|
Name |
Accession |
Description |
Interval |
E-value |
| Fe-ADH-like |
cd14861 |
Iron-containing alcohol dehydrogenases-like; This family contains proteins similar to ... |
8-394 |
0e+00 |
|
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: 555.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 8 YPTTVWFGSGRIVDLPKACKTLGIKKPLFVTDSDLVKTEMVASAIQSNNKNFIPTKVYSEVKGNPVSRYVTKGVEVFKSG 87
Cdd:cd14861 2 YPTRIRFGAGAIAELPEELKALGIRRPLLVTDPGLAALGIVDRVLEALGAAGLSPAVFSDVPPNPTEADVEAGVAAYREG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 88 NHDGVIAFGGGSSLDVGKSIALLESNNRPLWDFSgEGSFWAENDynesmaknkmsnPDEIKPIIAIPTTAGTGSEISRAA 167
Cdd:cd14861 82 GCDGIIALGGGSAIDAAKAIALMATHPGPLWDYE-DGEGGPAAI------------TPAVPPLIAIPTTAGTGSEVGRAA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 168 AIINEKTNEKKIVFHPKMLPTLTILDPQLTLGLPPFLTAATGMDALAHNLEAYCASGYHPMADGIALEGMWLIKKWLIIA 247
Cdd:cd14861 149 VITDDDTGRKKIIFSPKLLPKVAICDPELTLGLPPRLTAATGMDALTHCIEAYLSPGFHPMADGIALEGLRLISEWLPRA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 248 VKEGDNLEARGNMLTASSMGATAFQKGLGAIHSLSHPVNSVFNIHHGLSNAIFMPYVLTFNRSAIENKIAKLSEYLELKN 327
Cdd:cd14861 229 VADGSDLEARGEMMMAALMGAVAFQKGLGAVHALAHALGALYGLHHGLLNAILLPYVLRFNRPAVEDKLARLARALGLGL 308
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 167041165 328 PSFNSFIDWVLDLRDKIKIPHKLSEcAKITDKDIEKLSPMALNDPCTPENPKKTTLNDMKLMYRHSI 394
Cdd:cd14861 309 GGFDDFIAWVEDLNERLGLPATLSE-LGVTEDDLDELAELALADPCHATNPRPVTAEDYRALLREAL 374
|
|
| EutG |
COG1454 |
Alcohol dehydrogenase, class IV [Energy production and conversion]; |
5-393 |
1.18e-153 |
|
Alcohol dehydrogenase, class IV [Energy production and conversion];
Pssm-ID: 441063 [Multi-domain] Cd Length: 381 Bit Score: 438.78 E-value: 1.18e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 5 NWAYPTTVWFGSGRIVDLPKACKTLGIKKPLFVTDSDLVKTEMVASAIQSNNKNFIPTKVYSEVKGNPVSRYVTKGVEVF 84
Cdd:COG1454 4 TFRLPTRIVFGAGALAELGEELKRLGAKRALIVTDPGLAKLGLLDRVLDALEAAGIEVVVFDDVEPNPTVETVEAGAAAA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 85 KSGNHDGVIAFGGGSSLDVGKSIALLESNNRPLWDFSGEGSFwaendynesmaknkmsnPDEIKPIIAIPTTAGTGSEIS 164
Cdd:COG1454 84 REFGADVVIALGGGSAIDAAKAIALLATNPGDLEDYLGIKKV-----------------PGPPLPLIAIPTTAGTGSEVT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 165 RAAAIINEKTNEKKIVFHPKMLPTLTILDPQLTLGLPPFLTAATGMDALAHNLEAYCASGYHPMADGIALEGMWLIKKWL 244
Cdd:COG1454 147 PFAVITDPETGVKKGIADPELLPDVAILDPELTLTLPPSLTAATGMDALTHAIEAYVSKGANPLTDALALEAIRLIARNL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 245 IIAVKEGDNLEARGNMLTASSMGATAFQK-GLGAIHSLSHPVNSVFNIHHGLSNAIFMPYVLTFNRSAIENKIAKLSEYL 323
Cdd:COG1454 227 PRAVADGDDLEAREKMALASLLAGMAFANaGLGAVHALAHPLGGLFHVPHGLANAILLPHVLRFNAPAAPERYAEIARAL 306
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 167041165 324 ELKNPS-----FNSFIDWVLDLRDKIKIPHKLSECaKITDKDIEKLSPMALNDPCTPENPKKTTLNDMKLMYRHS 393
Cdd:COG1454 307 GLDVGLsdeeaAEALIEAIRELLRDLGIPTRLSEL-GVTEEDLPELAELALADRCLANNPRPLTEEDIEAILRAA 380
|
|
| Fe-ADH |
cd08551 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains large ... |
9-390 |
1.15e-133 |
|
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: 387.57 E-value: 1.15e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 9 PTTVWFGSGRIVDLPKACKTLGIKKPLFVTDSDLVKTEMVASAIQSNNKNFIPTKVYSEVKGNPVSRYVTKGVEVFKSGN 88
Cdd:cd08551 1 PTRIVFGAGALARLGEELKALGGKKVLLVTDPGLVKAGLLDKVLESLKAAGIEVEVFDDVEPNPTVETVEAAAELAREEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 89 HDGVIAFGGGSSLDVGKSIALLESNNRPLWDFSGEGSFwaendynesmaknkmsnPDEIKPIIAIPTTAGTGSEISRAAA 168
Cdd:cd08551 81 ADLVIAVGGGSVLDTAKAIAVLATNGGSIRDYEGIGKV-----------------PKPGLPLIAIPTTAGTGSEVTPNAV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 169 IINEKTNEKKIVFHPKMLPTLTILDPQLTLGLPPFLTAATGMDALAHNLEAYCASGYHPMADGIALEGMWLIKKWLIIAV 248
Cdd:cd08551 144 ITDPETGRKMGIVSPYLLPDVAILDPELTLSLPPSVTAATGMDALTHAIEAYTSKKANPISDALALEAIRLIGKNLRRAV 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 249 KEGDNLEARGNMLTASSMGATAF-QKGLGAIHSLSHPVNSVFNIHHGLSNAIFMPYVLTFNRSAIENKIAKLSEYLELKN 327
Cdd:cd08551 224 ADGSDLEAREAMLLASLLAGIAFgNAGLGAVHALAYPLGGRYHIPHGVANAILLPYVMEFNLPACPEKYAEIAEALGEDV 303
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 328 PSFN------SFIDWVLDLRDKIKIPHKLSECaKITDKDIEKLSPMALNDPCTPEN-PKKTTLNDMKLMY 390
Cdd:cd08551 304 EGLSdeeaaeAAVEAVRELLRDLGIPTSLSEL-GVTEEDIPELAEDAMKSGRLLSNnPRPLTEEDIREIY 372
|
|
| Fe-ADH |
pfam00465 |
Iron-containing alcohol dehydrogenase; |
9-386 |
1.25e-126 |
|
Iron-containing alcohol dehydrogenase;
Pssm-ID: 425696 [Multi-domain] Cd Length: 362 Bit Score: 369.24 E-value: 1.25e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 9 PTTVWFGSGRIVDLPKACKTLGiKKPLFVTDSDLVKTEMVASAIQSNNKNFIPTKVYSEVKGNPVSRYVTKGVEVFKSGN 88
Cdd:pfam00465 1 PTRIVFGAGALAELGEELKRLG-ARALIVTDPGSLKSGLLDKVLASLEEAGIEVVVFDGVEPEPTLEEVDEAAALAREAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 89 HDGVIAFGGGSSLDVGKSIALLESNNRPLWDFSGEGSFwaendynesmaknkmsnPDEIKPIIAIPTTAGTGSEISRAAA 168
Cdd:pfam00465 80 ADVIIAVGGGSVIDTAKAIALLLTNPGDVWDYLGGKPL-----------------TKPALPLIAIPTTAGTGSEVTPLAV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 169 IINEKTNEKKIVFHPKMLPTLTILDPQLTLGLPPFLTAATGMDALAHNLEAYCASGYHPMADGIALEGMWLIKKWLIIAV 248
Cdd:pfam00465 143 ITDTETGEKLGIFSPKLLPDLAILDPELTLTLPPRLTAATGMDALAHAVEAYVSKGANPLTDALALEAIRLIAENLPRAV 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 249 KEGDNLEARGNMLTASSMGATAFQK-GLGAIHSLSHPVNSVFNIHHGLSNAIFMPYVLTFNRSAIENKIAKLSEYLELKN 327
Cdd:pfam00465 223 ADGEDLEARENMLLASTLAGLAFSNaGLGAAHALAHALGGRYGIPHGLANAILLPYVLRFNAPAAPEKLAQLARALGEDS 302
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 167041165 328 P--SFNSFIDWVLDLRDKIKIPHKLSEcAKITDKDIEKLSPMALNDPCTPENPKKTTLNDM 386
Cdd:pfam00465 303 DeeAAEEAIEALRELLRELGLPTTLSE-LGVTEEDLDALAEAALRDRSLANNPRPLTAEDI 362
|
|
| Fe-ADH-like |
cd14863 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
5-387 |
2.97e-117 |
|
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: 346.06 E-value: 2.97e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 5 NWAYPTTVWFGSGRIVDLPKACKTLGIKKPLFVTDSDLVKTEMVASAIQSNNKNFIPTKVYSEVKGNPVSRYVTKGVEVF 84
Cdd:cd14863 1 TYSQLTPVIFGAGAVEQIGELLKELGCKKVLLVTDKGLKKAGIVDKIIDLLEEAGIEVVVFDDVEPDPPDEIVDEAAEIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 85 KSGNHDGVIAFGGGSSLDVGKSIALLESNNRPLWDFSgegsfwaendynesMAKNKMSNPDeiKPIIAIPTTAGTGSEIS 164
Cdd:cd14863 81 REEGADGVIGIGGGSVLDTAKAIAVLLTNPGPIIDYA--------------LAGPPVPKPG--IPLIAIPTTAGTGSEVT 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 165 RAAAIINEKTNEKKIVFHPKMLPTLTILDPQLTLGLPPFLTAATGMDALAHNLEAYCASGYHPMADGIALEGMWLIKKWL 244
Cdd:cd14863 145 PIAVITDEENGVKKSLLGPFLVPDLAILDPELTVGLPPSLTAATGMDALSHAIEAYTSKLANPMTDALALQAIRLIVKNL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 245 IIAVKEGDNLEARGNMLTASSMGATAFQK-GLGAIHSLSHPVNSVFNIHHGLSNAIFMPYVLTFNRSAIENKIAKLSEYL 323
Cdd:cd14863 225 PRAVKDGDNLEARENMLLASNLAGIAFNNaGTHIGHAIAHALGALYHIPHGLACALALPVVLEFNAEAYPEKVKKIAKAL 304
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 324 ELKNPSFNS------FIDWVLDLRDKIKIPHKLSECAkITDKDIEKLSPMALNDPCTPENPKKTTLNDMK 387
Cdd:cd14863 305 GVSFPGESDeelgeaVADAIREFMKELGIPSLFEDYG-IDKEDLDKIAEAVLKDPFAMFNPRPITEEEVA 373
|
|
| PDDH |
cd08188 |
1,3-Propanediol (1,3-PD) dehydrogenase; This family includes 1,3-propanediol (1,3-PD) ... |
9-391 |
5.91e-117 |
|
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: 345.27 E-value: 5.91e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 9 PTTVWFGSGRIVDLPKACKTLGIKKPLFVTDSDLVKTEMVASAIQSNNKNFIPTKVYSEVKGNPVSRYVTKGVEVFKSGN 88
Cdd:cd08188 6 PPVNLFGPGCLKEIGDELKKLGGKKALIVTDKGLVKLGLVKKVTDVLEEAGIEYVIFDGVQPNPTVTNVNEGLELFKENG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 89 HDGVIAFGGGSSLDVGKSIALLESNNRPLWDFSGegsfwaendynesmaKNKMSNPdeIKPIIAIPTTAGTGSEISRAAA 168
Cdd:cd08188 86 CDFIISVGGGSAHDCAKAIGILATNGGEIEDYEG---------------VDKSKKP--GLPLIAINTTAGTASEVTRFAV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 169 IINEKTNEKKIVFHPKMLPTLTILDPQLTLGLPPFLTAATGMDALAHNLEAYCASGYHPMADGIALEGMWLIKKWLIIAV 248
Cdd:cd08188 149 ITDEERHVKMVIVDWNVTPTIAVNDPELMLGMPPSLTAATGMDALTHAIEAYVSTGATPLTDALALEAIRLIAENLPKAV 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 249 KEGDNLEARGNMLTASSMGATAFQK-GLGAIHSLSHPVNSVFNIHHGLSNAIFMPYVLTFNRSAIENKIAKLSEYLELKN 327
Cdd:cd08188 229 ANGKDLEARENMAYAQFLAGMAFNNaGLGYVHAMAHQLGGFYNLPHGVCNAILLPHVMEFNLPACPERFADIARALGENT 308
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 328 PSFNS------FIDWVLDLRDKIKIPHKLSEcAKITDKDIEKLSPMALNDPCTPENPKKTTLNDMKLMYR 391
Cdd:cd08188 309 EGLSDeeaaeaAIEAIRKLSRRVGIPSGLKE-LGVKEEDFPLLAENALKDACGPTNPRQATKEDVIAIYR 377
|
|
| LPO |
cd08176 |
Lactadehyde:propanediol oxidoreductase (LPO) catalyzes the interconversion between ... |
8-391 |
4.34e-114 |
|
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: 337.98 E-value: 4.34e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 8 YPTTVWFGSGRIVDLPKACKTLGIKKPLFVTDSDLVKTEMVASAIQSNNKNFIPTKVYSEVKGNPVSRYVTKGVEVFKSG 87
Cdd:cd08176 5 LNPTSYFGWGAIEEIGEEAKKRGFKKALIVTDKGLVKFGIVDKVTDVLKEAGIAYTVFDEVKPNPTIENVMAGVAAYKES 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 88 NHDGVIAFGGGSSLDVGKSIALLESNnrplwDFsgegsfwAENDYNESMAKNKMSNPdeikPIIAIPTTAGTGSEISRAA 167
Cdd:cd08176 85 GADGIIAVGGGSSIDTAKAIGIIVAN-----PG-------ADVRSLEGVAPTKNPAV----PIIAVPTTAGTGSEVTINY 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 168 AIINEKTNEKKIVFHPKMLPTLTILDPQLTLGLPPFLTAATGMDALAHNLEAYCASGYHPMADGIALEGMWLIKKWLIIA 247
Cdd:cd08176 149 VITDTEKKRKFVCVDPHDIPTVAIVDPDLMSSMPKGLTAATGMDALTHAIEGYITKGAWELSDMLALKAIELIAKNLRKA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 248 VKEGDNLEARGNMLTASSMGATAF-QKGLGAIHSLSHPVNSVFNIHHGLSNAIFMPYVLTFNRSAIENKIAKLSEYLELK 326
Cdd:cd08176 229 VANPNNVEARENMALAQYIAGMAFsNVGLGIVHSMAHPLSAFYDTPHGVANAILLPYVMEFNAPATGEKYRDIARAMGVD 308
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 167041165 327 NPSF------NSFIDWVLDLRDKIKIPHKLSECaKITDKDIEKLSPMALNDPCTPENPKKTTLNDMKLMYR 391
Cdd:cd08176 309 TTGMsdeeaaEAAVDAVKKLSKDVGIPQKLSEL-GVKEEDIEALAEDALNDVCTPGNPREATKEDIIALYK 378
|
|
| Fe-ADH-like |
cd14865 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
9-391 |
1.01e-99 |
|
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: 301.38 E-value: 1.01e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 9 PTTVWFGSGRIVDLPKACKTLGIKKPLFVTDSDLVKTEMVASAIQSNNKNFIPTKVYSEVKGNPVSRYVTKGVEVFKSGN 88
Cdd:cd14865 6 PTKIVSGAGALENLPAELARLGARRPLIVTDKGLAAAGLLKKVEDALGDAIEIVGVFDDVPPDSSVAVVNEAAARAREAG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 89 HDGVIAFGGGSSLDVGKSIALLESNNrplwdfsGEgsfwAENDYnesMAKNKMSNPdeIKPIIAIPTTAGTGSEISRAAA 168
Cdd:cd14865 86 ADGIIAVGGGSVIDTAKGVNILLSEG-------GD----DLDDY---GGANRLTRP--LKPLIAIPTTAGTGSEVTLVAV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 169 IINEKTNEKKIVFHPKMLPTLTILDPQLTLGLPPFLTAATGMDALAHNLEAYCASGYHPMADGIALEGMWLIKKWLIIAV 248
Cdd:cd14865 150 IKDEEKKVKLLFVSPFLLPDVAILDPRLTLSLPPKLTAATGMDALTHAIEAYTSLQKNPISDALALQAIRLISENLPKAV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 249 KEGDNLEARGNMLTASSMGATAFQKGL-GAIHSLSHPVNSVFNIHHGLSNAIFMPYVLTFNRSAIENKIAKLSEYLELKN 327
Cdd:cd14865 230 KNGKDLEARLALAIAATMAGIAFSNSMvGLVHAIAHAVGAVAGVPHGLANSILLPHVMRYNLDAAAERYAELALALAYGV 309
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 167041165 328 PSFN--------SFIDWVLDLRDKIKIPHKLSEcAKITDKDIEKLSPMALNDPCTPENPKKTTLNDMKLMYR 391
Cdd:cd14865 310 TPAGrraeeaieAAIDLVRRLHELCGLPTRLRD-VGVPEEQLEAIAELALNDGAILFNPREVDPEDILAILE 380
|
|
| Fe-ADH-like |
cd08189 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
15-369 |
1.93e-99 |
|
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: 300.54 E-value: 1.93e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 15 GSGRIVDLPKACKTLGIKKPLFVTDSDLVKTEMVASAIQSNNKNFIPTKVYSEVKGNPVSRYVTKGVEVFKSGNHDGVIA 94
Cdd:cd08189 11 GAGSLLQLPEALKKLGIKRVLIVTDKGLVKLGLLDPLLDALKKAGIEYVVFDGVVPDPTIDNVEEGLALYKENGCDAIIA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 95 FGGGSSLDVGKSIALLESNNR-PLWDFSGegsfwaendynesMAKNKMSNPdeikPIIAIPTTAGTGSEISRAAAIINEK 173
Cdd:cd08189 91 IGGGSVIDCAKVIAARAANPKkSVRKLKG-------------LLKVRKKLP----PLIAVPTTAGTGSEATIAAVITDPE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 174 TNEKKIVFHPKMLPTLTILDPQLTLGLPPFLTAATGMDALAHNLEAYCASGYHPMADGIALEGMWLIKKWLIIAVKEGDN 253
Cdd:cd08189 154 THEKYAINDPKLIPDAAVLDPELTLGLPPAITAATGMDALTHAVEAYISRSATKETDEYALEAVKLIFENLPKAYEDGSD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 254 LEARGNMLTASSMGATAFQK-GLGAIHSLSHPVNSVFNIHHGLSNAIFMPYVLTFNRSAIENKIAKLSEYLELKNPSFNS 332
Cdd:cd08189 234 LEARENMLLASYYAGLAFTRaYVGYVHAIAHQLGGLYGVPHGLANAVVLPHVLEFYGPAAEKRLAELADAAGLGDSGESD 313
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 167041165 333 ------FIDWVLDLRDKIKIPHKLSEcakITDKDIEKLSPMAL 369
Cdd:cd08189 314 sekaeaFIAAIRELNRRMGIPTTLEE---LKEEDIPEIAKRAL 353
|
|
| Fe-ADH-like |
cd08194 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
9-392 |
4.50e-97 |
|
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: 294.44 E-value: 4.50e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 9 PTTVWFGSGRIVDLPKACKTLGIKKPLFVTDSDLVKTEMVASAIQSNNKNFIPTKVYSEVKGNPVSRYVTKGVEVFKSGN 88
Cdd:cd08194 1 PRTIIIGGGALEELGEEAASLGGKRALIVTDKVMVKLGLVDKVTQLLAEAGIAYAVFDDVVSEPTDEMVEEGLALYKEGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 89 HDGVIAFGGGSSLDVGKSIALLESNNRPLWDFsgegsfwaendynesMAKNKMSNPDeiKPIIAIPTTAGTGSEISRAAA 168
Cdd:cd08194 81 CDFIVALGGGSPIDTAKAIAVLATNGGPIRDY---------------MGPRKVDKPG--LPLIAIPTTAGTGSEVTRFTV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 169 IINEKTNEKKIVFHPKMLPTLTILDPQLTLGLPPFLTAATGMDALAHNLEAYCASGYHPMADGIALEGMWLIKKWLIIAV 248
Cdd:cd08194 144 ITDTETDVKMLLKGPALLPAVAIVDPELTLSMPPRVTAATGIDALTHAIEAYVSRKAQPLTDTLALSAIKLIGRNLRRAY 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 249 KEGDNLEARGNMLTASSMGATAFQKGLGA-IHSLSHPVNSVFNIHHGLSNAIFMPYVLTFNRSAIENKIAKLSEYLELKN 327
Cdd:cd08194 224 ADGDDLEAREAMMLAALEAGIAFSNSSVAlVHGMSRPIGALFHVPHGLSNAMLLPAVTEFSLPGAPERYAEIARAMGIAT 303
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 167041165 328 PSFN------SFIDWVLDLRDKIKIPhKLSECAkITDKD----IEKLSPMALNDPCTPENPKKTTLNDMKLMYRH 392
Cdd:cd08194 304 EGDSdeeaaeKLVEALERLCADLEIP-TLREYG-IDEEEfeaaLDKMAEDALASGSPANNPRVPTKEEIIELYRE 376
|
|
| Fe-ADH-like |
cd08185 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
9-391 |
5.41e-91 |
|
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: 279.00 E-value: 5.41e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 9 PTTVWFGSGRIVDLPKACKTLGiKKPLFVTDSD-LVKTEMVASAIQSNNKNFIPTKVYSEVKGNPVSRYVTKGVEVFKSG 87
Cdd:cd08185 4 PTRILFGAGKLNELGEEALRPG-KKALIVTGKGsSKKTGLLDRVKKLLEKAGVEVVVFDKVEPNPLTTTVMEGAALAKEE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 88 NHDGVIAFGGGSSLDVGKSIALLESNNRPLWDFSGEGsfwaendynesmaKNKMSNPDEIKPIIAIPTTAGTGSEISRAA 167
Cdd:cd08185 83 GCDFVIGLGGGSSMDAAKAIAFMATNPGDIWDYIFGG-------------TGKGPPPEKALPIIAIPTTAGTGSEVDPWA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 168 AIINEKTNEKKIVFHPKMLPTLTILDPQLTLGLPPFLTAATGMDALAHNLEAYCASGYHPMADGIALEGMWLIKKWLIIA 247
Cdd:cd08185 150 VITNPETKEKKGIGHPALFPKVSIVDPELMLTVPPRVTAYTGFDALFHAFESYISKNANPFSDMLALEAIRLVAKYLPRA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 248 VKEGDNLEARGNMLTASSMGATAFQ-KGLGAIHSLSHPVNSVF-NIHHGLSNAIFMPYVLTFN-RSAIE----NKIAKLS 320
Cdd:cd08185 230 VKDGSDLEAREKMAWASTLAGIVIAnSGTTLPHGLEHPLSGYHpNIPHGAGLAALYPAYFEFTiEKAPEkfafVARAEAS 309
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 167041165 321 EYLELKNPSfnSFIDWVLDLRDKIKIPHKLSEcAKITDKDIEKL--SPMALNDPCTPENPKKTTLNDMKLMYR 391
Cdd:cd08185 310 GLSDAKAAE--DFIEALRKLLKDIGLDDLLSD-LGVTEEDIPWLaeNAMETMGGLFANNPVELTEEDIVEIYE 379
|
|
| Fe-ADH-like |
cd17814 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
14-390 |
2.39e-87 |
|
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: 269.41 E-value: 2.39e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 14 FGSGRIVDLPKACKTLGIKKPLFVTDSDLVKTEMVASAIQSNNKNFIPTKVYSEVKGNPVSRYVTKGVEVFKSGNHDGVI 93
Cdd:cd17814 9 FGVGARKLAGRYAKNLGARKVLVVTDPGVIKAGWVDEVLDSLEAEGLEYVVFSDVTPNPRDFEVMEGAELYREEGCDGIV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 94 AFGGGSSLDVGKSIALLESNNRPLWDFSGegsfwaendynesmaKNKMSNPdeIKPIIAIPTTAGTGSEISRAAAIINEK 173
Cdd:cd17814 89 AVGGGSPIDCAKGIGIVVSNGGHILDYEG---------------VDKVRRP--LPPLICIPTTAGSSADVSQFAIITDTE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 174 TNEKKIVFHPKMLPTLTILDPQLTLGLPPFLTAATGMDALAHNLEAYCASGYHPMADGIALEGMWLIKKWLIIAVKEGDN 253
Cdd:cd17814 152 RRVKMAIISKTLVPDVSLIDPETLTTMDPELTACTGMDALTHAIEAYVSNASSPLTDLHALEAIRLISENLPKAVADPDD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 254 LEARGNMLTASSMGATAFQK-GLGAIHSLSHPVNSVFNIHHGLSNAIFMPYVLTFNRSAIENKIAKLSEYLELKNPSFNS 332
Cdd:cd17814 232 LEAREKMMLASLQAGLAFSNaSLGAVHAMAHSLGGLLDLPHGECNALLLPHVIRFNFPAAPERYRKIAEAMGLDVDGLDD 311
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 167041165 333 ------FIDWVLDLRDKIKIPHKLSECaKITDKDIEKLSPMALNDPCTPENPKKTTLNDMKLMY 390
Cdd:cd17814 312 eevaerLIEAIRDLREDLGIPETLSEL-GVDEEDIPELAKRAMKDPCLVTNPRRPTREDIEEIY 374
|
|
| HVD |
cd08193 |
5-hydroxyvalerate dehydrogenase (HVD) catalyzes the oxidation of 5-hydroxyvalerate to ... |
9-391 |
2.07e-86 |
|
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: 267.07 E-value: 2.07e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 9 PTTVwFGSGRIVDLPKACKTLGIKKPLFVTDSDLVKTEMVASAIQSNNKNFIPTKVYSEVKGNPVSRYVTKGVEVFKSGN 88
Cdd:cd08193 5 PRII-CGAGAAARLGELLRELGARRVLLVTDPGLVKAGLADPALAALEAAGIAVTVFDDVVADPPEAVVEAAVEQAREAG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 89 HDGVIAFGGGSSLDVGKSIALLESNNRPLWDFSGEGsfwaendynesMAKNKMsnpdeiKPIIAIPTTAGTGSEISrAAA 168
Cdd:cd08193 84 ADGVIGFGGGSSMDVAKLVALLAGSDQPLDDIYGVG-----------KATGPR------LPLILVPTTAGTGSEVT-PIS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 169 IINEKTNEKKIVFHPKMLPTLTILDPQLTLGLPPFLTAATGMDALAHNLEAYcaSGYH---PMADGIALEGMWLIKKWLI 245
Cdd:cd08193 146 IVTTGETEKKGVVSPQLLPDVALLDAELTLGLPPHVTAATGIDAMVHAIEAY--TSRHkknPISDALAREALRLLGANLR 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 246 IAVKEGDNLEARGNMLTASSMGATAFQKG-LGAIHSLSHPVNSVFNIHHGLSNAIFMPYVLTFNRSAIENKIAKLSEYLe 324
Cdd:cd08193 224 RAVEDGSDLEAREAMLLGSMLAGQAFANApVAAVHALAYPLGGHFHVPHGLSNALVLPHVLRFNLPAAEALYAELARAL- 302
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 167041165 325 LKNPSFNS-------FIDWVLDLRDKIKIPHKLSEcAKITDKDIEKLSPMA-LNDPCTPENPKKTTLNDMKLMYR 391
Cdd:cd08193 303 LPGLAFGSdaaaaeaFIDALEELVEASGLPTRLRD-VGVTEEDLPMLAEDAmKQTRLLVNNPREVTEEDALAIYQ 376
|
|
| Fe-ADH-like |
cd08196 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
6-390 |
1.84e-85 |
|
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: 264.44 E-value: 1.84e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 6 WAY--PTTVWFGSGRIVDLPKACKTLGIKKPLFVTDSDLVKTeMVASAIQSNNKNFIpTKVYSEVKGNPVSRYVTKGVEV 83
Cdd:cd08196 1 WSYyqPVKIIFGEGILKELPDIIKELGGKRGLLVTDPSFIKS-GLAKRIVESLKGRI-VAVFSDVEPNPTVENVDKCARL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 84 FKSGNHDGVIAFGGGSSLDVGKSIALLESNnrplwdfsgEGSFwaendynESMAKNKMSNPDEIKPIIAIPTTAGTGSEI 163
Cdd:cd08196 79 ARENGADFVIAIGGGSVLDTAKAAACLAKT---------DGSI-------EDYLEGKKKIPKKGLPLIAIPTTAGTGSEV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 164 SRAAAIINEKTNEKKIVFHPKMLPTLTILDPQLTLGLPPFLTAATGMDALAHNLEAYCASGYHPMADGIALEGMWLIKKW 243
Cdd:cd08196 143 TPVAVLTDKEKGKKAPLVSPGFYPDIAIVDPELTYSMPPKVTASTGIDALCHAIEAYWSINHQPISDALALEAAKLVLEN 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 244 LIIAVKEGDNLEARGNMLTASSMGATAF-QKGLGAIHSLSHPVNSVFNIHHGLSNAIFMPYVLTFNRSAIENKIAKLSEY 322
Cdd:cd08196 223 LEKAYNNPNDKEAREKMALASLLAGLAFsQTRTTASHACSYPLTSHFGIPHGEACALTLPSFIRLNAEALPGRLDELAKQ 302
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 167041165 323 LELKNPsfNSFIDWVLDLRDKIKIPHKLSECAkITDKDIEKLSPMALNDPCTPENPKKTTLNDMKLMY 390
Cdd:cd08196 303 LGFKDA--EELADKIEELKKRIGLRTRLSELG-ITEEDLEEIVEESFHPNRANNNPVEVTKEDLEKLL 367
|
|
| NADPH_BDH |
cd08179 |
NADPH-dependent butanol dehydrogenase involved in the butanol and ethanol formation pathway in ... |
8-392 |
1.10e-83 |
|
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: 260.20 E-value: 1.10e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 8 YPTTVWFGSGRIvdlpKACKTLGIKKPLFVTDSD-LVKTEMVASAIQSNNKNFIPTKVYSEVKGNPVSRYVTKGVEVFKS 86
Cdd:cd08179 4 VPRDIYFGEGAL----EYLKTLKGKRAFIVTGGGsMKRNGFLDKVEDYLKEAGMEVKVFEGVEPDPSVETVEKGAEAMRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 87 GNHDGVIAFGGGSSLDVGKSIALLESNnrPLWDFsgegsfwaendyNESMAKNKMSNPDEIKPIIAIPTTAGTGSEISRA 166
Cdd:cd08179 80 FEPDWIIAIGGGSVIDAAKAMWVFYEY--PELTF------------EDALVPFPLPELRKKARFIAIPSTSGTGSEVTRA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 167 AAIINEKTNEKKIVFHPKMLPTLTILDPQLTLGLPPFLTAATGMDALAHNLEAYCASGYHPMADGIALEGMWLIKKWLII 246
Cdd:cd08179 146 SVITDTEKGIKYPLASFEITPDVAILDPELTMTMPPHVTANTGMDALTHAIEAYVSTLANDFTDALALGAILDIFENLPK 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 247 AVKEGDNLEARGNMLTASSMGATAFQK-GLGAIHSLSHPVNSVFNIHHGLSNAIFMPYVLTFN-RSAIENKIAKLSEYLE 324
Cdd:cd08179 226 SYNGGKDLEAREKMHNASCLAGMAFSNsGLGIVHSMAHKGGAFFGIPHGLANAILLPYVIEFNsKDPEARARYAALLIGL 305
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 167041165 325 LKNPSFNSFIDWVLDLRDKIKIPHKLSEcAKITDKD----IEKLSPMALNDPCTPENPKKTTLNDMKLMYRH 392
Cdd:cd08179 306 TDEELVEDLIEAIEELNKKLGIPLSFKE-AGIDEDEffakLDEMAENAMNDACTGTNPRKPTVEEMKELLKA 376
|
|
| PRK10624 |
PRK10624 |
L-1,2-propanediol oxidoreductase; Provisional |
10-391 |
4.34e-83 |
|
L-1,2-propanediol oxidoreductase; Provisional
Pssm-ID: 182595 [Multi-domain] Cd Length: 382 Bit Score: 258.77 E-value: 4.34e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 10 TTVWFGSGRIVDLPKACKTLGIKKPLFVTDSDLVKTEMVASAIQSNNKNFIPTKVYSEVKGNPVSRYVTKGVEVFKSGNH 89
Cdd:PRK10624 9 ETAYFGRGAIGALTDEVKRRGFKKALIVTDKTLVKCGVVAKVTDVLDAAGLAYEIYDGVKPNPTIEVVKEGVEVFKASGA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 90 DGVIAFGGGSSLDVGKSIALLeSNNrPlwDFSGEGSFwaendynESMAKNKmsNPDeiKPIIAIPTTAGTGSEISRAAAI 169
Cdd:PRK10624 89 DYLIAIGGGSPQDTCKAIGII-SNN-P--EFADVRSL-------EGVAPTK--KPS--VPIIAIPTTAGTAAEVTINYVI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 170 INEKTNEKKIVFHPKMLPTLTILDPQLTLGLPPFLTAATGMDALAHNLEAYCASGYHPMADGIALEGMWLIKKWLIIAVK 249
Cdd:PRK10624 154 TDEEKRRKFVCVDPHDIPQVAFVDADMMDSMPPGLKAATGVDALTHAIEGYITRGAWALTDMLHLKAIEIIAGALRGAVA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 250 EgdNLEARGNMLTASSMGATAFQK-GLGAIHSLSHPVNSVFNIHHGLSNAIFMPYVLTFNRSAIENK---IAK------- 318
Cdd:PRK10624 234 G--DKEAGEGMALGQYIAGMGFSNvGLGLVHGMAHPLGAFYNTPHGVANAILLPHVMEYNADFTGEKyrdIARamgvkve 311
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 167041165 319 ---LSEYLElknpsfnSFIDWVLDLRDKIKIPHKLSEcAKITDKDIEKLSPMALNDPCTPENPKKTTLNDMKLMYR 391
Cdd:PRK10624 312 gmsLEEARN-------AAVEAVKALNRDVGIPPHLRD-VGVKEEDIPALAQAAFDDVCTGGNPREATLEDIVELYK 379
|
|
| PDD |
cd08180 |
1,3-propanediol dehydrogenase (PPD) catalyzes the reduction of 3-hydroxypropionaldehyde (3-HPA) ... |
9-391 |
3.65e-82 |
|
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: 254.73 E-value: 3.65e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 9 PTTVWFGSGRIVDLpkacKTLGIKKPLFVTDSDLVKTEMVASAIQSNNKNfIPTKVYSEVKGNPVSRYVTKGVEVFKSGN 88
Cdd:cd08180 4 KTKIYSGEDSLERL----KELKGKRVFIVTDPFMVKSGMVDKVTDELDKS-NEVEIFSDVVPDPSIEVVAKGLAKILEFK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 89 HDGVIAFGGGSSLDVGKSIALlesnnrplwdfsgegsfwaendynesMAKnKMSNPDEIKPIIAIPTTAGTGSEISRAAA 168
Cdd:cd08180 79 PDTIIALGGGSAIDAAKAIIY--------------------------FAL-KQKGNIKKPLFIAIPTTSGTGSEVTSFAV 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 169 IINEKTNEKKIVFHPKMLPTLTILDPQLTLGLPPFLTAATGMDALAHNLEAYCASGYHPMADGIALEGMWLIKKWLIIAV 248
Cdd:cd08180 132 ITDPEKGIKYPLVDDSMLPDIAILDPELVKSVPPKVTADTGMDVLTHALEAYVSTNANDFTDALAEKAIKLVFENLPRAY 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 249 KEGDNLEARGNMLTASSMGATAFQK-GLGAIHSLSHPVNSVFNIHHGLSNAIFMPYVLTFnrsaienkiaklseylelkn 327
Cdd:cd08180 212 RDGDDLEAREKMHNASCMAGIAFNNaGLGINHSLAHALGGRFHIPHGRANAILLPYVIEF-------------------- 271
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 167041165 328 psfnsFIDWVLDLRDKIKIPHKLSECAKITD---KDIEKLSPMALNDPCTPENPKKTTLNDMKLMYR 391
Cdd:cd08180 272 -----LIAAIRRLNKKLGIPSTLKELGIDEEefeKAIDEMAEAALADRCTATNPRKPTAEDLIELLR 333
|
|
| AAD_C |
cd08178 |
C-terminal alcohol dehydrogenase domain of the acetaldehyde dehydrogenase-alcohol ... |
9-391 |
1.59e-79 |
|
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: 250.18 E-value: 1.59e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 9 PTTVWFGSGRIVDLpkACKTLGIKKPLFVTDSDLVKTEMVASAIQSNNKNFIPTKVYSEVKGNPVSRYVTKGVEVFKSGN 88
Cdd:cd08178 3 PPKIYFEPGCLPYL--LLELPGVKRAFIVTDRVLYKLGYVDKVLDVLEARGVETEVFSDVEPDPTLSTVRKGLEAMNAFK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 89 HDGVIAFGGGSSLDVGKSIALLesNNRPLWDFSGEGSFWAEndynesMAKNKMSNPD--EIKPIIAIPTTAGTGSEISRA 166
Cdd:cd08178 81 PDVIIALGGGSAMDAAKIMWLF--YEHPETKFEDLAQRFMD------IRKRVYKFPKlgKKAKLVAIPTTSGTGSEVTPF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 167 AAIINEKTNEKKIVFHPKMLPTLTILDPQLTLGLPPFLTAATGMDALAHNLEAY---CASGYhpmADGIALEGMWLIKKW 243
Cdd:cd08178 153 AVITDDKTGKKYPLADYALTPDMAIVDPELVMTMPKRLTADTGIDALTHAIEAYvsvMASDY---TDGLALQAIKLIFEY 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 244 LIIAVKEGDNLEARGNMLTASSMGATAFQKG-LGAIHSLSHPVNSVFNIHHGLSNAIFMPYVLTFNRSAIENKI------ 316
Cdd:cd08178 230 LPRSYNNGNDIEAREKMHNAATIAGMAFANAfLGICHSLAHKLGAAFHIPHGRANAILLPHVIRYNATDPPTKQaafpqy 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 317 ---------AKLSEYLELKNPS----FNSFIDWVLDLRDKIKIPHKLSECAkITDKD----IEKLSPMALNDPCTPENPK 379
Cdd:cd08178 310 kyyvakeryAEIADLLGLGGKTpeekVESLIKAIEDLKKDLGIPTSIREAG-IDEADflaaVDKLAEDAFDDQCTGANPR 388
|
410
....*....|..
gi 167041165 380 KTTLNDMKLMYR 391
Cdd:cd08178 389 YPLISELKEILL 400
|
|
| Fe-ADH-like |
cd08183 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
9-386 |
2.71e-78 |
|
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contain different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341462 [Multi-domain] Cd Length: 377 Bit Score: 246.26 E-value: 2.71e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 9 PTTVWFGSGRIVDLPKACKTLGiKKPLFVTDSDLVKTEMVASAIQSNNKNFIPTKVYSeVKGNPVSRYVTKGVEVFKSGN 88
Cdd:cd08183 1 PPRIVFGRGSLQELGELAAELG-KRALLVTGRSSLRSGRLARLLEALEAAGIEVALFS-VSGEPTVETVDAAVALAREAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 89 HDGVIAFGGGSSLDVGKSIALLESNNRPLWDfsgegsfwaendYNESMAKNKmsnPDEIKPI--IAIPTTAGTGSEISRA 166
Cdd:cd08183 79 CDVVIAIGGGSVIDAAKAIAALLTNEGSVLD------------YLEVVGKGR---PLTEPPLpfIAIPTTAGTGSEVTKN 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 167 AAIINEKTNEKKIVFHPKMLPTLTILDPQLTLGLPPFLTAATGMDALAHNLEAYCASGYHPMADGIALEGMWLIKKWLII 246
Cdd:cd08183 144 AVLSSPEHGVKVSLRSPSMLPDVALVDPELTLSLPPEVTAASGLDALTQLIEPYVSRKANPLTDALAREGLRLAARSLRR 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 247 AVKEGDNLEARGNMLTASSMGATAF-QKGLGAIHSLSHPVNSVFNIHHGLSNAIFMPYVLTFNRSAIENK---IAKLSEY 322
Cdd:cd08183 224 AYEDGEDLEAREDMALASLLGGLALaNAGLGAVHGLAGPLGGMFGAPHGAICAALLPPVLEANLRALRERepdSPALARY 303
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 167041165 323 LEL-----KNP--SFNSFIDWVLDLRDKIKIPhKLSECaKITDKDIEKLSPMALNDPCTPENPKKTTLNDM 386
Cdd:cd08183 304 RELagiltGDPdaAAEDGVEWLEELCEELGIP-RLSEY-GLTEEDFPEIVEKARGSSSMKGNPIELSDEEL 372
|
|
| Fe-ADH-like |
cd08191 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
9-352 |
9.07e-76 |
|
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: 240.21 E-value: 9.07e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 9 PTTVWFGSGRIVDLPKACKTLGiKKPLFVTDSDLVKTEMVASAIQSNNKNFIPTKVYSEVKGNPVSRYVTKGVEVFKSGN 88
Cdd:cd08191 4 PSRLLFGPGARRALGRVAARLG-SRVLIVTDPRLASTPLVAELLAALTAAGVAVEVFDGGQPELPVSTVADAAAAARAFD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 89 HDGVIAFGGGSSLDVGKSIALLESNNRPLWDFSGEGSFwaendynesmaknkmsnPDEIKPIIAIPTTAGTGSEISrAAA 168
Cdd:cd08191 83 PDVVIGLGGGSNMDLAKVVALLLAHGGDPRDYYGEDRV-----------------PGPVLPLIAVPTTAGTGSEVT-PVA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 169 IINEKTNEKKI-VFHPKMLPTLTILDPQLTLGLPPFLTAATGMDALAHNLEAYCA---------------SGYHPMADGI 232
Cdd:cd08191 145 VLTDPARGMKVgVSSPYLRPAVAIVDPELTLTCPPGVTADSGIDALTHAIESYTArdfppfprldpdpvyVGKNPLTDLL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 233 ALEGMWLIKKWLIIAVKEGDNLEARGNMLTASSMGATAF-QKGLGAIHSLSHPVNSVFNIHHGLSNAIFMPYVLTFNRSA 311
Cdd:cd08191 225 ALEAIRLIGRHLPRAVRDGDDLEARSGMALAALLAGLAFgTAGTAAAHALQYPIGALTHTSHGVGNGLLLPYVMRFNRPA 304
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 167041165 312 IENKIAKLSEYLELKNPSFNS-----FIDWVLDLRDKIKIPHKLSE 352
Cdd:cd08191 305 RAAELAEIARALGVTTAGTSEeaadrAIERVEELLARIGIPTTLAD 350
|
|
| Fe-ADH-like |
cd14862 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
11-390 |
2.11e-74 |
|
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: 236.35 E-value: 2.11e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 11 TVWFGSGRIVDLPKACKTL---GIKKPLFVTDSDLVKTEMVASAIQSNNKNFIPTKVYSEVKGNPVSRYVTKGVEVFKSG 87
Cdd:cd14862 1 MWYFSSPKIVFGEDALSHLeqlSGKRALIVTDKVLVKLGLLKKVLKRLLQAGFEVEVFDEVEPEPPLETVLKGAEAMREF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 88 NHDGVIAFGGGSSLDVGKSI-ALLEsnnRPLWDFSGEGSFWaenDYNESmAKNKMsnpdeikpiIAIPTTAGTGSEISrA 166
Cdd:cd14862 81 EPDLIIALGGGSVMDAAKAAwVLYE---RPDLDPEDISPLD---LLGLR-KKAKL---------IAIPTTSGTGSEAT-W 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 167 AAIINEKTNEKKIVF-HPKMLPTLTILDPQLTLGLPPFLTAATGMDALAHNLEAYCASGYHPMADGIALEGMWLIKKWLI 245
Cdd:cd14862 144 AIVLTDTEEPRKIAVaNPELVPDVAILDPEFVLGMPPKLTAGTGLDALAHAVEAYLSTWSNDFSDALALKAIELIFKYLP 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 246 IAVKEGDNLEARGNMLTASSMGATAF-QKGLGAIHSLSHPVNSVFNIHHGLSNAIFMPYVLTFNRSAIENKIAKLSEYLE 324
Cdd:cd14862 224 RAYKDGDDLEAREKMHNAATIAGLAFgNSQAGLAHALGHSLGAVFHVPHGIAVGLFLPYVIEFYAKVTDERYDLLKLLGI 303
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 167041165 325 LKNPSF---NSFIDWVLDLRDKIKIPHKLSEcAKITDKDIEKLSP----MALNDPCTPENPKKTTLNDMKLMY 390
Cdd:cd14862 304 EARDEEealKKLVEAIRELYKEVGQPLSIKD-LGISEEEFEEKLDelveYAMEDSCTITSPRPPSEEDLKKLF 375
|
|
| HOT |
cd08190 |
Hydroxyacid-oxoacid transhydrogenase (HOT) involved in gamma-hydroxybutyrate metabolism; This ... |
10-364 |
4.38e-73 |
|
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: 233.98 E-value: 4.38e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 10 TTVWFGSGRIVDLPKACKTLGIKKPLFVTDSDLVKTEMVASAIQSNNKNFIPTKVYSEVKGNPVSRYVTKGVEVFKSGNH 89
Cdd:cd08190 2 SNIRFGPGATRELGMDLKRLGAKKVLVVTDPGLAKLGLVERVLESLEKAGIEVVVYDGVRVEPTDESFEEAIEFAKEGDF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 90 DGVIAFGGGSSLDVGKSIALLESNNRPLWDFsgegsfwaendYNESMAKNKmSNPDEIKPIIAIPTTAGTGSEISrAAAI 169
Cdd:cd08190 82 DAFVAVGGGSVIDTAKAANLYATHPGDFLDY-----------VNAPIGKGK-PVPGPLKPLIAIPTTAGTGSETT-GVAI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 170 IN-EKTNEKKIVFHPKMLPTLTILDPQLTLGLPPFLTAATGMDALAHNLEAYCASGYH------------------PMAD 230
Cdd:cd08190 149 FDlEELKVKTGISSRYLRPTLAIVDPLLTLTLPPRVTASSGFDVLCHALESYTARPYNarprpanpderpayqgsnPISD 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 231 GIALEGMWLIKKWLIIAVKEGDNLEARGNMLTASSMGATAF-QKGLGAIHSLSHPVNS-VFNIH------------HGLS 296
Cdd:cd08190 229 VWAEKAIELIGKYLRRAVNDGDDLEARSNMLLASTLAGIGFgNAGVHLPHAMAYPIAGlVKDYRppgypvdhphvpHGLS 308
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 167041165 297 NAIFMPYVLTFNRSAIENKIAKLSEYL--ELKNPSFNSFIDW----VLDLRDKIKIPHKLSECAkITDKDIEKL 364
Cdd:cd08190 309 VALTAPAVFRFTAPACPERHLEAAELLgaDTSGASDRDAGEVladaLIKLMRDIGIPNGLSALG-YSEDDIPAL 381
|
|
| PRK09860 |
PRK09860 |
putative alcohol dehydrogenase; Provisional |
1-391 |
8.56e-63 |
|
putative alcohol dehydrogenase; Provisional
Pssm-ID: 182118 [Multi-domain] Cd Length: 383 Bit Score: 206.34 E-value: 8.56e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 1 MIKSNWAYPTTVWFGSGRIVDLPKACKTLGIKKPLFVTDSDLVKTEMVASAIQSNNKNFIPTKVYSEVKGNPVSRYVTKG 80
Cdd:PRK09860 1 MAASTFFIPSVNVIGADSLTDAMNMMADYGFTRTLIVTDNMLTKLGMAGDVQKALEERNIFSVIYDGTQPNPTTENVAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 81 VEVFKSGNHDGVIAFGGGSSLDVGKSIALLESNNRPLWDFSGEgsfwaendynESMAKNKMsnpdeikPIIAIPTTAGTG 160
Cdd:PRK09860 81 LKLLKENNCDSVISLGGGSPHDCAKGIALVAANGGDIRDYEGV----------DRSAKPQL-------PMIAINTTAGTA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 161 SEISRAAAIINEKTNEKKIVFHPKMLPTLTILDPQLTLGLPPFLTAATGMDALAHNLEAYCASGYHPMADGIALEGMWLI 240
Cdd:PRK09860 144 SEMTRFCIITDEARHIKMAIVDKHVTPLLSVNDSSLMIGMPKSLTAATGMDALTHAIEAYVSIAATPITDACALKAVTMI 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 241 KKWLIIAVKEGDNLEARGNMLTASSMGATAFQKG-LGAIHSLSHPVNSVFNIHHGLSNAIFMPYVLTFNRSAIENKIAKL 319
Cdd:PRK09860 224 AENLPLAVEDGSNAKAREAMAYAQFLAGMAFNNAsLGYVHAMAHQLGGFYNLPHGVCNAVLLPHVQVFNSKVAAARLRDC 303
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 167041165 320 SEYLELKNPSFN------SFIDWVLDLRDKIKIPHKLSECaKITDKDIEKLSPMALNDPCTPENPKKTTLNDMKLMYR 391
Cdd:PRK09860 304 AAAMGVNVTGKNdaegaeACINAIRELAKKVDIPAGLRDL-NVKEEDFAVLATNALKDACGFTNPIQATHEEIVAIYR 380
|
|
| HEPD |
cd08182 |
Hydroxyethylphosphoate dehydrogenase (HEPD) catalyzes the reduction of phosphonoacetaldehyde ... |
9-364 |
1.09e-62 |
|
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: 205.54 E-value: 1.09e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 9 PTTVWFGSGRIVDLPKACKTLGIKKPLFVTDSDLVKtEMVASAIQSNNKNFIPTKVYSEVKGNPVSRYVTKGVEVFKSGN 88
Cdd:cd08182 1 PVKIIFGPGALAELKDLLGGLGARRVLLVTGPSAVR-ESGAADILDALGGRIPVVVFSDFSPNPDLEDLERGIELFRESG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 89 HDGVIAFGGGSSLDVGKSIALlesnnrplwdFSGEGSFwaENDYNESMAKnkmSNPDEIKPIIAIPTTAGTGSEISRAAA 168
Cdd:cd08182 80 PDVIIAVGGGSVIDTAKAIAA----------LLGSPGE--NLLLLRTGEK---APEENALPLIAIPTTAGTGSEVTPFAT 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 169 IINEKTNEKKIVFHPKMLPTLTILDPQLTLGLPPFLTAATGMDALAHNLEAYCASGYHPMADGIALEGMWLIKKWLIIAV 248
Cdd:cd08182 145 IWDEAEGKKYSLAHPSLYPDAAILDPELTLSLPLYLTASTGLDALSHAIESIWSVNANPESRAYALRAIRLILENLPLLL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 249 KEGDNLEARGNMLTASSMGATAF-QKGLGAIHSLSHPVNSVFNIHHGLSNAIFMPYVLTFNRSAIENKIAKLSEY---LE 324
Cdd:cd08182 225 ENLPNLEAREAMAEASLLAGLAIsITKTTAAHAISYPLTSRYGVPHGHACALTLPAVLRYNAGADDECDDDPRGReilLA 304
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 167041165 325 LKNPSFNSFIDWVLDLRDKIKIPHKLSEcAKITDKDIEKL 364
Cdd:cd08182 305 LGASDPAEAAERLRALLESLGLPTRLSE-YGVTAEDLEAL 343
|
|
| PRK13805 |
PRK13805 |
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional |
30-391 |
5.49e-62 |
|
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional
Pssm-ID: 237515 [Multi-domain] Cd Length: 862 Bit Score: 213.89 E-value: 5.49e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 30 GIKKPLFVTDSDLVKTEMVASAIQ--SNNKNFIPTKVYSEVKGNPVSRYVTKGVEVFKSGNHDGVIAFGGGSSLDVGKSI 107
Cdd:PRK13805 479 GKKRAFIVTDRFMVELGYVDKVTDvlKKRENGVEYEVFSEVEPDPTLSTVRKGAELMRSFKPDTIIALGGGSPMDAAKIM 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 108 ALLESNnrPLWDFSGegsfWAEN---------DYNESMAKNKMsnpdeikpiIAIPTTAGTGSEISRAAAIINEKTNEKk 178
Cdd:PRK13805 559 WLFYEH--PETDFED----LAQKfmdirkriyKFPKLGKKAKL---------VAIPTTSGTGSEVTPFAVITDDKTGVK- 622
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 179 ivfHP----KMLPTLTILDPQLTLGLPPFLTAATGMDALAHNLEAY---CASGYhpmADGIALEGMWLIKKWLIIAVKEG 251
Cdd:PRK13805 623 ---YPladyELTPDVAIVDPNLVMTMPKSLTADTGIDALTHALEAYvsvMASDY---TDGLALQAIKLVFEYLPRSYKNG 696
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 252 -DNLEARGNMLTASSMGATAFQKG-LGAIHSLSHPVNSVFNIHHGLSNAIFMPYVLTFNRS---------------AIEn 314
Cdd:PRK13805 697 aKDPEAREKMHNASTIAGMAFANAfLGICHSMAHKLGAEFHIPHGRANAILLPHVIRYNATdppkqaafpqyeyprADE- 775
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 315 KIAKLSEYLELKNPS----FNSFIDWVLDLRDKIKIPHKLSECAkITDKD----IEKLSPMALNDPCTPENPKKTTLNDM 386
Cdd:PRK13805 776 RYAEIARHLGLPGSTteekVESLIKAIEELKAELGIPMSIKEAG-VDEADflakLDELAELAFDDQCTGANPRYPLISEL 854
|
....*
gi 167041165 387 KLMYR 391
Cdd:PRK13805 855 KEILL 859
|
|
| BDH |
cd08187 |
Butanol dehydrogenase catalyzes the conversion of butyraldehyde to butanol with the cofactor ... |
5-391 |
2.35e-60 |
|
Butanol dehydrogenase catalyzes the conversion of butyraldehyde to butanol with the cofactor NAD(P)H being oxidized in the process; The butanol dehydrogenase (BDH) is involved in the final step of the butanol formation pathway in anaerobic micro-organism. Butanol dehydrogenase catalyzes the conversion of butyraldehyde to butanol with the cofactor NAD(P)H being oxidized in the process. Activity in the reverse direction is 50-fold lower than that in the forward direction. The NADH-BDH has higher activity with longer chained aldehydes and is inhibited by metabolites containing an adenine moiety. This protein family belongs to the so-called iron-containing alcohol dehydrogenase superfamily. Since members of this superfamily use different divalent ions, preferentially iron or zinc, it has been suggested to be renamed to family III metal-dependent polyol dehydrogenases. This family also includes E. coli YqhD enzyme, an NADP-dependent dehydrogenase whose activity measurements with several alcohols demonstrate preference for alcohols longer than C3. The active site of YqhD contains a Zn metal, and a modified NADPH cofactor bearing OH groups on the saturated C5 and C6 atoms, possibly due to oxygen stress on the enzyme, which would functionally work under anaerobic conditions.
Pssm-ID: 341466 [Multi-domain] Cd Length: 382 Bit Score: 199.97 E-value: 2.35e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 5 NWAYPTTVWFGSGRIVDLPKACKTLGiKKPLFVTDSDLVKT----EMVASAIQSNNKNFIptkVYSEVKGNPVSRYVTKG 80
Cdd:cd08187 3 TFYNPTKIIFGKGAIEELGEEIKKYG-KKVLLVYGGGSIKKnglyDRVVASLKEAGIEVV---EFGGVEPNPRLETVREG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 81 VEVFKSGNHDGVIAFGGGSSLDVGKSIALLESNNRPLWDFsgegsfwaendynesMAKNKMsnPDEIKPIIAIPTTAGTG 160
Cdd:cd08187 79 IELAREENVDFILAVGGGSVIDAAKAIAAGAKYDGDVWDF---------------FTGKAP--PEKALPVGTVLTLAATG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 161 SEISRAAAIINEKTNEKKIVFHPKMLPTLTILDPQLTLGLPPFLTAATGMDALAHNLEAYCASGYH-PMADGIAlEGmwL 239
Cdd:cd08187 142 SEMNGGAVITNEETKEKLGFGSPLLRPKFSILDPELTYTLPKYQTAAGIVDIFSHVLEQYFTGTEDaPLQDRLA-EG--L 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 240 IK---KWLIIAVKEGDNLEARGNMLTASSM---GATAFQKGLG-AIHSLSHPVNSVFNIHHGLSNAIFMPYVLTFNRSAI 312
Cdd:cd08187 219 LRtviENGPKALKDPDDYEARANLMWAATLalnGLLGAGRGGDwATHAIEHELSALYDITHGAGLAIVFPAWMRYVLKKK 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 313 ENKIAKLSEYLelknpsFNsfIDWVLD-----------LRD---KIKIPHKLSECaKITDKDIEKLSPMALNDPCTPENP 378
Cdd:cd08187 299 PERFAQFARRV------FG--IDPGGDdeetalegieaLEEffkSIGLPTTLSEL-GIDEEDIEEMAEKAVRGGGLGGGF 369
|
410
....*....|...
gi 167041165 379 KKTTLNDMKLMYR 391
Cdd:cd08187 370 KPLTREDIEEILK 382
|
|
| PPD-like |
cd08181 |
1,3-propanediol dehydrogenase-like (PPD); This family contains proteins similar to 1, ... |
9-391 |
8.47e-60 |
|
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: 197.81 E-value: 8.47e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 9 PTTVWFGSGRIVDLPKACKTLGiKKPLFVTDSDLVKT----EMVASAIQSNNKNFIptkVYSEVKGNPVSRYVTKGVEVF 84
Cdd:cd08181 4 PTKVYFGKNCVEKHADELAALG-KKALIVTGKHSAKKngslDDVTEALEENGIEYF---IFDEVEENPSIETVEKGAELA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 85 KSGNHDGVIAFGGGSSLDVGKSIALLESNNRPLWDFsgegsfwaendynesMAKNKMSNPdeiKPIIAIPTTAGTGSEIS 164
Cdd:cd08181 80 RKEGADFVIGIGGGSPLDAAKAIALLAANKDGDEDL---------------FQNGKYNPP---LPIVAIPTTAGTGSEVT 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 165 RAAAIINEKTNEKKIVFHPKMLPTLTILDPQLTLGLPPFLTAATGMDALAHNLEAYCASGYHPMADGIALEGMWLIKKWL 244
Cdd:cd08181 142 PYSILTDHEKGTKKSFGNPLIFPKLALLDPKYTLSLPEELTIDTAVDALSHAIEGYLSVKATPLSDALALEALRLIGECL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 245 IIAVKEGDNLEARGNMLTASSMGATAF-QKGLGAIHSLSHPVNSVFNIHHGLSNAIFMPYVLTFNRSAIENKIAKLSEYL 323
Cdd:cd08181 222 PNLLGDELDEEDREKLMYASTLAGMVIaQTGTTLPHGLGYPLTYFKGIPHGRANGILLPAYLKLCEKQEPEKVDKILKLL 301
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 167041165 324 ELKnpSFNSFIDWVLDLrdkikiphkLSECAKITDKDIEKLSPMALNDPCTPENPKKTTLNDMKLMYR 391
Cdd:cd08181 302 GFG--SIEEFQKFLNRL---------LGKKEELSEEELEKYADEAMKAKNKKNTPGNVTKEDILRIYR 358
|
|
| PRK15454 |
PRK15454 |
ethanolamine utilization ethanol dehydrogenase EutG; |
9-390 |
8.42e-58 |
|
ethanolamine utilization ethanol dehydrogenase EutG;
Pssm-ID: 185351 [Multi-domain] Cd Length: 395 Bit Score: 193.71 E-value: 8.42e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 9 PTTVWFGSGRIVDLPKACKTLGIKKPLFVTDSDLVKTEMVASAIQSNNKNFIPTKVYSEVKGNPVSRYVTKGVEVFKSGN 88
Cdd:PRK15454 27 PPVTLCGPGAVSSCGQQAQTRGLKHLFVMADSFLHQAGMTAGLTRSLAVKGIAMTLWPCPVGEPCITDVCAAVAQLRESG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 89 HDGVIAFGGGSSLDVGKSIALLESNnrplwdfsgEGSFWAEndynesMAKNKMSNPDeiKPIIAIPTTAGTGSEISRAAA 168
Cdd:PRK15454 107 CDGVIAFGGGSVLDAAKAVALLVTN---------PDSTLAE------MSETSVLQPR--LPLIAIPTTAGTGSETTNVTV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 169 IINEKTNEKKIVFHPKMLPTLTILDPQLTLGLPPFLTAATGMDALAHNLEAYCASGYHPMADGIALEGMWLIKKWLIIAV 248
Cdd:PRK15454 170 IIDAVSGRKQVLAHASLMPDVAILDAALTEGVPSHVTAMTGIDALTHAIEAYSALNATPFTDSLAIGAIAMIGKSLPKAV 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 249 KEGDNLEARGNMLTASSMGATAFQK-GLGAIHSLSHPVNSVFNIHHGLSNAIFMPYVLTFNRSAIENKIAKLSEYLELKN 327
Cdd:PRK15454 250 GYGHDLAARESMLLASCMAGMAFSSaGLGLCHAMAHQPGAALHIPHGLANAMLLPTVMEFNRMVCRERFSQIGRALRTKK 329
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 167041165 328 PSFNSFIDWVLDLRDKIKIPHKLSEcAKITDKDIEKLSPMALNDPCTPENPKKTTLNDMKLMY 390
Cdd:PRK15454 330 SDDRDAINAVSELIAEVGIGKRLGD-VGATSAHYGAWAQAALEDICLRSNPRTASLEQIVGLY 391
|
|
| MAR-like |
cd08192 |
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic ... |
9-378 |
3.91e-50 |
|
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: 173.20 E-value: 3.91e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 9 PTTVWFGSGRIVDLPKACKTLGIKKPLFVTDSDL-VKTEMVASAIQSNNKNFIptKVYSEVKGN-PVSRyVTKGVEVFKS 86
Cdd:cd08192 1 LERVSYGPGAVEALLHELATLGASRVFIVTSKSLaTKTDVIKRLEEALGDRHV--GVFSGVRQHtPRED-VLEAARAVRE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 87 GNHDGVIAFGGGSSLDVGKSIALLESNNRplWDFSGEGSFWAENDYNESMAKNKMsnpdeikPIIAIPTTAgTGSEISRA 166
Cdd:cd08192 78 AGADLLVSLGGGSPIDAAKAVALALAEDV--TDVDQLDALEDGKRIDPNVTGPTL-------PHIAIPTTL-SGAEFTAG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 167 AAIINEKTNEKKIVFHPKMLPTLTILDPQLTLGLPPFLTAATGMDALAHNLEAYCASGYHPMADGIALEGMWLIKKWLII 246
Cdd:cd08192 148 AGATDDDTGHKQGFAHPELGPDAVILDPELTLHTPERLWLSTGIRAVDHAVETLCSPQATPFVDALALKALRLLFEGLPR 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 247 AVKEGDNLEARGNMLTAS--SMGATAFQKGLGAIHSLSHPVNSVFNIHHGLSNAIFMPYVLTFNRSAIENKIAKLSEYLE 324
Cdd:cd08192 228 SKADPEDLEARLKCQLAAwlSLFGLGSGVPMGASHAIGHQLGPLYGVPHGITSCIMLPAVLRFNAPVNAERQRLIARALG 307
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 167041165 325 LKNPSFNSFIDWVLDLRDKI----KIPHKLSEcAKITDKDIEKLSPMALNDPCTPENP 378
Cdd:cd08192 308 LVTGGLGREAADAADAIDALirelGLPRTLRD-VGVGRDQLEKIAENALTDVWCRTNP 364
|
|
| Fe-ADH-like |
cd14864 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
9-385 |
3.01e-48 |
|
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: 168.25 E-value: 3.01e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 9 PTTVWFGSGRIVDLPKACKTLGiKKPLFVTDSDLVKTEMVASAIQSNNKNFIPTKVYSEVKGNPVSRYVTKGVEVFKSGN 88
Cdd:cd14864 4 PPNIVFGADSLERIGEEVKEYG-SRFLLITDPVLKESGLADKIVSSLEKAGISVIVFDEIPASATSDTIDEAAELARKAG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 89 HDGVIAFGGGSSLDVGKSIALLESNNRPLWDFsgegsfwaendynesMAKNKMSNPdeIKPIIAIPTTAGTGSEISRAAA 168
Cdd:cd14864 83 ADGIIAVGGGKVLDTAKAVAILANNDGGAYDF---------------LEGAKPKKK--PLPLIAVPTTPRSGFEFSDRFP 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 169 IINEKTNEKKIVFHPKMLPTLTILDPQLTLGLPPFLTAATGMDALAHNLEAYCASGYHPMADGIALEGMWLIKKWLIIAV 248
Cdd:cd14864 146 VVDSRSREVKLLKAQPGLPKAVIVDPNLMASLTGNQTAAMALAALALAVEAYLSKKSNFFSDALALKAIELVSENLDGAL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 249 KEGDNLEARGNMLTASSMGATAF-QKGLGAIHSLSHPVNSVFNIHHGLSNAIFMPYVLTFNRSAIENKIAKLSEYLELKN 327
Cdd:cd14864 226 ADPKNTPAEELLAQAGCLAGLAAsSSSPGLATALALAVNSRYKVSKSLVASILLPHVIEYAATSAPDKYAKIARALGEDV 305
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 167041165 328 PSF------NSFIDWVLDLRDKIKIPHKLSEcaKITDKDIEKLSPMALNDPCTPENPKKTTLND 385
Cdd:cd14864 306 EGAspeeaaIAAVEGVRRLIAQLNLPTRLKD--LDLASSLEQLAAIAEDAPKLNGLPRSMSSDD 367
|
|
| Fe-ADH-like |
cd08186 |
Iron-containing alcohol dehydrogenase; This family contains iron-containing alcohol ... |
10-372 |
1.63e-47 |
|
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: 166.29 E-value: 1.63e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 10 TTVWFGSGRIVDLPKACKTLGIKKPLFVTDSDLVKT----EMVASAIQSNNKNFIptkVYSEVKGNPVSRYVTKGVEVFK 85
Cdd:cd08186 2 TTLYFGVGAIAKIKDILKDLGIDKVIIVTGRSSYKKsgawDDVEKALEENGIEYV---VYDKVTPNPTVDQADEAAKLAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 86 SGNHDGVIAFGGGSSLDVGKSIA-LLESNNRPLWDFSGegsfwaendynesmaknKMSNPDEIKPIIAIPTTAGTGSEIS 164
Cdd:cd08186 79 DFGADAVIAIGGGSPIDTAKSVAvLLAYGGKTARDLYG-----------------FRFAPERALPLVAINLTHGTGSEVD 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 165 RAAAIINEKTNEKKIVFHPKMLPTLTILDPQLTLGLPPFLTAATGMDALAHNLEAYCASGYHPMADGIALEGMWLIKKWL 244
Cdd:cd08186 142 RFAVATIPEKGYKPGIAYDCIYPLYAIDDPRLTLTLPKEQTLYTSIDAFNHVYEAATTKVSSPYVITLAKEAIRLIAEYL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 245 IIAVKEGDNLEARGNMLTASSMGATAFQKGLGAI-HSLSHPVNSVF-NIHHGLSNAIFMPYVLTFNRSAIENKIAKLSEY 322
Cdd:cd08186 222 PRALANPKDLEARYWLLYASMIAGIAIDNGLLHLtHALEHPLSGLKpELPHGLGLALLGPAVVKYIYKAVPETLADILRP 301
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 167041165 323 L--ELK-NPS-----FNSFIDWVldlrDKIKIPHKLSECAkITDKDIEKLSPMALNDP 372
Cdd:cd08186 302 IvpGLKgTPDeaekaARGVEEFL----FSVGFTEKLSDYG-FTEDDVDRLVELAFTTP 354
|
|
| MAR |
cd08177 |
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic ... |
9-378 |
2.12e-42 |
|
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: 151.50 E-value: 2.12e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 9 PTTVWFGSGRIVDLPKACKTLGIKKPLFV-TDSDLVKTEMVASAIQSNNKNFIPtKVYSEVkgnPVSRyVTKGVEVFKSG 87
Cdd:cd08177 1 PQRVVFGAGTLAELAEELERLGARRALVLsTPRQRALAERVAALLGDRVAGVFD-GAVMHV---PVEV-AERALAAAREA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 88 NHDGVIAFGGGSSLDVGKSIALlesnnrplwdfsgegsfwaENDynesmaknkmsnpdeiKPIIAIPTT-AGtgSEisrA 166
Cdd:cd08177 76 GADGLVAIGGGSAIGLAKAIAL-------------------RTG----------------LPIVAVPTTyAG--SE---M 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 167 AAIINEKTNE-KKIVFHPKMLPTLTILDPQLTLGLPPFLTAATGMDALAHNLEAYCASGYHPMADGIALEGMWLIKKWLI 245
Cdd:cd08177 116 TPIWGETEDGvKTTGRDPRVLPRTVIYDPDLTLGLPAALSVASGLNALAHAVEALYAPDANPITSLLAEEGIRALARALP 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 246 IAVKEGDNLEARGNMLTASSMGATAFQKGLGAI-HSLSHPVNSVFNIHHGLSNAIFMPYVLTFNRSAIENKIAKLSEYLE 324
Cdd:cd08177 196 RLVADPSDLEARSDALYGAWLAGVVLGSVGMGLhHKLCHVLGGTFDLPHAETHAVVLPHVLAYNAPAAPDAMARLARALG 275
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 167041165 325 LKNPsfnsfIDWVLDLRDKIKIPHKLSEcAKITDKDIEKLSPMALNDPctPENP 378
Cdd:cd08177 276 GGDA-----AGGLYDLARRLGAPTSLRD-LGMPEDDIDRAADLALANP--YPNP 321
|
|
| YqdH |
COG1979 |
Alcohol dehydrogenase YqhD, Fe-dependent ADH family [Energy production and conversion]; |
9-364 |
2.31e-42 |
|
Alcohol dehydrogenase YqhD, Fe-dependent ADH family [Energy production and conversion];
Pssm-ID: 441582 [Multi-domain] Cd Length: 387 Bit Score: 152.53 E-value: 2.31e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 9 PTTVWFGSGRIVDLPKACKTLGiKKPLFVTDSDLVKT----EMVASAIQSNNKNFIptkVYSEVKGNPVSRYVTKGVEVF 84
Cdd:COG1979 9 PTKIIFGKGQIAKLGEEIPKYG-KKVLLVYGGGSIKKnglyDQVKAALKEAGIEVV---EFGGVEPNPRLETVRKGVELC 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 85 KSGNHDGVIAFGGGSSLDVGKSIALLESNNRPLWDFsgegsfwaendynesMAKNKMsnPDEIKPIIAIPTTAGTGSEIS 164
Cdd:COG1979 85 KEEGIDFILAVGGGSVIDGAKAIAAGAKYDGDPWDI---------------LTGKAP--VEKALPLGTVLTLPATGSEMN 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 165 RAAAIINEKTNEKKIVFHPKMLPTLTILDPQLTLGLPPFLTAATGMDALAHNLEAY-CASGYHPMADGIAlEG-MWLIKK 242
Cdd:COG1979 148 SGSVITNEETKEKLGFGSPLVFPKFSILDPELTYTLPKRQTANGIVDIFSHVMEQYfTYPVDAPLQDRFA-EGlLRTLIE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 243 WLIIAVKEGDNLEARGNMLTASSM---GATafqkGLG-----AIHSLSHPVNSVFNIHHGLSNAIFMPYVLTFNRsaiEN 314
Cdd:COG1979 227 EGPKALKDPEDYDARANLMWAATLalnGLI----GAGvpqdwATHMIEHELSALYDIDHGAGLAIVLPAWMRYVL---EE 299
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 167041165 315 KIAKLSEY------LELKNPsfnsfiDWVLD-----LRD---KIKIPHKLSECaKITDKDIEKL 364
Cdd:COG1979 300 KPEKFAQYaervwgITEGDD------EERALegieaTEEffeSLGLPTRLSEY-GIDEEDIEEM 356
|
|
| Fe-ADH-like |
cd14866 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
8-379 |
3.72e-40 |
|
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: 146.61 E-value: 3.72e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 8 YPTTVWFGSGRIVDLPKACKTLGIKKPLFVTDSDLVKT----EMVASAIQSNnknfiPTKVYSEVKGN-PVSRyVTKGVE 82
Cdd:cd14866 4 PPLRLFSGRGALARLGRELDRLGARRALVVCGSSVGANpdlmDPVRAALGDR-----LAGVFDGVRPHsPLET-VEAAAE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 83 VFKSGNHDGVIAFGGGSSLDVGKSIALLESNNRPLWD----FSGEGSfwaendynesMAKNKMSNPDeiKPIIAIPTTAg 158
Cdd:cd14866 78 ALREADADAVVAVGGGSAIVTARAASILLAEDRDVRElctrRAEDGL----------MVSPRLDAPK--LPIFVVPTTP- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 159 TGSEISRAAAIINEKTNEKKIVFHPKMLPTLTILDPQLTLGLPPFLTAATGMDALAHNLEAYCASGYHPMADGIALEGMW 238
Cdd:cd14866 145 TTADVKAGSAVTDPPAGQRLALFDPKTRPAAVFYDPELLATAPASLVAGAAMNGFDMAVEGLYSRHADPLADATLMHALR 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 239 LIKKWLiIAVKEGDNLEARGNMLTASSM-GATAFQKGLGAIHSLSHPVNSVFNIHHGLSNAIFMPYVLTFNRSAIENKIA 317
Cdd:cd14866 225 LLADGL-PRLADDDDPAARADLVLAAVLaGYGTDHTGGGVIHALGHAIGARYGVQNGVVHAILLPHVLRFNAPATDGRLD 303
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 167041165 318 KLSEYLELKNPSFN----SFIDWVLDLRDKIKIPHKLSEcAKITDKDIEKLSPMALNDPCTPENPK 379
Cdd:cd14866 304 RLAEALGVADAGDEasaaAVVDAVEALLDALGVPTRLRD-LGVSREDLPAIAEAAMDDWFMDNNPR 368
|
|
| 4HBD_NAD |
cd14860 |
4-hydroxybutyrate dehydrogenase, also called gamma-hydroxybutyrate dehydrogenase, catalyzes ... |
69-323 |
1.37e-29 |
|
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: 117.70 E-value: 1.37e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 69 KGNPVSRYVTKGVEVFKSGNHDGVIAFGGGSSLDVGKSIALleSNNRPLWD-FSGEgsfwaendynESMAKNKmsnpdei 147
Cdd:cd14860 59 TGEPSDEMVEAIYKDIKKYGYKRVIAIGGGTVIDIAKLLAL--KGISPVLDlFDGK----------IPLIKEK------- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 148 kPIIAIPTTAGTGSEISRAAAIINEKTNEKKIVFHPKMLPTLTILDPQLTLGLPPFLTAATGMDALAHNLEAYCASGYHP 227
Cdd:cd14860 120 -ELIIVPTTCGTGSEVTNISIVELTSLGTKKGLAVDELYADKAVLIPELLKGLPYKVFATSSIDALIHAIESYLSPKATP 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 228 MADGIALEGMWLIKKWLIIAVKEGdnLEAR----GNMLTASSMGATAFQK-GLGAIHSLSHPVNSVFNIHHGLSN-AIFM 301
Cdd:cd14860 199 YTEMFSYKAIEMILEGYQEIAEKG--EEARfpllGDFLIASNYAGIAFGNaGCAAVHALSYPLGGKYHVPHGEANyAVFT 276
|
250 260
....*....|....*....|..
gi 167041165 302 PYVLTFNRSAIENKIAKLSEYL 323
Cdd:cd14860 277 GVLKNYQEKNPDGEIKKLNEFL 298
|
|
| DHQ_Fe-ADH |
cd07766 |
Dehydroquinate synthase-like (DHQ-like) and iron-containing alcohol dehydrogenases (Fe-ADH); ... |
9-364 |
3.32e-29 |
|
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: 114.38 E-value: 3.32e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 9 PTTVWFGSGRIVDLpKACKTLGIKKPLFVTDSDLVKteMVASAIQSNNKNFIPTKVYSEVKGNPVSRYVTKGVEVFKSGN 88
Cdd:cd07766 1 PTRIVFGEGAIAKL-GEIKRRGFDRALVVSDEGVVK--GVGEKVADSLKKGLAVAIFDFVGENPTFEEVKNAVERARAAE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 89 HDGVIAFGGGSSLDVGKSIALlesnnrplwdfsgegsfwaendynesmaknkMSNPDeiKPIIAIPTTAGTGSEISrAAA 168
Cdd:cd07766 78 ADAVIAVGGGSTLDTAKAVAA-------------------------------LLNRG--IPFIIVPTTASTDSEVS-PKS 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 169 IINEKTNEKKIVFhPKMLPTLTILDPQLTLGLPPFLTAATGMDALAHNLEaycasgyhpmadgialegmwlikkwliiav 248
Cdd:cd07766 124 VITDKGGKNKQVG-PHYNPDVVFVDTDITKGLPPRQVASGGVDALAHAVE------------------------------ 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 249 kegdnLEARGNMLTASSMGATAfQKGLGAIHSLSHPVNSVFNIHHGLSNAIFMPYVLTFNRSAIENKIAKLSEYLElknp 328
Cdd:cd07766 173 -----LEKVVEAATLAGMGLFE-SPGLGLAHAIGHALTAFEGIPHGEAVAVGLPYVLKVANDMNPEPEAAIEAVFK---- 242
|
330 340 350
....*....|....*....|....*....|....*.
gi 167041165 329 sFNSFIDWVLDLRDKikiphklsecaKITDKDIEKL 364
Cdd:cd07766 243 -FLEDLGLPTHLADL-----------GVSKEDIPKL 266
|
|
| Fe-ADH_KdnB-like |
cd08184 |
Iron-containing alcohol dehydrogenase similar to Shewanella oneidensis KdnB required for Kdo8N ... |
14-369 |
4.32e-26 |
|
Iron-containing alcohol dehydrogenase similar to Shewanella oneidensis KdnB required for Kdo8N biosynthesis; This family contains iron-containing alcohol dehydrogenase-like proteins, many of which have not been characterized. Their specific function is unknown. The protein structure represents a dehydroquinate synthase-like fold and belongs to the iron-containing alcohol dehydrogenase-like superfamily. It is distinct from other alcohol dehydrogenases which contain different protein domains. Alcohol dehydrogenase catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron or zinc ions. This family also includes Shewanella oneidensis KdnB which is required for biosynthesis of 8-Amino-3,8-dideoxy-D-manno-octulosonic acid (Kdo8N), a unique amino sugar that has thus far only been observed on the lipopolysaccharides of marine bacteria belonging to the genus Shewanella, and thought to be important for the integrity of the bacterial cell outer membrane. KdnB requires NAD(P) and zinc ion for activity.
Pssm-ID: 341463 [Multi-domain] Cd Length: 348 Bit Score: 107.35 E-value: 4.32e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 14 FGSGRIVDLPKACKTLGI---KKPLFVTDsDLVKTEMVASAIQSNNKNFIptkVYSEVKGNPVSRYVTKGVEVFKSGNH- 89
Cdd:cd08184 6 FGRGSFDQLGELLAERRKsnnDYVVFFID-DVFKGKPLLDRLPLQNGDLL---IFVDTTDEPKTDQIDALRAQIRAENDk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 90 --DGVIAFGGGSSLDVGKSIALLESNNRPLWDFSGegsfWaendyneSMAKNKMSnpdeikPIIAIPTTAGTGSEISRAA 167
Cdd:cd08184 82 lpAAVVGIGGGSTMDIAKAVSNMLTNPGSAADYQG----W-------DLVKNPGI------YKIGVPTLSGTGAEASRTA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 168 AIINEktnEKKI-VFHPKMLPTLTILDPQLTLGLPPFLTAATGMDALAHNLEAYCASGYHPMADGIALEGMWLIKKwlII 246
Cdd:cd08184 145 VLTGP---EKKLgINSDYTVFDQVILDPELIATVPRDQYFYTGMDCYIHCVESLNGTYRNAFGDAYAEKALELCRD--VF 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 247 AVKEGDNLEARGNMLTASSMGATAFQKG-LGAIHSLSHPVNSVFNIHHGLSNAIFMpyvltfnrSAIE----NKIAKLSE 321
Cdd:cd08184 220 LSDDMMSPENREKLMVASYLGGSSIANSqVGVCHALSYGLSVVLGTHHGVANCIVF--------NVLEefypEGVKEFRE 291
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 167041165 322 YLELKNpsfnsfidwvldlrdkIKIPHKLseCAKITDKDIEKLSPMAL 369
Cdd:cd08184 292 MLEKQN----------------ITLPKGI--CKDLTDEQYEKMVAVTL 321
|
|
| PRK15138 |
PRK15138 |
alcohol dehydrogenase; |
9-324 |
7.10e-18 |
|
alcohol dehydrogenase;
Pssm-ID: 185092 [Multi-domain] Cd Length: 387 Bit Score: 84.46 E-value: 7.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 9 PTTVWFGSGRIVDL----PKACKTLgikkplfvtdsdlvktemVASAIQSNNKNFIPTKVYSEVKG-----------NPV 73
Cdd:PRK15138 9 PTRILFGKGAIAGLreqiPADARVL------------------ITYGGGSVKKTGVLDQVLDALKGmdvlefggiepNPT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 74 SRYVTKGVEVFKSGNHDGVIAFGGGSSLDVGKSIAllesnnrplwdfsgegsfwAENDYNES-----MAKNKMSNPDEIK 148
Cdd:PRK15138 71 YETLMKAVKLVREEKITFLLAVGGGSVLDGTKFIA-------------------AAANYPENidpwhILETGGKEIKSAI 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 149 PIIAIPTTAGTGSEISRAAAIINEKTNEKKIVFHPKMLPTLTILDPQLTLGLPPFLTAATGMDALAHNLEAYCAsgyHP- 227
Cdd:PRK15138 132 PMGSVLTLPATGSESNAGAVISRKTTGDKQAFHSPHVQPVFAVLDPVYTYTLPPRQVANGVVDAFVHTVEQYVT---YPv 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 228 ---MADGIAlEGMWLIkkwLI----IAVKEGDNLEARGNMLTASSM------GATAFQKglGAIHSLSHPVNSVFNIHHG 294
Cdd:PRK15138 209 dakIQDRFA-EGILLT---LIeegpKALKEPENYDVRANVMWAATQalngliGAGVPQD--WATHMLGHELTAMHGLDHA 282
|
330 340 350
....*....|....*....|....*....|
gi 167041165 295 LSNAIFMPYVLTFNRsaiENKIAKLSEYLE 324
Cdd:PRK15138 283 QTLAIVLPALWNEKR---DTKRAKLLQYAE 309
|
|
| GldA |
COG0371 |
Glycerol dehydrogenase or related enzyme, iron-containing ADH family [Energy production and ... |
15-235 |
1.60e-09 |
|
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: 59.02 E-value: 1.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 15 GSGRIVDLPKACKTLGiKKPLFVTDS---DLVKtEMVASAIQSNNKNFiptkVYSEVKGNPVSRYVTKGVEVFKSGNHDG 91
Cdd:COG0371 12 GEGALDELGEYLADLG-KRALIITGPtalKAAG-DRLEESLEDAGIEV----EVEVFGGECSEEEIERLAEEAKEQGADV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 92 VIAFGGGSSLDVGKSIAllesnnrplwdfsgegsfwaenDYNEsmaknkmsnpdeiKPIIAIPTTAGTGSEISRAAAIIN 171
Cdd:COG0371 86 IIGVGGGKALDTAKAVA----------------------YRLG-------------LPVVSVPTIASTDAPASPLSVIYT 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 167041165 172 EKTNEKKIVFHPKMlPTLTILDPQLTLGLPPFLTAAtGM-DALAHNLEAY-CASGYHPMADGIALE 235
Cdd:COG0371 131 EDGAFDGYSFLAKN-PDLVLVDTDIIAKAPVRLLAA-GIgDALAKWYEARdWSLAHRDLAGEYYTE 194
|
|
| GlyDH |
cd08170 |
Glycerol dehydrogenases (GlyDH) catalyzes oxidation of glycerol to dihydroxyacetone in ... |
15-219 |
1.92e-09 |
|
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: 58.58 E-value: 1.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 15 GSGRIVDLPKACKTLGiKKPLFVTDS---DLVKTEMVASAIQSNnknfipTKVYSEVKGNPVSRY-VTKGVEVFKSGNHD 90
Cdd:cd08170 7 GPGALDRLGEYLAPLG-KKALVIADPfvlDLVGERLEESLEKAG------LEVVFEVFGGECSREeIERLAAIARANGAD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 91 GVIAFGGGSSLDVGKSIAllesnnrplwDFSGegsfwaendynesmaknkmsnpdeiKPIIAIPTTAGTGSEISRAAAII 170
Cdd:cd08170 80 VVIGIGGGKTIDTAKAVA----------DYLG-------------------------LPVVIVPTIASTDAPCSALSVIY 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 167041165 171 NEKTNEKKIVFHPKMlPTLTILDPQLTLGLPP-FLTAatGM-DALAHNLEA 219
Cdd:cd08170 125 TEDGEFDEYLFLPRN-PDLVLVDTEIIAKAPVrFLVA--GMgDALATYFEA 172
|
|
| GlyDH-like |
cd08172 |
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins ... |
15-214 |
3.94e-06 |
|
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins that have yet to be characterized, but show sequence homology with glycerol dehydrogenase. Glycerol dehydrogenases (GlyDH) is a key enzyme in the glycerol dissimilation pathway. In anaerobic conditions, many microorganisms utilize glycerol as a source of carbon through coupled oxidative and reductive pathways. One of the pathways involves the oxidation of glycerol to dihydroxyacetone with the reduction of NAD+ to NADH catalyzed by glycerol dehydrogenases. Dihydroxyacetone is then phosphorylated by dihydroxyacetone kinase and enters the glycolytic pathway for further degradation. The activity of GlyDH is zinc-dependent; the zinc ion plays a role in stabilizing an alkoxide intermediate at the active site.
Pssm-ID: 341451 [Multi-domain] Cd Length: 346 Bit Score: 48.28 E-value: 3.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 15 GSGRIVDLPKACKTLGIKKPLFVTDsdlvktEMVASAIQSnnknFIPTKVYSEVkgnPVSRY--------VTKGVEVFKS 86
Cdd:cd08172 7 EEGALKELPELLSEFGIKRPLIIHG------EKSWQAAKP----YLPKLFEIEY---PVLRYdgecsyeeIDRLAEEAKE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 87 GNHDGVIAFGGGSSLDVGKSIAllesnnrplwdfsgegsfwaendynesmakNKMSnpdeiKPIIAIPTTAGTGSEISRA 166
Cdd:cd08172 74 HQADVIIGIGGGKVLDTAKAVA------------------------------DKLN-----IPLILIPTLASNCAAWTPL 118
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 167041165 167 AAIINEKTNEKKIVFHPKMlPTLTILDPQLTLGLP-PFLTAATGmDALA 214
Cdd:cd08172 119 SVIYDEDGEFIGYDYFPRS-AYLVLVDPRLLLDSPkDYFVAGIG-DTLA 165
|
|
| Gro1PDH |
cd08173 |
Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) catalyzes the reversible conversion between ... |
9-108 |
9.36e-06 |
|
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: 47.16 E-value: 9.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 9 PTTVWFGSGRIVDLPKACKTLGI-KKPLFVTDSDLVKTemVASAIQSNNKNFIPTKVYSEVKGNPVSRYVTKGVEVFKSG 87
Cdd:cd08173 2 PRNVVVGHGAINKIGEVLKKLLLgKRALIITGPNTYKI--AGKRVEDLLESSGVEVVIVDIATIEEAAEVEKVKKLIKES 79
|
90 100
....*....|....*....|.
gi 167041165 88 NHDGVIAFGGGSSLDVGKSIA 108
Cdd:cd08173 80 KADFIIGVGGGKVIDVAKYAA 100
|
|
| G1PDH-like |
cd08174 |
Glycerol-1-phosphate dehydrogenase-like; These glycerol-1-phosphate dehydrogenase-like ... |
29-117 |
9.05e-03 |
|
Glycerol-1-phosphate dehydrogenase-like; These glycerol-1-phosphate dehydrogenase-like proteins have not been characterized. The protein sequences have high similarity with that of glycerol-1-phosphate dehydrogenase (G1PDH) which plays a role in the synthesis of phosphoglycerolipids in Gram-positive bacterial species. It catalyzes the reversibly reduction of dihydroxyacetone phosphate (DHAP) to glycerol-1-phosphate (G1P) in a NADH-dependent manner. Its activity requires Ni++ ion.
Pssm-ID: 341453 [Multi-domain] Cd Length: 332 Bit Score: 37.89 E-value: 9.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167041165 29 LGIKKPLFVTDSDLvkTEMVASAIQSNNKNFiptKVYSEVKGNPVSRYVTKGVEVFKSGNHDGVIAFGGGSSLDVGKSIA 108
Cdd:cd08174 23 QGFGKVAIVTGEGI--DELLGEDILESLEEA---GEIVTVEENTDNSAEELAEKAFSLPKVDAIVGIGGGKVLDVAKYAA 97
|
....*....
gi 167041165 109 LLesNNRPL 117
Cdd:cd08174 98 FL--SKLPF 104
|
|
| |
