|
Name |
Accession |
Description |
Interval |
E-value |
| PDDH |
cd08188 |
1,3-Propanediol (1,3-PD) dehydrogenase; This family includes 1,3-propanediol (1,3-PD) ... |
5-377 |
0e+00 |
|
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: 615.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 5 TGFYIPPISFFGEGALEETADYIKNKDYKKALIVTDPGIAAIGLSGRVQKMLEERDLNVAIYDKTQPNPNIANVTAGLKV 84
Cdd:cd08188 1 FRFYIPPVNLFGPGCLKEIGDELKKLGGKKALIVTDKGLVKLGLVKKVTDVLEEAGIEYVIFDGVQPNPTVTNVNEGLEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 85 LKEQNSEIVVSIGGGSAHDNAKAIALLATNGGEIGDYEGVNQSKKAALPLFAINTTAGTASEMTRFTIISNEEKKIKMAI 164
Cdd:cd08188 81 FKENGCDFIISVGGGSAHDCAKAIGILATNGGEIEDYEGVDKSKKPGLPLIAINTTAGTASEVTRFAVITDEERHVKMVI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 165 IDNNVTPAVAVNDPSTMFGLPPALTAATGLDALTHCIEAYVSTASNPITDACALKGIDLINESLVAAYKDGKDKKARTDM 244
Cdd:cd08188 161 VDWNVTPTIAVNDPELMLGMPPSLTAATGMDALTHAIEAYVSTGATPLTDALALEAIRLIAENLPKAVANGKDLEARENM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 245 CYAEYLAGMAFNNASLGYVHALAHQLGGFYHLPHGVCNAVLLPHVQEANMQCPkaKKRLGEIALHFG------ASQEDPE 318
Cdd:cd08188 241 AYAQFLAGMAFNNAGLGYVHAMAHQLGGFYNLPHGVCNAILLPHVMEFNLPAC--PERFADIARALGenteglSDEEAAE 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 205831682 319 ETIKALHVLNRTMNIPRNLKELGVKTEDFEILAEHAMHDACHLTNPVQFTKEQVVAIIK 377
Cdd:cd08188 319 AAIEAIRKLSRRVGIPSGLKELGVKEEDFPLLAENALKDACGPTNPRQATKEDVIAIYR 377
|
|
| EutG |
COG1454 |
Alcohol dehydrogenase, class IV [Energy production and conversion]; |
7-380 |
2.32e-179 |
|
Alcohol dehydrogenase, class IV [Energy production and conversion];
Pssm-ID: 441063 [Multi-domain] Cd Length: 381 Bit Score: 503.11 E-value: 2.32e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 7 FYIPPISFFGEGALEETADYIKNKDYKKALIVTDPGIAAIGLSGRVQKMLEERDLNVAIYDKTQPNPNIANVTAGLKVLK 86
Cdd:COG1454 5 FRLPTRIVFGAGALAELGEELKRLGAKRALIVTDPGLAKLGLLDRVLDALEAAGIEVVVFDDVEPNPTVETVEAGAAAAR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 87 EQNSEIVVSIGGGSAHDNAKAIALLATNGGEIGDYEGVNQSKKAALPLFAINTTAGTASEMTRFTIISNEEKKIKMAIID 166
Cdd:COG1454 85 EFGADVVIALGGGSAIDAAKAIALLATNPGDLEDYLGIKKVPGPPLPLIAIPTTAGTGSEVTPFAVITDPETGVKKGIAD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 167 NNVTPAVAVNDPSTMFGLPPALTAATGLDALTHCIEAYVSTASNPITDACALKGIDLINESLVAAYKDGKDKKARTDMCY 246
Cdd:COG1454 165 PELLPDVAILDPELTLTLPPSLTAATGMDALTHAIEAYVSKGANPLTDALALEAIRLIARNLPRAVADGDDLEAREKMAL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 247 AEYLAGMAFNNASLGYVHALAHQLGGFYHLPHGVCNAVLLPHVQEANMqcPKAKKRLGEIALHFGAS-----QEDPEETI 321
Cdd:COG1454 245 ASLLAGMAFANAGLGAVHALAHPLGGLFHVPHGLANAILLPHVLRFNA--PAAPERYAEIARALGLDvglsdEEAAEALI 322
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 205831682 322 KALHVLNRTMNIPRNLKELGVKTEDFEILAEHAMHDACHLTNPVQFTKEQVVAIIKKAY 380
Cdd:COG1454 323 EAIRELLRDLGIPTRLSELGVTEEDLPELAELALADRCLANNPRPLTEEDIEAILRAAY 381
|
|
| PRK09860 |
PRK09860 |
putative alcohol dehydrogenase; Provisional |
7-379 |
1.39e-162 |
|
putative alcohol dehydrogenase; Provisional
Pssm-ID: 182118 [Multi-domain] Cd Length: 383 Bit Score: 460.96 E-value: 1.39e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 7 FYIPPISFFGEGALEETADYIKNKDYKKALIVTDPGIAAIGLSGRVQKMLEERDLNVAIYDKTQPNPNIANVTAGLKVLK 86
Cdd:PRK09860 6 FFIPSVNVIGADSLTDAMNMMADYGFTRTLIVTDNMLTKLGMAGDVQKALEERNIFSVIYDGTQPNPTTENVAAGLKLLK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 87 EQNSEIVVSIGGGSAHDNAKAIALLATNGGEIGDYEGVNQSKKAALPLFAINTTAGTASEMTRFTIISNEEKKIKMAIID 166
Cdd:PRK09860 86 ENNCDSVISLGGGSPHDCAKGIALVAANGGDIRDYEGVDRSAKPQLPMIAINTTAGTASEMTRFCIITDEARHIKMAIVD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 167 NNVTPAVAVNDPSTMFGLPPALTAATGLDALTHCIEAYVSTASNPITDACALKGIDLINESLVAAYKDGKDKKARTDMCY 246
Cdd:PRK09860 166 KHVTPLLSVNDSSLMIGMPKSLTAATGMDALTHAIEAYVSIAATPITDACALKAVTMIAENLPLAVEDGSNAKAREAMAY 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 247 AEYLAGMAFNNASLGYVHALAHQLGGFYHLPHGVCNAVLLPHVQEANMQCPKAKKRLGEIALHFGASQ----EDPEETIK 322
Cdd:PRK09860 246 AQFLAGMAFNNASLGYVHAMAHQLGGFYNLPHGVCNAVLLPHVQVFNSKVAAARLRDCAAAMGVNVTGkndaEGAEACIN 325
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 205831682 323 ALHVLNRTMNIPRNLKELGVKTEDFEILAEHAMHDACHLTNPVQFTKEQVVAIIKKA 379
Cdd:PRK09860 326 AIRELAKKVDIPAGLRDLNVKEEDFAVLATNALKDACGFTNPIQATHEEIVAIYRAA 382
|
|
| Fe-ADH |
cd08551 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains large ... |
15-376 |
1.19e-153 |
|
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: 437.65 E-value: 1.19e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 15 FGEGALEETADYIKNKDYKKALIVTDPGIAAIGLSGRVQKMLEERDLNVAIYDKTQPNPNIANVTAGLKVLKEQNSEIVV 94
Cdd:cd08551 6 FGAGALARLGEELKALGGKKVLLVTDPGLVKAGLLDKVLESLKAAGIEVEVFDDVEPNPTVETVEAAAELAREEGADLVI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 95 SIGGGSAHDNAKAIALLATNGGEIGDYEGVNQSKKAALPLFAINTTAGTASEMTRFTIISNEEKKIKMAIIDNNVTPAVA 174
Cdd:cd08551 86 AVGGGSVLDTAKAIAVLATNGGSIRDYEGIGKVPKPGLPLIAIPTTAGTGSEVTPNAVITDPETGRKMGIVSPYLLPDVA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 175 VNDPSTMFGLPPALTAATGLDALTHCIEAYVSTASNPITDACALKGIDLINESLVAAYKDGKDKKARTDMCYAEYLAGMA 254
Cdd:cd08551 166 ILDPELTLSLPPSVTAATGMDALTHAIEAYTSKKANPISDALALEAIRLIGKNLRRAVADGSDLEAREAMLLASLLAGIA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 255 FNNASLGYVHALAHQLGGFYHLPHGVCNAVLLPHVQEANMqcPKAKKRLGEIALHFGAS------QEDPEETIKALHVLN 328
Cdd:cd08551 246 FGNAGLGAVHALAYPLGGRYHIPHGVANAILLPYVMEFNL--PACPEKYAEIAEALGEDveglsdEEAAEAAVEAVRELL 323
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 205831682 329 RTMNIPRNLKELGVKTEDFEILAEHAMHDACHLTN-PVQFTKEQVVAII 376
Cdd:cd08551 324 RDLGIPTSLSELGVTEEDIPELAEDAMKSGRLLSNnPRPLTEEDIREIY 372
|
|
| LPO |
cd08176 |
Lactadehyde:propanediol oxidoreductase (LPO) catalyzes the interconversion between ... |
7-377 |
6.61e-147 |
|
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: 420.80 E-value: 6.61e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 7 FYIPPISFFGEGALEETADYIKNKDYKKALIVTDPGIAAIGLSGRVQKMLEERDLNVAIYDKTQPNPNIANVTAGLKVLK 86
Cdd:cd08176 3 FVLNPTSYFGWGAIEEIGEEAKKRGFKKALIVTDKGLVKFGIVDKVTDVLKEAGIAYTVFDEVKPNPTIENVMAGVAAYK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 87 EQNSEIVVSIGGGSAHDNAKAIALLATNGGE-IGDYEGVNQSKKAALPLFAINTTAGTASEMTRFTIISNEEKKIKMAII 165
Cdd:cd08176 83 ESGADGIIAVGGGSSIDTAKAIGIIVANPGAdVRSLEGVAPTKNPAVPIIAVPTTAGTGSEVTINYVITDTEKKRKFVCV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 166 DNNVTPAVAVNDPSTMFGLPPALTAATGLDALTHCIEAYVSTASNPITDACALKGIDLINESLVAAYKDGKDKKARTDMC 245
Cdd:cd08176 163 DPHDIPTVAIVDPDLMSSMPKGLTAATGMDALTHAIEGYITKGAWELSDMLALKAIELIAKNLRKAVANPNNVEARENMA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 246 YAEYLAGMAFNNASLGYVHALAHQLGGFYHLPHGVCNAVLLPHVQEANMqcPKAKKRLGEIALHFGASQEDP------EE 319
Cdd:cd08176 243 LAQYIAGMAFSNVGLGIVHSMAHPLSAFYDTPHGVANAILLPYVMEFNA--PATGEKYRDIARAMGVDTTGMsdeeaaEA 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 205831682 320 TIKALHVLNRTMNIPRNLKELGVKTEDFEILAEHAMHDACHLTNPVQFTKEQVVAIIK 377
Cdd:cd08176 321 AVDAVKKLSKDVGIPQKLSELGVKEEDIEALAEDALNDVCTPGNPREATKEDIIALYK 378
|
|
| Fe-ADH |
pfam00465 |
Iron-containing alcohol dehydrogenase; |
10-372 |
1.89e-141 |
|
Iron-containing alcohol dehydrogenase;
Pssm-ID: 425696 [Multi-domain] Cd Length: 362 Bit Score: 406.22 E-value: 1.89e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 10 PPISFFGEGALEETADYIKNKDyKKALIVTDPGIAAIGLSGRVQKMLEERDLNVAIYDKTQPNPNIANVTAGLKVLKEQN 89
Cdd:pfam00465 1 PTRIVFGAGALAELGEELKRLG-ARALIVTDPGSLKSGLLDKVLASLEEAGIEVVVFDGVEPEPTLEEVDEAAALAREAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 90 SEIVVSIGGGSAHDNAKAIALLATNGGEIGDYEGVNQSKKAALPLFAINTTAGTASEMTRFTIISNEEKKIKMAIIDNNV 169
Cdd:pfam00465 80 ADVIIAVGGGSVIDTAKAIALLLTNPGDVWDYLGGKPLTKPALPLIAIPTTAGTGSEVTPLAVITDTETGEKLGIFSPKL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 170 TPAVAVNDPSTMFGLPPALTAATGLDALTHCIEAYVSTASNPITDACALKGIDLINESLVAAYKDGKDKKARTDMCYAEY 249
Cdd:pfam00465 160 LPDLAILDPELTLTLPPRLTAATGMDALAHAVEAYVSKGANPLTDALALEAIRLIAENLPRAVADGEDLEARENMLLAST 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 250 LAGMAFNNASLGYVHALAHQLGGFYHLPHGVCNAVLLPHVQEANMqcPKAKKRLGEIALHFGAS--QEDPEETIKALHVL 327
Cdd:pfam00465 240 LAGLAFSNAGLGAAHALAHALGGRYGIPHGLANAILLPYVLRFNA--PAAPEKLAQLARALGEDsdEEAAEEAIEALREL 317
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 205831682 328 NRTMNIPRNLKELGVKTEDFEILAEHAMHDACHLTNPVQFTKEQV 372
Cdd:pfam00465 318 LRELGLPTTLSELGVTEEDLDALAEAALRDRSLANNPRPLTAEDI 362
|
|
| Fe-ADH-like |
cd08189 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
10-378 |
3.31e-135 |
|
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: 391.06 E-value: 3.31e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 10 PPISFFGEGALEETADYIKNKDYKKALIVTDPGIAAIGLSGRVQKMLEERDLNVAIYDKTQPNPNIANVTAGLKVLKEQN 89
Cdd:cd08189 5 EPELFEGAGSLLQLPEALKKLGIKRVLIVTDKGLVKLGLLDPLLDALKKAGIEYVVFDGVVPDPTIDNVEEGLALYKENG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 90 SEIVVSIGGGSAHDNAKAIALLATNGGE-IGDYEGVNQSKKAALPLFAINTTAGTASEMTRFTIISNEEKKIKMAIIDNN 168
Cdd:cd08189 85 CDAIIAIGGGSVIDCAKVIAARAANPKKsVRKLKGLLKVRKKLPPLIAVPTTAGTGSEATIAAVITDPETHEKYAINDPK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 169 VTPAVAVNDPSTMFGLPPALTAATGLDALTHCIEAYVSTASNPITDACALKGIDLINESLVAAYKDGKDKKARTDMCYAE 248
Cdd:cd08189 165 LIPDAAVLDPELTLGLPPAITAATGMDALTHAVEAYISRSATKETDEYALEAVKLIFENLPKAYEDGSDLEARENMLLAS 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 249 YLAGMAFNNASLGYVHALAHQLGGFYHLPHGVCNAVLLPHVQEANmqCPKAKKRLGEIALHFGASQEDPEETIKALHV-- 326
Cdd:cd08189 245 YYAGLAFTRAYVGYVHAIAHQLGGLYGVPHGLANAVVLPHVLEFY--GPAAEKRLAELADAAGLGDSGESDSEKAEAFia 322
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 205831682 327 ----LNRTMNIPRNLKELgvKTEDFEILAEHAMHDAcHLTNPV--QFTKEQVVAIIKK 378
Cdd:cd08189 323 aireLNRRMGIPTTLEEL--KEEDIPEIAKRALKEA-NPLYPVprIMDRKDCEELLRK 377
|
|
| Fe-ADH-like |
cd17814 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
7-375 |
6.49e-135 |
|
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: 389.98 E-value: 6.49e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 7 FYIPPIsFFGEGALEETADYIKNKDYKKALIVTDPGIAAIGLSGRVQKMLEERDLNVAIYDKTQPNPNIANVTAGLKVLK 86
Cdd:cd17814 2 FVAPEF-IFGVGARKLAGRYAKNLGARKVLVVTDPGVIKAGWVDEVLDSLEAEGLEYVVFSDVTPNPRDFEVMEGAELYR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 87 EQNSEIVVSIGGGSAHDNAKAIALLATNGGEIGDYEGVNQSKKAALPLFAINTTAGTASEMTRFTIISNEEKKIKMAIID 166
Cdd:cd17814 81 EEGCDGIVAVGGGSPIDCAKGIGIVVSNGGHILDYEGVDKVRRPLPPLICIPTTAGSSADVSQFAIITDTERRVKMAIIS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 167 NNVTPAVAVNDPSTMFGLPPALTAATGLDALTHCIEAYVSTASNPITDACALKGIDLINESLVAAYKDGKDKKARTDMCY 246
Cdd:cd17814 161 KTLVPDVSLIDPETLTTMDPELTACTGMDALTHAIEAYVSNASSPLTDLHALEAIRLISENLPKAVADPDDLEAREKMML 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 247 AEYLAGMAFNNASLGYVHALAHQLGGFYHLPHGVCNAVLLPHVQEANMqcPKAKKRLGEIALHFG------ASQEDPEET 320
Cdd:cd17814 241 ASLQAGLAFSNASLGAVHAMAHSLGGLLDLPHGECNALLLPHVIRFNF--PAAPERYRKIAEAMGldvdglDDEEVAERL 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 205831682 321 IKALHVLNRTMNIPRNLKELGVKTEDFEILAEHAMHDACHLTNPVQFTKEQVVAI 375
Cdd:cd17814 319 IEAIRDLREDLGIPETLSELGVDEEDIPELAKRAMKDPCLVTNPRRPTREDIEEI 373
|
|
| Fe-ADH-like |
cd14865 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
7-380 |
2.51e-130 |
|
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: 378.81 E-value: 2.51e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 7 FYIPPISFFGEGALEETADYIKNKDYKKALIVTDPGIAAIGLSGRVQKMLEERDLNVAIYDKTQPNPNIANVTAGLKVLK 86
Cdd:cd14865 3 FFNPTKIVSGAGALENLPAELARLGARRPLIVTDKGLAAAGLLKKVEDALGDAIEIVGVFDDVPPDSSVAVVNEAAARAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 87 EQNSEIVVSIGGGSAHDNAKAIALLATNGGE-IGDYEGVNQSKKAALPLFAINTTAGTASEMTRFTIISNEEKKIKMAII 165
Cdd:cd14865 83 EAGADGIIAVGGGSVIDTAKGVNILLSEGGDdLDDYGGANRLTRPLKPLIAIPTTAGTGSEVTLVAVIKDEEKKVKLLFV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 166 DNNVTPAVAVNDPSTMFGLPPALTAATGLDALTHCIEAYVSTASNPITDACALKGIDLINESLVAAYKDGKDKKARTDMC 245
Cdd:cd14865 163 SPFLLPDVAILDPRLTLSLPPKLTAATGMDALTHAIEAYTSLQKNPISDALALQAIRLISENLPKAVKNGKDLEARLALA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 246 YAEYLAGMAFNNASLGYVHALAHQLGGFYHLPHGVCNAVLLPHVQEANMqcPKAKKRLGEIALHFGASQEDP-------- 317
Cdd:cd14865 243 IAATMAGIAFSNSMVGLVHAIAHAVGAVAGVPHGLANSILLPHVMRYNL--DAAAERYAELALALAYGVTPAgrraeeai 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 205831682 318 EETIKALHVLNRTMNIPRNLKELGVKTEDFEILAEHAMHDACHLTNPVQFTKEQVVAIIKKAY 380
Cdd:cd14865 321 EAAIDLVRRLHELCGLPTRLRDVGVPEEQLEAIAELALNDGAILFNPREVDPEDILAILEAAY 383
|
|
| Fe-ADH-like |
cd08194 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
10-380 |
2.52e-130 |
|
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: 378.80 E-value: 2.52e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 10 PPISFFGEGALEETADYIKNKDYKKALIVTDPGIAAIGLSGRVQKMLEERDLNVAIYDKTQPNPNIANVTAGLKVLKEQN 89
Cdd:cd08194 1 PRTIIIGGGALEELGEEAASLGGKRALIVTDKVMVKLGLVDKVTQLLAEAGIAYAVFDDVVSEPTDEMVEEGLALYKEGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 90 SEIVVSIGGGSAHDNAKAIALLATNGGEIGDYEGVNQSKKAALPLFAINTTAGTASEMTRFTIISNEEKKIKMAIIDNNV 169
Cdd:cd08194 81 CDFIVALGGGSPIDTAKAIAVLATNGGPIRDYMGPRKVDKPGLPLIAIPTTAGTGSEVTRFTVITDTETDVKMLLKGPAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 170 TPAVAVNDPSTMFGLPPALTAATGLDALTHCIEAYVSTASNPITDACALKGIDLINESLVAAYKDGKDKKARTDMCYAEY 249
Cdd:cd08194 161 LPAVAIVDPELTLSMPPRVTAATGIDALTHAIEAYVSRKAQPLTDTLALSAIKLIGRNLRRAYADGDDLEAREAMMLAAL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 250 LAGMAFNNASLGYVHALAHQLGGFYHLPHGVCNAVLLPHVQEANMqcPKAKKRLGEIALHFGAS------QEDPEETIKA 323
Cdd:cd08194 241 EAGIAFSNSSVALVHGMSRPIGALFHVPHGLSNAMLLPAVTEFSL--PGAPERYAEIARAMGIAtegdsdEEAAEKLVEA 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 205831682 324 LHVLNRTMNIPRnLKELGVKTEDF----EILAEHAMHDACHLTNPVQFTKEQVVAIIKKAY 380
Cdd:cd08194 319 LERLCADLEIPT-LREYGIDEEEFeaalDKMAEDALASGSPANNPRVPTKEEIIELYREAW 378
|
|
| Fe-ADH-like |
cd14863 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
7-380 |
8.16e-127 |
|
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: 369.94 E-value: 8.16e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 7 FYIPPISFFGEGALEETADYIKNKDYKKALIVTDPGIAAIGLSGRVQKMLEERDLNVAIYDKTQPNPNIANVTAGLKVLK 86
Cdd:cd14863 2 YSQLTPVIFGAGAVEQIGELLKELGCKKVLLVTDKGLKKAGIVDKIIDLLEEAGIEVVVFDDVEPDPPDEIVDEAAEIAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 87 EQNSEIVVSIGGGSAHDNAKAIALLATNGGEIGDYEG-VNQSKKAALPLFAINTTAGTASEMTRFTIISNEEKKIKMAII 165
Cdd:cd14863 82 EEGADGVIGIGGGSVLDTAKAIAVLLTNPGPIIDYALaGPPVPKPGIPLIAIPTTAGTGSEVTPIAVITDEENGVKKSLL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 166 DNNVTPAVAVNDPSTMFGLPPALTAATGLDALTHCIEAYVSTASNPITDACALKGIDLINESLVAAYKDGKDKKARTDMC 245
Cdd:cd14863 162 GPFLVPDLAILDPELTVGLPPSLTAATGMDALSHAIEAYTSKLANPMTDALALQAIRLIVKNLPRAVKDGDNLEARENML 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 246 YAEYLAGMAFNNASLGYVHALAHQLGGFYHLPHGVCNAVLLPHVQEANMQ-CPKAKKRLGEIalhFGASQ--EDPEE--- 319
Cdd:cd14863 242 LASNLAGIAFNNAGTHIGHAIAHALGALYHIPHGLACALALPVVLEFNAEaYPEKVKKIAKA---LGVSFpgESDEElge 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 205831682 320 -TIKALHVLNRTMNIPRNLKELGVKTEDFEILAEHAMHDACHLTNPVQFTKEQVVAIIKKAY 380
Cdd:cd14863 319 aVADAIREFMKELGIPSLFEDYGIDKEDLDKIAEAVLKDPFAMFNPRPITEEEVAEILEAIY 380
|
|
| Fe-ADH-like |
cd14861 |
Iron-containing alcohol dehydrogenases-like; This family contains proteins similar to ... |
8-379 |
7.84e-125 |
|
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: 364.53 E-value: 7.84e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 8 YIPPIsFFGEGALEETADYIKNKDYKKALIVTDPGIAAIGLSGRVQKMLEERDLNVAIYDKTQPNPNIANVTAGLKVLKE 87
Cdd:cd14861 2 YPTRI-RFGAGAIAELPEELKALGIRRPLLVTDPGLAALGIVDRVLEALGAAGLSPAVFSDVPPNPTEADVEAGVAAYRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 88 QNSEIVVSIGGGSAHDNAKAIALLATNGGEIGDYE----GVNQSKKAALPLFAINTTAGTASEMTRFTIISNEEKKIKMA 163
Cdd:cd14861 81 GGCDGIIALGGGSAIDAAKAIALMATHPGPLWDYEdgegGPAAITPAVPPLIAIPTTAGTGSEVGRAAVITDDDTGRKKI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 164 IIDNNVTPAVAVNDPSTMFGLPPALTAATGLDALTHCIEAYVSTASNPITDACALKGIDLINESLVAAYKDGKDKKARTD 243
Cdd:cd14861 161 IFSPKLLPKVAICDPELTLGLPPRLTAATGMDALTHCIEAYLSPGFHPMADGIALEGLRLISEWLPRAVADGSDLEARGE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 244 MCYAEYLAGMAFNNaSLGYVHALAHQLGGFYHLPHGVCNAVLLPHVQEANMqcPKAKKRLGEIALHFGASQEDPEETIKA 323
Cdd:cd14861 241 MMMAALMGAVAFQK-GLGAVHALAHALGALYGLHHGLLNAILLPYVLRFNR--PAVEDKLARLARALGLGLGGFDDFIAW 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 205831682 324 LHVLNRTMNIPRNLKELGVKTEDFEILAEHAMHDACHLTNPVQFTKEQVVAIIKKA 379
Cdd:cd14861 318 VEDLNERLGLPATLSELGVTEDDLDELAELALADPCHATNPRPVTAEDYRALLREA 373
|
|
| PRK10624 |
PRK10624 |
L-1,2-propanediol oxidoreductase; Provisional |
11-380 |
4.99e-118 |
|
L-1,2-propanediol oxidoreductase; Provisional
Pssm-ID: 182595 [Multi-domain] Cd Length: 382 Bit Score: 347.37 E-value: 4.99e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 11 PISFFGEGALEETADYIKNKDYKKALIVTDPGIAAIGLSGRVQKMLEERDLNVAIYDKTQPNPNIANVTAGLKVLKEQNS 90
Cdd:PRK10624 9 ETAYFGRGAIGALTDEVKRRGFKKALIVTDKTLVKCGVVAKVTDVLDAAGLAYEIYDGVKPNPTIEVVKEGVEVFKASGA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 91 EIVVSIGGGSAHDNAKAIALLaTNGGEIGD---YEGVNQSKKAALPLFAINTTAGTASEMTRFTIISNEEKKIKMAIIDN 167
Cdd:PRK10624 89 DYLIAIGGGSPQDTCKAIGII-SNNPEFADvrsLEGVAPTKKPSVPIIAIPTTAGTAAEVTINYVITDEEKRRKFVCVDP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 168 NVTPAVAVNDPSTMFGLPPALTAATGLDALTHCIEAYVSTASNPITDACALKGIDLINESLVAAYKDgkDKKARTDMCYA 247
Cdd:PRK10624 168 HDIPQVAFVDADMMDSMPPGLKAATGVDALTHAIEGYITRGAWALTDMLHLKAIEIIAGALRGAVAG--DKEAGEGMALG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 248 EYLAGMAFNNASLGYVHALAHQLGGFYHLPHGVCNAVLLPHVQEANMQCPKAKKRlgEIALHFGASQED------PEETI 321
Cdd:PRK10624 246 QYIAGMGFSNVGLGLVHGMAHPLGAFYNTPHGVANAILLPHVMEYNADFTGEKYR--DIARAMGVKVEGmsleeaRNAAV 323
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 205831682 322 KALHVLNRTMNIPRNLKELGVKTEDFEILAEHAMHDACHLTNPVQFTKEQVVAIIKKAY 380
Cdd:PRK10624 324 EAVKALNRDVGIPPHLRDVGVKEEDIPALAQAAFDDVCTGGNPREATLEDIVELYKKAW 382
|
|
| NADPH_BDH |
cd08179 |
NADPH-dependent butanol dehydrogenase involved in the butanol and ethanol formation pathway in ... |
7-381 |
5.06e-118 |
|
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: 347.25 E-value: 5.06e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 7 FYIPPISFFGEGALEetadYIKNKDYKKALIVTDPGI-AAIGLSGRVQKMLEERDLNVAIYDKTQPNPNIANVTAGLKVL 85
Cdd:cd08179 2 FFVPRDIYFGEGALE----YLKTLKGKRAFIVTGGGSmKRNGFLDKVEDYLKEAGMEVKVFEGVEPDPSVETVEKGAEAM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 86 KEQNSEIVVSIGGGSAHDNAKAIALLAtnggEIGDYEGVNQSKKAALP-------LFAINTTAGTASEMTRFTIISNEEK 158
Cdd:cd08179 78 REFEPDWIIAIGGGSVIDAAKAMWVFY----EYPELTFEDALVPFPLPelrkkarFIAIPSTSGTGSEVTRASVITDTEK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 159 KIKMAIIDNNVTPAVAVNDPSTMFGLPPALTAATGLDALTHCIEAYVSTASNPITDACALKGIDLINESLVAAYKDGKDK 238
Cdd:cd08179 154 GIKYPLASFEITPDVAILDPELTMTMPPHVTANTGMDALTHAIEAYVSTLANDFTDALALGAILDIFENLPKSYNGGKDL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 239 KARTDMCYAEYLAGMAFNNASLGYVHALAHQLGGFYHLPHGVCNAVLLPHVQEANMQCPKAKKRLGEIaLHFGASQEDPE 318
Cdd:cd08179 234 EAREKMHNASCLAGMAFSNSGLGIVHSMAHKGGAFFGIPHGLANAILLPYVIEFNSKDPEARARYAAL-LIGLTDEELVE 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 205831682 319 ETIKALHVLNRTMNIPRNLKELGVKTEDF----EILAEHAMHDACHLTNPVQFTKEQVVAIIKKAYE 381
Cdd:cd08179 313 DLIEAIEELNKKLGIPLSFKEAGIDEDEFfaklDEMAENAMNDACTGTNPRKPTVEEMKELLKAAYY 379
|
|
| Fe-ADH-like |
cd08183 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
15-377 |
9.57e-115 |
|
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: 339.09 E-value: 9.57e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 15 FGEGALEETADYIKNKDyKKALIVTDPGIAAIGLSGRVQKMLEERDLNVAIYDKTqPNPNIANVTAGLKVLKEQNSEIVV 94
Cdd:cd08183 6 FGRGSLQELGELAAELG-KRALLVTGRSSLRSGRLARLLEALEAAGIEVALFSVS-GEPTVETVDAAVALAREAGCDVVI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 95 SIGGGSAHDNAKAIALLATNGGEIGDY-EGVNQSKK---AALPLFAINTTAGTASEMTRFTIISNEEKKIKMAIIDNNVT 170
Cdd:cd08183 84 AIGGGSVIDAAKAIAALLTNEGSVLDYlEVVGKGRPltePPLPFIAIPTTAGTGSEVTKNAVLSSPEHGVKVSLRSPSML 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 171 PAVAVNDPSTMFGLPPALTAATGLDALTHCIEAYVSTASNPITDACALKGIDLINESLVAAYKDGKDKKARTDMCYAEYL 250
Cdd:cd08183 164 PDVALVDPELTLSLPPEVTAASGLDALTQLIEPYVSRKANPLTDALAREGLRLAARSLRRAYEDGEDLEAREDMALASLL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 251 AGMAFNNASLGYVHALAHQLGGFYHLPHG-VCnAVLLPHVQEAN-------MQCPKAKKRLGEIA-LHFGASQEDPEETI 321
Cdd:cd08183 244 GGLALANAGLGAVHGLAGPLGGMFGAPHGaIC-AALLPPVLEANlralrerEPDSPALARYRELAgILTGDPDAAAEDGV 322
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 205831682 322 KALHVLNRTMNIPRnLKELGVKTEDFEILAEHAMHDACHLTNPVQFTKEQVVAIIK 377
Cdd:cd08183 323 EWLEELCEELGIPR-LSEYGLTEEDFPEIVEKARGSSSMKGNPIELSDEELLEILE 377
|
|
| Fe-ADH-like |
cd08185 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
7-377 |
6.82e-113 |
|
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: 334.47 E-value: 6.82e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 7 FYIPPISFFGEGALEETADYIKnKDYKKALIVTDPGIAAI-GLSGRVQKMLEERDLNVAIYDKTQPNPNIANVTAGLKVL 85
Cdd:cd08185 1 YYQPTRILFGAGKLNELGEEAL-RPGKKALIVTGKGSSKKtGLLDRVKKLLEKAGVEVVVFDKVEPNPLTTTVMEGAALA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 86 KEQNSEIVVSIGGGSAHDNAKAIALLATNGGEIGDY----EGVNQSKKAALPLFAINTTAGTASEMTRFTIISNEEKKIK 161
Cdd:cd08185 80 KEEGCDFVIGLGGGSSMDAAKAIAFMATNPGDIWDYifggTGKGPPPEKALPIIAIPTTAGTGSEVDPWAVITNPETKEK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 162 MAIIDNNVTPAVAVNDPSTMFGLPPALTAATGLDALTHCIEAYVSTASNPITDACALKGIDLINESLVAAYKDGKDKKAR 241
Cdd:cd08185 160 KGIGHPALFPKVSIVDPELMLTVPPRVTAYTGFDALFHAFESYISKNANPFSDMLALEAIRLVAKYLPRAVKDGSDLEAR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 242 TDMCYAEYLAGMAFNNASLGYVHALAHQLGGFY-HLPHGVCNAVLLPHVQEANmqCPKAKKRLGEIALHFGAS---QEDP 317
Cdd:cd08185 240 EKMAWASTLAGIVIANSGTTLPHGLEHPLSGYHpNIPHGAGLAALYPAYFEFT--IEKAPEKFAFVARAEASGlsdAKAA 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 205831682 318 EETIKALHVLNRTMNIPRNLKELGVKTEDFEILAEHAM--HDACHLTNPVQFTKEQVVAIIK 377
Cdd:cd08185 318 EDFIEALRKLLKDIGLDDLLSDLGVTEEDIPWLAENAMetMGGLFANNPVELTEEDIVEIYE 379
|
|
| PDD |
cd08180 |
1,3-propanediol dehydrogenase (PPD) catalyzes the reduction of 3-hydroxypropionaldehyde (3-HPA) ... |
7-377 |
7.03e-111 |
|
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: 327.53 E-value: 7.03e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 7 FYIPPISFFGEGALEetadYIKNKDYKKALIVTDPGIAAIGLSGRVQKMLEERDlNVAIYDKTQPNPNIANVTAGLKVLK 86
Cdd:cd08180 1 FSLKTKIYSGEDSLE----RLKELKGKRVFIVTDPFMVKSGMVDKVTDELDKSN-EVEIFSDVVPDPSIEVVAKGLAKIL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 87 EQNSEIVVSIGGGSAHDNAKAIALLAtnggeigdYEGVNQSKKAalPLFAINTTAGTASEMTRFTIISNEEKKIKMAIID 166
Cdd:cd08180 76 EFKPDTIIALGGGSAIDAAKAIIYFA--------LKQKGNIKKP--LFIAIPTTSGTGSEVTSFAVITDPEKGIKYPLVD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 167 NNVTPAVAVNDPSTMFGLPPALTAATGLDALTHCIEAYVSTASNPITDACALKGIDLINESLVAAYKDGKDKKARTDMCY 246
Cdd:cd08180 146 DSMLPDIAILDPELVKSVPPKVTADTGMDVLTHALEAYVSTNANDFTDALAEKAIKLVFENLPRAYRDGDDLEAREKMHN 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 247 AEYLAGMAFNNASLGYVHALAHQLGGFYHLPHGVCNAVLLPHVQEAnmqcpkakkrlgeialhfgasqedpeeTIKALHV 326
Cdd:cd08180 226 ASCMAGIAFNNAGLGINHSLAHALGGRFHIPHGRANAILLPYVIEF---------------------------LIAAIRR 278
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 205831682 327 LNRTMNIPRNLKELGVKTEDFE----ILAEHAMHDACHLTNPVQFTKEQVVAIIK 377
Cdd:cd08180 279 LNKKLGIPSTLKELGIDEEEFEkaidEMAEAALADRCTATNPRKPTAEDLIELLR 333
|
|
| AAD_C |
cd08178 |
C-terminal alcohol dehydrogenase domain of the acetaldehyde dehydrogenase-alcohol ... |
9-365 |
3.27e-103 |
|
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: 310.27 E-value: 3.27e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 9 IPPISFFGEGALEETADyiKNKDYKKALIVTDPGIAAIGLSGRVQKMLEERDLNVAIYDKTQPNPNIANVTAGLKVLKEQ 88
Cdd:cd08178 2 VPPKIYFEPGCLPYLLL--ELPGVKRAFIVTDRVLYKLGYVDKVLDVLEARGVETEVFSDVEPDPTLSTVRKGLEAMNAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 89 NSEIVVSIGGGSAHDNAKAIALLATNGGEigDYEGVNQS---------------KKAALplFAINTTAGTASEMTRFTII 153
Cdd:cd08178 80 KPDVIIALGGGSAMDAAKIMWLFYEHPET--KFEDLAQRfmdirkrvykfpklgKKAKL--VAIPTTSGTGSEVTPFAVI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 154 SNEEKKIKMAIIDNNVTPAVAVNDPSTMFGLPPALTAATGLDALTHCIEAYVSTASNPITDACALKGIDLINESLVAAYK 233
Cdd:cd08178 156 TDDKTGKKYPLADYALTPDMAIVDPELVMTMPKRLTADTGIDALTHAIEAYVSVMASDYTDGLALQAIKLIFEYLPRSYN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 234 DGKDKKARTDMCYAEYLAGMAFNNASLGYVHALAHQLGGFYHLPHGVCNAVLLPHVQEANMQC-------------PKAK 300
Cdd:cd08178 236 NGNDIEAREKMHNAATIAGMAFANAFLGICHSLAHKLGAAFHIPHGRANAILLPHVIRYNATDpptkqaafpqykyYVAK 315
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 205831682 301 KRLGEIA--LHFGASQEDP--EETIKALHVLNRTMNIPRNLKELGVKTEDF----EILAEHAMHDACHLTNPV 365
Cdd:cd08178 316 ERYAEIAdlLGLGGKTPEEkvESLIKAIEDLKKDLGIPTSIREAGIDEADFlaavDKLAEDAFDDQCTGANPR 388
|
|
| Fe-ADH-like |
cd08196 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
7-375 |
7.91e-103 |
|
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: 308.35 E-value: 7.91e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 7 FYIPPISFFGEGALEETADYIKNKDYKKALIVTDPGIAAIGLSGRVQKMLEERDlnVAIYDKTQPNPNIANVTAGLKVLK 86
Cdd:cd08196 3 YYQPVKIIFGEGILKELPDIIKELGGKRGLLVTDPSFIKSGLAKRIVESLKGRI--VAVFSDVEPNPTVENVDKCARLAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 87 EQNSEIVVSIGGGSAHDNAKAIALLATNGGEIGDY-EGVNQSKKAALPLFAINTTAGTASEMTRFTIISNEEKKIKMAII 165
Cdd:cd08196 81 ENGADFVIAIGGGSVLDTAKAAACLAKTDGSIEDYlEGKKKIPKKGLPLIAIPTTAGTGSEVTPVAVLTDKEKGKKAPLV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 166 DNNVTPAVAVNDPSTMFGLPPALTAATGLDALTHCIEAYVSTASNPITDACALKGIDLINESLVAAYKDGKDKKARTDMC 245
Cdd:cd08196 161 SPGFYPDIAIVDPELTYSMPPKVTASTGIDALCHAIEAYWSINHQPISDALALEAAKLVLENLEKAYNNPNDKEAREKMA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 246 YAEYLAGMAFNNASLGYVHALAHQLGGFYHLPHGVCNAVLLPHVQEANMqcPKAKKRLGEIALHFGAsqEDPEETIKALH 325
Cdd:cd08196 241 LASLLAGLAFSQTRTTASHACSYPLTSHFGIPHGEACALTLPSFIRLNA--EALPGRLDELAKQLGF--KDAEELADKIE 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 205831682 326 VLNRTMNIPRNLKELGVKTEDFEILAEHAMHDACHLTNPVQFTKEQVVAI 375
Cdd:cd08196 317 ELKKRIGLRTRLSELGITEEDLEEIVEESFHPNRANNNPVEVTKEDLEKL 366
|
|
| HVD |
cd08193 |
5-hydroxyvalerate dehydrogenase (HVD) catalyzes the oxidation of 5-hydroxyvalerate to ... |
7-380 |
2.90e-100 |
|
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: 302.12 E-value: 2.90e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 7 FYIPPISFFGEGALEETADYIKNKDYKKALIVTDPGIAAIGLSGRVQKMLEERDLNVAIYDKTQPNPNIANVTAGLKVLK 86
Cdd:cd08193 1 FQTVPRIICGAGAAARLGELLRELGARRVLLVTDPGLVKAGLADPALAALEAAGIAVTVFDDVVADPPEAVVEAAVEQAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 87 EQNSEIVVSIGGGSAHDNAKAIALLATNGGEIGDYEGVNQSKKAALPLFAINTTAGTASEMTRFTIISNEEKKiKMAIID 166
Cdd:cd08193 81 EAGADGVIGFGGGSSMDVAKLVALLAGSDQPLDDIYGVGKATGPRLPLILVPTTAGTGSEVTPISIVTTGETE-KKGVVS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 167 NNVTPAVAVNDPSTMFGLPPALTAATGLDALTHCIEAYVS-TASNPITDACALKGIDLINESLVAAYKDGKDKKARTDMC 245
Cdd:cd08193 160 PQLLPDVALLDAELTLGLPPHVTAATGIDAMVHAIEAYTSrHKKNPISDALAREALRLLGANLRRAVEDGSDLEAREAML 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 246 YAEYLAGMAFNNASLGYVHALAHQLGGFYHLPHGVCNAVLLPHVQEANMqcPKAKKRLGEIA------LHFGASQEDPEE 319
Cdd:cd08193 240 LGSMLAGQAFANAPVAAVHALAYPLGGHFHVPHGLSNALVLPHVLRFNL--PAAEALYAELArallpgLAFGSDAAAAEA 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 205831682 320 TIKALHVLNRTMNIPRNLKELGVKTEDFEILAEHAMHDACHLT-NPVQFTKEQVVAIIKKAY 380
Cdd:cd08193 318 FIDALEELVEASGLPTRLRDVGVTEEDLPMLAEDAMKQTRLLVnNPREVTEEDALAIYQAAL 379
|
|
| Fe-ADH-like |
cd08191 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
7-380 |
4.03e-98 |
|
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: 297.22 E-value: 4.03e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 7 FYIPPISFFGEGALEETADYIKNKDYKkALIVTDPGIAAIGLSGRVQKMLEERDLNVAIYDKTQPNPNIANVTAGLKVLK 86
Cdd:cd08191 1 LRSPSRLLFGPGARRALGRVAARLGSR-VLIVTDPRLASTPLVAELLAALTAAGVAVEVFDGGQPELPVSTVADAAAAAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 87 EQNSEIVVSIGGGSAHDNAKAIALLATNGGEIGDYEGVNQSKKAALPLFAINTTAGTASEMTRFTIISNEEKKIKMAIID 166
Cdd:cd08191 80 AFDPDVVIGLGGGSNMDLAKVVALLLAHGGDPRDYYGEDRVPGPVLPLIAVPTTAGTGSEVTPVAVLTDPARGMKVGVSS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 167 NNVTPAVAVNDPSTMFGLPPALTAATGLDALTHCIEAYVSTA---------------SNPITDACALKGIDLINESLVAA 231
Cdd:cd08191 160 PYLRPAVAIVDPELTLTCPPGVTADSGIDALTHAIESYTARDfppfprldpdpvyvgKNPLTDLLALEAIRLIGRHLPRA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 232 YKDGKDKKARTDMCYAEYLAGMAFNNASLGYVHALAHQLGGFYHLPHGVCNAVLLPHVQEANmqCPKAKKRLGEIALHFG 311
Cdd:cd08191 240 VRDGDDLEARSGMALAALLAGLAFGTAGTAAAHALQYPIGALTHTSHGVGNGLLLPYVMRFN--RPARAAELAEIARALG 317
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 205831682 312 ASQEDPEE-----TIKALHVLNRTMNIPRNLKELGVKTEDFEILAEHAMhDACHL--TNPVQFTKEQVVAIIKKAY 380
Cdd:cd08191 318 VTTAGTSEeaadrAIERVEELLARIGIPTTLADLGVTEADLPGLAEKAL-SVTRLiaNNPRPPTEEDLLRILRAAF 392
|
|
| Fe-ADH-like |
cd14862 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
5-372 |
1.12e-95 |
|
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: 290.28 E-value: 1.12e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 5 TGFYIPPISFFGEGALEETADYIKnkdyKKALIVTDPGIAAIGLSGRVQKMLEERDLNVAIYDKTQPNPNIANVTAGLKV 84
Cdd:cd14862 1 MWYFSSPKIVFGEDALSHLEQLSG----KRALIVTDKVLVKLGLLKKVLKRLLQAGFEVEVFDEVEPEPPLETVLKGAEA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 85 LKEQNSEIVVSIGGGSAHDNAKAIALLATNGGEigDYEGVN------QSKKAALplFAINTTAGTASEMTRFTIISNEEK 158
Cdd:cd14862 77 MREFEPDLIIALGGGSVMDAAKAAWVLYERPDL--DPEDISpldllgLRKKAKL--IAIPTTSGTGSEATWAIVLTDTEE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 159 KIKMAIIDNNVTPAVAVNDPSTMFGLPPALTAATGLDALTHCIEAYVSTASNPITDACALKGIDLINESLVAAYKDGKDK 238
Cdd:cd14862 153 PRKIAVANPELVPDVAILDPEFVLGMPPKLTAGTGLDALAHAVEAYLSTWSNDFSDALALKAIELIFKYLPRAYKDGDDL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 239 KARTDMCYAEYLAGMAFNNASLGYVHALAHQLGGFYHLPHGVCNAVLLPHVQEanMQCPKAKKRLGEIALHFGASQEDPE 318
Cdd:cd14862 233 EAREKMHNAATIAGLAFGNSQAGLAHALGHSLGAVFHVPHGIAVGLFLPYVIE--FYAKVTDERYDLLKLLGIEARDEEE 310
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 205831682 319 ---ETIKALHVLNRTMNIPRNLKELGVKTEDFE----ILAEHAMHDACHLTNPVQFTKEQV 372
Cdd:cd14862 311 alkKLVEAIRELYKEVGQPLSIKDLGISEEEFEekldELVEYAMEDSCTITSPRPPSEEDL 371
|
|
| HOT |
cd08190 |
Hydroxyacid-oxoacid transhydrogenase (HOT) involved in gamma-hydroxybutyrate metabolism; This ... |
15-380 |
6.00e-94 |
|
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: 287.13 E-value: 6.00e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 15 FGEGALEETADYIKNKDYKKALIVTDPGIAAIGLSGRVQKMLEERDLNVAIYDKTQPNPNIANVTAGLKVLKEQNSEIVV 94
Cdd:cd08190 6 FGPGATRELGMDLKRLGAKKVLVVTDPGLAKLGLVERVLESLEKAGIEVVVYDGVRVEPTDESFEEAIEFAKEGDFDAFV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 95 SIGGGSAHDNAKAIALLATNGGEIGDYegVN-------QSKKAALPLFAINTTAGTASEMTRFTIISNEEKKIKMAIIDN 167
Cdd:cd08190 86 AVGGGSVIDTAKAANLYATHPGDFLDY--VNapigkgkPVPGPLKPLIAIPTTAGTGSETTGVAIFDLEELKVKTGISSR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 168 NVTPAVAVNDPSTMFGLPPALTAATGLDALTHCIEAYvsTA--------------------SNPITDACALKGIDLINES 227
Cdd:cd08190 164 YLRPTLAIVDPLLTLTLPPRVTASSGFDVLCHALESY--TArpynarprpanpderpayqgSNPISDVWAEKAIELIGKY 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 228 LVAAYKDGKDKKARTDMCYAEYLAGMAFNNASLGYVHALAHQLGG-------------FYHLPHGVCNAVLLPHVQEANM 294
Cdd:cd08190 242 LRRAVNDGDDLEARSNMLLASTLAGIGFGNAGVHLPHAMAYPIAGlvkdyrppgypvdHPHVPHGLSVALTAPAVFRFTA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 295 Q-CPkakKRLGEIALHFGA-----SQEDPEETIK-ALHVLNRTMNIPRNLKELGVKTEDFEILAEHAMHDACHL-TNPVQ 366
Cdd:cd08190 322 PaCP---ERHLEAAELLGAdtsgaSDRDAGEVLAdALIKLMRDIGIPNGLSALGYSEDDIPALVEGTLPQQRLLkLNPRP 398
|
410
....*....|....
gi 205831682 367 FTKEQVVAIIKKAY 380
Cdd:cd08190 399 VTEEDLEEIFEDAL 412
|
|
| PRK13805 |
PRK13805 |
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional |
7-380 |
1.36e-89 |
|
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional
Pssm-ID: 237515 [Multi-domain] Cd Length: 862 Bit Score: 287.85 E-value: 1.36e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 7 FYIPPISFFGEGALEETADYIKNKdyKKALIVTDPGIAAIGLSGRVQKMLEERDLNVA--IYDKTQPNPNIANVTAGLKV 84
Cdd:PRK13805 457 FKVPKKIYFERGSLPYLLDELDGK--KRAFIVTDRFMVELGYVDKVTDVLKKRENGVEyeVFSEVEPDPTLSTVRKGAEL 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 85 LKEQNSEIVVSIGGGSAHDNAKAIALLATNGgEIgDYEGVNQ---------------SKKAALplFAINTTAGTASEMTR 149
Cdd:PRK13805 535 MRSFKPDTIIALGGGSPMDAAKIMWLFYEHP-ET-DFEDLAQkfmdirkriykfpklGKKAKL--VAIPTTSGTGSEVTP 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 150 FTIISNEEKKIKMAIIDNNVTPAVAVNDPSTMFGLPPALTAATGLDALTHCIEAYVSTASNPITDACALKGIDLINESLV 229
Cdd:PRK13805 611 FAVITDDKTGVKYPLADYELTPDVAIVDPNLVMTMPKSLTADTGIDALTHALEAYVSVMASDYTDGLALQAIKLVFEYLP 690
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 230 AAYKDG-KDKKARTDMCYAEYLAGMAFNNASLGYVHALAHQLGGFYHLPHGVCNAVLLPHVQEANMQ------------C 296
Cdd:PRK13805 691 RSYKNGaKDPEAREKMHNASTIAGMAFANAFLGICHSMAHKLGAEFHIPHGRANAILLPHVIRYNATdppkqaafpqyeY 770
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 297 PKAKKRLGEIALHFGASQEDPEET----IKALHVLNRTMNIPRNLKELGVKTEDFEI----LAEHAMHDACHLTNPVQFT 368
Cdd:PRK13805 771 PRADERYAEIARHLGLPGSTTEEKveslIKAIEELKAELGIPMSIKEAGVDEADFLAkldeLAELAFDDQCTGANPRYPL 850
|
410
....*....|..
gi 205831682 369 KEQVVAIIKKAY 380
Cdd:PRK13805 851 ISELKEILLDAY 862
|
|
| HEPD |
cd08182 |
Hydroxyethylphosphoate dehydrogenase (HEPD) catalyzes the reduction of phosphonoacetaldehyde ... |
14-376 |
3.69e-78 |
|
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: 245.21 E-value: 3.69e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 14 FFGEGALEETADYIKNKDYKKALIVTDPGIAAIGLSGRVQKMLEERDlNVAIYDKTQPNPNIANVTAGLKVLKEQNSEIV 93
Cdd:cd08182 5 IFGPGALAELKDLLGGLGARRVLLVTGPSAVRESGAADILDALGGRI-PVVVFSDFSPNPDLEDLERGIELFRESGPDVI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 94 VSIGGGSAHDNAKAIALLATNGGEIGDY--EGVNQSKKAALPLFAINTTAGTASEMTRFTIISNEEKKIKMAIIDNNVTP 171
Cdd:cd08182 84 IAVGGGSVIDTAKAIAALLGSPGENLLLlrTGEKAPEENALPLIAIPTTAGTGSEVTPFATIWDEAEGKKYSLAHPSLYP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 172 AVAVNDPSTMFGLPPALTAATGLDALTHCIEAYVSTASNPITDACALKGIDLINESLVAAYKDGKDKKARTDMCYAEYLA 251
Cdd:cd08182 164 DAAILDPELTLSLPLYLTASTGLDALSHAIESIWSVNANPESRAYALRAIRLILENLPLLLENLPNLEAREAMAEASLLA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 252 GMAFNNASLGYVHALAHQLGGFYHLPHGVCNAVLLPHVQEANMQCPKAK---KRLGEIALHFGASqeDPEETIKALHVLN 328
Cdd:cd08182 244 GLAISITKTTAAHAISYPLTSRYGVPHGHACALTLPAVLRYNAGADDECdddPRGREILLALGAS--DPAEAAERLRALL 321
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 205831682 329 RTMNIPRNLKELGVKTEDFEILAEHAMHDACHLTNPVQFTKEQVVAII 376
Cdd:cd08182 322 ESLGLPTRLSEYGVTAEDLEALAASVNTPERLKNNPVRLSEEDLLRLL 369
|
|
| PPD-like |
cd08181 |
1,3-propanediol dehydrogenase-like (PPD); This family contains proteins similar to 1, ... |
7-377 |
9.67e-76 |
|
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: 238.64 E-value: 9.67e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 7 FYIPPISFFGEGALEETADYIKnKDYKKALIVTdpGIAAIGLSG---RVQKMLEERDLNVAIYDKTQPNPNIANVTAGLK 83
Cdd:cd08181 1 FYMPTKVYFGKNCVEKHADELA-ALGKKALIVT--GKHSAKKNGsldDVTEALEENGIEYFIFDEVEENPSIETVEKGAE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 84 VLKEQNSEIVVSIGGGSAHDNAKAIALLATNGGEIGDYEGVNQSKKAaLPLFAINTTAGTASEMTRFTIISNEEKKIKMA 163
Cdd:cd08181 78 LARKEGADFVIGIGGGSPLDAAKAIALLAANKDGDEDLFQNGKYNPP-LPIVAIPTTAGTGSEVTPYSILTDHEKGTKKS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 164 IIDNNVTPAVAVNDPSTMFGLPPALTAATGLDALTHCIEAYVSTASNPITDACALKGIDLINESLVAAYKDGKDKKARTD 243
Cdd:cd08181 157 FGNPLIFPKLALLDPKYTLSLPEELTIDTAVDALSHAIEGYLSVKATPLSDALALEALRLIGECLPNLLGDELDEEDREK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 244 MCYAEYLAGMAFNNASLGYVHALAHQLGGFYHLPHGVCNAVLLPHVQEANMQCPKAKKRLGEIALHFGaSQEDPEETIKA 323
Cdd:cd08181 237 LMYASTLAGMVIAQTGTTLPHGLGYPLTYFKGIPHGRANGILLPAYLKLCEKQEPEKVDKILKLLGFG-SIEEFQKFLNR 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 205831682 324 LhvlnrtmnIPRNLKelgVKTEDFEILAEHAMHDACHLTNPVQFTKEQVVAIIK 377
Cdd:cd08181 316 L--------LGKKEE---LSEEELEKYADEAMKAKNKKNTPGNVTKEDILRIYR 358
|
|
| BDH |
cd08187 |
Butanol dehydrogenase catalyzes the conversion of butyraldehyde to butanol with the cofactor ... |
7-377 |
1.10e-75 |
|
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: 239.26 E-value: 1.10e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 7 FYIPPISFFGEGALEETADYIKNKDyKKALIVTDPG-IAAIGLSGRVQKMLEERDLNVAIYDKTQPNPNIANVTAGLKVL 85
Cdd:cd08187 4 FYNPTKIIFGKGAIEELGEEIKKYG-KKVLLVYGGGsIKKNGLYDRVVASLKEAGIEVVEFGGVEPNPRLETVREGIELA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 86 KEQNSEIVVSIGGGSAHDNAKAIALLATNGGEIGDYEGVNQSKKAALPLFAINTTAGTASEMTRFTIISNEEKKIKMAII 165
Cdd:cd08187 83 REENVDFILAVGGGSVIDAAKAIAAGAKYDGDVWDFFTGKAPPEKALPVGTVLTLAATGSEMNGGAVITNEETKEKLGFG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 166 DNNVTPAVAVNDPSTMFGLPPALTAATGLDALTHCIEAYVS-TASNPITDAcalkgidlINESLV--------AAYKDGK 236
Cdd:cd08187 163 SPLLRPKFSILDPELTYTLPKYQTAAGIVDIFSHVLEQYFTgTEDAPLQDR--------LAEGLLrtviengpKALKDPD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 237 DKKARTDMCYAeylAGMAFNN-ASLGY-----VHALAHQLGGFYHLPHGVCNAVLLPHVqeANMQCPKAKKRLGEIA--- 307
Cdd:cd08187 235 DYEARANLMWA---ATLALNGlLGAGRggdwaTHAIEHELSALYDITHGAGLAIVFPAW--MRYVLKKKPERFAQFArrv 309
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 205831682 308 --LHFGASQED-PEETIKALHVLNRTMNIPRNLKELGVKTEDFEILAEHAMHDACHLTNPVQFTKEQVVAIIK 377
Cdd:cd08187 310 fgIDPGGDDEEtALEGIEALEEFFKSIGLPTTLSELGIDEEDIEEMAEKAVRGGGLGGGFKPLTREDIEEILK 382
|
|
| PRK15454 |
PRK15454 |
ethanolamine utilization ethanol dehydrogenase EutG; |
1-379 |
1.93e-70 |
|
ethanolamine utilization ethanol dehydrogenase EutG;
Pssm-ID: 185351 [Multi-domain] Cd Length: 395 Bit Score: 226.06 E-value: 1.93e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 1 MSSVTGFYIPPISFFGEGALEETADYIKNKDYKKALIVTDPGIAAIGLSGRVQKMLEERDLNVAIYDKTQPNPNIANVTA 80
Cdd:PRK15454 18 LQRVKTFSVPPVTLCGPGAVSSCGQQAQTRGLKHLFVMADSFLHQAGMTAGLTRSLAVKGIAMTLWPCPVGEPCITDVCA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 81 GLKVLKEQNSEIVVSIGGGSAHDNAKAIALLATNGGEIGDYEGVNQSKKAALPLFAINTTAGTASEMTRFTIISNEEKKI 160
Cdd:PRK15454 98 AVAQLRESGCDGVIAFGGGSVLDAAKAVALLVTNPDSTLAEMSETSVLQPRLPLIAIPTTAGTGSETTNVTVIIDAVSGR 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 161 KMAIIDNNVTPAVAVNDPSTMFGLPPALTAATGLDALTHCIEAYVSTASNPITDACALKGIDLINESLVAAYKDGKDKKA 240
Cdd:PRK15454 178 KQVLAHASLMPDVAILDAALTEGVPSHVTAMTGIDALTHAIEAYSALNATPFTDSLAIGAIAMIGKSLPKAVGYGHDLAA 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 241 RTDMCYAEYLAGMAFNNASLGYVHALAHQLGGFYHLPHGVCNAVLLPHVQEAN-MQCpkaKKRLGEIALHFGASQEDPEE 319
Cdd:PRK15454 258 RESMLLASCMAGMAFSSAGLGLCHAMAHQPGAALHIPHGLANAMLLPTVMEFNrMVC---RERFSQIGRALRTKKSDDRD 334
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 320 TIKALHVLNRTMNIPRNLKELGVKTEDFEILAEHAMHDACHLTNPVQFTKEQVVAIIKKA 379
Cdd:PRK15454 335 AINAVSELIAEVGIGKRLGDVGATSAHYGAWAQAALEDICLRSNPRTASLEQIVGLYAAA 394
|
|
| Fe-ADH-like |
cd14864 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
7-380 |
2.56e-68 |
|
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: 219.87 E-value: 2.56e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 7 FYIPPISFFGEGALEETADYIKnKDYKKALIVTDPGIAAIGLSGRVQKMLEERDLNVAIYDKTQPNPNIANVTAGLKVLK 86
Cdd:cd14864 1 FKIPPNIVFGADSLERIGEEVK-EYGSRFLLITDPVLKESGLADKIVSSLEKAGISVIVFDEIPASATSDTIDEAAELAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 87 EQNSEIVVSIGGGSAHDNAKAIALLATNGGEIGDYEGVNQSKKAALPLFAINTTAGTASEMT-RFTIISNEEKKIKMAII 165
Cdd:cd14864 80 KAGADGIIAVGGGKVLDTAKAVAILANNDGGAYDFLEGAKPKKKPLPLIAVPTTPRSGFEFSdRFPVVDSRSREVKLLKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 166 DNNVtPAVAVNDPSTMFGLPPALTAATGLDALTHCIEAYVSTASNPITDACALKGIDLINESLVAAYKDGKDKKARTDMC 245
Cdd:cd14864 160 QPGL-PKAVIVDPNLMASLTGNQTAAMALAALALAVEAYLSKKSNFFSDALALKAIELVSENLDGALADPKNTPAEELLA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 246 YAEYLAGMAFNNASLGYVHALAHQLGGFYHLPHGVCNAVLLPHVQEANMqcPKAKKRLGEIALHFGASQE--DPEETIKA 323
Cdd:cd14864 239 QAGCLAGLAASSSSPGLATALALAVNSRYKVSKSLVASILLPHVIEYAA--TSAPDKYAKIARALGEDVEgaSPEEAAIA 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 205831682 324 ----LHVLNRTMNIPRNLKELGVKTeDFEILAEHAMHDACHLTNPVQFTKEQVVAIIKKAY 380
Cdd:cd14864 317 avegVRRLIAQLNLPTRLKDLDLAS-SLEQLAAIAEDAPKLNGLPRSMSSDDIFDILKAAF 376
|
|
| Fe-ADH-like |
cd08186 |
Iron-containing alcohol dehydrogenase; This family contains iron-containing alcohol ... |
14-379 |
2.69e-64 |
|
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: 209.43 E-value: 2.69e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 14 FFGEGALEETADYIKNKDYKKALIVTDPGIA-AIGLSGRVQKMLEERDLNVAIYDKTQPNPNIANVTAGLKVLKEQNSEI 92
Cdd:cd08186 5 YFGVGAIAKIKDILKDLGIDKVIIVTGRSSYkKSGAWDDVEKALEENGIEYVVYDKVTPNPTVDQADEAAKLARDFGADA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 93 VVSIGGGSAHDNAKAIALLATNGGEIGD--YEGVNQSKKAaLPLFAINTTAGTASEMTRFTIISNEEKKIKMAIIDNNVT 170
Cdd:cd08186 85 VIAIGGGSPIDTAKSVAVLLAYGGKTARdlYGFRFAPERA-LPLVAINLTHGTGSEVDRFAVATIPEKGYKPGIAYDCIY 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 171 PAVAVNDPSTMFGLPPALTAATGLDALTHCIEAYVSTASNPITDACALKGIDLINESLVAAYKDGKDKKARTDMCYAEYL 250
Cdd:cd08186 164 PLYAIDDPRLTLTLPKEQTLYTSIDAFNHVYEAATTKVSSPYVITLAKEAIRLIAEYLPRALANPKDLEARYWLLYASMI 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 251 AGMAFNNASLGYVHALAHQLGGFY-HLPHGVCNAVLLPHVQEanmQCPKAK-----KRLGEIALHFGASQEDPEETIKAL 324
Cdd:cd08186 244 AGIAIDNGLLHLTHALEHPLSGLKpELPHGLGLALLGPAVVK---YIYKAVpetlaDILRPIVPGLKGTPDEAEKAARGV 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 205831682 325 HVLNRTMNIPRNLKELGVKTEDFEILAEHAM----HDACHLTNPVQFTKEQVVAIIKKA 379
Cdd:cd08186 321 EEFLFSVGFTEKLSDYGFTEDDVDRLVELAFttpsLDLLLSLAPVEVTEEVVREIYEES 379
|
|
| MAR |
cd08177 |
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic ... |
15-380 |
1.43e-63 |
|
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: 206.20 E-value: 1.43e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 15 FGEGALEETADYIKNKDYKKALIVTDPGIAAigLSGRVQKMLeeRDLNVAIYDKTQPNPNIANVTAGLKVLKEQNSEIVV 94
Cdd:cd08177 6 FGAGTLAELAEELERLGARRALVLSTPRQRA--LAERVAALL--GDRVAGVFDGAVMHVPVEVAERALAAAREAGADGLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 95 SIGGGSAHDNAKAIALlatnggeigdyegvnqskKAALPLFAINTT-AGtaSEMT-RFTIISNEEKKIKmaiIDNNVTPA 172
Cdd:cd08177 82 AIGGGSAIGLAKAIAL------------------RTGLPIVAVPTTyAG--SEMTpIWGETEDGVKTTG---RDPRVLPR 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 173 VAVNDPSTMFGLPPALTAATGLDALTHCIEAYVSTASNPITDACALKGIDLINESLVAAYKDGKDKKARTDMCYAEYLAG 252
Cdd:cd08177 139 TVIYDPDLTLGLPAALSVASGLNALAHAVEALYAPDANPITSLLAEEGIRALARALPRLVADPSDLEARSDALYGAWLAG 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 253 MAFNNASLGYVHALAHQLGGFYHLPHGVCNAVLLPHVQEANMqcPKAKKRLGEIALHFGAsqEDPEEtikALHVLNRTMN 332
Cdd:cd08177 219 VVLGSVGMGLHHKLCHVLGGTFDLPHAETHAVVLPHVLAYNA--PAAPDAMARLARALGG--GDAAG---GLYDLARRLG 291
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 205831682 333 IPRNLKELGVKTEDFEILAEHAMHDACHltNPVQFTKEQVVAIIKKAY 380
Cdd:cd08177 292 APTSLRDLGMPEDDIDRAADLALANPYP--NPRPVERDALRALLERAW 337
|
|
| YqdH |
COG1979 |
Alcohol dehydrogenase YqhD, Fe-dependent ADH family [Energy production and conversion]; |
7-380 |
3.07e-63 |
|
Alcohol dehydrogenase YqhD, Fe-dependent ADH family [Energy production and conversion];
Pssm-ID: 441582 [Multi-domain] Cd Length: 387 Bit Score: 206.85 E-value: 3.07e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 7 FYIPPISFFGEGALEETADYIKnKDYKKALIVTDPG-IAAIGLSGRVQKMLEERDLNVAIYDKTQPNPNIANVTAGLKVL 85
Cdd:COG1979 6 FYNPTKIIFGKGQIAKLGEEIP-KYGKKVLLVYGGGsIKKNGLYDQVKAALKEAGIEVVEFGGVEPNPRLETVRKGVELC 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 86 KEQNSEIVVSIGGGSAHDNAKAIALLATNGGEIGDYEGVNQSKKAALPLFAINTTAGTASEMTRFTIISNEEKKIKMAII 165
Cdd:COG1979 85 KEEGIDFILAVGGGSVIDGAKAIAAGAKYDGDPWDILTGKAPVEKALPLGTVLTLPATGSEMNSGSVITNEETKEKLGFG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 166 DNNVTPAVAVNDPSTMFGLPPALTAATGLDALTHCIEAYVS-TASNPITD--ACA-LKGidLINESLVaAYKDGKDKKAR 241
Cdd:COG1979 165 SPLVFPKFSILDPELTYTLPKRQTANGIVDIFSHVMEQYFTyPVDAPLQDrfAEGlLRT--LIEEGPK-ALKDPEDYDAR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 242 TDMCYAeylAGMAFNN-ASLGY-----VHALAHQLGGFYHLPHGVCNAVLLPHVQEANMQcpKAKKRLGEIALH-FGASQ 314
Cdd:COG1979 242 ANLMWA---ATLALNGlIGAGVpqdwaTHMIEHELSALYDIDHGAGLAIVLPAWMRYVLE--EKPEKFAQYAERvWGITE 316
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 205831682 315 EDPEET----IKALHVLNRTMNIPRNLKELGVKTEDFEILAEHAM-HDACHLTNPVQFTKEQVVAIIKKAY 380
Cdd:COG1979 317 GDDEERalegIEATEEFFESLGLPTRLSEYGIDEEDIEEMAEKATaHGMTALGEFKDLTPEDVREILELAL 387
|
|
| MAR-like |
cd08192 |
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic ... |
14-379 |
3.31e-59 |
|
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: 196.32 E-value: 3.31e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 14 FFGEGALEETADYIKNKDYKKALIVTDPGIA----AIGlsgRVQKMLEERdlNVAIYDKTQPNPNIANVTAGLKVLKEQN 89
Cdd:cd08192 5 SYGPGAVEALLHELATLGASRVFIVTSKSLAtktdVIK---RLEEALGDR--HVGVFSGVRQHTPREDVLEAARAVREAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 90 SEIVVSIGGGSAHDNAKAIALL----ATNGGEIGDYEGVNQS----KKAALPLFAINTTAgTASEMTRFTIISNEEKKIK 161
Cdd:cd08192 80 ADLLVSLGGGSPIDAAKAVALAlaedVTDVDQLDALEDGKRIdpnvTGPTLPHIAIPTTL-SGAEFTAGAGATDDDTGHK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 162 MAIIDNNVTPAVAVNDPSTMFGLPPALTAATGLDALTHCIEAYVSTASNPITDACALKGIDLINESLVAAYKDGKDKKAR 241
Cdd:cd08192 159 QGFAHPELGPDAVILDPELTLHTPERLWLSTGIRAVDHAVETLCSPQATPFVDALALKALRLLFEGLPRSKADPEDLEAR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 242 TDMCYAEYLAGMAF-NNASLGYVHALAHQLGGFYHLPHGVCNAVLLPHVQEANMqcPKAKKRLGEIALHFGASQEDPEET 320
Cdd:cd08192 239 LKCQLAAWLSLFGLgSGVPMGASHAIGHQLGPLYGVPHGITSCIMLPAVLRFNA--PVNAERQRLIARALGLVTGGLGRE 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 205831682 321 IKALHV----LNRTMNIPRNLKELGVKTEDFEILAEHAMHDACHLTNPVQ-FTKEQVVAIIKKA 379
Cdd:cd08192 317 AADAADaidaLIRELGLPRTLRDVGVGRDQLEKIAENALTDVWCRTNPRPiTDKDDVLEILESA 380
|
|
| Fe-ADH-like |
cd14866 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
14-379 |
3.25e-56 |
|
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: 188.59 E-value: 3.25e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 14 FFGEGALEETADYIKNKDYKKALIVTDPGIAAIG-LSGRVQKMLEERdlNVAIYDKTQPNPNIANVTAGLKVLKEQNSEI 92
Cdd:cd14866 9 FSGRGALARLGRELDRLGARRALVVCGSSVGANPdLMDPVRAALGDR--LAGVFDGVRPHSPLETVEAAAEALREADADA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 93 VVSIGGGSAHDNAKAIALLATNGGEIGDY------EGVNQS---KKAALPLFAINTTAGTASeMTRFTIISNEEKKIKMA 163
Cdd:cd14866 87 VVAVGGGSAIVTARAASILLAEDRDVRELctrraeDGLMVSprlDAPKLPIFVVPTTPTTAD-VKAGSAVTDPPAGQRLA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 164 IIDNNVTPAVAVNDPSTMFGLPPALTAATGLDALTHCIEAYVSTASNPITDACALKGIDLINESLVAAyKDGKDKKARTD 243
Cdd:cd14866 166 LFDPKTRPAAVFYDPELLATAPASLVAGAAMNGFDMAVEGLYSRHADPLADATLMHALRLLADGLPRL-ADDDDPAARAD 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 244 MCYAEYLAGMAFNNASLGYVHALAHQLGGFYHLPHGVCNAVLLPHVQEANMqcPKAKKRLGEIALHFGASQEDPEET--- 320
Cdd:cd14866 245 LVLAAVLAGYGTDHTGGGVIHALGHAIGARYGVQNGVVHAILLPHVLRFNA--PATDGRLDRLAEALGVADAGDEASaaa 322
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 205831682 321 -IKALHVLNRTMNIPRNLKELGVKTEDFEILAEHAMHDACHLTNPVQF-TKEQVVAIIKKA 379
Cdd:cd14866 323 vVDAVEALLDALGVPTRLRDLGVSREDLPAIAEAAMDDWFMDNNPRPVpTAEELEALLEAA 383
|
|
| 4HBD_NAD |
cd14860 |
4-hydroxybutyrate dehydrogenase, also called gamma-hydroxybutyrate dehydrogenase, catalyzes ... |
66-380 |
1.66e-37 |
|
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: 138.89 E-value: 1.66e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 66 YDKTQPNPNIANvtAGLKVLKEQNSEIVVSIGGGSAHDNAKAIALlATNGGEIGDYEGVNQSKKAAlPLFAINTTAGTAS 145
Cdd:cd14860 57 YGTGEPSDEMVE--AIYKDIKKYGYKRVIAIGGGTVIDIAKLLAL-KGISPVLDLFDGKIPLIKEK-ELIIVPTTCGTGS 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 146 EMTRFTIISNEEKKIKMAIIDNNVTPAVAVNDPSTMFGLPPALTAATGLDALTHCIEAYVSTASNPITDACALKGIDLIN 225
Cdd:cd14860 133 EVTNISIVELTSLGTKKGLAVDELYADKAVLIPELLKGLPYKVFATSSIDALIHAIESYLSPKATPYTEMFSYKAIEMIL 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 226 ESLVAAYKDGKDKKAR--TDMCYAEYLAGMAFNNASLGYVHALAHQLGGFYHLPHGVCNAVLLPHVqeanMQCPKAKKRL 303
Cdd:cd14860 213 EGYQEIAEKGEEARFPllGDFLIASNYAGIAFGNAGCAAVHALSYPLGGKYHVPHGEANYAVFTGV----LKNYQEKNPD 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 304 GEI-------ALHFGASQEDPEETIKALhvLNRTmnIPR-NLKELGVKTEDFEILAEHAMHDACHLT--NPVQFTKEQVV 373
Cdd:cd14860 289 GEIkklneflAKILGCDEEDVYDELEEL--LNKI--LPKkPLHEYGMKEEEIDEFADSVMENQQRLLanNYVPLDREDVA 364
|
....*..
gi 205831682 374 AIIKKAY 380
Cdd:cd14860 365 EIYKELY 371
|
|
| DHQ_Fe-ADH |
cd07766 |
Dehydroquinate synthase-like (DHQ-like) and iron-containing alcohol dehydrogenases (Fe-ADH); ... |
10-354 |
5.89e-34 |
|
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: 126.71 E-value: 5.89e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 10 PPISFFGEGALEETAdYIKNKDYKKALIVTDPGIAAiGLSGRVQKMLEERdLNVAIYDKTQPNPNIANVTAGLKVLKEQN 89
Cdd:cd07766 1 PTRIVFGEGAIAKLG-EIKRRGFDRALVVSDEGVVK-GVGEKVADSLKKG-LAVAIFDFVGENPTFEEVKNAVERARAAE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 90 SEIVVSIGGGSAHDNAKAIALLAtnggeigdyegvnqskKAALPLFAINTTAGTASEMTRFTIISNEEKKIKMaiIDNNV 169
Cdd:cd07766 78 ADAVIAVGGGSTLDTAKAVAALL----------------NRGIPFIIVPTTASTDSEVSPKSVITDKGGKNKQ--VGPHY 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 170 TPAVAVNDPSTMFGLPPALTAATGLDALTHCIEayvstasnpitdacalkgidlineslvaaykdgkdkkaRTDMCYAEY 249
Cdd:cd07766 140 NPDVVFVDTDITKGLPPRQVASGGVDALAHAVE--------------------------------------LEKVVEAAT 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 250 LAGMA-FNNASLGYVHALAHQLGGFYHLPHGVCNAVLLPHVQEANmqcpKAKKRLGEIAlhfgasqedpeetIKALHVLN 328
Cdd:cd07766 182 LAGMGlFESPGLGLAHAIGHALTAFEGIPHGEAVAVGLPYVLKVA----NDMNPEPEAA-------------IEAVFKFL 244
|
330 340
....*....|....*....|....*.
gi 205831682 329 RTMNIPRNLKELGVKTEDFEILAEHA 354
Cdd:cd07766 245 EDLGLPTHLADLGVSKEDIPKLAEKA 270
|
|
| Fe-ADH_KdnB-like |
cd08184 |
Iron-containing alcohol dehydrogenase similar to Shewanella oneidensis KdnB required for Kdo8N ... |
10-291 |
3.57e-31 |
|
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: 121.22 E-value: 3.57e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 10 PPISFFGEGALEETADYIKNK---DYKKALIVTDPGIAAIGLSGRVQkmLEERDLnvAIYDKTQPNPN---IANVTAGLK 83
Cdd:cd08184 1 VPKYLFGRGSFDQLGELLAERrksNNDYVVFFIDDVFKGKPLLDRLP--LQNGDL--LIFVDTTDEPKtdqIDALRAQIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 84 VLKEQNSEIVVSIGGGSAHDNAKAIALLATNGGEIGDYEGVNQSKKAALPLFAINTTAGTASEMTRFTIISNEEKKIKMa 163
Cdd:cd08184 77 AENDKLPAAVVGIGGGSTMDIAKAVSNMLTNPGSAADYQGWDLVKNPGIYKIGVPTLSGTGAEASRTAVLTGPEKKLGI- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 164 iidnnvtpavavNDPSTMFG---LPPALTAA--------TGLDALTHCIEAYVSTASNPITDACALKGIDLINEslVAAY 232
Cdd:cd08184 156 ------------NSDYTVFDqviLDPELIATvprdqyfyTGMDCYIHCVESLNGTYRNAFGDAYAEKALELCRD--VFLS 221
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 205831682 233 KDGKDKKARTDMCYAEYLAGMAFNNASLGYVHALAHQLGGFYHLPHGVCNAVLLPHVQE 291
Cdd:cd08184 222 DDMMSPENREKLMVASYLGGSSIANSQVGVCHALSYGLSVVLGTHHGVANCIVFNVLEE 280
|
|
| GldA |
COG0371 |
Glycerol dehydrogenase or related enzyme, iron-containing ADH family [Energy production and ... |
7-379 |
2.58e-19 |
|
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: 87.91 E-value: 2.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 7 FYIPPISFFGEGALEETADYIKNKDyKKALIVTDPGIAAIgLSGRVQKMLEERDLNVAIYdKTQPNPNIANVTAGLKVLK 86
Cdd:COG0371 3 IILPRRYVQGEGALDELGEYLADLG-KRALIITGPTALKA-AGDRLEESLEDAGIEVEVE-VFGGECSEEEIERLAEEAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 87 EQNSEIVVSIGGGSAHDNAKAIAllatnggeigdyegvnqsKKAALPLFAINTTAGTASEMTRFTIISNEEKK-IKMAII 165
Cdd:COG0371 80 EQGADVIIGVGGGKALDTAKAVA------------------YRLGLPVVSVPTIASTDAPASPLSVIYTEDGAfDGYSFL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 166 DNNvtPAVAVNDPSTMFGLPPALTAAtGL-DALTHCIEAYVSTASN------PITDAC---ALKGIDLINESLVAAYKDG 235
Cdd:COG0371 142 AKN--PDLVLVDTDIIAKAPVRLLAA-GIgDALAKWYEARDWSLAHrdlageYYTEAAvalARLCAETLLEYGEAAIKAV 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 236 KDKKARTD----MCYAEYLAGMAFN----NASLGYVHALAH---QLGGFYHLPHG----VCNAVLLphvqeanmqcpkak 300
Cdd:COG0371 219 EAGVVTPAlervVEANLLLSGLAMGigssRPGSGAAHAIHNgltALPETHHALHGekvaFGTLVQL-------------- 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 301 krlgeiALHfgasqEDPEEtIKALHVLNRTMNIPRNLKELGVKTEDFEIL---AEHAMHDACHLTN-PVQFTKEQVVAII 376
Cdd:COG0371 285 ------VLE-----GRPEE-IEELLDFLRSVGLPTTLADLGLDDETEEELltvAEAARPERYTILNlPFEVTPEAVEAAI 352
|
...
gi 205831682 377 KKA 379
Cdd:COG0371 353 LAT 355
|
|
| PRK15138 |
PRK15138 |
alcohol dehydrogenase; |
15-355 |
1.47e-17 |
|
alcohol dehydrogenase;
Pssm-ID: 185092 [Multi-domain] Cd Length: 387 Bit Score: 83.31 E-value: 1.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 15 FGEGALEETADYIKNKdyKKALIVTDPG-IAAIGLSGRVQKMLEERDlnVAIYDKTQPNPNIANVTAGLKVLKEQNSEIV 93
Cdd:PRK15138 14 FGKGAIAGLREQIPAD--ARVLITYGGGsVKKTGVLDQVLDALKGMD--VLEFGGIEPNPTYETLMKAVKLVREEKITFL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 94 VSIGGGSAHDNAKAIA-------------LLATNGGEIgdyegvnqskKAALPLFAINTTAGTASEMTRFTIISNEEKKI 160
Cdd:PRK15138 90 LAVGGGSVLDGTKFIAaaanypenidpwhILETGGKEI----------KSAIPMGSVLTLPATGSESNAGAVISRKTTGD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 161 KMAIIDNNVTPAVAVNDPSTMFGLPPALTAATGLDALTHCIEAYVSTASN-PITDACAlKGIDL-INESLVAAYKDGKDK 238
Cdd:PRK15138 160 KQAFHSPHVQPVFAVLDPVYTYTLPPRQVANGVVDAFVHTVEQYVTYPVDaKIQDRFA-EGILLtLIEEGPKALKEPENY 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 239 KARTDMCYAeylAGMAFNNASLGYV------HALAHQLGGFYHLPHGVCNAVLLPHVQEANMQCPKAKkrLGEIA----- 307
Cdd:PRK15138 239 DVRANVMWA---ATQALNGLIGAGVpqdwatHMLGHELTAMHGLDHAQTLAIVLPALWNEKRDTKRAK--LLQYAervwn 313
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 205831682 308 LHFGASQEDPEETIKALHVLNRTMNIPRNLKELGVKTEDFEI----LAEHAM 355
Cdd:PRK15138 314 ITEGSDDERIDAAIAATRNFFEQMGVPTRLSDYGLDGSSIPAllkkLEEHGM 365
|
|
| Fe-ADH_2 |
pfam13685 |
Iron-containing alcohol dehydrogenase; |
15-279 |
2.38e-14 |
|
Iron-containing alcohol dehydrogenase;
Pssm-ID: 404557 [Multi-domain] Cd Length: 251 Bit Score: 71.95 E-value: 2.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 15 FGEGALEETADYIKNKDYKKALIVTDPGIAAIgLSGRVQKMLEERDLNVAIYDKTQPNPNIANVTAGLKVLKEQNSEIVV 94
Cdd:pfam13685 2 IGPGALGRLGEYLAELGFRRVALVADANTYAA-AGRKVAESLKRAGIEVETRLEVAGNADMETAEKLVGALRERDADAVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 95 SIGGGSAHDNAKAIALlatnggeigdyegvnqskKAALPLFAINTTA---GTASemTRFTIISNEEKKIKMAiidnnVTP 171
Cdd:pfam13685 81 GVGGGTVIDLAKYAAF------------------KLGKPFISVPTAAsndGFAS--PGASLTVDGKKRSIPA-----AAP 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 172 AVAVNDPSTMFGLPPALTAATGLDALTHCIEAYVSTASN--PITDACALKGIDLINESLVAAYKDGKDKKARTDMCYAEY 249
Cdd:pfam13685 136 FGVIADTDVIAAAPRRLLASGVGDLLAKITAVADWELAHaeEVAAPLALLSAAMVMNFADRPLRDPGDIEALAELLSALA 215
|
250 260 270
....*....|....*....|....*....|..
gi 205831682 250 LAGMAFNNASLGYVHALAHQLGGFY--HLPHG 279
Cdd:pfam13685 216 MGGAGSSRPASGSEHLISHALDMIApkQALHG 247
|
|
| GlyDH-like |
cd08550 |
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins. ... |
16-379 |
2.91e-11 |
|
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins. Glycerol dehydrogenases (GlyDH) is a key enzyme in the glycerol dissimilation pathway. In anaerobic conditions, many microorganisms utilize glycerol as a source of carbon through coupled oxidative and reductive pathways. One of the pathways involves the oxidation of glycerol to dihydroxyacetone with the reduction of NAD+ to NADH catalyzed by glycerol dehydrogenases. Dihydroxyacetone is then phosphorylated by dihydroxyacetone kinase and enters the glycolytic pathway for further degradation. The activity of GlyDH is zinc-dependent; the zinc ion plays a role in stabilizing an alkoxide intermediate at the active site. Some subfamilies have yet to be characterized.
Pssm-ID: 341480 [Multi-domain] Cd Length: 347 Bit Score: 64.09 E-value: 2.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 16 GEGALEETADYIKnKDYKKALIVTDP-GIAAIGlsGRVQKMLEER--DLNVAIYdktQPNPNIANVTAGLKVLKEQNSEI 92
Cdd:cd08550 7 EPGILAKAGEYIA-PLGKKALIIGGKtALEAVG--EKLEKSLEEAgiDYEVEVF---GGECTEENIERLAEKAKEEGADV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 93 VVSIGGGSAHDNAKAIALlatnggeigdyegvnqskKAALPLFAINTTAGTASEMTRFTIISNEEKKIKmAIIDNNVTPA 172
Cdd:cd08550 81 IIGIGGGKVLDTAKAVAD------------------RLGLPVVTVPTIAATCAAWSALSVLYDEEGEFL-GYSLLKRSPD 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 173 VAVNDPSTMFGLPPALTAATGLDALTHCIEAYVSTASNP--ITDACALK----GIDLINESLVAAYKDGKDKKAR----- 241
Cdd:cd08550 142 LVLVDTDIIAAAPVRYLAAGIGDTLAKWYEARPSSRGGPddLALQAAVQlaklAYDLLLEYGVQAVEDVRQGKVTpaled 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 242 -TDMCYaeYLAGMAFNNASLGYVHALAHqlgGFYhlpHGVCnavllphvqeanmQCPKAKKRL-GEI-AlhFG-----AS 313
Cdd:cd08550 222 vVDAII--LLAGLVGSLGGGGCRTAAAH---AIH---NGLT-------------KLPETHGTLhGEKvA--FGllvqlAL 278
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 205831682 314 QEDPEETIKALHVLNRTMNIPRNLKELGVKT--EDFEILAEHAMH---DACHLTNPVqfTKEQVVAIIKKA 379
Cdd:cd08550 279 EGRSEEEIEELIEFLRRLGLPVTLEDLGLELteEELRKIAEYACDppdMAHMLPFPV--TPEMLAEAILAA 347
|
|
| GlyDH |
cd08170 |
Glycerol dehydrogenases (GlyDH) catalyzes oxidation of glycerol to dihydroxyacetone in ... |
16-382 |
3.46e-07 |
|
Glycerol dehydrogenases (GlyDH) catalyzes oxidation of glycerol to dihydroxyacetone in glycerol dissmilation; Glycerol dehydrogenases (GlyDH) is a key enzyme in the glycerol dissimilation pathway. In anaerobic conditions, many microorganisms utilize glycerol as a source of carbon through coupled oxidative and reductive pathways. One of the pathways involves the oxidation of glycerol to dihydroxyacetone with the reduction of NAD+ to NADH catalyzed by glycerol dehydrogenases. Dihydroxyacetone is then phosphorylated by dihydroxyacetone kinase and enters the glycolytic pathway for further degradation. The activity of GlyDH is zinc-dependent; the zinc ion plays a role in stabilizing an alkoxide intermediate at the active site.
Pssm-ID: 341449 [Multi-domain] Cd Length: 351 Bit Score: 51.64 E-value: 3.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 16 GEGALEETADYIKnkDY-KKALIVTDPGIAAIgLSGRVQKMLEERDLNVAIYDKTQP--NPNIANVTAglkVLKEQNSEI 92
Cdd:cd08170 7 GPGALDRLGEYLA--PLgKKALVIADPFVLDL-VGERLEESLEKAGLEVVFEVFGGEcsREEIERLAA---IARANGADV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 93 VVSIGGGSAHDNAKAIAllatnggeigDYEGvnqskkaaLPLFAINTTAGTASEMTRFTIISNEE-KKIKMAIIDNNvtP 171
Cdd:cd08170 81 VIGIGGGKTIDTAKAVA----------DYLG--------LPVVIVPTIASTDAPCSALSVIYTEDgEFDEYLFLPRN--P 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 172 AVAVNDPSTMFGLPPALTAAtGL-DALTHCIEA---YVSTASNP-----------ITDACAlkgiDLINESLVAAYKDGK 236
Cdd:cd08170 141 DLVLVDTEIIAKAPVRFLVA-GMgDALATYFEAracARSGAPNMaggrptlaalaLAELCY----DTLLEYGVAAKAAVE 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 237 DKK----------ARTdmcyaeYLAGMAFNNASLGYVHALAH---QLGGFYHLPHG-------VCNAVLlphvqEanmqc 296
Cdd:cd08170 216 AGVvtpaleavieANT------LLSGLGFESGGLAAAHAIHNgltALPETHHLLHGekvafgtLVQLVL-----E----- 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 297 pkakkrlgeialhfGASQEDPEETIKalhvLNRTMNIPRNLKELGVK---TEDFEILAEHAMhDACHLTN--PVQFTKEQ 371
Cdd:cd08170 280 --------------GRPDEEIEEVIR----FCRSVGLPVTLADLGLEdvtDEELRKVAEAAC-APGETIHnmPFPVTPED 340
|
410
....*....|.
gi 205831682 372 VVAIIKKAYEY 382
Cdd:cd08170 341 VVDAILAADAL 351
|
|
| Gro1PDH |
cd08173 |
Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) catalyzes the reversible conversion between ... |
15-145 |
1.38e-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: 49.86 E-value: 1.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 15 FGEGALEETADYIKNKDY-KKALIVTDPGIAAIgLSGRVQKMLEERDLNVAIYDKTQPNpNIANVTAGLKVLKEQNSEIV 93
Cdd:cd08173 7 VGHGAINKIGEVLKKLLLgKRALIITGPNTYKI-AGKRVEDLLESSGVEVVIVDIATIE-EAAEVEKVKKLIKESKADFI 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 205831682 94 VSIGGGSAHDNAKAIAllatnggeigdyegvnqsKKAALPLFAINTTA---GTAS 145
Cdd:cd08173 85 IGVGGGKVIDVAKYAA------------------YKLNLPFISIPTSAshdGIAS 121
|
|
| gldA |
PRK09423 |
glycerol dehydrogenase; Provisional |
16-109 |
1.58e-06 |
|
glycerol dehydrogenase; Provisional
Pssm-ID: 181843 Cd Length: 366 Bit Score: 49.43 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 16 GEGALEETADYIKnkDY-KKALIVTDPGIAAIgLSGRVQKMLEERDLNVAiYDKTQPNPNIANVTAGLKVLKEQNSEIVV 94
Cdd:PRK09423 14 GKGALARLGEYLK--PLgKRALVIADEFVLGI-VGDRVEASLKEAGLTVV-FEVFNGECSDNEIDRLVAIAEENGCDVVI 89
|
90
....*....|....*
gi 205831682 95 SIGGGSAHDNAKAIA 109
Cdd:PRK09423 90 GIGGGKTLDTAKAVA 104
|
|
| G1PDH_related |
cd08549 |
Glycerol-1-phosphate dehydrogenase and related proteins; This family contains bacterial and ... |
10-191 |
8.36e-06 |
|
Glycerol-1-phosphate dehydrogenase and related proteins; This family contains bacterial and archeal glycerol-1-phosphate dehydrogenase-like oxidoreductases. These proteins have similarity with glycerol-1-phosphate dehydrogenase (G1PDH) which plays a role in the synthesis of phosphoglycerolipids in gram-positive bacterial species. It catalyzes the reversibly reduction of dihydroxyacetone phosphate (DHAP) to glycerol-1-phosphate (G1P) in a NADH-dependent manner. Its activity requires Ni++ ion. It also contains archaeal Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) that plays an important role in the formation of the enantiomeric configuration of the glycerophosphate backbone (sn-glycerol-1-phosphate) of archaeal ether lipids.
Pssm-ID: 341479 [Multi-domain] Cd Length: 331 Bit Score: 47.17 E-value: 8.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 10 PPISFFGEGALEETADYIKNKDYKKALIVTDPGIAAIgLSGRVQKMLEERDLnvaiydkTQPNPNIANVTAGLKvlKEQN 89
Cdd:cd08549 1 PRYTIVGDGAINKIEEILKKLNLKRVLIITGKNTKAK-YCRFFYDQLKTVCD-------IVYYDNIDNLEDELK--KYTF 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 90 SEIVVSIGGGSAHDNAKAIALlatnggeigdyegvnqskKAALPLFAINTTA---GTASEMTRFTIisNEEKKIKMAiid 166
Cdd:cd08549 71 YDCVIGIGGGRSIDTGKYLAY------------------KLKIPFISVPTSAsndGIASPIVSLRI--PGVKKTFMA--- 127
|
170 180
....*....|....*....|....*
gi 205831682 167 nnVTPAVAVNDPSTMFGLPPALTAA 191
Cdd:cd08549 128 --DAPIAIIADTEIIKKSPRRLLSA 150
|
|
| GlyDH-like |
cd08172 |
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins ... |
16-378 |
3.80e-04 |
|
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins that have yet to be characterized, but show sequence homology with glycerol dehydrogenase. Glycerol dehydrogenases (GlyDH) is a key enzyme in the glycerol dissimilation pathway. In anaerobic conditions, many microorganisms utilize glycerol as a source of carbon through coupled oxidative and reductive pathways. One of the pathways involves the oxidation of glycerol to dihydroxyacetone with the reduction of NAD+ to NADH catalyzed by glycerol dehydrogenases. Dihydroxyacetone is then phosphorylated by dihydroxyacetone kinase and enters the glycolytic pathway for further degradation. The activity of GlyDH is zinc-dependent; the zinc ion plays a role in stabilizing an alkoxide intermediate at the active site.
Pssm-ID: 341451 [Multi-domain] Cd Length: 346 Bit Score: 42.12 E-value: 3.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 16 GEGALEETADYIKNKDYKKALIVTDP-GIAAiglsgrVQKML---EERDLNVAIYDKTQPNPNIANVTaglKVLKEQNSE 91
Cdd:cd08172 7 EEGALKELPELLSEFGIKRPLIIHGEkSWQA------AKPYLpklFEIEYPVLRYDGECSYEEIDRLA---EEAKEHQAD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 92 IVVSIGGGSAHDNAKAIAllatnggeigdyegvnqsKKAALPLFAINTTAGTASEMTRFTIISNEEKKIKMAIIDNNVTP 171
Cdd:cd08172 78 VIIGIGGGKVLDTAKAVA------------------DKLNIPLILIPTLASNCAAWTPLSVIYDEDGEFIGYDYFPRSAY 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 172 AVAVnDPSTMFGLPPALTAAtGL-DALTHCIEAYV---STASNPITDACALKGIDLINESLVaayKDGKDKkartdmcya 247
Cdd:cd08172 140 LVLV-DPRLLLDSPKDYFVA-GIgDTLAKWYEADAilrQLEELPAFLQLARQAAKLCRDILL---KDSEQA--------- 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 248 eyLAGMAFNNASLGYVH------ALAHQLGGF---Y---HLPHGVCNAVllphvqeanMQCPKAKKRL-GEI-------- 306
Cdd:cd08172 206 --LADLEAGKLTPAFIKvvetiiALAGMVGGFgdeYgrsAGAHAIHNGL---------TKLPETHHFLhGEKvaygilvq 274
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 205831682 307 -ALhfgasqEDPEETIKALHVLNRTMNIPRNLKELGVK---TEDFEILAEHAMHDAC-HLTNPVQFTKEQVVAIIKK 378
Cdd:cd08172 275 lAL------EGKWDEIKKLLPFYRRLGLPTSLADLGLTddtEEALQKIAAFAASPEEsIHLLPPDVTAEEVLQAIEK 345
|
|
| G1PDH |
cd08175 |
Glycerol-1-phosphate dehydrogenase (G1PDH) catalyzes the reversible reduction of ... |
16-109 |
4.23e-04 |
|
Glycerol-1-phosphate dehydrogenase (G1PDH) catalyzes the reversible reduction of dihydroxyacetone phosphate (DHAP) to glycerol-1-phosphate (G1P) in an NADH-dependent manner; Glycerol-1-phosphate dehydrogenase (G1PDH) 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 a Ni++ ion. In Bacillus subtilis, it has been described as AraM gene in L-arabinose (ara) operon. AraM protein forms homodimer.
Pssm-ID: 341454 Cd Length: 340 Bit Score: 42.11 E-value: 4.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 16 GEGALEETADYIKNKD-YKKALIVTDPGI-AAIGLsgRVQKMLEERDLNVAIY---DKTQPNPNIANVTAGLKVLKEQNs 90
Cdd:cd08175 7 GEGALKKLPEYLKELFgGKKVLVVADENTyAAAGE--EVEAALEEAGVTVCLLifpGEGDLIADEAAVGKVLLELEKDT- 83
|
90
....*....|....*....
gi 205831682 91 EIVVSIGGGSAHDNAKAIA 109
Cdd:cd08175 84 DLIIAVGSGTINDLTKYAA 102
|
|
| DHQS |
cd08195 |
Dehydroquinate synthase (DHQS) catalyzes the conversion of DAHP to DHQ in shikimate pathway ... |
14-99 |
2.67e-03 |
|
Dehydroquinate synthase (DHQS) catalyzes the conversion of DAHP to DHQ in shikimate pathway for aromatic compounds synthesis; Dehydroquinate synthase (DHQS) catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate-7-phosphate (DAHP) to dehydroquinate (DHQ) in the second step of the shikimate pathway. This pathway, which involves seven sequential enzymatic steps in the conversion of erythrose 4-phosphate and phosphoenolpyruvate into chorismate for subsequent synthesis of aromatic compounds, is found in bacteria, microbial eukaryotes, and plants, but not in mammals. Therefore, enzymes of this pathway are attractive targets for the development of non-toxic antimicrobial compounds, herbicides and anti-parasitic agents. The activity of DHQS requires nicotinamide adenine dinucleotide (NAD) as cofactor. A single active site in DHQS catalyzes five sequential reactions involving alcohol oxidation, phosphate elimination, carbonyl reduction, ring opening, and intramolecular aldol condensation. The binding of substrates and ligands induces domain conformational changes. In some fungi and protozoa, this domain is fused with the other four domains in shikimate pathway and forms a penta-domain AROM protein, which catalyzes steps 2-6 in the shikimate pathway.
Pssm-ID: 341474 Cd Length: 343 Bit Score: 39.35 E-value: 2.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205831682 14 FFGEGALEETADYIKNKDYKKALIVTDPGIAAIGLSgRVQKMLEERDLNVAIYD-------KtqpnpNIANVTAGLKVLK 86
Cdd:cd08195 5 LIGSGLLDKLGELLELKKGSKVVIVTDENVAKLYGE-LLLKSLEAAGFKVEVIVipageksK-----SLETVERIYDFLL 78
|
90
....*....|....*.
gi 205831682 87 EQN---SEIVVSIGGG 99
Cdd:cd08195 79 EAGldrDSLLIALGGG 94
|
|
| |
