|
Name |
Accession |
Description |
Interval |
E-value |
| PDDH |
cd08188 |
1,3-Propanediol (1,3-PD) dehydrogenase; This family includes 1,3-propanediol (1,3-PD) ... |
6-384 |
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: 636.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 6 YDFLVPNVNFFGPGAVSVVGERCKLLGGKKALLVTDKGLraIKDGAVDQTVKHLREAGIDVVIFDGVEPNPKDTNVRDGL 85
Cdd:cd08188 1 FRFYIPPVNLFGPGCLKEIGDELKKLGGKKALIVTDKGL--VKLGLVKKVTDVLEEAGIEYVIFDGVQPNPTVTNVNEGL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 86 AVFQKEHCDMIITVGGGSPHDCGKGIGIAATHPGDLYSYAGIETLTHALPPIIAVNTTAGTASEVTRHCVLTNTKTKVKF 165
Cdd:cd08188 79 ELFKENGCDFIISVGGGSAHDCAKAIGILATNGGEIEDYEGVDKSKKPGLPLIAINTTAGTASEVTRFAVITDEERHVKM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 166 VIVSWRNLPSVSINDPLLMVGKPAGLTAATGMDALTHAVEAYISKDANPVTDASAIQAIKLIATNLRQAVALGTNIKARE 245
Cdd:cd08188 159 VIVDWNVTPTIAVNDPELMLGMPPSLTAATGMDALTHAIEAYVSTGATPLTDALALEAIRLIAENLPKAVANGKDLEARE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 246 NMACASLLAGMAFNNANLGYVHAMAHQLGGLYDMAHGVANAVLLPHVCRYNLIANPEKFADIATFMGENTTGLSTMDAAE 325
Cdd:cd08188 239 NMAYAQFLAGMAFNNAGLGYVHAMAHQLGGFYNLPHGVCNAILLPHVMEFNLPACPERFADIARALGENTEGLSDEEAAE 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 490200396 326 CAINAIARLSKDVGIPQHLNELGVKEADFPYMAEMALKDGNAFSNPRKGNEKEIVEIFR 384
Cdd:cd08188 319 AAIEAIRKLSRRVGIPSGLKELGVKEEDFPLLAENALKDACGPTNPRQATKEDVIAIYR 377
|
|
| EutG |
COG1454 |
Alcohol dehydrogenase, class IV [Energy production and conversion]; |
4-387 |
0e+00 |
|
Alcohol dehydrogenase, class IV [Energy production and conversion];
Pssm-ID: 441063 [Multi-domain] Cd Length: 381 Bit Score: 528.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 4 RMYDFLVPNVNFFGPGAVSVVGERCKLLGGKKALLVTDKGLRAIkdGAVDQTVKHLREAGIDVVIFDGVEPNPKDTNVRD 83
Cdd:COG1454 1 MMFTFRLPTRIVFGAGALAELGEELKRLGAKRALIVTDPGLAKL--GLLDRVLDALEAAGIEVVVFDDVEPNPTVETVEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 84 GLAVFQKEHCDMIITVGGGSPHDCGKGIGIAATHPGDLYSYAGIETLTHALPPIIAVNTTAGTASEVTRHCVLTNTKTKV 163
Cdd:COG1454 79 GAAAAREFGADVVIALGGGSAIDAAKAIALLATNPGDLEDYLGIKKVPGPPLPLIAIPTTAGTGSEVTPFAVITDPETGV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 164 KFVIVSWRNLPSVSINDPLLMVGKPAGLTAATGMDALTHAVEAYISKDANPVTDASAIQAIKLIATNLRQAVALGTNIKA 243
Cdd:COG1454 159 KKGIADPELLPDVAILDPELTLTLPPSLTAATGMDALTHAIEAYVSKGANPLTDALALEAIRLIARNLPRAVADGDDLEA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 244 RENMACASLLAGMAFNNANLGYVHAMAHQLGGLYDMAHGVANAVLLPHVCRYNLIANPEKFADIATFMGENtTGLSTMDA 323
Cdd:COG1454 239 REKMALASLLAGMAFANAGLGAVHALAHPLGGLFHVPHGLANAILLPHVLRFNAPAAPERYAEIARALGLD-VGLSDEEA 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490200396 324 AECAINAIARLSKDVGIPQHLNELGVKEADFPYMAEMALKDGNAFSNPRKGNEKEIVEIFRQAF 387
Cdd:COG1454 318 AEALIEAIRELLRDLGIPTRLSELGVTEEDLPELAELALADRCLANNPRPLTEEDIEAILRAAY 381
|
|
| LPO |
cd08176 |
Lactadehyde:propanediol oxidoreductase (LPO) catalyzes the interconversion between ... |
8-384 |
0e+00 |
|
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: 510.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 8 FLVPNVNFFGPGAVSVVGERCKLLGGKKALLVTDKGLraIKDGAVDQTVKHLREAGIDVVIFDGVEPNPKDTNVRDGLAV 87
Cdd:cd08176 3 FVLNPTSYFGWGAIEEIGEEAKKRGFKKALIVTDKGL--VKFGIVDKVTDVLKEAGIAYTVFDEVKPNPTIENVMAGVAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 88 FQKEHCDMIITVGGGSPHDCGKGIGIAATHPG-DLYSYAGIETLTHALPPIIAVNTTAGTASEVTRHCVLTNTKTKVKFV 166
Cdd:cd08176 81 YKESGADGIIAVGGGSSIDTAKAIGIIVANPGaDVRSLEGVAPTKNPAVPIIAVPTTAGTGSEVTINYVITDTEKKRKFV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 167 IVSWRNLPSVSINDPLLMVGKPAGLTAATGMDALTHAVEAYISKDANPVTDASAIQAIKLIATNLRQAVALGTNIKAREN 246
Cdd:cd08176 161 CVDPHDIPTVAIVDPDLMSSMPKGLTAATGMDALTHAIEGYITKGAWELSDMLALKAIELIAKNLRKAVANPNNVEAREN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 247 MACASLLAGMAFNNANLGYVHAMAHQLGGLYDMAHGVANAVLLPHVCRYNLIANPEKFADIATFMGENTTGLSTMDAAEC 326
Cdd:cd08176 241 MALAQYIAGMAFSNVGLGIVHSMAHPLSAFYDTPHGVANAILLPYVMEFNAPATGEKYRDIARAMGVDTTGMSDEEAAEA 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 490200396 327 AINAIARLSKDVGIPQHLNELGVKEADFPYMAEMALKDGNAFSNPRKGNEKEIVEIFR 384
Cdd:cd08176 321 AVDAVKKLSKDVGIPQKLSELGVKEEDIEALAEDALNDVCTPGNPREATKEDIIALYK 378
|
|
| Fe-ADH |
cd08551 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains large ... |
11-383 |
2.88e-179 |
|
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: 502.75 E-value: 2.88e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 11 PNVNFFGPGAVSVVGERCKLLGGKKALLVTDKGLRAIkdGAVDQTVKHLREAGIDVVIFDGVEPNPKDTNVRDGLAVFQK 90
Cdd:cd08551 1 PTRIVFGAGALARLGEELKALGGKKVLLVTDPGLVKA--GLLDKVLESLKAAGIEVEVFDDVEPNPTVETVEAAAELARE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 91 EHCDMIITVGGGSPHDCGKGIGIAATHPGDLYSYAGIETLTHALPPIIAVNTTAGTASEVTRHCVLTNTKTKVKFVIVSW 170
Cdd:cd08551 79 EGADLVIAVGGGSVLDTAKAIAVLATNGGSIRDYEGIGKVPKPGLPLIAIPTTAGTGSEVTPNAVITDPETGRKMGIVSP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 171 RNLPSVSINDPLLMVGKPAGLTAATGMDALTHAVEAYISKDANPVTDASAIQAIKLIATNLRQAVALGTNIKARENMACA 250
Cdd:cd08551 159 YLLPDVAILDPELTLSLPPSVTAATGMDALTHAIEAYTSKKANPISDALALEAIRLIGKNLRRAVADGSDLEAREAMLLA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 251 SLLAGMAFNNANLGYVHAMAHQLGGLYDMAHGVANAVLLPHVCRYNLIANPEKFADIATFMGENTTGLSTMDAAECAINA 330
Cdd:cd08551 239 SLLAGIAFGNAGLGAVHALAYPLGGRYHIPHGVANAILLPYVMEFNLPACPEKYAEIAEALGEDVEGLSDEEAAEAAVEA 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 490200396 331 IARLSKDVGIPQHLNELGVKEADFPYMAEMALKDGN-AFSNPRKGNEKEIVEIF 383
Cdd:cd08551 319 VRELLRDLGIPTSLSELGVTEEDIPELAEDAMKSGRlLSNNPRPLTEEDIREIY 372
|
|
| Fe-ADH-like |
cd17814 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
8-383 |
9.27e-164 |
|
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: 463.55 E-value: 9.27e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 8 FLVPNVnFFGPGAVSVVGERCKLLGGKKALLVTDKGLRAIkdGAVDQTVKHLREAGIDVVIFDGVEPNPKDTNVRDGLAV 87
Cdd:cd17814 2 FVAPEF-IFGVGARKLAGRYAKNLGARKVLVVTDPGVIKA--GWVDEVLDSLEAEGLEYVVFSDVTPNPRDFEVMEGAEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 88 FQKEHCDMIITVGGGSPHDCGKGIGIAATHPGDLYSYAGIETLTHALPPIIAVNTTAGTASEVTRHCVLTNTKTKVKFVI 167
Cdd:cd17814 79 YREEGCDGIVAVGGGSPIDCAKGIGIVVSNGGHILDYEGVDKVRRPLPPLICIPTTAGSSADVSQFAIITDTERRVKMAI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 168 VSWRNLPSVSINDPLLMVGKPAGLTAATGMDALTHAVEAYISKDANPVTDASAIQAIKLIATNLRQAVALGTNIKARENM 247
Cdd:cd17814 159 ISKTLVPDVSLIDPETLTTMDPELTACTGMDALTHAIEAYVSNASSPLTDLHALEAIRLISENLPKAVADPDDLEAREKM 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 248 ACASLLAGMAFNNANLGYVHAMAHQLGGLYDMAHGVANAVLLPHVCRYNLIANPEKFADIATFMGENTTGLSTMDAAECA 327
Cdd:cd17814 239 MLASLQAGLAFSNASLGAVHAMAHSLGGLLDLPHGECNALLLPHVIRFNFPAAPERYRKIAEAMGLDVDGLDDEEVAERL 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 490200396 328 INAIARLSKDVGIPQHLNELGVKEADFPYMAEMALKDGNAFSNPRKGNEKEIVEIF 383
Cdd:cd17814 319 IEAIRDLREDLGIPETLSELGVDEEDIPELAKRAMKDPCLVTNPRRPTREDIEEIY 374
|
|
| Fe-ADH-like |
cd08194 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
16-387 |
3.71e-153 |
|
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: 436.96 E-value: 3.71e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 16 FGPGAVSVVGERCKLLGGKKALLVTDKGLRaiKDGAVDQTVKHLREAGIDVVIFDGVEPNPKDTNVRDGLAVFQKEHCDM 95
Cdd:cd08194 6 IGGGALEELGEEAASLGGKRALIVTDKVMV--KLGLVDKVTQLLAEAGIAYAVFDDVVSEPTDEMVEEGLALYKEGGCDF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 96 IITVGGGSPHDCGKGIGIAATHPGDLYSYAGIETLTHALPPIIAVNTTAGTASEVTRHCVLTNTKTKVKFVIVSWRNLPS 175
Cdd:cd08194 84 IVALGGGSPIDTAKAIAVLATNGGPIRDYMGPRKVDKPGLPLIAIPTTAGTGSEVTRFTVITDTETDVKMLLKGPALLPA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 176 VSINDPLLMVGKPAGLTAATGMDALTHAVEAYISKDANPVTDASAIQAIKLIATNLRQAVALGTNIKARENMACASLLAG 255
Cdd:cd08194 164 VAIVDPELTLSMPPRVTAATGIDALTHAIEAYVSRKAQPLTDTLALSAIKLIGRNLRRAYADGDDLEAREAMMLAALEAG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 256 MAFNNANLGYVHAMAHQLGGLYDMAHGVANAVLLPHVCRYNLIANPEKFADIATFMGENTTGLSTMDAAECAINAIARLS 335
Cdd:cd08194 244 IAFSNSSVALVHGMSRPIGALFHVPHGLSNAMLLPAVTEFSLPGAPERYAEIARAMGIATEGDSDEEAAEKLVEALERLC 323
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 490200396 336 KDVGIPQhLNELGVKEADF----PYMAEMALKDGNAFSNPRKGNEKEIVEIFRQAF 387
Cdd:cd08194 324 ADLEIPT-LREYGIDEEEFeaalDKMAEDALASGSPANNPRVPTKEEIIELYREAW 378
|
|
| Fe-ADH |
pfam00465 |
Iron-containing alcohol dehydrogenase; |
11-379 |
3.96e-151 |
|
Iron-containing alcohol dehydrogenase;
Pssm-ID: 425696 [Multi-domain] Cd Length: 362 Bit Score: 431.26 E-value: 3.96e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 11 PNVNFFGPGAVSVVGERCKLLGgKKALLVTDKGLraIKDGAVDQTVKHLREAGIDVVIFDGVEPNPKDTNVRDGLAVFQK 90
Cdd:pfam00465 1 PTRIVFGAGALAELGEELKRLG-ARALIVTDPGS--LKSGLLDKVLASLEEAGIEVVVFDGVEPEPTLEEVDEAAALARE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 91 EHCDMIITVGGGSPHDCGKGIGIAATHPGDLYSYAGIETLTHALPPIIAVNTTAGTASEVTRHCVLTNTKTKVKFVIVSW 170
Cdd:pfam00465 78 AGADVIIAVGGGSVIDTAKAIALLLTNPGDVWDYLGGKPLTKPALPLIAIPTTAGTGSEVTPLAVITDTETGEKLGIFSP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 171 RNLPSVSINDPLLMVGKPAGLTAATGMDALTHAVEAYISKDANPVTDASAIQAIKLIATNLRQAVALGTNIKARENMACA 250
Cdd:pfam00465 158 KLLPDLAILDPELTLTLPPRLTAATGMDALAHAVEAYVSKGANPLTDALALEAIRLIAENLPRAVADGEDLEARENMLLA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 251 SLLAGMAFNNANLGYVHAMAHQLGGLYDMAHGVANAVLLPHVCRYNLIANPEKFADIATFMGENttglSTMDAAECAINA 330
Cdd:pfam00465 238 STLAGLAFSNAGLGAAHALAHALGGRYGIPHGLANAILLPYVLRFNAPAAPEKLAQLARALGED----SDEEAAEEAIEA 313
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 490200396 331 IARLSKDVGIPQHLNELGVKEADFPYMAEMALKDGNAFSNPRKGNEKEI 379
Cdd:pfam00465 314 LRELLRELGLPTTLSELGVTEEDLDALAEAALRDRSLANNPRPLTAEDI 362
|
|
| lactal_redase |
TIGR02638 |
lactaldehyde reductase; This clade of genes encoding iron-containing alcohol dehydrogenase ... |
8-383 |
7.59e-146 |
|
lactaldehyde reductase; This clade of genes encoding iron-containing alcohol dehydrogenase (pfam00465) proteins is generally found in apparent operons for the catabolism of rhamnose or fucose. Catabolism of both of these monosaccharides results in lactaldehyde which is reduced by this enzyme to 1,2 propanediol. This protein is alternatively known by the name 1,2 propanediol oxidoreductase. This enzyme is active under anaerobic conditions in E. coli while being inactivated by reactive oxygen species under aerobic conditions. Under aerobic conditions the lactaldehyde product of rhamnose and fucose catabolism is believed to be oxidized to lactate by a separate enzyme, lactaldehyde dehydrogenase. [Energy metabolism, Sugars]
Pssm-ID: 131686 [Multi-domain] Cd Length: 379 Bit Score: 418.38 E-value: 7.59e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 8 FLVPNVNFFGPGAVSVVGERCKLLGGKKALLVTDKGLraIKDGAVDQTVKHLREAGIDVVIFDGVEPNPKDTNVRDGLAV 87
Cdd:TIGR02638 4 LILNETSYFGAGAIEDIVDEVKRRGFKKALVVTDKDL--IKFGVADKVTDLLDEAGIAYELFDEVKPNPTITVVKAGVAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 88 FQKEHCDMIITVGGGSPHDCGKGIGIAATHP--GDLYSYAGIETLTHALPPIIAVNTTAGTASEVTRHCVLTNTKTKVKF 165
Cdd:TIGR02638 82 FKASGADYLIAIGGGSPIDTAKAIGIISNNPefADVRSLEGVAPTKKPGVPIIAIPTTAGTAAEVTINYVITDEENKRKF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 166 VIVSWRNLPSVSINDPLLMVGKPAGLTAATGMDALTHAVEAYISKDANPVTDASAIQAIKLIATNLRQAVALGTNIKARE 245
Cdd:TIGR02638 162 VCVDPHDIPDVAVIDAEMMYSMPKSLTAATGMDALTHAIEGYITKGAWELTDMLHLKAIEIIARWLRSAVEGGKDLEARE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 246 NMACASLLAGMAFNNANLGYVHAMAHQLGGLYDMAHGVANAVLLPHVCRYNLIANPEKFADIATFMGENTTGLSTMDAAE 325
Cdd:TIGR02638 242 QMALGQYVAGMGFSNVGLGLVHGMAHPLGAFYNTPHGVANAILLPHVMEFNAEFTGEKYREIAKAMGVKTEGMSDEEARD 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 490200396 326 CAINAIARLSKDVGIPQHLNELGVKEADFPYMAEMALKDGNAFSNPRKGNEKEIVEIF 383
Cdd:TIGR02638 322 AAVEAVKTLSKRVGIPEGLSELGVKEEDIPALAEAALADVCTGGNPRETTVEEIEELY 379
|
|
| Fe-ADH-like |
cd08189 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
17-385 |
3.91e-144 |
|
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: 413.79 E-value: 3.91e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 17 GPGAVSVVGERCKLLGGKKALLVTDKGLraIKDGAVDQTVKHLREAGIDVVIFDGVEPNPKDTNVRDGLAVFQKEHCDMI 96
Cdd:cd08189 11 GAGSLLQLPEALKKLGIKRVLIVTDKGL--VKLGLLDPLLDALKKAGIEYVVFDGVVPDPTIDNVEEGLALYKENGCDAI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 97 ITVGGGSPHDCGKGIGIAATHPG-DLYSYAGIETLTHALPPIIAVNTTAGTASEVTRHCVLTNTKTKVKFVIVSWRNLPS 175
Cdd:cd08189 89 IAIGGGSVIDCAKVIAARAANPKkSVRKLKGLLKVRKKLPPLIAVPTTAGTGSEATIAAVITDPETHEKYAINDPKLIPD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 176 VSINDPLLMVGKPAGLTAATGMDALTHAVEAYISKDANPVTDASAIQAIKLIATNLRQAVALGTNIKARENMACASLLAG 255
Cdd:cd08189 169 AAVLDPELTLGLPPAITAATGMDALTHAVEAYISRSATKETDEYALEAVKLIFENLPKAYEDGSDLEARENMLLASYYAG 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 256 MAFNNANLGYVHAMAHQLGGLYDMAHGVANAVLLPHVCRYNLIANPEKFADIATFMGENTTGLSTMDAAECAINAIARLS 335
Cdd:cd08189 249 LAFTRAYVGYVHAIAHQLGGLYGVPHGLANAVVLPHVLEFYGPAAEKRLAELADAAGLGDSGESDSEKAEAFIAAIRELN 328
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 490200396 336 KDVGIPQHLNELgvKEADFPYMAEMALKDGN-AFSNPRKGNEKEIVEIFRQ 385
Cdd:cd08189 329 RRMGIPTTLEEL--KEEDIPEIAKRALKEANpLYPVPRIMDRKDCEELLRK 377
|
|
| PRK10624 |
PRK10624 |
L-1,2-propanediol oxidoreductase; Provisional |
1-387 |
1.62e-139 |
|
L-1,2-propanediol oxidoreductase; Provisional
Pssm-ID: 182595 [Multi-domain] Cd Length: 382 Bit Score: 402.45 E-value: 1.62e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 1 MSDRMydfLVPNVNFFGPGAVSVVGERCKLLGGKKALLVTDKGLraIKDGAVDQTVKHLREAGIDVVIFDGVEPNPKDTN 80
Cdd:PRK10624 1 MANRM---ILNETAYFGRGAIGALTDEVKRRGFKKALIVTDKTL--VKCGVVAKVTDVLDAAGLAYEIYDGVKPNPTIEV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 81 VRDGLAVFQKEHCDMIITVGGGSPHDCGKGIGIAATHP--GDLYSYAGIETLTHALPPIIAVNTTAGTASEVTRHCVLTN 158
Cdd:PRK10624 76 VKEGVEVFKASGADYLIAIGGGSPQDTCKAIGIISNNPefADVRSLEGVAPTKKPSVPIIAIPTTAGTAAEVTINYVITD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 159 TKTKVKFVIVSWRNLPSVSINDPLLMVGKPAGLTAATGMDALTHAVEAYISKDANPVTDASAIQAIKLIATNLRQAVAlg 238
Cdd:PRK10624 156 EEKRRKFVCVDPHDIPQVAFVDADMMDSMPPGLKAATGVDALTHAIEGYITRGAWALTDMLHLKAIEIIAGALRGAVA-- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 239 TNIKARENMACASLLAGMAFNNANLGYVHAMAHQLGGLYDMAHGVANAVLLPHVCRYNLIANPEKFADIATFMGENTTGL 318
Cdd:PRK10624 234 GDKEAGEGMALGQYIAGMGFSNVGLGLVHGMAHPLGAFYNTPHGVANAILLPHVMEYNADFTGEKYRDIARAMGVKVEGM 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490200396 319 STMDAAECAINAIARLSKDVGIPQHLNELGVKEADFPYMAEMALKDGNAFSNPRKGNEKEIVEIFRQAF 387
Cdd:PRK10624 314 SLEEARNAAVEAVKALNRDVGIPPHLRDVGVKEEDIPALAQAAFDDVCTGGNPREATLEDIVELYKKAW 382
|
|
| Fe-ADH-like |
cd14861 |
Iron-containing alcohol dehydrogenases-like; This family contains proteins similar to ... |
16-387 |
2.99e-138 |
|
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: 398.81 E-value: 2.99e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 16 FGPGAVSVVGERCKLLGGKKALLVTDKGLRAIkdGAVDQTVKHLREAGIDVVIFDGVEPNPKDTNVRDGLAVFQKEHCDM 95
Cdd:cd14861 8 FGAGAIAELPEELKALGIRRPLLVTDPGLAAL--GIVDRVLEALGAAGLSPAVFSDVPPNPTEADVEAGVAAYREGGCDG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 96 IITVGGGSPHDCGKGIGIAATHPGDLYSYAGIET----LTHALPPIIAVNTTAGTASEVTRHCVLTNTKTKVKFVIVSWR 171
Cdd:cd14861 86 IIALGGGSAIDAAKAIALMATHPGPLWDYEDGEGgpaaITPAVPPLIAIPTTAGTGSEVGRAAVITDDDTGRKKIIFSPK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 172 NLPSVSINDPLLMVGKPAGLTAATGMDALTHAVEAYISKDANPVTDASAIQAIKLIATNLRQAVALGTNIKARENMACAS 251
Cdd:cd14861 166 LLPKVAICDPELTLGLPPRLTAATGMDALTHCIEAYLSPGFHPMADGIALEGLRLISEWLPRAVADGSDLEARGEMMMAA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 252 LLAGMAFNNAnLGYVHAMAHQLGGLYDMAHGVANAVLLPHVCRYNLIANPEKFADIATFMGentTGLSTMDAaecAINAI 331
Cdd:cd14861 246 LMGAVAFQKG-LGAVHALAHALGALYGLHHGLLNAILLPYVLRFNRPAVEDKLARLARALG---LGLGGFDD---FIAWV 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 490200396 332 ARLSKDVGIPQHLNELGVKEADFPYMAEMALKDGNAFSNPRKGNEKEIVEIFRQAF 387
Cdd:cd14861 319 EDLNERLGLPATLSELGVTEDDLDELAELALADPCHATNPRPVTAEDYRALLREAL 374
|
|
| Fe-ADH-like |
cd14865 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
6-387 |
2.52e-137 |
|
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: 396.91 E-value: 2.52e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 6 YDFLVPNVNFFGPGAVSVVGERCKLLGGKKALLVTDKGLRaiKDGAVDQTVKHLREAGIDVVIFDGVEPNPKDTNVRDGL 85
Cdd:cd14865 1 FEFFNPTKIVSGAGALENLPAELARLGARRPLIVTDKGLA--AAGLLKKVEDALGDAIEIVGVFDDVPPDSSVAVVNEAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 86 AVFQKEHCDMIITVGGGSPHDCGKGIGIAATHPG-DLYSYAGIETLTHALPPIIAVNTTAGTASEVTRHCVLTNTKTKVK 164
Cdd:cd14865 79 ARAREAGADGIIAVGGGSVIDTAKGVNILLSEGGdDLDDYGGANRLTRPLKPLIAIPTTAGTGSEVTLVAVIKDEEKKVK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 165 FVIVSWRNLPSVSINDPLLMVGKPAGLTAATGMDALTHAVEAYISKDANPVTDASAIQAIKLIATNLRQAVALGTNIKAR 244
Cdd:cd14865 159 LLFVSPFLLPDVAILDPRLTLSLPPKLTAATGMDALTHAIEAYTSLQKNPISDALALQAIRLISENLPKAVKNGKDLEAR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 245 ENMACASLLAGMAFNNANLGYVHAMAHQLGGLYDMAHGVANAVLLPHVCRYNLIANPEKFADIATFM--GENTTGLSTMD 322
Cdd:cd14865 239 LALAIAATMAGIAFSNSMVGLVHAIAHAVGAVAGVPHGLANSILLPHVMRYNLDAAAERYAELALALayGVTPAGRRAEE 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490200396 323 AAECAINAIARLSKDVGIPQHLNELGVKEADFPYMAEMALKDGNAFSNPRKGNEKEIVEIFRQAF 387
Cdd:cd14865 319 AIEAAIDLVRRLHELCGLPTRLRDVGVPEEQLEAIAELALNDGAILFNPREVDPEDILAILEAAY 383
|
|
| Fe-ADH-like |
cd14863 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
15-387 |
1.43e-136 |
|
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: 394.98 E-value: 1.43e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 15 FFGPGAVSVVGERCKLLGGKKALLVTDKGLRAIkdGAVDQTVKHLREAGIDVVIFDGVEPNPKDTNVRDGLAVFQKEHCD 94
Cdd:cd14863 9 IFGAGAVEQIGELLKELGCKKVLLVTDKGLKKA--GIVDKIIDLLEEAGIEVVVFDDVEPDPPDEIVDEAAEIAREEGAD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 95 MIITVGGGSPHDCGKGIGIAATHPGDLYSYAGI-ETLTHALPPIIAVNTTAGTASEVTRHCVLTNTKTKVKFVIVSWRNL 173
Cdd:cd14863 87 GVIGIGGGSVLDTAKAIAVLLTNPGPIIDYALAgPPVPKPGIPLIAIPTTAGTGSEVTPIAVITDEENGVKKSLLGPFLV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 174 PSVSINDPLLMVGKPAGLTAATGMDALTHAVEAYISKDANPVTDASAIQAIKLIATNLRQAVALGTNIKARENMACASLL 253
Cdd:cd14863 167 PDLAILDPELTVGLPPSLTAATGMDALSHAIEAYTSKLANPMTDALALQAIRLIVKNLPRAVKDGDNLEARENMLLASNL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 254 AGMAFNNANLGYVHAMAHQLGGLYDMAHGVANAVLLPHVCRYNLIANPEKFADIATFMGENTTGLSTMDAAECAINAIAR 333
Cdd:cd14863 247 AGIAFNNAGTHIGHAIAHALGALYHIPHGLACALALPVVLEFNAEAYPEKVKKIAKALGVSFPGESDEELGEAVADAIRE 326
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 490200396 334 LSKDVGIPQHLNELGVKEADFPYMAEMALKDGNAFSNPRKGNEKEIVEIFRQAF 387
Cdd:cd14863 327 FMKELGIPSLFEDYGIDKEDLDKIAEAVLKDPFAMFNPRPITEEEVAEILEAIY 380
|
|
| PRK09860 |
PRK09860 |
putative alcohol dehydrogenase; Provisional |
8-386 |
9.21e-133 |
|
putative alcohol dehydrogenase; Provisional
Pssm-ID: 182118 [Multi-domain] Cd Length: 383 Bit Score: 385.46 E-value: 9.21e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 8 FLVPNVNFFGPGAVSVVGERCKLLGGKKALLVTDKGLRAIkdGAVDQTVKHLREAGIDVVIFDGVEPNPKDTNVRDGLAV 87
Cdd:PRK09860 6 FFIPSVNVIGADSLTDAMNMMADYGFTRTLIVTDNMLTKL--GMAGDVQKALEERNIFSVIYDGTQPNPTTENVAAGLKL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 88 FQKEHCDMIITVGGGSPHDCGKGIGIAATHPGDLYSYAGIETLTHALPPIIAVNTTAGTASEVTRHCVLTNTKTKVKFVI 167
Cdd:PRK09860 84 LKENNCDSVISLGGGSPHDCAKGIALVAANGGDIRDYEGVDRSAKPQLPMIAINTTAGTASEMTRFCIITDEARHIKMAI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 168 VSWRNLPSVSINDPLLMVGKPAGLTAATGMDALTHAVEAYISKDANPVTDASAIQAIKLIATNLRQAVALGTNIKARENM 247
Cdd:PRK09860 164 VDKHVTPLLSVNDSSLMIGMPKSLTAATGMDALTHAIEAYVSIAATPITDACALKAVTMIAENLPLAVEDGSNAKAREAM 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 248 ACASLLAGMAFNNANLGYVHAMAHQLGGLYDMAHGVANAVLLPHVCRYNLIANPEKFADIATFMGENTTGLSTMDAAECA 327
Cdd:PRK09860 244 AYAQFLAGMAFNNASLGYVHAMAHQLGGFYNLPHGVCNAVLLPHVQVFNSKVAAARLRDCAAAMGVNVTGKNDAEGAEAC 323
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 490200396 328 INAIARLSKDVGIPQHLNELGVKEADFPYMAEMALKDGNAFSNPRKGNEKEIVEIFRQA 386
Cdd:PRK09860 324 INAIRELAKKVDIPAGLRDLNVKEEDFAVLATNALKDACGFTNPIQATHEEIVAIYRAA 382
|
|
| Fe-ADH-like |
cd08185 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
15-384 |
1.05e-129 |
|
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: 377.22 E-value: 1.05e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 15 FFGPGAVSVVGERCKLLGgKKALLVTDKGlRAIKDGAVDQTVKHLREAGIDVVIFDGVEPNPKDTNVRDGLAVFQKEHCD 94
Cdd:cd08185 8 LFGAGKLNELGEEALRPG-KKALIVTGKG-SSKKTGLLDRVKKLLEKAGVEVVVFDKVEPNPLTTTVMEGAALAKEEGCD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 95 MIITVGGGSPHDCGKGIGIAATHPGDLYSYA----GIETLTHALPPIIAVNTTAGTASEVTRHCVLTNTKTKVKFVIVSW 170
Cdd:cd08185 86 FVIGLGGGSSMDAAKAIAFMATNPGDIWDYIfggtGKGPPPEKALPIIAIPTTAGTGSEVDPWAVITNPETKEKKGIGHP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 171 RNLPSVSINDPLLMVGKPAGLTAATGMDALTHAVEAYISKDANPVTDASAIQAIKLIATNLRQAVALGTNIKARENMACA 250
Cdd:cd08185 166 ALFPKVSIVDPELMLTVPPRVTAYTGFDALFHAFESYISKNANPFSDMLALEAIRLVAKYLPRAVKDGSDLEAREKMAWA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 251 SLLAGMAFNNANLGYVHAMAHQLGGLY-DMAHGVANAVLLPHVCRYNLIANPEKFADIATFMGEnttGLSTMDAAECAIN 329
Cdd:cd08185 246 STLAGIVIANSGTTLPHGLEHPLSGYHpNIPHGAGLAALYPAYFEFTIEKAPEKFAFVARAEAS---GLSDAKAAEDFIE 322
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 490200396 330 AIARLSKDVGIPQHLNELGVKEADFPYMAEMALK--DGNAFSNPRKGNEKEIVEIFR 384
Cdd:cd08185 323 ALRKLLKDIGLDDLLSDLGVTEEDIPWLAENAMEtmGGLFANNPVELTEEDIVEIYE 379
|
|
| HOT |
cd08190 |
Hydroxyacid-oxoacid transhydrogenase (HOT) involved in gamma-hydroxybutyrate metabolism; This ... |
16-387 |
2.19e-118 |
|
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: 349.54 E-value: 2.19e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 16 FGPGAVSVVGERCKLLGGKKALLVTDKGLRAIkdGAVDQTVKHLREAGIDVVIFDGVEPNPKDTNVRDGLAVFQKEHCDM 95
Cdd:cd08190 6 FGPGATRELGMDLKRLGAKKVLVVTDPGLAKL--GLVERVLESLEKAGIEVVVYDGVRVEPTDESFEEAIEFAKEGDFDA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 96 IITVGGGSPHDCGKGIGIAATHPGDLYSYAGIET-----LTHALPPIIAVNTTAGTASEVTRHCVLTNTKTKVKFVIVSW 170
Cdd:cd08190 84 FVAVGGGSVIDTAKAANLYATHPGDFLDYVNAPIgkgkpVPGPLKPLIAIPTTAGTGSETTGVAIFDLEELKVKTGISSR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 171 RNLPSVSINDPLLMVGKPAGLTAATGMDALTHAVEAYISKD------------------ANPVTDASAIQAIKLIATNLR 232
Cdd:cd08190 164 YLRPTLAIVDPLLTLTLPPRVTASSGFDVLCHALESYTARPynarprpanpderpayqgSNPISDVWAEKAIELIGKYLR 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 233 QAVALGTNIKARENMACASLLAGMAFNNANLGYVHAMAHQLGGL--------YDMA-----HGVANAVLLPHVCRYNLIA 299
Cdd:cd08190 244 RAVNDGDDLEARSNMLLASTLAGIGFGNAGVHLPHAMAYPIAGLvkdyrppgYPVDhphvpHGLSVALTAPAVFRFTAPA 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 300 NPEKFADIATFMGENTTGLSTMDAAECAINAIARLSKDVGIPQHLNELGVKEADFPYMAEMALK-----DGnafsNPRKG 374
Cdd:cd08190 324 CPERHLEAAELLGADTSGASDRDAGEVLADALIKLMRDIGIPNGLSALGYSEDDIPALVEGTLPqqrllKL----NPRPV 399
|
410
....*....|...
gi 490200396 375 NEKEIVEIFRQAF 387
Cdd:cd08190 400 TEEDLEEIFEDAL 412
|
|
| Fe-ADH-like |
cd08183 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
16-384 |
2.43e-112 |
|
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: 332.93 E-value: 2.43e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 16 FGPGAVSVVGERCKLLGgKKALLVTdkGLRAIKDGAVDQTVKHLREAGIDVVIFDGV-EPNPKDtnVRDGLAVFQKEHCD 94
Cdd:cd08183 6 FGRGSLQELGELAAELG-KRALLVT--GRSSLRSGRLARLLEALEAAGIEVALFSVSgEPTVET--VDAAVALAREAGCD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 95 MIITVGGGSPHDCGKGIGIAATHPGDLYSY-----AGIETLTHALPpIIAVNTTAGTASEVTRHCVLTNTKTKVKfviVS 169
Cdd:cd08183 81 VVIAIGGGSVIDAAKAIAALLTNEGSVLDYlevvgKGRPLTEPPLP-FIAIPTTAGTGSEVTKNAVLSSPEHGVK---VS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 170 WRN---LPSVSINDPLLMVGKPAGLTAATGMDALTHAVEAYISKDANPVTDASAIQAIKLIATNLRQAVALGTNIKAREN 246
Cdd:cd08183 157 LRSpsmLPDVALVDPELTLSLPPEVTAASGLDALTQLIEPYVSRKANPLTDALAREGLRLAARSLRRAYEDGEDLEARED 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 247 MACASLLAGMAFNNANLGYVHAMAHQLGGLYDMAHGVANAVLLPHVCRYNLIANPEKFADIA-----TFMGENTTGLSTm 321
Cdd:cd08183 237 MALASLLGGLALANAGLGAVHGLAGPLGGMFGAPHGAICAALLPPVLEANLRALREREPDSPalaryRELAGILTGDPD- 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490200396 322 DAAECAINAIARLSKDVGIPqHLNELGVKEADFPYMAEMALKDGNAFSNPRKGNEKEIVEIFR 384
Cdd:cd08183 316 AAAEDGVEWLEELCEELGIP-RLSEYGLTEEDFPEIVEKARGSSSMKGNPIELSDEELLEILE 377
|
|
| AAD_C |
cd08178 |
C-terminal alcohol dehydrogenase domain of the acetaldehyde dehydrogenase-alcohol ... |
10-384 |
5.47e-112 |
|
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: 333.00 E-value: 5.47e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 10 VPNVNFFGPGAVSVVgeRCKLLGGKKALLVTDKGLraIKDGAVDQTVKHLREAGIDVVIFDGVEPNPKDTNVRDGLAVFQ 89
Cdd:cd08178 2 VPPKIYFEPGCLPYL--LLELPGVKRAFIVTDRVL--YKLGYVDKVLDVLEARGVETEVFSDVEPDPTLSTVRKGLEAMN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 90 KEHCDMIITVGGGSPHDCGKGIGIAATHPG----DLY-SYAGIETLTHALPPI------IAVNTTAGTASEVTRHCVLTN 158
Cdd:cd08178 78 AFKPDVIIALGGGSAMDAAKIMWLFYEHPEtkfeDLAqRFMDIRKRVYKFPKLgkkaklVAIPTTSGTGSEVTPFAVITD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 159 TKTKVKFVIVSWRNLPSVSINDPLLMVGKPAGLTAATGMDALTHAVEAYISKDANPVTDASAIQAIKLIATNLRQAVALG 238
Cdd:cd08178 158 DKTGKKYPLADYALTPDMAIVDPELVMTMPKRLTADTGIDALTHAIEAYVSVMASDYTDGLALQAIKLIFEYLPRSYNNG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 239 TNIKARENMACASLLAGMAFNNANLGYVHAMAHQLGGLYDMAHGVANAVLLPHVCRYNLIANPEKF-------------- 304
Cdd:cd08178 238 NDIEAREKMHNAATIAGMAFANAFLGICHSLAHKLGAAFHIPHGRANAILLPHVIRYNATDPPTKQaafpqykyyvaker 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 305 -ADIATFMGenTTGLSTMDAAECAINAIARLSKDVGIPQHLNELGVKEADF----PYMAEMALKDGNAFSNPRKGNEKEI 379
Cdd:cd08178 318 yAEIADLLG--LGGKTPEEKVESLIKAIEDLKKDLGIPTSIREAGIDEADFlaavDKLAEDAFDDQCTGANPRYPLISEL 395
|
....*
gi 490200396 380 VEIFR 384
Cdd:cd08178 396 KEILL 400
|
|
| NADPH_BDH |
cd08179 |
NADPH-dependent butanol dehydrogenase involved in the butanol and ethanol formation pathway in ... |
8-387 |
1.30e-111 |
|
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: 331.08 E-value: 1.30e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 8 FLVPNVNFFGPGAVSVVgercKLLGGKKALLVTDKGLRaIKDGAVDQTVKHLREAGIDVVIFDGVEPNPKDTNVRDGLAV 87
Cdd:cd08179 2 FFVPRDIYFGEGALEYL----KTLKGKRAFIVTGGGSM-KRNGFLDKVEDYLKEAGMEVKVFEGVEPDPSVETVEKGAEA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 88 FQKEHCDMIITVGGGSPHDCGKGIGIAATHPgdlySYAGIETLT-HALPPI------IAVNTTAGTASEVTRHCVLTNTK 160
Cdd:cd08179 77 MREFEPDWIIAIGGGSVIDAAKAMWVFYEYP----ELTFEDALVpFPLPELrkkarfIAIPSTSGTGSEVTRASVITDTE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 161 TKVKFVIVSWRNLPSVSINDPLLMVGKPAGLTAATGMDALTHAVEAYISKDANPVTDASAIQAIKLIATNLRQAVALGTN 240
Cdd:cd08179 153 KGIKYPLASFEITPDVAILDPELTMTMPPHVTANTGMDALTHAIEAYVSTLANDFTDALALGAILDIFENLPKSYNGGKD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 241 IKARENMACASLLAGMAFNNANLGYVHAMAHQLGGLYDMAHGVANAVLLPHVCRYNLIANPEKFADIATFmgentTGLST 320
Cdd:cd08179 233 LEAREKMHNASCLAGMAFSNSGLGIVHSMAHKGGAFFGIPHGLANAILLPYVIEFNSKDPEARARYAALL-----IGLTD 307
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490200396 321 MDAAECAINAIARLSKDVGIPQHLNELGVKEADF----PYMAEMALKDGNAFSNPRKGNEKEIVEIFRQAF 387
Cdd:cd08179 308 EELVEDLIEAIEELNKKLGIPLSFKEAGIDEDEFfaklDEMAENAMNDACTGTNPRKPTVEEMKELLKAAY 378
|
|
| HVD |
cd08193 |
5-hydroxyvalerate dehydrogenase (HVD) catalyzes the oxidation of 5-hydroxyvalerate to ... |
10-387 |
1.84e-104 |
|
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: 312.91 E-value: 1.84e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 10 VPNVnFFGPGAVSVVGERCKLLGGKKALLVTDKGLRAIkdGAVDQTVKHLREAGIDVVIFDGVEPNPKDTNVRDGLAVFQ 89
Cdd:cd08193 4 VPRI-ICGAGAAARLGELLRELGARRVLLVTDPGLVKA--GLADPALAALEAAGIAVTVFDDVVADPPEAVVEAAVEQAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 90 KEHCDMIITVGGGSPHDCGKGIGIAATHPGDLYSYAGIETLTHALPPIIAVNTTAGTASEVTRHCVLTnTKTKVKFVIVS 169
Cdd:cd08193 81 EAGADGVIGFGGGSSMDVAKLVALLAGSDQPLDDIYGVGKATGPRLPLILVPTTAGTGSEVTPISIVT-TGETEKKGVVS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 170 WRNLPSVSINDPLLMVGKPAGLTAATGMDALTHAVEAYISKDA-NPVTDASAIQAIKLIATNLRQAVALGTNIKARENMA 248
Cdd:cd08193 160 PQLLPDVALLDAELTLGLPPHVTAATGIDAMVHAIEAYTSRHKkNPISDALAREALRLLGANLRRAVEDGSDLEAREAML 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 249 CASLLAGMAFNNANLGYVHAMAHQLGGLYDMAHGVANAVLLPHVCRYNLIANPEKFADIATFMGENTTGLSTMDAAECAI 328
Cdd:cd08193 240 LGSMLAGQAFANAPVAAVHALAYPLGGHFHVPHGLSNALVLPHVLRFNLPAAEALYAELARALLPGLAFGSDAAAAEAFI 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490200396 329 NAIARLSKDVGIPQHLNELGVKEADFPYMAEMALKD----GNafsNPRKGNEKEIVEIFRQAF 387
Cdd:cd08193 320 DALEELVEASGLPTRLRDVGVTEEDLPMLAEDAMKQtrllVN---NPREVTEEDALAIYQAAL 379
|
|
| PDD |
cd08180 |
1,3-propanediol dehydrogenase (PPD) catalyzes the reduction of 3-hydroxypropionaldehyde (3-HPA) ... |
15-384 |
1.03e-98 |
|
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: 296.71 E-value: 1.03e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 15 FFGPGAVsvvgERCKLLGGKKALLVTDKGLraIKDGAVDQTVKHLREAgIDVVIFDGVEPNPKDTNVRDGLAVFQKEHCD 94
Cdd:cd08180 8 YSGEDSL----ERLKELKGKRVFIVTDPFM--VKSGMVDKVTDELDKS-NEVEIFSDVVPDPSIEVVAKGLAKILEFKPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 95 MIITVGGGSPHDCGKGIGIAAthpgdlYSYAGIEtlthALPPIIAVNTTAGTASEVTRHCVLTNTKTKVKFVIVSWRNLP 174
Cdd:cd08180 81 TIIALGGGSAIDAAKAIIYFA------LKQKGNI----KKPLFIAIPTTSGTGSEVTSFAVITDPEKGIKYPLVDDSMLP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 175 SVSINDPLLMVGKPAGLTAATGMDALTHAVEAYISKDANPVTDASAIQAIKLIATNLRQAVALGTNIKARENMACASLLA 254
Cdd:cd08180 151 DIAILDPELVKSVPPKVTADTGMDVLTHALEAYVSTNANDFTDALAEKAIKLVFENLPRAYRDGDDLEAREKMHNASCMA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 255 GMAFNNANLGYVHAMAHQLGGLYDMAHGVANAVLLPHVCRYnLIAnpekfadiatfmgenttglstmdaaecainAIARL 334
Cdd:cd08180 231 GIAFNNAGLGINHSLAHALGGRFHIPHGRANAILLPYVIEF-LIA------------------------------AIRRL 279
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 490200396 335 SKDVGIPQHLNELGVKEADF----PYMAEMALKDGNAFSNPRKGNEKEIVEIFR 384
Cdd:cd08180 280 NKKLGIPSTLKELGIDEEEFekaiDEMAEAALADRCTATNPRKPTAEDLIELLR 333
|
|
| PRK13805 |
PRK13805 |
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional |
3-387 |
5.67e-98 |
|
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional
Pssm-ID: 237515 [Multi-domain] Cd Length: 862 Bit Score: 310.19 E-value: 5.67e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 3 DRMYDFLVPNVNFFGPGAVSVVgeRCKLLGGKKALLVTDKGLraIKDGAVDQTVKHL--REAGIDVVIFDGVEPNPKDTN 80
Cdd:PRK13805 452 ENMQWFKVPKKIYFERGSLPYL--LDELDGKKRAFIVTDRFM--VELGYVDKVTDVLkkRENGVEYEVFSEVEPDPTLST 527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 81 VRDGLAVFQKEHCDMIITVGGGSPHDCGKGIGIAATHPG----DLYS-YAGIETLTHALPPI------IAVNTTAGTASE 149
Cdd:PRK13805 528 VRKGAELMRSFKPDTIIALGGGSPMDAAKIMWLFYEHPEtdfeDLAQkFMDIRKRIYKFPKLgkkaklVAIPTTSGTGSE 607
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 150 VTRHCVLTNTKTKVKFVIVSWRNLPSVSINDPLLMVGKPAGLTAATGMDALTHAVEAYISKDANPVTDASAIQAIKLIAT 229
Cdd:PRK13805 608 VTPFAVITDDKTGVKYPLADYELTPDVAIVDPNLVMTMPKSLTADTGIDALTHALEAYVSVMASDYTDGLALQAIKLVFE 687
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 230 NLRQAVALG-TNIKARENMACASLLAGMAFNNANLGYVHAMAHQLGGLYDMAHGVANAVLLPHVCRYNLIANP------- 301
Cdd:PRK13805 688 YLPRSYKNGaKDPEAREKMHNASTIAGMAFANAFLGICHSMAHKLGAEFHIPHGRANAILLPHVIRYNATDPPkqaafpq 767
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 302 -------EKFADIATFMGenTTGLSTMDAAECAINAIARLSKDVGIPQHLNELGVKEADF----PYMAEMALKDGNAFSN 370
Cdd:PRK13805 768 yeypradERYAEIARHLG--LPGSTTEEKVESLIKAIEELKAELGIPMSIKEAGVDEADFlaklDELAELAFDDQCTGAN 845
|
410
....*....|....*..
gi 490200396 371 PRKGNEKEIVEIFRQAF 387
Cdd:PRK13805 846 PRYPLISELKEILLDAY 862
|
|
| Fe-ADH-like |
cd08191 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
15-387 |
1.49e-97 |
|
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: 295.68 E-value: 1.49e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 15 FFGPGAVSVVGERCKLLGgKKALLVTDKglRAIKDGAVDQTVKHLREAGIDVVIFDGVEPNPKDTNVRDGLAVFQKEHCD 94
Cdd:cd08191 8 LFGPGARRALGRVAARLG-SRVLIVTDP--RLASTPLVAELLAALTAAGVAVEVFDGGQPELPVSTVADAAAAARAFDPD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 95 MIITVGGGSPHDCGKGIGIAATHPGDLYSYAGIETLTHALPPIIAVNTTAGTASEVTRHCVLTNTKTKVKFVIVSWRNLP 174
Cdd:cd08191 85 VVIGLGGGSNMDLAKVVALLLAHGGDPRDYYGEDRVPGPVLPLIAVPTTAGTGSEVTPVAVLTDPARGMKVGVSSPYLRP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 175 SVSINDPLLMVGKPAGLTAATGMDALTHAVEAYISKD---------------ANPVTDASAIQAIKLIATNLRQAVALGT 239
Cdd:cd08191 165 AVAIVDPELTLTCPPGVTADSGIDALTHAIESYTARDfppfprldpdpvyvgKNPLTDLLALEAIRLIGRHLPRAVRDGD 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 240 NIKARENMACASLLAGMAFNNANLGYVHAMAHQLGGLYDMAHGVANAVLLPHVCRYNLIANPEKFADIATFMGENTTGLS 319
Cdd:cd08191 245 DLEARSGMALAALLAGLAFGTAGTAAAHALQYPIGALTHTSHGVGNGLLLPYVMRFNRPARAAELAEIARALGVTTAGTS 324
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490200396 320 TmDAAECAINAIARLSKDVGIPQHLNELGVKEADFPYMAEMALKDGN-AFSNPRKGNEKEIVEIFRQAF 387
Cdd:cd08191 325 E-EAADRAIERVEELLARIGIPTTLADLGVTEADLPGLAEKALSVTRlIANNPRPPTEEDLLRILRAAF 392
|
|
| Fe-ADH-like |
cd08196 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
16-383 |
7.73e-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: 341475 [Multi-domain] Cd Length: 367 Bit Score: 287.94 E-value: 7.73e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 16 FGPGAVSVVGERCKLLGGKKALLVTDKglRAIKDGAVDQTVKHLreAGIDVVIFDGVEPNPKDTNVRDGLAVFQKEHCDM 95
Cdd:cd08196 11 FGEGILKELPDIIKELGGKRGLLVTDP--SFIKSGLAKRIVESL--KGRIVAVFSDVEPNPTVENVDKCARLARENGADF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 96 IITVGGGSPHDCGKGIGIAATHPGDLYSY-AGIETLTHALPPIIAVNTTAGTASEVTRHCVLTNTKTKVKFVIVSWRNLP 174
Cdd:cd08196 87 VIAIGGGSVLDTAKAAACLAKTDGSIEDYlEGKKKIPKKGLPLIAIPTTAGTGSEVTPVAVLTDKEKGKKAPLVSPGFYP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 175 SVSINDPLLMVGKPAGLTAATGMDALTHAVEAYISKDANPVTDASAIQAIKLIATNLRQAVALGTNIKARENMACASLLA 254
Cdd:cd08196 167 DIAIVDPELTYSMPPKVTASTGIDALCHAIEAYWSINHQPISDALALEAAKLVLENLEKAYNNPNDKEAREKMALASLLA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 255 GMAFNNANLGYVHAMAHQLGGLYDMAHGVANAVLLPHVCRYNLIANPEKFADIATFMGenttglstMDAAECAINAIARL 334
Cdd:cd08196 247 GLAFSQTRTTASHACSYPLTSHFGIPHGEACALTLPSFIRLNAEALPGRLDELAKQLG--------FKDAEELADKIEEL 318
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 490200396 335 SKDVGIPQHLNELGVKEADFPYMAEMALKDGNAFSNPRKGNEKEIVEIF 383
Cdd:cd08196 319 KKRIGLRTRLSELGITEEDLEEIVEESFHPNRANNNPVEVTKEDLEKLL 367
|
|
| Fe-ADH-like |
cd14862 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
5-383 |
4.75e-92 |
|
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: 281.04 E-value: 4.75e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 5 MYDFLVPNVnFFGPGAVSVVGErcklLGGKKALLVTDKGLRAIkdGAVDQTVKHLREAGIDVVIFDGVEPNPKDTNVRDG 84
Cdd:cd14862 1 MWYFSSPKI-VFGEDALSHLEQ----LSGKRALIVTDKVLVKL--GLLKKVLKRLLQAGFEVEVFDEVEPEPPLETVLKG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 85 LAVFQKEHCDMIITVGGGSPHDCGKGIGI---------AATHPGDLYSYAGIETLthalppiIAVNTTAGTASEVTRHCV 155
Cdd:cd14862 74 AEAMREFEPDLIIALGGGSVMDAAKAAWVlyerpdldpEDISPLDLLGLRKKAKL-------IAIPTTSGTGSEATWAIV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 156 LTNTKTKVKFVIVSWRNLPSVSINDPLLMVGKPAGLTAATGMDALTHAVEAYISKDANPVTDASAIQAIKLIATNLRQAV 235
Cdd:cd14862 147 LTDTEEPRKIAVANPELVPDVAILDPEFVLGMPPKLTAGTGLDALAHAVEAYLSTWSNDFSDALALKAIELIFKYLPRAY 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 236 ALGTNIKARENMACASLLAGMAFNNANLGYVHAMAHQLGGLYDMAHGVANAVLLPHVCRYNLIANPEKFADIATFMGEnt 315
Cdd:cd14862 227 KDGDDLEAREKMHNAATIAGLAFGNSQAGLAHALGHSLGAVFHVPHGIAVGLFLPYVIEFYAKVTDERYDLLKLLGIE-- 304
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490200396 316 tglsTMDAAECA---INAIARLSKDVGIPQHLNELGVKEADF----PYMAEMALKDGNAFSNPRKGNEKEIVEIF 383
Cdd:cd14862 305 ----ARDEEEALkklVEAIRELYKEVGQPLSIKDLGISEEEFeeklDELVEYAMEDSCTITSPRPPSEEDLKKLF 375
|
|
| BDH |
cd08187 |
Butanol dehydrogenase catalyzes the conversion of butyraldehyde to butanol with the cofactor ... |
15-384 |
8.35e-88 |
|
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: 270.46 E-value: 8.35e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 15 FFGPGAVSVVGERCKLLGgKKALLVTDKGlRAIKDGAVDQTVKHLREAGIDVVIFDGVEPNPKDTNVRDGLAVFQKEHCD 94
Cdd:cd08187 11 IFGKGAIEELGEEIKKYG-KKVLLVYGGG-SIKKNGLYDRVVASLKEAGIEVVEFGGVEPNPRLETVREGIELAREENVD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 95 MIITVGGGSPHDCGKGIGIAATHPGDLYS-YAGIETLTHALpPIIAVNTTAGTASEVTRHCVLTNTKTKVKFVIVSWRNL 173
Cdd:cd08187 89 FILAVGGGSVIDAAKAIAAGAKYDGDVWDfFTGKAPPEKAL-PVGTVLTLAATGSEMNGGAVITNEETKEKLGFGSPLLR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 174 PSVSINDPLLMVGKPAGLTAATGMDALTHAVEAYISKDAN-PVTDASAIQAIKLIATNLRQAVALGTNIKAREN-MACAS 251
Cdd:cd08187 168 PKFSILDPELTYTLPKYQTAAGIVDIFSHVLEQYFTGTEDaPLQDRLAEGLLRTVIENGPKALKDPDDYEARANlMWAAT 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 252 llagMAFNN-ANLGY-----VHAMAHQLGGLYDMAHGVANAVLLPHVCRYNLIANPEKFADiatfMGEN----TTGLSTM 321
Cdd:cd08187 248 ----LALNGlLGAGRggdwaTHAIEHELSALYDITHGAGLAIVFPAWMRYVLKKKPERFAQ----FARRvfgiDPGGDDE 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490200396 322 DAAECAINAIARLSKDVGIPQHLNELGVKEADFPYMAEMALKDGNAFSNPRKGNEKEIVEIFR 384
Cdd:cd08187 320 ETALEGIEALEEFFKSIGLPTTLSELGIDEEDIEEMAEKAVRGGGLGGGFKPLTREDIEEILK 382
|
|
| HEPD |
cd08182 |
Hydroxyethylphosphoate dehydrogenase (HEPD) catalyzes the reduction of phosphonoacetaldehyde ... |
15-384 |
2.31e-83 |
|
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: 258.69 E-value: 2.31e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 15 FFGPGAVSVVGERCKLLGGKKALLVTDKGlrAIKDGAVDQTVKHLREaGIDVVIFDGVEPNPKDTNVRDGLAVFQKEHCD 94
Cdd:cd08182 5 IFGPGALAELKDLLGGLGARRVLLVTGPS--AVRESGAADILDALGG-RIPVVVFSDFSPNPDLEDLERGIELFRESGPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 95 MIITVGGGSPHDCGKGIGIAATHPGD--LYSYAGIETLTHALPPIIAVNTTAGTASEVTRHCVLTNTKTKVKFVIVSWRN 172
Cdd:cd08182 82 VIIAVGGGSVIDTAKAIAALLGSPGEnlLLLRTGEKAPEENALPLIAIPTTAGTGSEVTPFATIWDEAEGKKYSLAHPSL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 173 LPSVSINDPLLMVGKPAGLTAATGMDALTHAVEAYISKDANPVTDASAIQAIKLIATNLRQAVALGTNIKARENMACASL 252
Cdd:cd08182 162 YPDAAILDPELTLSLPLYLTASTGLDALSHAIESIWSVNANPESRAYALRAIRLILENLPLLLENLPNLEAREAMAEASL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 253 LAGMAFNNANLGYVHAMAHQLGGLYDMAHGVANAVLLPHVCRYNLIANPEKFAD-----IATFMGenttglsTMDAAECA 327
Cdd:cd08182 242 LAGLAISITKTTAAHAISYPLTSRYGVPHGHACALTLPAVLRYNAGADDECDDDprgreILLALG-------ASDPAEAA 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 490200396 328 iNAIARLSKDVGIPQHLNELGVKEADFPYMAEMALKDGNAFSNPRKGNEKEIVEIFR 384
Cdd:cd08182 315 -ERLRALLESLGLPTRLSEYGVTAEDLEALAASVNTPERLKNNPVRLSEEDLLRLLE 370
|
|
| YqdH |
COG1979 |
Alcohol dehydrogenase YqhD, Fe-dependent ADH family [Energy production and conversion]; |
15-386 |
3.08e-76 |
|
Alcohol dehydrogenase YqhD, Fe-dependent ADH family [Energy production and conversion];
Pssm-ID: 441582 [Multi-domain] Cd Length: 387 Bit Score: 240.74 E-value: 3.08e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 15 FFGPGAVSVVGERCKLlGGKKALLVTDKGlRAIKDGAVDQTVKHLREAGIDVVIFDGVEPNPKDTNVRDGLAVFQKEHCD 94
Cdd:COG1979 13 IFGKGQIAKLGEEIPK-YGKKVLLVYGGG-SIKKNGLYDQVKAALKEAGIEVVEFGGVEPNPRLETVRKGVELCKEEGID 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 95 MIITVGGGSPHDCGKGIGIAATHPGDLYS-YAGIETLTHALpPIIAVNTTAGTASEVTRHCVLTNTKTKVKFVIVSWRNL 173
Cdd:COG1979 91 FILAVGGGSVIDGAKAIAAGAKYDGDPWDiLTGKAPVEKAL-PLGTVLTLPATGSEMNSGSVITNEETKEKLGFGSPLVF 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 174 PSVSINDPLLMVGKPAGLTAATGMDALTHAVEAYISKDAN-PVTDASAIQAIKLIATNLRQAVALGTNIKAREN-MACAS 251
Cdd:COG1979 170 PKFSILDPELTYTLPKRQTANGIVDIFSHVMEQYFTYPVDaPLQDRFAEGLLRTLIEEGPKALKDPEDYDARANlMWAAT 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 252 llagMAFNN-ANLGY-----VHAMAHQLGGLYDMAHGVANAVLLPHVCRYNLIANPEKFADiatfMGENTTGLSTMDAAE 325
Cdd:COG1979 250 ----LALNGlIGAGVpqdwaTHMIEHELSALYDIDHGAGLAIVLPAWMRYVLEEKPEKFAQ----YAERVWGITEGDDEE 321
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490200396 326 CAINAIARLS---KDVGIPQHLNELGVKEADFPYMAEMALKDG-NAFSNPRKGNEKEIVEIFRQA 386
Cdd:COG1979 322 RALEGIEATEeffESLGLPTRLSEYGIDEEDIEEMAEKATAHGmTALGEFKDLTPEDVREILELA 386
|
|
| Fe-ADH-like |
cd08186 |
Iron-containing alcohol dehydrogenase; This family contains iron-containing alcohol ... |
15-387 |
1.49e-73 |
|
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: 233.70 E-value: 1.49e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 15 FFGPGAVSVVGERCKLLGGKKALLVTDKGlRAIKDGAVDQTVKHLREAGIDVVIFDGVEPNPKDTNVRDGLAVFQKEHCD 94
Cdd:cd08186 5 YFGVGAIAKIKDILKDLGIDKVIIVTGRS-SYKKSGAWDDVEKALEENGIEYVVYDKVTPNPTVDQADEAAKLARDFGAD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 95 MIITVGGGSPHDCGKGIGIAATHPGDL--YSYAGIETLTHALPpIIAVNTTAGTASEVTRHCVLTNTKTKVKFVIVSWRN 172
Cdd:cd08186 84 AVIAIGGGSPIDTAKSVAVLLAYGGKTarDLYGFRFAPERALP-LVAINLTHGTGSEVDRFAVATIPEKGYKPGIAYDCI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 173 LPSVSINDPLLMVGKPAGLTAATGMDALTHAVEAYISKDANPVTDASAIQAIKLIATNLRQAVALGTNIKARENMACASL 252
Cdd:cd08186 163 YPLYAIDDPRLTLTLPKEQTLYTSIDAFNHVYEAATTKVSSPYVITLAKEAIRLIAEYLPRALANPKDLEARYWLLYASM 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 253 LAGMAFNNANLGYVHAMAHQLGGLY-DMAHGVANAVLLPHVCRYNLIANPEKFADIATFMGENTTGLStmDAAECAINAI 331
Cdd:cd08186 243 IAGIAIDNGLLHLTHALEHPLSGLKpELPHGLGLALLGPAVVKYIYKAVPETLADILRPIVPGLKGTP--DEAEKAARGV 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 332 ARLSKDVGIPQHLNELGVKEADFPYMAEMALK----DGNAFSNPRKGNEKEIVEIFRQAF 387
Cdd:cd08186 321 EEFLFSVGFTEKLSDYGFTEDDVDRLVELAFTtpslDLLLSLAPVEVTEEVVREIYEESL 380
|
|
| PPD-like |
cd08181 |
1,3-propanediol dehydrogenase-like (PPD); This family contains proteins similar to 1, ... |
15-384 |
4.76e-72 |
|
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: 229.01 E-value: 4.76e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 15 FFGPGAVSVVGERCKLLGgKKALLVTdkGLRAIK-DGAVDQTVKHLREAGIDVVIFDGVEPNPKDTNVRDGLAVFQKEHC 93
Cdd:cd08181 8 YFGKNCVEKHADELAALG-KKALIVT--GKHSAKkNGSLDDVTEALEENGIEYFIFDEVEENPSIETVEKGAELARKEGA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 94 DMIITVGGGSPHDCGKGIGIAATHPGDLYS-YAGIETLTHAlpPIIAVNTTAGTASEVTRHCVLTNTKTKVKFVIVSWRN 172
Cdd:cd08181 85 DFVIGIGGGSPLDAAKAIALLAANKDGDEDlFQNGKYNPPL--PIVAIPTTAGTGSEVTPYSILTDHEKGTKKSFGNPLI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 173 LPSVSINDPLLMVGKPAGLTAATGMDALTHAVEAYISKDANPVTDASAIQAIKLIATNLRQAVALGTNIKARENMACASL 252
Cdd:cd08181 163 FPKLALLDPKYTLSLPEELTIDTAVDALSHAIEGYLSVKATPLSDALALEALRLIGECLPNLLGDELDEEDREKLMYAST 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 253 LAGMAFNNANLGYVHAMAHQLGGLYDMAHGVANAVLLPHVCRYNLIANPEKFADIATFMGENTTG-LSTMdaaecainai 331
Cdd:cd08181 243 LAGMVIAQTGTTLPHGLGYPLTYFKGIPHGRANGILLPAYLKLCEKQEPEKVDKILKLLGFGSIEeFQKF---------- 312
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 490200396 332 arLSKDVGIPQHlnelgVKEADFPYMAEMALKDGNAFSNPRKGNEKEIVEIFR 384
Cdd:cd08181 313 --LNRLLGKKEE-----LSEEELEKYADEAMKAKNKKNTPGNVTKEDILRIYR 358
|
|
| Fe-ADH-like |
cd14864 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
11-387 |
1.53e-70 |
|
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: 226.03 E-value: 1.53e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 11 PNVnFFGPGAVSVVGERCKLLGGKKaLLVTDKGLRAikDGAVDQTVKHLREAGIDVVIFDGVEPNPKDTNVRDGLAVFQK 90
Cdd:cd14864 5 PNI-VFGADSLERIGEEVKEYGSRF-LLITDPVLKE--SGLADKIVSSLEKAGISVIVFDEIPASATSDTIDEAAELARK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 91 EHCDMIITVGGGSPHDCGKGIGIAATHPGDLYSYAGIETLTHALPPIIAVNTTAGTASEVTRHCVLTNTKTKVKFVIVSW 170
Cdd:cd14864 81 AGADGIIAVGGGKVLDTAKAVAILANNDGGAYDFLEGAKPKKKPLPLIAVPTTPRSGFEFSDRFPVVDSRSREVKLLKAQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 171 RNLPSVSINDPLLMVGKPAGLTAATGMDALTHAVEAYISKDANPVTDASAIQAIKLIATNLRQAVALGTNIKARENMACA 250
Cdd:cd14864 161 PGLPKAVIVDPNLMASLTGNQTAAMALAALALAVEAYLSKKSNFFSDALALKAIELVSENLDGALADPKNTPAEELLAQA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 251 SLLAGMAFNNANLGYVHAMAHQLGGLYDMAHGVANAVLLPHVCRYNLIANPEKFADIATFMGENTTGLSTMDAAECAINA 330
Cdd:cd14864 241 GCLAGLAASSSSPGLATALALAVNSRYKVSKSLVASILLPHVIEYAATSAPDKYAKIARALGEDVEGASPEEAAIAAVEG 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 490200396 331 IARLSKDVGIPQHLNELGVKeADFPYMAEMALKDGNAFSNPRKGNEKEIVEIFRQAF 387
Cdd:cd14864 321 VRRLIAQLNLPTRLKDLDLA-SSLEQLAAIAEDAPKLNGLPRSMSSDDIFDILKAAF 376
|
|
| PRK15454 |
PRK15454 |
ethanolamine utilization ethanol dehydrogenase EutG; |
4-386 |
1.49e-69 |
|
ethanolamine utilization ethanol dehydrogenase EutG;
Pssm-ID: 185351 [Multi-domain] Cd Length: 395 Bit Score: 224.14 E-value: 1.49e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 4 RMYDFLVPNVNFFGPGAVSVVGERCKLLGGKKALLVTDKGLRaiKDGAVDQTVKHLREAGIDVVIFDGVEPNPKDTNVRD 83
Cdd:PRK15454 20 RVKTFSVPPVTLCGPGAVSSCGQQAQTRGLKHLFVMADSFLH--QAGMTAGLTRSLAVKGIAMTLWPCPVGEPCITDVCA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 84 GLAVFQKEHCDMIITVGGGSPHDCGKGIGIAATHPGDLYSYAGIETLTHALPPIIAVNTTAGTASEVTRHCVLTNTKTKV 163
Cdd:PRK15454 98 AVAQLRESGCDGVIAFGGGSVLDAAKAVALLVTNPDSTLAEMSETSVLQPRLPLIAIPTTAGTGSETTNVTVIIDAVSGR 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 164 KFVIVSWRNLPSVSINDPLLMVGKPAGLTAATGMDALTHAVEAYISKDANPVTDASAIQAIKLIATNLRQAVALGTNIKA 243
Cdd:PRK15454 178 KQVLAHASLMPDVAILDAALTEGVPSHVTAMTGIDALTHAIEAYSALNATPFTDSLAIGAIAMIGKSLPKAVGYGHDLAA 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 244 RENMACASLLAGMAFNNANLGYVHAMAHQLGGLYDMAHGVANAVLLPHVCRYNLIANPEKFADIatfmGENTTGLSTMDA 323
Cdd:PRK15454 258 RESMLLASCMAGMAFSSAGLGLCHAMAHQPGAALHIPHGLANAMLLPTVMEFNRMVCRERFSQI----GRALRTKKSDDR 333
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490200396 324 AecAINAIARLSKDVGIPQHLNELGVKEADFPYMAEMALKDGNAFSNPRKGNEKEIVEIFRQA 386
Cdd:PRK15454 334 D--AINAVSELIAEVGIGKRLGDVGATSAHYGAWAQAALEDICLRSNPRTASLEQIVGLYAAA 394
|
|
| MAR-like |
cd08192 |
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic ... |
15-386 |
2.61e-67 |
|
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: 217.50 E-value: 2.61e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 15 FFGPGAVSVVGERCKLLGGKKALLVTDKGLRAIKDgavdqTVKHLREA-GIDVV-IFDGVEPNPKDTNVRDGLAVFQKEH 92
Cdd:cd08192 5 SYGPGAVEALLHELATLGASRVFIVTSKSLATKTD-----VIKRLEEAlGDRHVgVFSGVRQHTPREDVLEAARAVREAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 93 CDMIITVGGGSPHDCGKGIGIA----ATHPGDLYSY----AGIETLTHALPPIIAVNTTAgTASEVTRHCVLTNTKTKVK 164
Cdd:cd08192 80 ADLLVSLGGGSPIDAAKAVALAlaedVTDVDQLDALedgkRIDPNVTGPTLPHIAIPTTL-SGAEFTAGAGATDDDTGHK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 165 fVIVSWRNL-PSVSINDPLLMVGKPAGLTAATGMDALTHAVEAYISKDANPVTDASAIQAIKLIATNLRQAVALGTNIKA 243
Cdd:cd08192 159 -QGFAHPELgPDAVILDPELTLHTPERLWLSTGIRAVDHAVETLCSPQATPFVDALALKALRLLFEGLPRSKADPEDLEA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 244 RENMACASLLAGMAF-NNANLGYVHAMAHQLGGLYDMAHGVANAVLLPHVCRYNLIANPEKFADIATFMGENTTGLS--T 320
Cdd:cd08192 238 RLKCQLAAWLSLFGLgSGVPMGASHAIGHQLGPLYGVPHGITSCIMLPAVLRFNAPVNAERQRLIARALGLVTGGLGreA 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490200396 321 MDAAEcainAIARLSKDVGIPQHLNELGVKEADFPYMAEMALKDGNAFSNPRKGNEKE-IVEIFRQA 386
Cdd:cd08192 318 ADAAD----AIDALIRELGLPRTLRDVGVGRDQLEKIAENALTDVWCRTNPRPITDKDdVLEILESA 380
|
|
| MAR |
cd08177 |
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic ... |
16-387 |
4.24e-65 |
|
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: 210.44 E-value: 4.24e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 16 FGPGAVSVVGERCKLLGGKKALLVTDKGLRAikdgAVDQTVKHLREAGidVVIFDGVEPN-PKDTnVRDGLAVFQKEHCD 94
Cdd:cd08177 6 FGAGTLAELAEELERLGARRALVLSTPRQRA----LAERVAALLGDRV--AGVFDGAVMHvPVEV-AERALAAAREAGAD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 95 MIITVGGGSPHDCGKGIgiaathpgdlysyagieTLTHALPpIIAVNTT-AGtaSEVTRhcVLTNTKTKVKFVIVSWRNL 173
Cdd:cd08177 79 GLVAIGGGSAIGLAKAI-----------------ALRTGLP-IVAVPTTyAG--SEMTP--IWGETEDGVKTTGRDPRVL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 174 PSVSINDPLLMVGKPAGLTAATGMDALTHAVEAYISKDANPVTDASAIQAIKLIATNLRQAVALGTNIKARENMACASLL 253
Cdd:cd08177 137 PRTVIYDPDLTLGLPAALSVASGLNALAHAVEALYAPDANPITSLLAEEGIRALARALPRLVADPSDLEARSDALYGAWL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 254 AGMAFNNANLGYVHAMAHQLGGLYDMAHGVANAVLLPHVCRYNLIANPEKFADIATFMGENttglstmDAAEcainAIAR 333
Cdd:cd08177 217 AGVVLGSVGMGLHHKLCHVLGGTFDLPHAETHAVVLPHVLAYNAPAAPDAMARLARALGGG-------DAAG----GLYD 285
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 490200396 334 LSKDVGIPQHLNELGVKEADFPYMAEMALKdgNAFSNPRKGNEKEIVEIFRQAF 387
Cdd:cd08177 286 LARRLGAPTSLRDLGMPEDDIDRAADLALA--NPYPNPRPVERDALRALLERAW 337
|
|
| Fe-ADH-like |
cd14866 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
15-386 |
2.79e-59 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341488 [Multi-domain] Cd Length: 384 Bit Score: 196.68 E-value: 2.79e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 15 FFGPGAVSVVGERCKLLGGKKALLVTDKGLRAikDGAVDQTVKHL---REAGIdvviFDGVEPNPKDTNVRDGLAVFQKE 91
Cdd:cd14866 9 FSGRGALARLGRELDRLGARRALVVCGSSVGA--NPDLMDPVRAAlgdRLAGV----FDGVRPHSPLETVEAAAEALREA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 92 HCDMIITVGGGSPHDCGKGIGIAATHPGDLYSYA---------GIETLTHALPPIIAVNTTAGTASeVTRHCVLTNTKTK 162
Cdd:cd14866 83 DADAVVAVGGGSAIVTARAASILLAEDRDVRELCtrraedglmVSPRLDAPKLPIFVVPTTPTTAD-VKAGSAVTDPPAG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 163 VKFVIVSWRNLPSVSINDPLLMVGKPAGLTAATGMDALTHAVEAYISKDANPVTDASAIQAIKLIATNLRQAVAlGTNIK 242
Cdd:cd14866 162 QRLALFDPKTRPAAVFYDPELLATAPASLVAGAAMNGFDMAVEGLYSRHADPLADATLMHALRLLADGLPRLAD-DDDPA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 243 ARENMACASLLAGMAFNNANLGYVHAMAHQLGGLYDMAHGVANAVLLPHVCRYNLIANPEKFADIATFMGENTTGlsTMD 322
Cdd:cd14866 241 ARADLVLAAVLAGYGTDHTGGGVIHALGHAIGARYGVQNGVVHAILLPHVLRFNAPATDGRLDRLAEALGVADAG--DEA 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490200396 323 AAECAINAIARLSKDVGIPQHLNELGVKEADFPYMAEMALKDGNAFSNPRKG-NEKEIVEIFRQA 386
Cdd:cd14866 319 SAAAVVDAVEALLDALGVPTRLRDLGVSREDLPAIAEAAMDDWFMDNNPRPVpTAEELEALLEAA 383
|
|
| 4HBD_NAD |
cd14860 |
4-hydroxybutyrate dehydrogenase, also called gamma-hydroxybutyrate dehydrogenase, catalyzes ... |
76-387 |
7.53e-39 |
|
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: 142.74 E-value: 7.53e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 76 PKDTNVRDGLAVFQKEHCDMIITVGGGSPHDCGKGIGIAATHP-GDLYsyAGIETLTHALPpIIAVNTTAGTASEVTRHC 154
Cdd:cd14860 62 PSDEMVEAIYKDIKKYGYKRVIAIGGGTVIDIAKLLALKGISPvLDLF--DGKIPLIKEKE-LIIVPTTCGTGSEVTNIS 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 155 VLTNTKTKVKFVIVSWRNLPSVSINDPLLMVGKPAGLTAATGMDALTHAVEAYISKDANPVTDASAIQAIKLIATNLRQA 234
Cdd:cd14860 139 IVELTSLGTKKGLAVDELYADKAVLIPELLKGLPYKVFATSSIDALIHAIESYLSPKATPYTEMFSYKAIEMILEGYQEI 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 235 VALGtnIKAR----ENMACASLLAGMAFNNANLGYVHAMAHQLGGLYDMAHGVANAVLLPHVCRYNLIANPE-KFADIAT 309
Cdd:cd14860 219 AEKG--EEARfpllGDFLIASNYAGIAFGNAGCAAVHALSYPLGGKYHVPHGEANYAVFTGVLKNYQEKNPDgEIKKLNE 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 310 FMGE--NTTGLSTMDAAECAINAIarlskdvgIPQH-LNELGVKEADFPYMAEMALKD-----GNafsNPRKGNEKEIVE 381
Cdd:cd14860 297 FLAKilGCDEEDVYDELEELLNKI--------LPKKpLHEYGMKEEEIDEFADSVMENqqrllAN---NYVPLDREDVAE 365
|
....*.
gi 490200396 382 IFRQAF 387
Cdd:cd14860 366 IYKELY 371
|
|
| DHQ_Fe-ADH |
cd07766 |
Dehydroquinate synthase-like (DHQ-like) and iron-containing alcohol dehydrogenases (Fe-ADH); ... |
15-362 |
7.67e-38 |
|
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: 137.50 E-value: 7.67e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 15 FFGPGAVSVVGErCKLLGGKKALLVTDKGlraIKDGAVDQTVKHLREaGIDVVIFDGVEPNPKDTNVRDGLAVFQKEHCD 94
Cdd:cd07766 5 VFGEGAIAKLGE-IKRRGFDRALVVSDEG---VVKGVGEKVADSLKK-GLAVAIFDFVGENPTFEEVKNAVERARAAEAD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 95 MIITVGGGSPHDCGKGIGIaathpgdlysyagieTLTHALpPIIAVNTTAGTASEVTRHCVLTNTKTKVKFviVSWRNLP 174
Cdd:cd07766 80 AVIAVGGGSTLDTAKAVAA---------------LLNRGI-PFIIVPTTASTDSEVSPKSVITDKGGKNKQ--VGPHYNP 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 175 SVSINDPLLMVGKPAGLTAATGMDALTHAVEayiskdanpvtdasaiqaikliatnlrqavalgtnikaRENMACASLLA 254
Cdd:cd07766 142 DVVFVDTDITKGLPPRQVASGGVDALAHAVE--------------------------------------LEKVVEAATLA 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 255 GMA-FNNANLGYVHAMAHQLGGLYDMAHGVANAVLLPHVCRYNLIANPEKFADIAtfmgenttglstmdaaecainAIAR 333
Cdd:cd07766 184 GMGlFESPGLGLAHAIGHALTAFEGIPHGEAVAVGLPYVLKVANDMNPEPEAAIE---------------------AVFK 242
|
330 340
....*....|....*....|....*....
gi 490200396 334 LSKDVGIPQHLNELGVKEADFPYMAEMAL 362
Cdd:cd07766 243 FLEDLGLPTHLADLGVSKEDIPKLAEKAL 271
|
|
| Fe-ADH_KdnB-like |
cd08184 |
Iron-containing alcohol dehydrogenase similar to Shewanella oneidensis KdnB required for Kdo8N ... |
10-285 |
2.45e-25 |
|
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: 105.04 E-value: 2.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 10 VPNVNFfGPGAVSVVGE---RCKLLGGKKALLVTDKGLRAikdgavDQTVKHLREAGIDVVIFDGVEPNPKDTNV---RD 83
Cdd:cd08184 1 VPKYLF-GRGSFDQLGEllaERRKSNNDYVVFFIDDVFKG------KPLLDRLPLQNGDLLIFVDTTDEPKTDQIdalRA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 84 GLAVFQKEHCDMIITVGGGSPHDCGKGIGIAATHPGDLYSYAGIETLTHALPPIIAVNTTAGTASEVTRHCVLTNtKTKv 163
Cdd:cd08184 74 QIRAENDKLPAAVVGIGGGSTMDIAKAVSNMLTNPGSAADYQGWDLVKNPGIYKIGVPTLSGTGAEASRTAVLTG-PEK- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 164 KFVIVSWRNLPSVSINDPLLMVGKPAGLTAATGMDALTHAVEAYISKDANPVTDASAIQAIKLIatnlRQaVALG---TN 240
Cdd:cd08184 152 KLGINSDYTVFDQVILDPELIATVPRDQYFYTGMDCYIHCVESLNGTYRNAFGDAYAEKALELC----RD-VFLSddmMS 226
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 490200396 241 IKARENMACASLLAGMAFNNANLGYVHAMAHQLGGLYDMAHGVAN 285
Cdd:cd08184 227 PENREKLMVASYLGGSSIANSQVGVCHALSYGLSVVLGTHHGVAN 271
|
|
| PRK15138 |
PRK15138 |
alcohol dehydrogenase; |
16-357 |
7.82e-17 |
|
alcohol dehydrogenase;
Pssm-ID: 185092 [Multi-domain] Cd Length: 387 Bit Score: 81.38 E-value: 7.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 16 FGPGAVSVVGERcklLGGKKALLVTDKGLRAIKDGAVDQTVKHLreAGIDVVIFDGVEPNPKDTNVRDGLAVFQKEHCDM 95
Cdd:PRK15138 14 FGKGAIAGLREQ---IPADARVLITYGGGSVKKTGVLDQVLDAL--KGMDVLEFGGIEPNPTYETLMKAVKLVREEKITF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 96 IITVGGGSPHDCGKGIGIAATHPGDLYSYAGIET----LTHALpPIIAVNTTAGTASEVTRHCVLTNTKTKVKFVIVSWR 171
Cdd:PRK15138 89 LLAVGGGSVLDGTKFIAAAANYPENIDPWHILETggkeIKSAI-PMGSVLTLPATGSESNAGAVISRKTTGDKQAFHSPH 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 172 NLPSVSINDPLLMVGKPAGLTAATGMDALTHAVEAYISKDAN-PVTDASAIQAIKLIATNLRQAVALGTNIKARENMACA 250
Cdd:PRK15138 168 VQPVFAVLDPVYTYTLPPRQVANGVVDAFVHTVEQYVTYPVDaKIQDRFAEGILLTLIEEGPKALKEPENYDVRANVMWA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 251 sllAGMAFNNANLGYV------HAMAHQLGGLYDMAHGVANAVLLPHVCRYNLIANPEKFADIATFMGENTTGlSTMDAA 324
Cdd:PRK15138 248 ---ATQALNGLIGAGVpqdwatHMLGHELTAMHGLDHAQTLAIVLPALWNEKRDTKRAKLLQYAERVWNITEG-SDDERI 323
|
330 340 350
....*....|....*....|....*....|...
gi 490200396 325 ECAINAIARLSKDVGIPQHLNELGVKEADFPYM 357
Cdd:PRK15138 324 DAAIAATRNFFEQMGVPTRLSDYGLDGSSIPAL 356
|
|
| GldA |
COG0371 |
Glycerol dehydrogenase or related enzyme, iron-containing ADH family [Energy production and ... |
17-386 |
2.60e-16 |
|
Glycerol dehydrogenase or related enzyme, iron-containing ADH family [Energy production and conversion]; Glycerol dehydrogenase or related enzyme, iron-containing ADH family is part of the Pathway/BioSystem: Isoprenoid biosynthesis
Pssm-ID: 440140 [Multi-domain] Cd Length: 355 Bit Score: 79.44 E-value: 2.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 17 GPGAVSVVGERCKLLGgKKALLVTDKGLRAIkdgAVDQTVKHLREAGIDVVIFDgVEPNPKDTNVRDGLAVFQKEHCDMI 96
Cdd:COG0371 12 GEGALDELGEYLADLG-KRALIITGPTALKA---AGDRLEESLEDAGIEVEVEV-FGGECSEEEIERLAEEAKEQGADVI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 97 ITVGGGSPHDCGKGIGIaathpgdlysYAGIetlthalpPIIAVNTTAGTASEVTRHCVLTNTKTKVKFVIVSWRNlPSV 176
Cdd:COG0371 87 IGVGGGKALDTAKAVAY----------RLGL--------PVVSVPTIASTDAPASPLSVIYTEDGAFDGYSFLAKN-PDL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 177 SINDPLLMVGKPAGLTAAtGM-DALTHAVEAYISKDAN-----PVTDASAIQAIKLIATNLRQ-------AVALGTNIKA 243
Cdd:COG0371 148 VLVDTDIIAKAPVRLLAA-GIgDALAKWYEARDWSLAHrdlagEYYTEAAVALARLCAETLLEygeaaikAVEAGVVTPA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 244 RENMACAS-LLAGMAFN----NANLGYVHAMAH---QLGGLYDMAHGvanavllphvcrynlianpEKFAdIATFMgent 315
Cdd:COG0371 227 LERVVEANlLLSGLAMGigssRPGSGAAHAIHNgltALPETHHALHG-------------------EKVA-FGTLV---- 282
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490200396 316 tgLSTMDAAECAINAIARLSKDVGIPQHLNELGVKEADF---PYMAEMALKDGNAFSN-PRKGNEKEIVEIFRQA 386
Cdd:COG0371 283 --QLVLEGRPEEIEELLDFLRSVGLPTTLADLGLDDETEeelLTVAEAARPERYTILNlPFEVTPEAVEAAILAT 355
|
|
| GlyDH |
cd08170 |
Glycerol dehydrogenases (GlyDH) catalyzes oxidation of glycerol to dihydroxyacetone in ... |
17-386 |
9.06e-09 |
|
Glycerol dehydrogenases (GlyDH) catalyzes oxidation of glycerol to dihydroxyacetone in glycerol dissmilation; Glycerol dehydrogenases (GlyDH) is a key enzyme in the glycerol dissimilation pathway. In anaerobic conditions, many microorganisms utilize glycerol as a source of carbon through coupled oxidative and reductive pathways. One of the pathways involves the oxidation of glycerol to dihydroxyacetone with the reduction of NAD+ to NADH catalyzed by glycerol dehydrogenases. Dihydroxyacetone is then phosphorylated by dihydroxyacetone kinase and enters the glycolytic pathway for further degradation. The activity of GlyDH is zinc-dependent; the zinc ion plays a role in stabilizing an alkoxide intermediate at the active site.
Pssm-ID: 341449 [Multi-domain] Cd Length: 351 Bit Score: 56.65 E-value: 9.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 17 GPGAVSVVGERCKLLGgKKALLVTDKGlraIKDGAVDQTVKHLREAGIDV--VIFDGvEPNpkDTNVRDGLAVFQKEHCD 94
Cdd:cd08170 7 GPGALDRLGEYLAPLG-KKALVIADPF---VLDLVGERLEESLEKAGLEVvfEVFGG-ECS--REEIERLAAIARANGAD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 95 MIITVGGGSPHDCGKGIGIaathpgdlysYAGIetlthalpPIIAVNTTAGTASEVTRHCVLTNTKTKVKFVIVSWRNlP 174
Cdd:cd08170 80 VVIGIGGGKTIDTAKAVAD----------YLGL--------PVVIVPTIASTDAPCSALSVIYTEDGEFDEYLFLPRN-P 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 175 SVSINDPLLMVGKPAGLTAAtGM-DALTHAVEAYISKDANPVTDASAIQ-----AI-KLIATNLR-------QAVALGTN 240
Cdd:cd08170 141 DLVLVDTEIIAKAPVRFLVA-GMgDALATYFEARACARSGAPNMAGGRPtlaalALaELCYDTLLeygvaakAAVEAGVV 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 241 IKARENM--ACAsLLAGMAFNNANLGYVHAMAH---QLGGLYDMAHG--VAnavllphvcrynlianpekFADIATFMGE 313
Cdd:cd08170 220 TPALEAVieANT-LLSGLGFESGGLAAAHAIHNgltALPETHHLLHGekVA-------------------FGTLVQLVLE 279
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490200396 314 NttglstmdAAECAINAIARLSKDVGIPQHLNELGVK---EADFPYMAEMALKDGNAFSN-PRKGNEKEIVEIFRQA 386
Cdd:cd08170 280 G--------RPDEEIEEVIRFCRSVGLPVTLADLGLEdvtDEELRKVAEAACAPGETIHNmPFPVTPEDVVDAILAA 348
|
|
| GlyDH-like |
cd08550 |
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins. ... |
17-259 |
7.40e-08 |
|
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: 53.69 E-value: 7.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 17 GPGAVSVVGERCKLLGgKKALLVTDKglRAIKdgAVDQTVKH-LREAGID--VVIFDGVepnPKDTNVRDGLAVFQKEHC 93
Cdd:cd08550 7 EPGILAKAGEYIAPLG-KKALIIGGK--TALE--AVGEKLEKsLEEAGIDyeVEVFGGE---CTEENIERLAEKAKEEGA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 94 DMIITVGGGSPHDCGKGIGiaathpgdlySYAGIetlthalpPIIAVNTTAGTASEVTRHCVLTNTKTKVKFVIVSWRNl 173
Cdd:cd08550 79 DVIIGIGGGKVLDTAKAVA----------DRLGL--------PVVTVPTIAATCAAWSALSVLYDEEGEFLGYSLLKRS- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 174 PSVSINDPLLMVGKPAGLTAAtGM-DALT--HAVEAYISKDANPVTDASAIQAIKL-------IATNLRQAVALGTNIKA 243
Cdd:cd08550 140 PDLVLVDTDIIAAAPVRYLAA-GIgDTLAkwYEARPSSRGGPDDLALQAAVQLAKLaydllleYGVQAVEDVRQGKVTPA 218
|
250
....*....|....*..
gi 490200396 244 RENMACAS-LLAGMAFN 259
Cdd:cd08550 219 LEDVVDAIiLLAGLVGS 235
|
|
| Gro1PDH |
cd08173 |
Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) catalyzes the reversible conversion between ... |
16-109 |
1.18e-04 |
|
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: 43.70 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 16 FGPGAVSVVGERC-KLLGGKKALLVTDKGLRAIKDGAVdqtVKHLREAGIDVVIFDGVEPNpKDTNVRDGLAVFQKEHCD 94
Cdd:cd08173 7 VGHGAINKIGEVLkKLLLGKRALIITGPNTYKIAGKRV---EDLLESSGVEVVIVDIATIE-EAAEVEKVKKLIKESKAD 82
|
90
....*....|....*
gi 490200396 95 MIITVGGGSPHDCGK 109
Cdd:cd08173 83 FIIGVGGGKVIDVAK 97
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| G1PDH |
cd08175 |
Glycerol-1-phosphate dehydrogenase (G1PDH) catalyzes the reversible reduction of ... |
17-109 |
2.43e-03 |
|
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: 39.42 E-value: 2.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490200396 17 GPGAVSVVGERCK-LLGGKKALLVTDkglRAIKDGAVDQTVKHLREAGIDVVIFdgvEPNPKDTNVRDGLAVFQ-----K 90
Cdd:cd08175 7 GEGALKKLPEYLKeLFGGKKVLVVAD---ENTYAAAGEEVEAALEEAGVTVCLL---IFPGEGDLIADEAAVGKvllelE 80
|
90
....*....|....*....
gi 490200396 91 EHCDMIITVGGGSPHDCGK 109
Cdd:cd08175 81 KDTDLIIAVGSGTINDLTK 99
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