGGGSPQDTCKAIG-----------IISNNPEFADvrslegvaptkkpSVPIIAIPTTAGTAAEVTIN 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 152 SVITNWETKEKLGWTSSHVFPVFSILDPAYTFSVPRDQTVYGIVDSMSHALEHYFHRTEnTPMIDGF-------IESLLR 224
Cdd:PRK10624 151 YVITDEEKRRKFVCVDPHDIPQVAFVDADMMDSMPPGLKAATGVDALTHAIEGYITRGA-WALTDMLhlkaieiIAGALR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 225 TAVQEGPkllkdltsyKYRETM---MYISTTAF-NGSLAngtdggdwATHRIEHALSAVYDIPHGGGLAILFPNWLEHVL 300
Cdd:PRK10624 230 GAVAGDK---------EAGEGMalgQYIAGMGFsNVGLG--------LVHGMAHPLGAFYNTPHGVANAILLPHVMEYNA 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 301 KEDPSRVKQLAVnVFGIDPAGKSDEETAMEGAKALRTFWNDLGAPNSLRDYDIDDSEFDAIVEKTF--VKPGvGTYKEld 378
Cdd:PRK10624 293 DFTGEKYRDIAR-AMGVKVEGMSLEEARNAAVEAVKALNRDVGIPPHLRDVGVKEEDIPALAQAAFddVCTG-GNPRE-- 368
|
....*....
gi 1265435555 379 yASVRDILE 387
Cdd:PRK10624 369 -ATLEDIVE 376
|
|
| MAR-like |
cd08192 |
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic ... |
9-388 |
3.62e-29 |
|
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: 116.58 E-value: 3.62e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 9 PTKLYFGENQITKLSQELASYHKQvNVLLVYGGgSIKRN-GVYDEVKAELQsiNAVVHELSGVEPNPRLTTVAKGVDICK 87
Cdd:cd08192 1 LERVSYGPGAVEALLHELATLGAS-RVFIVTSK-SLATKtDVIKRLEEALG--DRHVGVFSGVRQHTPREDVLEAARAVR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 88 KENIGFLLAVGGGSVIDCTKAIA---AGAVYEGNTWDLITRKKEITDAL--PFGTVL----TLAatGSEMNSTSVITNWE 158
Cdd:cd08192 77 EAGADLLVSLGGGSPIDAAKAVAlalAEDVTDVDQLDALEDGKRIDPNVtgPTLPHIaiptTLS--GAEFTAGAGATDDD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 159 TKEKLGWTSSHVFPVFSILDPAYTFSVPRD---QTvyGI--VDsmsHALEHYFHRTeNTPMIDGFIESLLRTAVQEGPKL 233
Cdd:cd08192 155 TGHKQGFAHPELGPDAVILDPELTLHTPERlwlST--GIraVD---HAVETLCSPQ-ATPFVDALALKALRLLFEGLPRS 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 234 LKDLTSYKYReTMMYISTTAFNGSLANGTDGGdwATHRIEHALSAVYDIPHGGGLAILFPNWLEHVLKEDPSRVKQLAVN 313
Cdd:cd08192 229 KADPEDLEAR-LKCQLAAWLSLFGLGSGVPMG--ASHAIGHQLGPLYGVPHGITSCIMLPAVLRFNAPVNAERQRLIARA 305
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1265435555 314 VFGIDPAGKSDEETAmegAKALRTFWNDLGAPNSLRDYDIDDSEFDAIVEKTFVKPGVGT--YKELDYASVRDILER 388
Cdd:cd08192 306 LGLVTGGLGREAADA---ADAIDALIRELGLPRTLRDVGVGRDQLEKIAENALTDVWCRTnpRPITDKDDVLEILES 379
|
|
| AAD_C |
cd08178 |
C-terminal alcohol dehydrogenase domain of the acetaldehyde dehydrogenase-alcohol ... |
9-364 |
1.12e-28 |
|
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: 115.36 E-value: 1.12e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 9 PTKLYFGENQITKLSQELASYHKqvnVLLVYGGGSIKrNGVYDEVKAELQSINAVVHELSGVEPNPRLTTVAKGVDIC-- 86
Cdd:cd08178 3 PPKIYFEPGCLPYLLLELPGVKR---AFIVTDRVLYK-LGYVDKVLDVLEARGVETEVFSDVEPDPTLSTVRKGLEAMna 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 87 -KKENIgflLAVGGGSVIDCTKAIaaGAVYE--GNTWDLITRK-----KEITDALPFGTVLTLAA------TGSEMNSTS 152
Cdd:cd08178 79 fKPDVI---IALGGGSAMDAAKIM--WLFYEhpETKFEDLAQRfmdirKRVYKFPKLGKKAKLVAipttsgTGSEVTPFA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 153 VITNWETKEKLGWTSSHVFPVFSILDPAYTFSVPRDQTVYGIVDSMSHALEHYF--HRTENTpmiDGFIESLLRTAVQEG 230
Cdd:cd08178 154 VITDDKTGKKYPLADYALTPDMAIVDPELVMTMPKRLTADTGIDALTHAIEAYVsvMASDYT---DGLALQAIKLIFEYL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 231 PKLLKDLTSYKYRETMMYIST-------TAFNGslangtdggdwATHRIEHALSAVYDIPHGGGLAILFPnwleHVLK-- 301
Cdd:cd08178 231 PRSYNNGNDIEAREKMHNAATiagmafaNAFLG-----------ICHSLAHKLGAAFHIPHGRANAILLP----HVIRyn 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 302 -----------------EDPSRVKQLAVNvfgIDPAGKSDEETAMEGAKALRTFWNDLGAPNSLRDYDIDDSEFDAIVEK 364
Cdd:cd08178 296 atdpptkqaafpqykyyVAKERYAEIADL---LGLGGKTPEEKVESLIKAIEDLKKDLGIPTSIREAGIDEADFLAAVDK 372
|
|
| HVD |
cd08193 |
5-hydroxyvalerate dehydrogenase (HVD) catalyzes the oxidation of 5-hydroxyvalerate to ... |
14-356 |
1.57e-27 |
|
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: 111.84 E-value: 1.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 14 FGENQITKLSqELASYHKQVNVLLVYGGGsIKRNGVYDEVKAELQSINAVVHELSGVEPNPRLTTVAKGVDICKKEN--- 90
Cdd:cd08193 9 CGAGAAARLG-ELLRELGARRVLLVTDPG-LVKAGLADPALAALEAAGIAVTVFDDVVADPPEAVVEAAVEQAREAGadg 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 91 -IGFllavGGGSVIDCTKAIAAgavyegntwdLITRKKEITDA----------LPFGTVLTLAATGSEMNSTSVITNWET 159
Cdd:cd08193 87 vIGF----GGGSSMDVAKLVAL----------LAGSDQPLDDIygvgkatgprLPLILVPTTAGTGSEVTPISIVTTGET 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 160 kEKLGWTSSHVFPVFSILDPAYTFSVPRDQTVYGIVDSMSHALEHYFHRTENTPMIDGF-IESL------LRTAVQEGpk 232
Cdd:cd08193 153 -EKKGVVSPQLLPDVALLDAELTLGLPPHVTAATGIDAMVHAIEAYTSRHKKNPISDALaREALrllganLRRAVEDG-- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 233 llKDLtsyKYRETMMYIST---TAF-NGSLAngtdggdwATHRIEHALSAVYDIPHGGGLAILFPnwleHVLKEDPSRVK 308
Cdd:cd08193 230 --SDL---EAREAMLLGSMlagQAFaNAPVA--------AVHALAYPLGGHFHVPHGLSNALVLP----HVLRFNLPAAE 292
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1265435555 309 Q----LAVNVFgIDPAGKSDEETAMEGAKALRTFWNDLGAPNSLRDYDIDDS 356
Cdd:cd08193 293 AlyaeLARALL-PGLAFGSDAAAAEAFIDALEELVEASGLPTRLRDVGVTEE 343
|
|
| Fe-ADH-like |
cd14864 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
7-363 |
3.83e-25 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341486 [Multi-domain] Cd Length: 376 Bit Score: 105.08 E-value: 3.83e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 7 HNPTKLYFGENQITKLSQELASYHKqvNVLLVYGGGSiKRNGVYDEVKAELQSINAVVHELSGVEPNPRLTTVAKGVDIC 86
Cdd:cd14864 2 KIPPNIVFGADSLERIGEEVKEYGS--RFLLITDPVL-KESGLADKIVSSLEKAGISVIVFDEIPASATSDTIDEAAELA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 87 KKENIGFLLAVGGGSVIDCTKAIAAGAVYEGNTWDLITRKKEITDALPFGTVLTLAATGSEMNSTSVITNWETKE-KLgW 165
Cdd:cd14864 79 RKAGADGIIAVGGGKVLDTAKAVAILANNDGGAYDFLEGAKPKKKPLPLIAVPTTPRSGFEFSDRFPVVDSRSREvKL-L 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 166 TSSHVFPVFSILDPAYTFSVPRDQTVYGIVDSMSHALEHYFHRTENTpmidgFIESLLRTAVQ---EG-PKLLKDLTSYK 241
Cdd:cd14864 158 KAQPGLPKAVIVDPNLMASLTGNQTAAMALAALALAVEAYLSKKSNF-----FSDALALKAIElvsENlDGALADPKNTP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 242 YRETMMYISttAFNGSLANGTDGGdwATHRIEHALSAVYDIPHGGGLAILFPNWLEHVLKEDPSRVKQLAvNVFGIDPAG 321
Cdd:cd14864 233 AEELLAQAG--CLAGLAASSSSPG--LATALALAVNSRYKVSKSLVASILLPHVIEYAATSAPDKYAKIA-RALGEDVEG 307
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1265435555 322 KSDEETAMEGAKALRTFWNDLGAPNSLRDYDIDDSeFDAIVE 363
Cdd:cd14864 308 ASPEEAAIAAVEGVRRLIAQLNLPTRLKDLDLASS-LEQLAA 348
|
|
| Fe-ADH-like |
cd14866 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
9-387 |
2.42e-24 |
|
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: 103.08 E-value: 2.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 9 PTKLYFGENQITKLSQELASYHKQVNVLLVygGGSIKRNG-VYDEVKAELQSinAVVHELSGVEPNPRLTTVAKGVDICK 87
Cdd:cd14866 5 PLRLFSGRGALARLGRELDRLGARRALVVC--GSSVGANPdLMDPVRAALGD--RLAGVFDGVRPHSPLETVEAAAEALR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 88 KENIGFLLAVGGGSVIDCTKAIAAGAVYEGNTWDLITRK---------KEITDALPFGTVLTlAATGSEMNSTSVITNWE 158
Cdd:cd14866 81 EADADAVVAVGGGSAIVTARAASILLAEDRDVRELCTRRaedglmvspRLDAPKLPIFVVPT-TPTTADVKAGSAVTDPP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 159 TKEKLGWTSSHVFPVFSILDPAYTFSVPRDQTVYGIVDSMSHALEHYFHRTENtPMIDGFIESLLRTAVQEGPKLLKDLT 238
Cdd:cd14866 160 AGQRLALFDPKTRPAAVFYDPELLATAPASLVAGAAMNGFDMAVEGLYSRHAD-PLADATLMHALRLLADGLPRLADDDD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 239 SYKYRETMMYISttafngsLAN-GTD-GGDWATHRIEHALSAVYDIPHGGGLAILFPNWLEHVLKEDPSRVKQLAvNVFG 316
Cdd:cd14866 239 PAARADLVLAAV-------LAGyGTDhTGGGVIHALGHAIGARYGVQNGVVHAILLPHVLRFNAPATDGRLDRLA-EALG 310
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1265435555 317 IDPAGksDEETAMEGAKALRTFWNDLGAPNSLRDYDIDDSEFDAIVEKT----FVKPgvGTYKELDYASVRDILE 387
Cdd:cd14866 311 VADAG--DEASAAAVVDAVEALLDALGVPTRLRDLGVSREDLPAIAEAAmddwFMDN--NPRPVPTAEELEALLE 381
|
|
| PRK13805 |
PRK13805 |
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional |
9-364 |
1.83e-22 |
|
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional
Pssm-ID: 237515 [Multi-domain] Cd Length: 862 Bit Score: 99.49 E-value: 1.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 9 PTKLYFGENQITKLSQELASYHKqvnVLLVYGGGSIKrNGVYDEVKAELQSI-NAVVHEL-SGVEPNPRLTTVAKGVDIC 86
Cdd:PRK13805 460 PKKIYFERGSLPYLLDELDGKKR---AFIVTDRFMVE-LGYVDKVTDVLKKReNGVEYEVfSEVEPDPTLSTVRKGAELM 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 87 KKENIGFLLAVGGGSVIDCTKAIaagavyegntW-----------DLITR----KKEITDALPFGT------VLTLAATG 145
Cdd:PRK13805 536 RSFKPDTIIALGGGSPMDAAKIM----------WlfyehpetdfeDLAQKfmdiRKRIYKFPKLGKkaklvaIPTTSGTG 605
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 146 SEMNSTSVITNWETKEKLGWTSSHVFPVFSILDPAYTFSVPRDQTVYGIVDSMSHALEHYFH--RTENTpmiDGF-IESL 222
Cdd:PRK13805 606 SEVTPFAVITDDKTGVKYPLADYELTPDVAIVDPNLVMTMPKSLTADTGIDALTHALEAYVSvmASDYT---DGLaLQAI 682
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 223 ------LRTAVQEGPKllkdltSYKYRETMMYISTTAfnG-SLANGTDGgdwATHRIEHALSAVYDIPHGGGLAILFPnw 295
Cdd:PRK13805 683 klvfeyLPRSYKNGAK------DPEAREKMHNASTIA--GmAFANAFLG---ICHSMAHKLGAEFHIPHGRANAILLP-- 749
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 296 leHVLK---EDPS---------------RVKQLAVNVfGIdpAGKSDEETAMEGAKALRTFWNDLGAPNSLRDYDIDDSE 357
Cdd:PRK13805 750 --HVIRynaTDPPkqaafpqyeypradeRYAEIARHL-GL--PGSTTEEKVESLIKAIEELKAELGIPMSIKEAGVDEAD 824
|
....*..
gi 1265435555 358 FDAIVEK 364
Cdd:PRK13805 825 FLAKLDE 831
|
|
| PRK15454 |
PRK15454 |
ethanolamine utilization ethanol dehydrogenase EutG; |
74-293 |
1.63e-17 |
|
ethanolamine utilization ethanol dehydrogenase EutG;
Pssm-ID: 185351 [Multi-domain] Cd Length: 395 Bit Score: 83.54 E-value: 1.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 74 PRLTTVAKGVDICKKENIGFLLAVGGGSVIDCTKAIAAGAVYEGNTWDLITRKKEITDALPFGTVLTLAATGSEMNSTSV 153
Cdd:PRK15454 90 PCITDVCAAVAQLRESGCDGVIAFGGGSVLDAAKAVALLVTNPDSTLAEMSETSVLQPRLPLIAIPTTAGTGSETTNVTV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 154 ITNWETKEKLGWTSSHVFPVFSILDPAYTFSVPRDQTVYGIVDSMSHALEHYFHRTEnTPMIDGFIESLLRTAVQEGPKL 233
Cdd:PRK15454 170 IIDAVSGRKQVLAHASLMPDVAILDAALTEGVPSHVTAMTGIDALTHAIEAYSALNA-TPFTDSLAIGAIAMIGKSLPKA 248
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 234 LKDLTSYKYRETMMYISTTAfngSLANgTDGGDWATHRIEHALSAVYDIPHGGGLAILFP 293
Cdd:PRK15454 249 VGYGHDLAARESMLLASCMA---GMAF-SSAGLGLCHAMAHQPGAALHIPHGLANAMLLP 304
|
|
| Fe-ADH_KdnB-like |
cd08184 |
Iron-containing alcohol dehydrogenase similar to Shewanella oneidensis KdnB required for Kdo8N ... |
74-311 |
1.33e-12 |
|
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: 68.06 E-value: 1.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 74 PRLTTVAKGVDICKKENIGFLLAV---GGGSVIDCTKAIA-------AGAVYEGntWDLITRKKEITDALPfgtvlTLAA 143
Cdd:cd08184 63 PKTDQIDALRAQIRAENDKLPAAVvgiGGGSTMDIAKAVSnmltnpgSAADYQG--WDLVKNPGIYKIGVP-----TLSG 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 144 TGSEMNSTSVITNWEtkEKLGWTSSHVFPVFSILDPAYTFSVPRDQTVYGIVDSMSHALEHyFHRTENTPMIDGFIESLL 223
Cdd:cd08184 136 TGAEASRTAVLTGPE--KKLGINSDYTVFDQVILDPELIATVPRDQYFYTGMDCYIHCVES-LNGTYRNAFGDAYAEKAL 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 224 RTAVQegpKLLKDLT-SYKYRETMMYISttAFNG-SLANGTDGgdwATHRIEHALSAVYDIPHGGGLAILFpNWLEHVLK 301
Cdd:cd08184 213 ELCRD---VFLSDDMmSPENREKLMVAS--YLGGsSIANSQVG---VCHALSYGLSVVLGTHHGVANCIVF-NVLEEFYP 283
|
250
....*....|
gi 1265435555 302 EDPSRVKQLA 311
Cdd:cd08184 284 EGVKEFREML 293
|
|
| MAR |
cd08177 |
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic ... |
9-388 |
1.26e-11 |
|
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: 65.22 E-value: 1.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 9 PTKLYFGENQITKLSQELASYHKQvNVLLVYGGGsikRNGVYDEVKAELQSINAVVHelSGVEPNPRLTTVAKGVDICKK 88
Cdd:cd08177 1 PQRVVFGAGTLAELAEELERLGAR-RALVLSTPR---QRALAERVAALLGDRVAGVF--DGAVMHVPVEVAERALAAARE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 89 ENIGFLLAVGGGSVIDCTKAIAagavyegntwdlitrkkeITDALPFGTVLTLAAtGSEMnsTSVITNWETKEKLGWTSS 168
Cdd:cd08177 75 AGADGLVAIGGGSAIGLAKAIA------------------LRTGLPIVAVPTTYA-GSEM--TPIWGETEDGVKTTGRDP 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 169 HVFPVFSILDPAYTFSVPRDQTVYGIVDSMSHALEHYFHRTENtPMIDGFIESLLRTAVQEGPKLLKDLTSYKYRETMMY 248
Cdd:cd08177 134 RVLPRTVIYDPDLTLGLPAALSVASGLNALAHAVEALYAPDAN-PITSLLAEEGIRALARALPRLVADPSDLEARSDALY 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 249 ISTTAfnGSLANGTDGGdwATHRIEHALSAVYDIPHGGGLAILFPNWLEHVLKEDPSRVKQLAVNVFGIDPAGksdeeta 328
Cdd:cd08177 213 GAWLA--GVVLGSVGMG--LHHKLCHVLGGTFDLPHAETHAVVLPHVLAYNAPAAPDAMARLARALGGGDAAG------- 281
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1265435555 329 megakALRTFWNDLGAPNSLRDYDIDDSEFDAIVEKTFVKPgvgtY---KELDYASVRDILER 388
Cdd:cd08177 282 -----GLYDLARRLGAPTSLRDLGMPEDDIDRAADLALANP----YpnpRPVERDALRALLER 335
|
|
| GldA |
COG0371 |
Glycerol dehydrogenase or related enzyme, iron-containing ADH family [Energy production and ... |
9-144 |
4.85e-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: 63.65 E-value: 4.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 9 PTKLYFGENQITKLSQELASYHKqvNVLLVYGGGSIKRNGvyDEVKAELQS--INAVVHELSGvepNPRLTTVAKGVDIC 86
Cdd:COG0371 6 PRRYVQGEGALDELGEYLADLGK--RALIITGPTALKAAG--DRLEESLEDagIEVEVEVFGG---ECSEEEIERLAEEA 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1265435555 87 KKENIGFLLAVGGGSVIDCTKAIAagavYEGNtwdlitrkkeitdaLPFGTVLTLAAT 144
Cdd:COG0371 79 KEQGADVIIGVGGGKALDTAKAVA----YRLG--------------LPVVSVPTIAST 118
|
|
| 4HBD_NAD |
cd14860 |
4-hydroxybutyrate dehydrogenase, also called gamma-hydroxybutyrate dehydrogenase, catalyzes ... |
96-385 |
3.84e-10 |
|
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: 60.69 E-value: 3.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 96 AVGGGSVIDCTKAIAAGavYEGNTWDLITRKKEITDALPFGTVLTLAATGSEMNSTSVITNWETKEKLGWTSSHVFPVFS 175
Cdd:cd14860 84 AIGGGTVIDIAKLLALK--GISPVLDLFDGKIPLIKEKELIIVPTTCGTGSEVTNISIVELTSLGTKKGLAVDELYADKA 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 176 ILDPAYTFSVPRDQTVYGIVDSMSHALEHYF--HRTENTPM-----IDGFIESLLRTAvQEGPkllkdltsyKYRETMMY 248
Cdd:cd14860 162 VLIPELLKGLPYKVFATSSIDALIHAIESYLspKATPYTEMfsykaIEMILEGYQEIA-EKGE---------EARFPLLG 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 249 ISTTAFN-GSLANGTdGGDWATHRIEHALSAVYDIPHGGGLAILFPNWLEHVLKEDP----SRVKQLAVNVFGIdpagks 323
Cdd:cd14860 232 DFLIASNyAGIAFGN-AGCAAVHALSYPLGGKYHVPHGEANYAVFTGVLKNYQEKNPdgeiKKLNEFLAKILGC------ 304
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1265435555 324 DEETAMEgakALRTFWNDLGAPNSLRDYDIDDS---EFDAIVEKTFVKPGVGTYKELDYASVRDI 385
Cdd:cd14860 305 DEEDVYD---ELEELLNKILPKKPLHEYGMKEEeidEFADSVMENQQRLLANNYVPLDREDVAEI 366
|
|
| Fe-ADH_2 |
pfam13685 |
Iron-containing alcohol dehydrogenase; |
13-111 |
8.32e-08 |
|
Iron-containing alcohol dehydrogenase;
Pssm-ID: 404557 [Multi-domain] Cd Length: 251 Bit Score: 52.69 E-value: 8.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 13 YFGENQITKLSqELASYHKQVNVLLVYGGGSIKRNGvyDEVKAELQSINAVVHELSGVEPNPRLTTVAKGVDICKKENIG 92
Cdd:pfam13685 1 VIGPGALGRLG-EYLAELGFRRVALVADANTYAAAG--RKVAESLKRAGIEVETRLEVAGNADMETAEKLVGALRERDAD 77
|
90
....*....|....*....
gi 1265435555 93 FLLAVGGGSVIDCTKAIAA 111
Cdd:pfam13685 78 AVVGVGGGTVIDLAKYAAF 96
|
|
| egsA |
PRK00843 |
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed |
9-110 |
6.62e-07 |
|
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed
Pssm-ID: 179139 Cd Length: 350 Bit Score: 50.66 E-value: 6.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 9 PTKLYFGENQITKLSQELASYHKQVNVLLVYGGGSIKRNGvyDEVKAELQSINAVVHELSGvepNPRLTTVAKGVDICKK 88
Cdd:PRK00843 11 PRDVVVGHGVLDDIGDVCSDLKLTGRALIVTGPTTKKIAG--DRVEENLEDAGDVEVVIVD---EATMEEVEKVEEKAKD 85
|
90 100
....*....|....*....|..
gi 1265435555 89 ENIGFLLAVGGGSVIDCTKAIA 110
Cdd:PRK00843 86 VNAGFLIGVGGGKVIDVAKLAA 107
|
|
| Gro1PDH |
cd08173 |
Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) catalyzes the reversible conversion between ... |
9-110 |
2.32e-05 |
|
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: 46.01 E-value: 2.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 9 PTKLYFGENQITKLSQELASYHKQVNVLLVYGGGSIKRNGvyDEVKAELQSINAVVHELSGVEPNpRLTTVAKGVDICKK 88
Cdd:cd08173 2 PRNVVVGHGAINKIGEVLKKLLLGKRALIITGPNTYKIAG--KRVEDLLESSGVEVVIVDIATIE-EAAEVEKVKKLIKE 78
|
90 100
....*....|....*....|..
gi 1265435555 89 ENIGFLLAVGGGSVIDCTKAIA 110
Cdd:cd08173 79 SKADFIIGVGGGKVIDVAKYAA 100
|
|
| GlyDH-like |
cd08550 |
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins. ... |
9-372 |
3.55e-04 |
|
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: 42.14 E-value: 3.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 9 PTKLYFGENQITKLSQELASYHKqvNVLLVYGGGSIKRngVYDEVKAELQS--INAVVHELSGvEPNPRltTVAKGVDIC 86
Cdd:cd08550 1 PGRYIQEPGILAKAGEYIAPLGK--KALIIGGKTALEA--VGEKLEKSLEEagIDYEVEVFGG-ECTEE--NIERLAEKA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 87 KKENIGFLLAVGGGSVIDCTKAIAagavyegntwdlitrkkEITDaLPFGTVLTLAATGSEMNSTSVITNWETKEKLGWT 166
Cdd:cd08550 74 KEEGADVIIGIGGGKVLDTAKAVA-----------------DRLG-LPVVTVPTIAATCAAWSALSVLYDEEGEFLGYSL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 167 SSHvFPVFSILDPAYTFSVPRDQTVYGIVDSMSHALEHYFHRTENTPMIDGFI-----ESLLRTAVQEGPKLLKDLTSYK 241
Cdd:cd08550 136 LKR-SPDLVLVDTDIIAAAPVRYLAAGIGDTLAKWYEARPSSRGGPDDLALQAavqlaKLAYDLLLEYGVQAVEDVRQGK 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 242 ----YRETM-MYISTTAFNGSLANGTDGGDWAtHRIEHALSAVYDIP---HGG--GLAILFpnwlehvlkedpsrvkQLA 311
Cdd:cd08550 215 vtpaLEDVVdAIILLAGLVGSLGGGGCRTAAA-HAIHNGLTKLPETHgtlHGEkvAFGLLV----------------QLA 277
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1265435555 312 VNvfgidpaGKSDEEtamegAKALRTFWNDLGAPNSLRDYDIDDSE--FDAIVEKTFVKPGVG 372
Cdd:cd08550 278 LE-------GRSEEE-----IEELIEFLRRLGLPVTLEDLGLELTEeeLRKIAEYACDPPDMA 328
|
|
| GlyDH |
cd08170 |
Glycerol dehydrogenases (GlyDH) catalyzes oxidation of glycerol to dihydroxyacetone in ... |
15-144 |
4.27e-04 |
|
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: 42.01 E-value: 4.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265435555 15 GENQITKLSQELASYHKqvNVLLVYGGGSIKRNGvyDEVKAELQSINAVVH------ELSGVEpnprlttVAKGVDICKK 88
Cdd:cd08170 7 GPGALDRLGEYLAPLGK--KALVIADPFVLDLVG--ERLEESLEKAGLEVVfevfggECSREE-------IERLAAIARA 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1265435555 89 ENIGFLLAVGGGSVIDCTKAIAAgavYEGntwdlitrkkeitdaLPFGTVLTLAAT 144
Cdd:cd08170 76 NGADVVIGIGGGKTIDTAKAVAD---YLG---------------LPVVIVPTIAST 113
|
|
| |
