|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10624 |
PRK10624 |
L-1,2-propanediol oxidoreductase; Provisional |
1-383 |
0e+00 |
|
L-1,2-propanediol oxidoreductase; Provisional
Pssm-ID: 182595 [Multi-domain] Cd Length: 382 Bit Score: 731.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 1 MTHRMILNETSYFGEGAINHLVEEIQKRQFNKALIVTDADLVKFNVVSKVTQLLDNAKLDYAIYDAVIPNPTIDTVQQGL 80
Cdd:PRK10624 1 MANRMILNETAYFGRGAIGALTDEVKRRGFKKALIVTDKTLVKCGVVAKVTDVLDAAGLAYEIYDGVKPNPTIEVVKEGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 81 KHFKQFNADYLIAIGGGSPQDTAKAIGIIINNPQYEDVVSLEGVAPTQNPAVPIIAIPTTAGTAAEVTINYVITDNKLCR 160
Cdd:PRK10624 81 EVFKASGADYLIAIGGGSPQDTCKAIGIISNNPEFADVRSLEGVAPTKKPSVPIIAIPTTAGTAAEVTINYVITDEEKRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 161 KFVCVDPHSIPIVAIIDPLMMASMPASLKAATGVDALTHAIEGYITKGAWALTDALHLKSIELISNSLRQSVKGDPQGVE 240
Cdd:PRK10624 161 KFVCVDPHDIPQVAFVDADMMDSMPPGLKAATGVDALTHAIEGYITRGAWALTDMLHLKAIEIIAGALRGAVAGDKEAGE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 241 TMALAQYMAGMGFSNVGLGLVHGMAHPLGAFYNTPHGVANAILLPHIMAYNANYTGEKYRDIARAMGVKnIDSLPLQEAR 320
Cdd:PRK10624 241 GMALGQYIAGMGFSNVGLGLVHGMAHPLGAFYNTPHGVANAILLPHVMEYNADFTGEKYRDIARAMGVK-VEGMSLEEAR 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491051849 321 DTAIAAVFALNKNVGIPEKLREIGMKPEDIPSLAQAAFDDVCTGGNPRDATLEDIAELYQAIY 383
Cdd:PRK10624 320 NAAVEAVKALNRDVGIPPHLRDVGVKEEDIPALAQAAFDDVCTGGNPREATLEDIVELYKKAW 382
|
|
| lactal_redase |
TIGR02638 |
lactaldehyde reductase; This clade of genes encoding iron-containing alcohol dehydrogenase ... |
4-379 |
0e+00 |
|
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: 625.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 4 RMILNETSYFGEGAINHLVEEIQKRQFNKALIVTDADLVKFNVVSKVTQLLDNAKLDYAIYDAVIPNPTIDTVQQGLKHF 83
Cdd:TIGR02638 3 RLILNETSYFGAGAIEDIVDEVKRRGFKKALVVTDKDLIKFGVADKVTDLLDEAGIAYELFDEVKPNPTITVVKAGVAAF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 84 KQFNADYLIAIGGGSPQDTAKAIGIIINNPQYEDVVSLEGVAPTQNPAVPIIAIPTTAGTAAEVTINYVITDNKLCRKFV 163
Cdd:TIGR02638 83 KASGADYLIAIGGGSPIDTAKAIGIISNNPEFADVRSLEGVAPTKKPGVPIIAIPTTAGTAAEVTINYVITDEENKRKFV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 164 CVDPHSIPIVAIIDPLMMASMPASLKAATGVDALTHAIEGYITKGAWALTDALHLKSIELISNSLRQSVKG--DPQGVET 241
Cdd:TIGR02638 163 CVDPHDIPDVAVIDAEMMYSMPKSLTAATGMDALTHAIEGYITKGAWELTDMLHLKAIEIIARWLRSAVEGgkDLEAREQ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 242 MALAQYMAGMGFSNVGLGLVHGMAHPLGAFYNTPHGVANAILLPHIMAYNANYTGEKYRDIARAMGVKnIDSLPLQEARD 321
Cdd:TIGR02638 243 MALGQYVAGMGFSNVGLGLVHGMAHPLGAFYNTPHGVANAILLPHVMEFNAEFTGEKYREIAKAMGVK-TEGMSDEEARD 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 491051849 322 TAIAAVFALNKNVGIPEKLREIGMKPEDIPSLAQAAFDDVCTGGNPRDATLEDIAELY 379
Cdd:TIGR02638 322 AAVEAVKTLSKRVGIPEGLSELGVKEEDIPALAEAALADVCTGGNPRETTVEEIEELY 379
|
|
| LPO |
cd08176 |
Lactadehyde:propanediol oxidoreductase (LPO) catalyzes the interconversion between ... |
4-380 |
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: 621.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 4 RMILNETSYFGEGAINHLVEEIQKRQFNKALIVTDADLVKFNVVSKVTQLLDNAKLDYAIYDAVIPNPTIDTVQQGLKHF 83
Cdd:cd08176 2 RFVLNPTSYFGWGAIEEIGEEAKKRGFKKALIVTDKGLVKFGIVDKVTDVLKEAGIAYTVFDEVKPNPTIENVMAGVAAY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 84 KQFNADYLIAIGGGSPQDTAKAIGIIINNPqYEDVVSLEGVAPTQNPAVPIIAIPTTAGTAAEVTINYVITDNKLCRKFV 163
Cdd:cd08176 82 KESGADGIIAVGGGSSIDTAKAIGIIVANP-GADVRSLEGVAPTKNPAVPIIAVPTTAGTGSEVTINYVITDTEKKRKFV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 164 CVDPHSIPIVAIIDPLMMASMPASLKAATGVDALTHAIEGYITKGAWALTDALHLKSIELISNSLRQSVKGD--PQGVET 241
Cdd:cd08176 161 CVDPHDIPTVAIVDPDLMSSMPKGLTAATGMDALTHAIEGYITKGAWELSDMLALKAIELIAKNLRKAVANPnnVEAREN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 242 MALAQYMAGMGFSNVGLGLVHGMAHPLGAFYNTPHGVANAILLPHIMAYNANYTGEKYRDIARAMGVKNIDSLpLQEARD 321
Cdd:cd08176 241 MALAQYIAGMAFSNVGLGIVHSMAHPLSAFYDTPHGVANAILLPYVMEFNAPATGEKYRDIARAMGVDTTGMS-DEEAAE 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 491051849 322 TAIAAVFALNKNVGIPEKLREIGMKPEDIPSLAQAAFDDVCTGGNPRDATLEDIAELYQ 380
Cdd:cd08176 320 AAVDAVKKLSKDVGIPQKLSELGVKEEDIEALAEDALNDVCTPGNPREATKEDIIALYK 378
|
|
| PDDH |
cd08188 |
1,3-Propanediol (1,3-PD) dehydrogenase; This family includes 1,3-propanediol (1,3-PD) ... |
10-379 |
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: 506.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 10 TSYFGEGAINHLVEEIQKRQFNKALIVTDADLVKFNVVSKVTQLLDNAKLDYAIYDAVIPNPTIDTVQQGLKHFKQFNAD 89
Cdd:cd08188 8 VNLFGPGCLKEIGDELKKLGGKKALIVTDKGLVKLGLVKKVTDVLEEAGIEYVIFDGVQPNPTVTNVNEGLELFKENGCD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 90 YLIAIGGGSPQDTAKAIGIIINNPQyeDVVSLEGVAPTQNPAVPIIAIPTTAGTAAEVTINYVITDNKLCRKFVCVDPHS 169
Cdd:cd08188 88 FIISVGGGSAHDCAKAIGILATNGG--EIEDYEGVDKSKKPGLPLIAINTTAGTASEVTRFAVITDEERHVKMVIVDWNV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 170 IPIVAIIDPLMMASMPASLKAATGVDALTHAIEGYITKGAWALTDALHLKSIELISNSLRQSVKgDPQGVET---MALAQ 246
Cdd:cd08188 166 TPTIAVNDPELMLGMPPSLTAATGMDALTHAIEAYVSTGATPLTDALALEAIRLIAENLPKAVA-NGKDLEArenMAYAQ 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 247 YMAGMGFSNVGLGLVHGMAHPLGAFYNTPHGVANAILLPHIMAYNANYTGEKYRDIARAMGVkNIDSLPLQEARDTAIAA 326
Cdd:cd08188 245 FLAGMAFNNAGLGYVHAMAHQLGGFYNLPHGVCNAILLPHVMEFNLPACPERFADIARALGE-NTEGLSDEEAAEAAIEA 323
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 491051849 327 VFALNKNVGIPEKLREIGMKPEDIPSLAQAAFDDVCTGGNPRDATLEDIAELY 379
Cdd:cd08188 324 IRKLSRRVGIPSGLKELGVKEEDFPLLAENALKDACGPTNPRQATKEDVIAIY 376
|
|
| EutG |
COG1454 |
Alcohol dehydrogenase, class IV [Energy production and conversion]; |
1-383 |
1.44e-173 |
|
Alcohol dehydrogenase, class IV [Energy production and conversion];
Pssm-ID: 441063 [Multi-domain] Cd Length: 381 Bit Score: 488.48 E-value: 1.44e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 1 MTHRMILNETSYFGEGAINHLVEEIQKRQFNKALIVTDADLVKFNVVSKVTQLLDNAKLDYAIYDAVIPNPTIDTVQQGL 80
Cdd:COG1454 1 MMFTFRLPTRIVFGAGALAELGEELKRLGAKRALIVTDPGLAKLGLLDRVLDALEAAGIEVVVFDDVEPNPTVETVEAGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 81 KHFKQFNADYLIAIGGGSPQDTAKAIGIIINNPqyEDVVSLEGVAPTQNPAVPIIAIPTTAGTAAEVTINYVITDNKLCR 160
Cdd:COG1454 81 AAAREFGADVVIALGGGSAIDAAKAIALLATNP--GDLEDYLGIKKVPGPPLPLIAIPTTAGTGSEVTPFAVITDPETGV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 161 KFVCVDPHSIPIVAIIDPLMMASMPASLKAATGVDALTHAIEGYITKGAWALTDALHLKSIELISNSLRQSVK--GDPQG 238
Cdd:COG1454 159 KKGIADPELLPDVAILDPELTLTLPPSLTAATGMDALTHAIEAYVSKGANPLTDALALEAIRLIARNLPRAVAdgDDLEA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 239 VETMALAQYMAGMGFSNVGLGLVHGMAHPLGAFYNTPHGVANAILLPHIMAYNANYTGEKYRDIARAMGVKniDSLPLQE 318
Cdd:COG1454 239 REKMALASLLAGMAFANAGLGAVHALAHPLGGLFHVPHGLANAILLPHVLRFNAPAAPERYAEIARALGLD--VGLSDEE 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491051849 319 ARDTAIAAVFALNKNVGIPEKLREIGMKPEDIPSLAQAAFDDVCTGGNPRDATLEDIAELYQAIY 383
Cdd:COG1454 317 AAEALIEAIRELLRDLGIPTRLSELGVTEEDLPELAELALADRCLANNPRPLTEEDIEAILRAAY 381
|
|
| Fe-ADH |
cd08551 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains large ... |
12-379 |
8.94e-158 |
|
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: 448.05 E-value: 8.94e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 12 YFGEGAINHLVEEIQKRQFNKALIVTDADLVKFNVVSKVTQLLDNAKLDYAIYDAVIPNPTIDTVQQGLKHFKQFNADYL 91
Cdd:cd08551 5 VFGAGALARLGEELKALGGKKVLLVTDPGLVKAGLLDKVLESLKAAGIEVEVFDDVEPNPTVETVEAAAELAREEGADLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 92 IAIGGGSPQDTAKAIGIIINNPQyeDVVSLEGVAPTQNPAVPIIAIPTTAGTAAEVTINYVITDNKLCRKFVCVDPHSIP 171
Cdd:cd08551 85 IAVGGGSVLDTAKAIAVLATNGG--SIRDYEGIGKVPKPGLPLIAIPTTAGTGSEVTPNAVITDPETGRKMGIVSPYLLP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 172 IVAIIDPLMMASMPASLKAATGVDALTHAIEGYITKGAWALTDALHLKSIELISNSLRQSVKgDPQGVE---TMALAQYM 248
Cdd:cd08551 163 DVAILDPELTLSLPPSVTAATGMDALTHAIEAYTSKKANPISDALALEAIRLIGKNLRRAVA-DGSDLEareAMLLASLL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 249 AGMGFSNVGLGLVHGMAHPLGAFYNTPHGVANAILLPHIMAYNANYTGEKYRDIARAMGVkNIDSLPLQEARDTAIAAVF 328
Cdd:cd08551 242 AGIAFGNAGLGAVHALAYPLGGRYHIPHGVANAILLPYVMEFNLPACPEKYAEIAEALGE-DVEGLSDEEAAEAAVEAVR 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 491051849 329 ALNKNVGIPEKLREIGMKPEDIPSLAQAAFDDVCTGGN-PRDATLEDIAELY 379
Cdd:cd08551 321 ELLRDLGIPTSLSELGVTEEDIPELAEDAMKSGRLLSNnPRPLTEEDIREIY 372
|
|
| Fe-ADH |
pfam00465 |
Iron-containing alcohol dehydrogenase; |
12-375 |
5.77e-141 |
|
Iron-containing alcohol dehydrogenase;
Pssm-ID: 425696 [Multi-domain] Cd Length: 362 Bit Score: 405.06 E-value: 5.77e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 12 YFGEGAINHLVEEIQKRQFnKALIVTDADLVKFNVVSKVTQLLDNAKLDYAIYDAVIPNPTIDTVQQGLKHFKQFNADYL 91
Cdd:pfam00465 5 VFGAGALAELGEELKRLGA-RALIVTDPGSLKSGLLDKVLASLEEAGIEVVVFDGVEPEPTLEEVDEAAALAREAGADVI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 92 IAIGGGSPQDTAKAIGIIINNPqyEDVVSLEGVAPTQNPAVPIIAIPTTAGTAAEVTINYVITDNKLCRKFVCVDPHSIP 171
Cdd:pfam00465 84 IAVGGGSVIDTAKAIALLLTNP--GDVWDYLGGKPLTKPALPLIAIPTTAGTGSEVTPLAVITDTETGEKLGIFSPKLLP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 172 IVAIIDPLMMASMPASLKAATGVDALTHAIEGYITKGAWALTDALHLKSIELISNSLRQSVK--GDPQGVETMALAQYMA 249
Cdd:pfam00465 162 DLAILDPELTLTLPPRLTAATGMDALAHAVEAYVSKGANPLTDALALEAIRLIAENLPRAVAdgEDLEARENMLLASTLA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 250 GMGFSNVGLGLVHGMAHPLGAFYNTPHGVANAILLPHIMAYNANYTGEKYRDIARAMGVKNIDslplqEARDTAIAAVFA 329
Cdd:pfam00465 242 GLAFSNAGLGAAHALAHALGGRYGIPHGLANAILLPYVLRFNAPAAPEKLAQLARALGEDSDE-----EAAEEAIEALRE 316
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 491051849 330 LNKNVGIPEKLREIGMKPEDIPSLAQAAFDDVCTGGNPRDATLEDI 375
Cdd:pfam00465 317 LLRELGLPTTLSELGVTEEDLDALAEAALRDRSLANNPRPLTAEDI 362
|
|
| Fe-ADH-like |
cd08194 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
12-383 |
4.06e-132 |
|
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: 383.42 E-value: 4.06e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 12 YFGEGAINHLVEEIQKRQFNKALIVTDADLVKFNVVSKVTQLLDNAKLDYAIYDAVIPNPTIDTVQQGLKHFKQFNADYL 91
Cdd:cd08194 5 IIGGGALEELGEEAASLGGKRALIVTDKVMVKLGLVDKVTQLLAEAGIAYAVFDDVVSEPTDEMVEEGLALYKEGGCDFI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 92 IAIGGGSPQDTAKAIGIIINNPqyEDVVSLEGVAPTQNPAVPIIAIPTTAGTAAEVTINYVITDNKLCRKFVCVDPHSIP 171
Cdd:cd08194 85 VALGGGSPIDTAKAIAVLATNG--GPIRDYMGPRKVDKPGLPLIAIPTTAGTGSEVTRFTVITDTETDVKMLLKGPALLP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 172 IVAIIDPLMMASMPASLKAATGVDALTHAIEGYITKGAWALTDALHLKSIELISNSLRQSVK--GDPQGVETMALAQYMA 249
Cdd:cd08194 163 AVAIVDPELTLSMPPRVTAATGIDALTHAIEAYVSRKAQPLTDTLALSAIKLIGRNLRRAYAdgDDLEAREAMMLAALEA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 250 GMGFSNVGLGLVHGMAHPLGAFYNTPHGVANAILLPHIMAYNANYTGEKYRDIARAMGVkNIDSLPLQEARDTAIAAVFA 329
Cdd:cd08194 243 GIAFSNSSVALVHGMSRPIGALFHVPHGLSNAMLLPAVTEFSLPGAPERYAEIARAMGI-ATEGDSDEEAAEKLVEALER 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 491051849 330 LNKNVGIPeKLREIGMKPED----IPSLAQAAFDDVCTGGNPRDATLEDIAELYQAIY 383
Cdd:cd08194 322 LCADLEIP-TLREYGIDEEEfeaaLDKMAEDALASGSPANNPRVPTKEEIIELYREAW 378
|
|
| Fe-ADH-like |
cd17814 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
13-379 |
6.34e-123 |
|
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: 359.55 E-value: 6.34e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 13 FGEGAINHLVEEIQKRQFNKALIVTDADLVKFNVVSKVTQLLDNAKLDYAIYDAVIPNPTIDTVQQGLKHFKQFNADYLI 92
Cdd:cd17814 9 FGVGARKLAGRYAKNLGARKVLVVTDPGVIKAGWVDEVLDSLEAEGLEYVVFSDVTPNPRDFEVMEGAELYREEGCDGIV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 93 AIGGGSPQDTAKAIGIIINNPQyeDVVSLEGVAPTQNPAVPIIAIPTTAGTAAEVTINYVITDNKLCRKFVCVDPHSIPI 172
Cdd:cd17814 89 AVGGGSPIDCAKGIGIVVSNGG--HILDYEGVDKVRRPLPPLICIPTTAGSSADVSQFAIITDTERRVKMAIISKTLVPD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 173 VAIIDPLMMASMPASLKAATGVDALTHAIEGYITKGAWALTDALHLKSIELISNSLRQSVK--GDPQGVETMALAQYMAG 250
Cdd:cd17814 167 VSLIDPETLTTMDPELTACTGMDALTHAIEAYVSNASSPLTDLHALEAIRLISENLPKAVAdpDDLEAREKMMLASLQAG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 251 MGFSNVGLGLVHGMAHPLGAFYNTPHGVANAILLPHIMAYNANYTGEKYRDIARAMGVKnIDSLPLQEARDTAIAAVFAL 330
Cdd:cd17814 247 LAFSNASLGAVHAMAHSLGGLLDLPHGECNALLLPHVIRFNFPAAPERYRKIAEAMGLD-VDGLDDEEVAERLIEAIRDL 325
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 491051849 331 NKNVGIPEKLREIGMKPEDIPSLAQAAFDDVCTGGNPRDATLEDIAELY 379
Cdd:cd17814 326 REDLGIPETLSELGVDEEDIPELAKRAMKDPCLVTNPRRPTREDIEEIY 374
|
|
| Fe-ADH-like |
cd14861 |
Iron-containing alcohol dehydrogenases-like; This family contains proteins similar to ... |
12-381 |
3.35e-118 |
|
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: 347.58 E-value: 3.35e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 12 YFGEGAINHLVEEIQKRQFNKALIVTDADLVKFNVVSKVTQLLDNAKLDYAIYDAVIPNPTIDTVQQGLKHFKQFNADYL 91
Cdd:cd14861 7 RFGAGAIAELPEELKALGIRRPLLVTDPGLAALGIVDRVLEALGAAGLSPAVFSDVPPNPTEADVEAGVAAYREGGCDGI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 92 IAIGGGSPQDTAKAIGIIINNP----QYEDVvsLEGVAPTQNPAVPIIAIPTTAGTAAEVTINYVITDNKLCRKFVCVDP 167
Cdd:cd14861 87 IALGGGSAIDAAKAIALMATHPgplwDYEDG--EGGPAAITPAVPPLIAIPTTAGTGSEVGRAAVITDDDTGRKKIIFSP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 168 HSIPIVAIIDPLMMASMPASLKAATGVDALTHAIEGYITKGAWALTDALHLKSIELISNSLRQSVK--GDPQGVETMALA 245
Cdd:cd14861 165 KLLPKVAICDPELTLGLPPRLTAATGMDALTHCIEAYLSPGFHPMADGIALEGLRLISEWLPRAVAdgSDLEARGEMMMA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 246 QYMAGMGFSNvGLGLVHGMAHPLGAFYNTPHGVANAILLPHIMAYNANYTGEKYRDIARAMGVKNIDSlplqearDTAIA 325
Cdd:cd14861 245 ALMGAVAFQK-GLGAVHALAHALGALYGLHHGLLNAILLPYVLRFNRPAVEDKLARLARALGLGLGGF-------DDFIA 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 491051849 326 AVFALNKNVGIPEKLREIGMKPEDIPSLAQAAFDDVCTGGNPRDATLEDIAELYQA 381
Cdd:cd14861 317 WVEDLNERLGLPATLSELGVTEDDLDELAELALADPCHATNPRPVTAEDYRALLRE 372
|
|
| Fe-ADH-like |
cd14865 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
13-383 |
5.57e-117 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341487 [Multi-domain] Cd Length: 383 Bit Score: 344.91 E-value: 5.57e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 13 FGEGAINHLVEEIQKRQFNKALIVTDADLVKFNVVSKVTQLLDNAKLDYAIYDAVIPNPTIDTVQQGLKHFKQFNADYLI 92
Cdd:cd14865 11 SGAGALENLPAELARLGARRPLIVTDKGLAAAGLLKKVEDALGDAIEIVGVFDDVPPDSSVAVVNEAAARAREAGADGII 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 93 AIGGGSPQDTAKAIGIIINNpQYEDVVSLEGVAPTQNPAVPIIAIPTTAGTAAEVTINYVITDNKLCRKFVCVDPHSIPI 172
Cdd:cd14865 91 AVGGGSVIDTAKGVNILLSE-GGDDLDDYGGANRLTRPLKPLIAIPTTAGTGSEVTLVAVIKDEEKKVKLLFVSPFLLPD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 173 VAIIDPLMMASMPASLKAATGVDALTHAIEGYITKGAWALTDALHLKSIELISNSLRQSVK--GDPQGVETMALAQYMAG 250
Cdd:cd14865 170 VAILDPRLTLSLPPKLTAATGMDALTHAIEAYTSLQKNPISDALALQAIRLISENLPKAVKngKDLEARLALAIAATMAG 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 251 MGFSNVGLGLVHGMAHPLGAFYNTPHGVANAILLPHIMAYNANYTGEKYRDIARAMGV-KNIDSLPLQEARDTAIAAVFA 329
Cdd:cd14865 250 IAFSNSMVGLVHAIAHAVGAVAGVPHGLANSILLPHVMRYNLDAAAERYAELALALAYgVTPAGRRAEEAIEAAIDLVRR 329
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 491051849 330 LNKNVGIPEKLREIGMKPEDIPSLAQAAFDDVCTGGNPRDATLEDIAELYQAIY 383
Cdd:cd14865 330 LHELCGLPTRLRDVGVPEEQLEAIAELALNDGAILFNPREVDPEDILAILEAAY 383
|
|
| Fe-ADH-like |
cd14863 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
13-383 |
9.05e-116 |
|
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: 341.82 E-value: 9.05e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 13 FGEGAINHLVEEIQKRQFNKALIVTDADLVKFNVVSKVTQLLDNAKLDYAIYDAVIPNPTIDTVQQGLKHFKQFNADYLI 92
Cdd:cd14863 10 FGAGAVEQIGELLKELGCKKVLLVTDKGLKKAGIVDKIIDLLEEAGIEVVVFDDVEPDPPDEIVDEAAEIAREEGADGVI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 93 AIGGGSPQDTAKAIGIIINNP----QYEDvvsleGVAPTQNPAVPIIAIPTTAGTAAEVTINYVITDNKLCRKFVCVDPH 168
Cdd:cd14863 90 GIGGGSVLDTAKAIAVLLTNPgpiiDYAL-----AGPPVPKPGIPLIAIPTTAGTGSEVTPIAVITDEENGVKKSLLGPF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 169 SIPIVAIIDPLMMASMPASLKAATGVDALTHAIEGYITKGAWALTDALHLKSIELISNSLRQSVKgDPQGVET---MALA 245
Cdd:cd14863 165 LVPDLAILDPELTVGLPPSLTAATGMDALSHAIEAYTSKLANPMTDALALQAIRLIVKNLPRAVK-DGDNLEArenMLLA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 246 QYMAGMGFSNVGLGLVHGMAHPLGAFYNTPHGVANAILLPHIMAYNANYTGEKYRDIARAMGVKnIDSLPLQEARDTAIA 325
Cdd:cd14863 244 SNLAGIAFNNAGTHIGHAIAHALGALYHIPHGLACALALPVVLEFNAEAYPEKVKKIAKALGVS-FPGESDEELGEAVAD 322
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 491051849 326 AVFALNKNVGIPEKLREIGMKPEDIPSLAQAAFDDVCTGGNPRDATLEDIAELYQAIY 383
Cdd:cd14863 323 AIREFMKELGIPSLFEDYGIDKEDLDKIAEAVLKDPFAMFNPRPITEEEVAEILEAIY 380
|
|
| Fe-ADH-like |
cd08189 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
14-382 |
4.61e-113 |
|
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: 334.82 E-value: 4.61e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 14 GEGAINHLVEEIQKRQFNKALIVTDADLVKFNVVSKVTQLLDNAKLDYAIYDAVIPNPTIDTVQQGLKHFKQFNADYLIA 93
Cdd:cd08189 11 GAGSLLQLPEALKKLGIKRVLIVTDKGLVKLGLLDPLLDALKKAGIEYVVFDGVVPDPTIDNVEEGLALYKENGCDAIIA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 94 IGGGSPQDTAKAIGIIINNPQyEDVVSLEGVAPTQNPAVPIIAIPTTAGTAAEVTINYVITDNKLCRKFVCVDPHSIPIV 173
Cdd:cd08189 91 IGGGSVIDCAKVIAARAANPK-KSVRKLKGLLKVRKKLPPLIAVPTTAGTGSEATIAAVITDPETHEKYAINDPKLIPDA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 174 AIIDPLMMASMPASLKAATGVDALTHAIEGYITKGAWALTDALHLKSIELISNSLRQSVKgDPQGVE---TMALAQYMAG 250
Cdd:cd08189 170 AVLDPELTLGLPPAITAATGMDALTHAVEAYISRSATKETDEYALEAVKLIFENLPKAYE-DGSDLEareNMLLASYYAG 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 251 MGFSNVGLGLVHGMAHPLGAFYNTPHGVANAILLPHIMAYNANYTGEKYRDIARAMGVKNiDSLPLQEARDTAIAAVFAL 330
Cdd:cd08189 249 LAFTRAYVGYVHAIAHQLGGLYGVPHGLANAVVLPHVLEFYGPAAEKRLAELADAAGLGD-SGESDSEKAEAFIAAIREL 327
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 491051849 331 NKNVGIPEKLREIgmKPEDIPSLAQAAFDDvctgGN-----PRDATLEDIAELYQAI 382
Cdd:cd08189 328 NRRMGIPTTLEEL--KEEDIPEIAKRALKE----ANplypvPRIMDRKDCEELLRKV 378
|
|
| NADPH_BDH |
cd08179 |
NADPH-dependent butanol dehydrogenase involved in the butanol and ethanol formation pathway in ... |
12-383 |
5.63e-112 |
|
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: 331.85 E-value: 5.63e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 12 YFGEGAInhlvEEIQKRQFNKALIVTDAD-LVKFNVVSKVTQLLDNAKLDYAIYDAVIPNPTIDTVQQGLKHFKQFNADY 90
Cdd:cd08179 9 YFGEGAL----EYLKTLKGKRAFIVTGGGsMKRNGFLDKVEDYLKEAGMEVKVFEGVEPDPSVETVEKGAEAMREFEPDW 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 91 LIAIGGGSPQDTAKAIGIIINNPQY--EDVVSLEGVAPTQNPAVpIIAIPTTAGTAAEVTINYVITDNKLCRKFVCVDPH 168
Cdd:cd08179 85 IIAIGGGSVIDAAKAMWVFYEYPELtfEDALVPFPLPELRKKAR-FIAIPSTSGTGSEVTRASVITDTEKGIKYPLASFE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 169 SIPIVAIIDPLMMASMPASLKAATGVDALTHAIEGYITKGAWALTDALHLKSIELISNSLRQSVKGDP--QGVETMALAQ 246
Cdd:cd08179 164 ITPDVAILDPELTMTMPPHVTANTGMDALTHAIEAYVSTLANDFTDALALGAILDIFENLPKSYNGGKdlEAREKMHNAS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 247 YMAGMGFSNVGLGLVHGMAHPLGAFYNTPHGVANAILLPHIMAYNANYTGEKYRDIAR------AMGVKNIdslplqear 320
Cdd:cd08179 244 CLAGMAFSNSGLGIVHSMAHKGGAFFGIPHGLANAILLPYVIEFNSKDPEARARYAALligltdEELVEDL--------- 314
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491051849 321 dtaIAAVFALNKNVGIPEKLREIGMKPED----IPSLAQAAFDDVCTGGNPRDATLEDIAELYQAIY 383
Cdd:cd08179 315 ---IEAIEELNKKLGIPLSFKEAGIDEDEffakLDEMAENAMNDACTGTNPRKPTVEEMKELLKAAY 378
|
|
| Fe-ADH-like |
cd14862 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
12-379 |
4.64e-104 |
|
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: 311.85 E-value: 4.64e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 12 YFGEGAINHLVEEIQKRqfnkALIVTDADLVKFNVVSKVTQLLDNAKLDYAIYDAVIPNPTIDTVQQGLKHFKQFNADYL 91
Cdd:cd14862 10 VFGEDALSHLEQLSGKR----ALIVTDKVLVKLGLLKKVLKRLLQAGFEVEVFDEVEPEPPLETVLKGAEAMREFEPDLI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 92 IAIGGGSPQDTAKAIGIIINNPQyedvVSLEGVAPTQ----NPAVPIIAIPTTAGTAAEVTINYVITDNKLCRKFVCVDP 167
Cdd:cd14862 86 IALGGGSVMDAAKAAWVLYERPD----LDPEDISPLDllglRKKAKLIAIPTTSGTGSEATWAIVLTDTEEPRKIAVANP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 168 HSIPIVAIIDPLMMASMPASLKAATGVDALTHAIEGYITkgAWA--LTDALHLKSIELISNSLRQSVKG--DPQGVETMA 243
Cdd:cd14862 162 ELVPDVAILDPEFVLGMPPKLTAGTGLDALAHAVEAYLS--TWSndFSDALALKAIELIFKYLPRAYKDgdDLEAREKMH 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 244 LAQYMAGMGFSNVGLGLVHGMAHPLGAFYNTPHGVANAILLPHIMAYNANYTGEKYRDIARamgvKNIDSLPLQEARDTA 323
Cdd:cd14862 240 NAATIAGLAFGNSQAGLAHALGHSLGAVFHVPHGIAVGLFLPYVIEFYAKVTDERYDLLKL----LGIEARDEEEALKKL 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 324 IAAVFALNKNVGIPEKLREIGMKPED----IPSLAQAAFDDVCTGGNPRDATLEDIAELY 379
Cdd:cd14862 316 VEAIRELYKEVGQPLSIKDLGISEEEfeekLDELVEYAMEDSCTITSPRPPSEEDLKKLF 375
|
|
| PRK09860 |
PRK09860 |
putative alcohol dehydrogenase; Provisional |
14-381 |
1.93e-102 |
|
putative alcohol dehydrogenase; Provisional
Pssm-ID: 182118 [Multi-domain] Cd Length: 383 Bit Score: 308.04 E-value: 1.93e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 14 GEGAINHLVEEIQKRQFNKALIVTDADLVKFNVVSKVTQLLDNAKLDYAIYDAVIPNPTIDTVQQGLKHFKQFNADYLIA 93
Cdd:PRK09860 15 GADSLTDAMNMMADYGFTRTLIVTDNMLTKLGMAGDVQKALEERNIFSVIYDGTQPNPTTENVAAGLKLLKENNCDSVIS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 94 IGGGSPQDTAKAIGIIINNPQyeDVVSLEGVAPTQNPAVPIIAIPTTAGTAAEVTINYVITDNKLCRKFVCVDPHSIPIV 173
Cdd:PRK09860 95 LGGGSPHDCAKGIALVAANGG--DIRDYEGVDRSAKPQLPMIAINTTAGTASEMTRFCIITDEARHIKMAIVDKHVTPLL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 174 AIIDPLMMASMPASLKAATGVDALTHAIEGYITKGAWALTDALHLKSIELISNSLRQSVK--GDPQGVETMALAQYMAGM 251
Cdd:PRK09860 173 SVNDSSLMIGMPKSLTAATGMDALTHAIEAYVSIAATPITDACALKAVTMIAENLPLAVEdgSNAKAREAMAYAQFLAGM 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 252 GFSNVGLGLVHGMAHPLGAFYNTPHGVANAILLPHIMAYNANYTGEKYRDIARAMGVkNIDSLPLQEARDTAIAAVFALN 331
Cdd:PRK09860 253 AFNNASLGYVHAMAHQLGGFYNLPHGVCNAVLLPHVQVFNSKVAAARLRDCAAAMGV-NVTGKNDAEGAEACINAIRELA 331
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 491051849 332 KNVGIPEKLREIGMKPEDIPSLAQAAFDDVCTGGNPRDATLEDIAELYQA 381
Cdd:PRK09860 332 KKVDIPAGLRDLNVKEEDFAVLATNALKDACGFTNPIQATHEEIVAIYRA 381
|
|
| Fe-ADH-like |
cd08183 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
12-378 |
6.18e-102 |
|
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: 306.35 E-value: 6.18e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 12 YFGEGAINHLVEEIqKRQFNKALIVTDADLVKFNVVSKVTQLLDNAKLDYAIYDaVIPNPTIDTVQQGLKHFKQFNADYL 91
Cdd:cd08183 5 VFGRGSLQELGELA-AELGKRALLVTGRSSLRSGRLARLLEALEAAGIEVALFS-VSGEPTVETVDAAVALAREAGCDVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 92 IAIGGGSPQDTAKAIGIIINNPqyEDVVS-LEGV---APTQNPAVPIIAIPTTAGTAAEVTINYVITDNKLCRKFVCVDP 167
Cdd:cd08183 83 IAIGGGSVIDAAKAIAALLTNE--GSVLDyLEVVgkgRPLTEPPLPFIAIPTTAGTGSEVTKNAVLSSPEHGVKVSLRSP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 168 HSIPIVAIIDPLMMASMPASLKAATGVDALTHAIEGYITKGAWALTDALHLKSIELISNSLRQSVK--GDPQGVETMALA 245
Cdd:cd08183 161 SMLPDVALVDPELTLSLPPEVTAASGLDALTQLIEPYVSRKANPLTDALAREGLRLAARSLRRAYEdgEDLEAREDMALA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 246 QYMAGMGFSNVGLGLVHGMAHPLGAFYNTPHGVANAILLPHIMAYNANYTGEKYRDI---ARAMGVKNIDSLPLQEARDT 322
Cdd:cd08183 241 SLLGGLALANAGLGAVHGLAGPLGGMFGAPHGAICAALLPPVLEANLRALREREPDSpalARYRELAGILTGDPDAAAED 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 491051849 323 AIAAVFALNKNVGIPeKLREIGMKPEDIPSLAQAAFDDVCTGGNPRDATLEDIAEL 378
Cdd:cd08183 321 GVEWLEELCEELGIP-RLSEYGLTEEDFPEIVEKARGSSSMKGNPIELSDEELLEI 375
|
|
| AAD_C |
cd08178 |
C-terminal alcohol dehydrogenase domain of the acetaldehyde dehydrogenase-alcohol ... |
12-380 |
2.30e-101 |
|
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: 305.65 E-value: 2.30e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 12 YFGEGAINHLVEEiqKRQFNKALIVTDADLVKFNVVSKVTQLLDNAKLDYAIYDAVIPNPTIDTVQQGLKHFKQFNADYL 91
Cdd:cd08178 7 YFEPGCLPYLLLE--LPGVKRAFIVTDRVLYKLGYVDKVLDVLEARGVETEVFSDVEPDPTLSTVRKGLEAMNAFKPDVI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 92 IAIGGGSPQDTAKAIGIIINNPQyedvVSLEGVAPT---------QNPA----VPIIAIPTTAGTAAEVTINYVITDNKL 158
Cdd:cd08178 85 IALGGGSAMDAAKIMWLFYEHPE----TKFEDLAQRfmdirkrvyKFPKlgkkAKLVAIPTTSGTGSEVTPFAVITDDKT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 159 CRKFVCVDPHSIPIVAIIDPLMMASMPASLKAATGVDALTHAIEGYITKGAWALTDALHLKSIELISNSLRQSVKG--DP 236
Cdd:cd08178 161 GKKYPLADYALTPDMAIVDPELVMTMPKRLTADTGIDALTHAIEAYVSVMASDYTDGLALQAIKLIFEYLPRSYNNgnDI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 237 QGVETMALAQYMAGMGFSNVGLGLVHGMAHPLGAFYNTPHGVANAILLPHIMAYNAN-----------YTG----EKYRD 301
Cdd:cd08178 241 EAREKMHNAATIAGMAFANAFLGICHSLAHKLGAAFHIPHGRANAILLPHVIRYNATdpptkqaafpqYKYyvakERYAE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 302 IARAMGVK-NIDSlplqEARDTAIAAVFALNKNVGIPEKLREIGMKPED----IPSLAQAAFDDVCTGGNPRDATLEDIA 376
Cdd:cd08178 321 IADLLGLGgKTPE----EKVESLIKAIEDLKKDLGIPTSIREAGIDEADflaaVDKLAEDAFDDQCTGANPRYPLISELK 396
|
....
gi 491051849 377 ELYQ 380
Cdd:cd08178 397 EILL 400
|
|
| Fe-ADH-like |
cd08185 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
12-380 |
1.93e-100 |
|
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: 302.49 E-value: 1.93e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 12 YFGEGAINHLvEEIQKRQFNKALIVTDAD-LVKFNVVSKVTQLLDNAKLDYAIYDAVIPNPTIDTVQQGLKHFKQFNADY 90
Cdd:cd08185 8 LFGAGKLNEL-GEEALRPGKKALIVTGKGsSKKTGLLDRVKKLLEKAGVEVVVFDKVEPNPLTTTVMEGAALAKEEGCDF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 91 LIAIGGGSPQDTAKAIGIIINNPQ-YED-VVSLEGVAPTQNPAVPIIAIPTTAGTAAEVTINYVITDNKLCRKFVCVDPH 168
Cdd:cd08185 87 VIGLGGGSSMDAAKAIAFMATNPGdIWDyIFGGTGKGPPPEKALPIIAIPTTAGTGSEVDPWAVITNPETKEKKGIGHPA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 169 SIPIVAIIDPLMMASMPASLKAATGVDALTHAIEGYITKGAWALTDALHLKSIELISNSLRQSVKgDPQGVET---MALA 245
Cdd:cd08185 167 LFPKVSIVDPELMLTVPPRVTAYTGFDALFHAFESYISKNANPFSDMLALEAIRLVAKYLPRAVK-DGSDLEArekMAWA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 246 QYMAGMGFSNVGLGLVHGMAHPLGAFY-NTPHGVANAILLPHIMAYNANYTGEKYRDIARA--MGVKNIDSlplqeARDt 322
Cdd:cd08185 246 STLAGIVIANSGTTLPHGLEHPLSGYHpNIPHGAGLAALYPAYFEFTIEKAPEKFAFVARAeaSGLSDAKA-----AED- 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491051849 323 AIAAVFALNKNVGIPEKLREIGMKPEDIPSLAQAAFDDvcTGG----NPRDATLEDIAELYQ 380
Cdd:cd08185 320 FIEALRKLLKDIGLDDLLSDLGVTEEDIPWLAENAMET--MGGlfanNPVELTEEDIVEIYE 379
|
|
| PDD |
cd08180 |
1,3-propanediol dehydrogenase (PPD) catalyzes the reduction of 3-hydroxypropionaldehyde (3-HPA) ... |
12-379 |
1.16e-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: 296.33 E-value: 1.16e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 12 YFGEGAINHLvEEIQKRqfnKALIVTDADLVKFNVVSKVTQLLDNAKlDYAIYDAVIPNPTIDTVQQGLKHFKQFNADYL 91
Cdd:cd08180 8 YSGEDSLERL-KELKGK---RVFIVTDPFMVKSGMVDKVTDELDKSN-EVEIFSDVVPDPSIEVVAKGLAKILEFKPDTI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 92 IAIGGGSPQDTAKAIGIIINNpqyedvvslegvAPTQNPAVPIIAIPTTAGTAAEVTINYVITDNKLCRKFVCVDPHSIP 171
Cdd:cd08180 83 IALGGGSAIDAAKAIIYFALK------------QKGNIKKPLFIAIPTTSGTGSEVTSFAVITDPEKGIKYPLVDDSMLP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 172 IVAIIDPLMMASMPASLKAATGVDALTHAIEGYITKGAWALTDALHLKSIELISNSLRQSVK--GDPQGVETMALAQYMA 249
Cdd:cd08180 151 DIAILDPELVKSVPPKVTADTGMDVLTHALEAYVSTNANDFTDALAEKAIKLVFENLPRAYRdgDDLEAREKMHNASCMA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 250 GMGFSNVGLGLVHGMAHPLGAFYNTPHGVANAILLPHIMAYnanytgekyrdiaramgvknidslplqeardtAIAAVFA 329
Cdd:cd08180 231 GIAFNNAGLGINHSLAHALGGRFHIPHGRANAILLPYVIEF--------------------------------LIAAIRR 278
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 491051849 330 LNKNVGIPEKLREIGMKPED----IPSLAQAAFDDVCTGGNPRDATLEDIAELY 379
Cdd:cd08180 279 LNKKLGIPSTLKELGIDEEEfekaIDEMAEAALADRCTATNPRKPTAEDLIELL 332
|
|
| HOT |
cd08190 |
Hydroxyacid-oxoacid transhydrogenase (HOT) involved in gamma-hydroxybutyrate metabolism; This ... |
13-381 |
2.63e-97 |
|
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: 295.61 E-value: 2.63e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 13 FGEGAINHLVEEIQKRQFNKALIVTDADLVKFNVVSKVTQLLDNAKLDYAIYDAVIPNPTIDTVQQGLKHFKQFNADYLI 92
Cdd:cd08190 6 FGPGATRELGMDLKRLGAKKVLVVTDPGLAKLGLVERVLESLEKAGIEVVVYDGVRVEPTDESFEEAIEFAKEGDFDAFV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 93 AIGGGSPQDTAKAIGIIINNPQ--YEDVVSLEGVA-PTQNPAVPIIAIPTTAGTAAEVTINYVITDNKLCRKFVCVDPHS 169
Cdd:cd08190 86 AVGGGSVIDTAKAANLYATHPGdfLDYVNAPIGKGkPVPGPLKPLIAIPTTAGTGSETTGVAIFDLEELKVKTGISSRYL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 170 IPIVAIIDPLMMASMPASLKAATGVDALTHAIEGYITK------------------GAWALTDALHLKSIELISNSLRQS 231
Cdd:cd08190 166 RPTLAIVDPLLTLTLPPRVTASSGFDVLCHALESYTARpynarprpanpderpayqGSNPISDVWAEKAIELIGKYLRRA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 232 VKgDPQGVE---TMALAQYMAGMGFSNVGLGLVHGMAHPLG--------AFYN-----TPHGVANAILLPHIMAYNANYT 295
Cdd:cd08190 246 VN-DGDDLEarsNMLLASTLAGIGFGNAGVHLPHAMAYPIAglvkdyrpPGYPvdhphVPHGLSVALTAPAVFRFTAPAC 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 296 GEKYRDIARAMGVkNIDSLPLQEARDTAIAAVFALNKNVGIPEKLREIGMKPEDIPSLAQAAFDDV-CTGGNPRDATLED 374
Cdd:cd08190 325 PERHLEAAELLGA-DTSGASDRDAGEVLADALIKLMRDIGIPNGLSALGYSEDDIPALVEGTLPQQrLLKLNPRPVTEED 403
|
....*..
gi 491051849 375 IAELYQA 381
Cdd:cd08190 404 LEEIFED 410
|
|
| PRK13805 |
PRK13805 |
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional |
12-383 |
5.06e-95 |
|
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional
Pssm-ID: 237515 [Multi-domain] Cd Length: 862 Bit Score: 302.10 E-value: 5.06e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 12 YFGEGAINHLVEEIQKRqfNKALIVTDADLVKFNVVSKVTQLLDN--AKLDYAIYDAVIPNPTIDTVQQGLKHFKQFNAD 89
Cdd:PRK13805 464 YFERGSLPYLLDELDGK--KRAFIVTDRFMVELGYVDKVTDVLKKreNGVEYEVFSEVEPDPTLSTVRKGAELMRSFKPD 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 90 YLIAIGGGSPQDTAKAIGIIINNPQyedvVSLEGVA-------------PTQNPAVPIIAIPTTAGTAAEVTINYVITDN 156
Cdd:PRK13805 542 TIIALGGGSPMDAAKIMWLFYEHPE----TDFEDLAqkfmdirkriykfPKLGKKAKLVAIPTTSGTGSEVTPFAVITDD 617
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 157 KLCRKFVCVDPHSIPIVAIIDPLMMASMPASLKAATGVDALTHAIEGYITKGAWALTDALHLKSIELISNSLRQSVKGDP 236
Cdd:PRK13805 618 KTGVKYPLADYELTPDVAIVDPNLVMTMPKSLTADTGIDALTHALEAYVSVMASDYTDGLALQAIKLVFEYLPRSYKNGA 697
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 237 QGV---ETMALAQYMAGMGFSNVGLGLVHGMAHPLGAFYNTPHGVANAILLPHIMAYNAN----------Y----TGEKY 299
Cdd:PRK13805 698 KDPearEKMHNASTIAGMAFANAFLGICHSMAHKLGAEFHIPHGRANAILLPHVIRYNATdppkqaafpqYeyprADERY 777
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 300 RDIARAMGVKNIDSlplQEARDTAIAAVFALNKNVGIPEKLREIGMKPED----IPSLAQAAFDDVCTGGNPRDATLEDI 375
Cdd:PRK13805 778 AEIARHLGLPGSTT---EEKVESLIKAIEELKAELGIPMSIKEAGVDEADflakLDELAELAFDDQCTGANPRYPLISEL 854
|
....*...
gi 491051849 376 AELYQAIY 383
Cdd:PRK13805 855 KEILLDAY 862
|
|
| Fe-ADH-like |
cd08196 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
12-379 |
3.50e-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: 341475 [Multi-domain] Cd Length: 367 Bit Score: 281.00 E-value: 3.50e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 12 YFGEGAINHLVEEIQKRQFNKALIVTDADLVKFNVVSKVTQLLDNAKLDyaIYDAVIPNPTIDTVQQGLKHFKQFNADYL 91
Cdd:cd08196 10 IFGEGILKELPDIIKELGGKRGLLVTDPSFIKSGLAKRIVESLKGRIVA--VFSDVEPNPTVENVDKCARLARENGADFV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 92 IAIGGGSPQDTAKAIGIIINNPqyEDVVS-LEGVAPTQNPAVPIIAIPTTAGTAAEVTINYVITDNKLCRKFVCVDPHSI 170
Cdd:cd08196 88 IAIGGGSVLDTAKAAACLAKTD--GSIEDyLEGKKKIPKKGLPLIAIPTTAGTGSEVTPVAVLTDKEKGKKAPLVSPGFY 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 171 PIVAIIDPLMMASMPASLKAATGVDALTHAIEGYITKGAWALTDALHLKSIELISNSLRQSVKG--DPQGVETMALAQYM 248
Cdd:cd08196 166 PDIAIVDPELTYSMPPKVTASTGIDALCHAIEAYWSINHQPISDALALEAAKLVLENLEKAYNNpnDKEAREKMALASLL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 249 AGMGFSNVGLGLVHGMAHPLGAFYNTPHGVANAILLPHIMAYNANYTGEKYRDIARAMGVKNIDSLplqeardtaIAAVF 328
Cdd:cd08196 246 AGLAFSQTRTTASHACSYPLTSHFGIPHGEACALTLPSFIRLNAEALPGRLDELAKQLGFKDAEEL---------ADKIE 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 491051849 329 ALNKNVGIPEKLREIGMKPEDIPSLAQAAFDDVCTGGNPRDATLEDIAELY 379
Cdd:cd08196 317 ELKKRIGLRTRLSELGITEEDLEEIVEESFHPNRANNNPVEVTKEDLEKLL 367
|
|
| Fe-ADH-like |
cd08191 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
13-383 |
4.53e-91 |
|
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: 279.11 E-value: 4.53e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 13 FGEGAInHLVEEIQKRQFNKALIVTDADLVKFNVVSKVTQLLDNAKLDYAIYDAVIPNPTIDTVQQGLKHFKQFNADYLI 92
Cdd:cd08191 9 FGPGAR-RALGRVAARLGSRVLIVTDPRLASTPLVAELLAALTAAGVAVEVFDGGQPELPVSTVADAAAAARAFDPDVVI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 93 AIGGGSPQDTAKAIGIIINNP-QYEDVVSlEGVAPtqNPAVPIIAIPTTAGTAAEVTINYVITDNKLCRKFVCVDPHSIP 171
Cdd:cd08191 88 GLGGGSNMDLAKVVALLLAHGgDPRDYYG-EDRVP--GPVLPLIAVPTTAGTGSEVTPVAVLTDPARGMKVGVSSPYLRP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 172 IVAIIDPLMMASMPASLKAATGVDALTHAIEGYITK---------------GAWALTDALHLKSIELISNSLRQSVK--G 234
Cdd:cd08191 165 AVAIVDPELTLTCPPGVTADSGIDALTHAIESYTARdfppfprldpdpvyvGKNPLTDLLALEAIRLIGRHLPRAVRdgD 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 235 DPQGVETMALAQYMAGMGFSNVGLGLVHGMAHPLGAFYNTPHGVANAILLPHIMAYNANYTGEKYRDIARAMGVKniDSL 314
Cdd:cd08191 245 DLEARSGMALAALLAGLAFGTAGTAAAHALQYPIGALTHTSHGVGNGLLLPYVMRFNRPARAAELAEIARALGVT--TAG 322
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 315 PLQEARDTAIAAVFALNKNVGIPEKLREIGMKPEDIPSLAQAAFDDV-CTGGNPRDATLEDIAELYQAIY 383
Cdd:cd08191 323 TSEEAADRAIERVEELLARIGIPTTLADLGVTEADLPGLAEKALSVTrLIANNPRPPTEEDLLRILRAAF 392
|
|
| HVD |
cd08193 |
5-hydroxyvalerate dehydrogenase (HVD) catalyzes the oxidation of 5-hydroxyvalerate to ... |
13-383 |
2.06e-83 |
|
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: 258.98 E-value: 2.06e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 13 FGEGAINHLVEEIQKRQFNKALIVTDADLVKFNVVSKVTQLLDNAKLDYAIYDAVIPNPTIDTVQQGLKHFKQFNADYLI 92
Cdd:cd08193 9 CGAGAAARLGELLRELGARRVLLVTDPGLVKAGLADPALAALEAAGIAVTVFDDVVADPPEAVVEAAVEQAREAGADGVI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 93 AIGGGSPQDTAKAIGIIINNPQyeDVVSLEGVAPTQNPAVPIIAIPTTAGTAAEVTINYVITDNKLcRKFVCVDPHSIPI 172
Cdd:cd08193 89 GFGGGSSMDVAKLVALLAGSDQ--PLDDIYGVGKATGPRLPLILVPTTAGTGSEVTPISIVTTGET-EKKGVVSPQLLPD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 173 VAIIDPLMMASMPASLKAATGVDALTHAIEGYITK-GAWALTDALHLKSIELISNSLRQSVK--GDPQGVETMALAQYMA 249
Cdd:cd08193 166 VALLDAELTLGLPPHVTAATGIDAMVHAIEAYTSRhKKNPISDALAREALRLLGANLRRAVEdgSDLEAREAMLLGSMLA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 250 GMGFSNVGLGLVHGMAHPLGAFYNTPHGVANAILLPHIMAYNANYTGEKYRDIARAMGVkNIDSLPLQEARDTAIAAVFA 329
Cdd:cd08193 246 GQAFANAPVAAVHALAYPLGGHFHVPHGLSNALVLPHVLRFNLPAAEALYAELARALLP-GLAFGSDAAAAEAFIDALEE 324
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 491051849 330 LNKNVGIPEKLREIGMKPEDIPSLAQAAF-DDVCTGGNPRDATLEDIAELYQAIY 383
Cdd:cd08193 325 LVEASGLPTRLRDVGVTEEDLPMLAEDAMkQTRLLVNNPREVTEEDALAIYQAAL 379
|
|
| HEPD |
cd08182 |
Hydroxyethylphosphoate dehydrogenase (HEPD) catalyzes the reduction of phosphonoacetaldehyde ... |
12-380 |
4.74e-77 |
|
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: 242.13 E-value: 4.74e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 12 YFGEGAINHLVEEIQKRQFNKALIVTDADLVKFNVVSKVTQLLDNaKLDYAIYDAVIPNPTIDTVQQGLKHFKQFNADYL 91
Cdd:cd08182 5 IFGPGALAELKDLLGGLGARRVLLVTGPSAVRESGAADILDALGG-RIPVVVFSDFSPNPDLEDLERGIELFRESGPDVI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 92 IAIGGGSPQDTAKAIGIIINNPQYEDVVSLEGVAPTQNPAVPIIAIPTTAGTAAEVTINYVITDNKLCRKFVCVDPHSIP 171
Cdd:cd08182 84 IAVGGGSVIDTAKAIAALLGSPGENLLLLRTGEKAPEENALPLIAIPTTAGTGSEVTPFATIWDEAEGKKYSLAHPSLYP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 172 IVAIIDPLMMASMPASLKAATGVDALTHAIEGYITKGAWALTDALHLKSIELISNSLRQSVK--GDPQGVETMALAQYMA 249
Cdd:cd08182 164 DAAILDPELTLSLPLYLTASTGLDALSHAIESIWSVNANPESRAYALRAIRLILENLPLLLEnlPNLEAREAMAEASLLA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 250 GMGFSNVGLGLVHGMAHPLGAFYNTPHGVANAILLPHIMAYNANYTGEK-----YRDIARAMGVKNIDSlplqeardtAI 324
Cdd:cd08182 244 GLAISITKTTAAHAISYPLTSRYGVPHGHACALTLPAVLRYNAGADDECdddprGREILLALGASDPAE---------AA 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 491051849 325 AAVFALNKNVGIPEKLREIGMKPEDIPSLAQAAFDDVCTGGNPRDATLEDIAELYQ 380
Cdd:cd08182 315 ERLRALLESLGLPTRLSEYGVTAEDLEALAASVNTPERLKNNPVRLSEEDLLRLLE 370
|
|
| PPD-like |
cd08181 |
1,3-propanediol dehydrogenase-like (PPD); This family contains proteins similar to 1, ... |
12-380 |
6.77e-73 |
|
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: 231.32 E-value: 6.77e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 12 YFGEGAINHLVEEIQKRQfNKALIVTDADLVKFN-VVSKVTQLLDNAKLDYAIYDAVIPNPTIDTVQQGLKHFKQFNADY 90
Cdd:cd08181 8 YFGKNCVEKHADELAALG-KKALIVTGKHSAKKNgSLDDVTEALEENGIEYFIFDEVEENPSIETVEKGAELARKEGADF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 91 LIAIGGGSPQDTAKAIGIIINNPQyEDVVSLEGVAPtqNPAVPIIAIPTTAGTAAEVTINYVITDNKLCRKFVCVDPHSI 170
Cdd:cd08181 87 VIGIGGGSPLDAAKAIALLAANKD-GDEDLFQNGKY--NPPLPIVAIPTTAGTGSEVTPYSILTDHEKGTKKSFGNPLIF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 171 PIVAIIDPLMMASMPASLKAATGVDALTHAIEGYITKGAWALTDALHLKSIELISNSLrQSVKGDPQGVET---MALAQY 247
Cdd:cd08181 164 PKLALLDPKYTLSLPEELTIDTAVDALSHAIEGYLSVKATPLSDALALEALRLIGECL-PNLLGDELDEEDrekLMYAST 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 248 MAGMGFSNVGLGLVHGMAHPLGAFYNTPHGVANAILLPHIMAYNANYTGEKYRDIARAMGVKNIDSLplqeaRDTaiaav 327
Cdd:cd08181 243 LAGMVIAQTGTTLPHGLGYPLTYFKGIPHGRANGILLPAYLKLCEKQEPEKVDKILKLLGFGSIEEF-----QKF----- 312
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 491051849 328 faLNKNVGIPEKLREigmkpEDIPSLAQAAFDDVCTGGNPRDATLEDIAELYQ 380
Cdd:cd08181 313 --LNRLLGKKEELSE-----EELEKYADEAMKAKNKKNTPGNVTKEDILRIYR 358
|
|
| PRK15454 |
PRK15454 |
ethanolamine utilization ethanol dehydrogenase EutG; |
14-381 |
8.05e-73 |
|
ethanolamine utilization ethanol dehydrogenase EutG;
Pssm-ID: 185351 [Multi-domain] Cd Length: 395 Bit Score: 232.23 E-value: 8.05e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 14 GEGAINHLVEEIQKRQFNKALIVTDADLVKFNVVSKVTQLLDNAKLDYAIYDAVIPNPTIDTVQQGLKHFKQFNADYLIA 93
Cdd:PRK15454 33 GPGAVSSCGQQAQTRGLKHLFVMADSFLHQAGMTAGLTRSLAVKGIAMTLWPCPVGEPCITDVCAAVAQLRESGCDGVIA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 94 IGGGSPQDTAKAIGIIINNPqyEDVVSLEGVAPTQNPAVPIIAIPTTAGTAAEVTINYVITDNKLCRKFVCVDPHSIPIV 173
Cdd:PRK15454 113 FGGGSVLDAAKAVALLVTNP--DSTLAEMSETSVLQPRLPLIAIPTTAGTGSETTNVTVIIDAVSGRKQVLAHASLMPDV 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 174 AIIDPLMMASMPASLKAATGVDALTHAIEGYITKGAWALTDALHLKSIELISNSLRQSVKG--DPQGVETMALAQYMAGM 251
Cdd:PRK15454 191 AILDAALTEGVPSHVTAMTGIDALTHAIEAYSALNATPFTDSLAIGAIAMIGKSLPKAVGYghDLAARESMLLASCMAGM 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 252 GFSNVGLGLVHGMAHPLGAFYNTPHGVANAILLPHIMAYNANYTGEKYRDIARAMGVKNIDSlplqeaRDtAIAAVFALN 331
Cdd:PRK15454 271 AFSSAGLGLCHAMAHQPGAALHIPHGLANAMLLPTVMEFNRMVCRERFSQIGRALRTKKSDD------RD-AINAVSELI 343
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 491051849 332 KNVGIPEKLREIGMKPEDIPSLAQAAFDDVCTGGNPRDATLEDIAELYQA 381
Cdd:PRK15454 344 AEVGIGKRLGDVGATSAHYGAWAQAALEDICLRSNPRTASLEQIVGLYAA 393
|
|
| BDH |
cd08187 |
Butanol dehydrogenase catalyzes the conversion of butyraldehyde to butanol with the cofactor ... |
12-380 |
8.49e-72 |
|
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: 229.24 E-value: 8.49e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 12 YFGEGAINHLVEEIqKRQFNKALIVTDADLVKFN-VVSKVTQLLDNAKLDYAIYDAVIPNPTIDTVQQGLKHFKQFNADY 90
Cdd:cd08187 11 IFGKGAIEELGEEI-KKYGKKVLLVYGGGSIKKNgLYDRVVASLKEAGIEVVEFGGVEPNPRLETVREGIELAREENVDF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 91 LIAIGGGSPQDTAKAIGIIINNPqyEDVVSLEGVAPTQNPAVPIIAIPTTAGTAAEVTINYVITDNKLCRKFVCVDPHSI 170
Cdd:cd08187 90 ILAVGGGSVIDAAKAIAAGAKYD--GDVWDFFTGKAPPEKALPVGTVLTLAATGSEMNGGAVITNEETKEKLGFGSPLLR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 171 PIVAIIDPLMMASMPASLKAATGVDALTHAIEGYITKGAWA-LTDALhlksIE-----LISNSLRqsVKGDPQGVEtmAL 244
Cdd:cd08187 168 PKFSILDPELTYTLPKYQTAAGIVDIFSHVLEQYFTGTEDApLQDRL----AEgllrtVIENGPK--ALKDPDDYE--AR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 245 AQYM--AGMGFSN-VGLGL-----VHGMAHPLGAFYNTPHGVANAILLPHIMAYNANYTGEKYRDIARA-MGVKNIDSlP 315
Cdd:cd08187 240 ANLMwaATLALNGlLGAGRggdwaTHAIEHELSALYDITHGAGLAIVFPAWMRYVLKKKPERFAQFARRvFGIDPGGD-D 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491051849 316 LQEARDtAIAAVFALNKNVGIPEKLREIGMKPEDIPSLAQAAFDDVCTGGNPRDATLEDIAELYQ 380
Cdd:cd08187 319 EETALE-GIEALEEFFKSIGLPTTLSELGIDEEDIEEMAEKAVRGGGLGGGFKPLTREDIEEILK 382
|
|
| Fe-ADH-like |
cd14864 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
12-383 |
3.88e-66 |
|
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: 214.47 E-value: 3.88e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 12 YFGEGAINHLVEEIqKRQFNKALIVTDADLVKFNVVSKVTQLLDNAKLDYAIYDAVIPNPTIDTVQQGLKHFKQFNADYL 91
Cdd:cd14864 8 VFGADSLERIGEEV-KEYGSRFLLITDPVLKESGLADKIVSSLEKAGISVIVFDEIPASATSDTIDEAAELARKAGADGI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 92 IAIGGGSPQDTAKAIGIIINNPQYEDVvSLEGVAPTqNPAVPIIAIPTTAGTAAEVTINYVITDNKLCRKFVCVDPHSIP 171
Cdd:cd14864 87 IAVGGGKVLDTAKAVAILANNDGGAYD-FLEGAKPK-KKPLPLIAVPTTPRSGFEFSDRFPVVDSRSREVKLLKAQPGLP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 172 IVAIIDPLMMASMPASLKAATGVDALTHAIEGYITKGAWALTDALHLKSIELISNSLRQSV---KGDPQgVETMALAQYM 248
Cdd:cd14864 165 KAVIVDPNLMASLTGNQTAAMALAALALAVEAYLSKKSNFFSDALALKAIELVSENLDGALadpKNTPA-EELLAQAGCL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 249 AGMGFSNVGLGLVHGMAHPLGAFYNTPHGVANAILLPHIMAYNANYTGEKYRDIARAMGVkNIDSLPLQEARDTAIAAVF 328
Cdd:cd14864 244 AGLAASSSSPGLATALALAVNSRYKVSKSLVASILLPHVIEYAATSAPDKYAKIARALGE-DVEGASPEEAAIAAVEGVR 322
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 491051849 329 ALNKNVGIPEKLREIGMKpEDIPSLAQAAFDDVCTGGNPRDATLEDIAELYQAIY 383
Cdd:cd14864 323 RLIAQLNLPTRLKDLDLA-SSLEQLAAIAEDAPKLNGLPRSMSSDDIFDILKAAF 376
|
|
| DHQ_Fe-ADH |
cd07766 |
Dehydroquinate synthase-like (DHQ-like) and iron-containing alcohol dehydrogenases (Fe-ADH); ... |
8-357 |
9.00e-62 |
|
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: 199.51 E-value: 9.00e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 8 NETSYFGEGAINHlVEEIQKRQFNKALIVTDADLVKFnVVSKVTQLLDnAKLDYAIYDAVIPNPTIDTVQQGLKHFKQFN 87
Cdd:cd07766 1 PTRIVFGEGAIAK-LGEIKRRGFDRALVVSDEGVVKG-VGEKVADSLK-KGLAVAIFDFVGENPTFEEVKNAVERARAAE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 88 ADYLIAIGGGSPQDTAKAIGIIInnpqyedvvslegvaptqNPAVPIIAIPTTAGTAAEVTINYVITDNKLCRKFVCvdP 167
Cdd:cd07766 78 ADAVIAVGGGSTLDTAKAVAALL------------------NRGIPFIIVPTTASTDSEVSPKSVITDKGGKNKQVG--P 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 168 HSIPIVAIIDPLMMASMPASLKAATGVDALTHAIEGyitkgawaltdalhlksielisnslrqsvkgdpqgvETMALAQY 247
Cdd:cd07766 138 HYNPDVVFVDTDITKGLPPRQVASGGVDALAHAVEL------------------------------------EKVVEAAT 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 248 MAGMGFSN-VGLGLVHGMAHPLGAFYNTPHGVANAILLPHIMAYNANYTGEkyrdiaramgvknidslplqeaRDTAIAA 326
Cdd:cd07766 182 LAGMGLFEsPGLGLAHAIGHALTAFEGIPHGEAVAVGLPYVLKVANDMNPE----------------------PEAAIEA 239
|
330 340 350
....*....|....*....|....*....|.
gi 491051849 327 VFALNKNVGIPEKLREIGMKPEDIPSLAQAA 357
Cdd:cd07766 240 VFKFLEDLGLPTHLADLGVSKEDIPKLAEKA 270
|
|
| Fe-ADH-like |
cd14866 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
12-381 |
1.30e-61 |
|
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: 202.85 E-value: 1.30e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 12 YFGEGAINHLVEEIQKRQFNKALIVTDADlvkfnvVSKVTQLLDnaKLDYA-------IYDAVIPNPTIDTVQQGLKHFK 84
Cdd:cd14866 9 FSGRGALARLGRELDRLGARRALVVCGSS------VGANPDLMD--PVRAAlgdrlagVFDGVRPHSPLETVEAAAEALR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 85 QFNADYLIAIGGGSPQDTAKAIGIIINNP--------QYEDVVSLEGVAPTQnPAVPIIAIPTTAGTAaEVTINYVITDN 156
Cdd:cd14866 81 EADADAVVAVGGGSAIVTARAASILLAEDrdvrelctRRAEDGLMVSPRLDA-PKLPIFVVPTTPTTA-DVKAGSAVTDP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 157 KLCRKFVCVDPHSIPIVAIIDPLMMASMPASLKAATGVDALTHAIEGYITKGAWALTDALHLKSIELISNSLRQSVKG-D 235
Cdd:cd14866 159 PAGQRLALFDPKTRPAAVFYDPELLATAPASLVAGAAMNGFDMAVEGLYSRHADPLADATLMHALRLLADGLPRLADDdD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 236 PQGVETMALAQYMAGMGFSNVGLGLVHGMAHPLGAFYNTPHGVANAILLPHIMAYNANYTGEKYRDIARAMGVkniDSLP 315
Cdd:cd14866 239 PAARADLVLAAVLAGYGTDHTGGGVIHALGHAIGARYGVQNGVVHAILLPHVLRFNAPATDGRLDRLAEALGV---ADAG 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491051849 316 LQEARDTAIAAVFALNKNVGIPEKLREIGMKPEDIPSLAQAAFDDVCTGGNPR-DATLEDIAELYQA 381
Cdd:cd14866 316 DEASAAAVVDAVEALLDALGVPTRLRDLGVSREDLPAIAEAAMDDWFMDNNPRpVPTAEELEALLEA 382
|
|
| MAR |
cd08177 |
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic ... |
13-383 |
6.77e-57 |
|
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: 189.25 E-value: 6.77e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 13 FGEGAINHLVEEIQKRQFNKALIVT---DADLVKfnvvsKVTQLLDNAKLdyAIYDAVIPNPTIDTVQQGLKHFKQFNAD 89
Cdd:cd08177 6 FGAGTLAELAEELERLGARRALVLStprQRALAE-----RVAALLGDRVA--GVFDGAVMHVPVEVAERALAAAREAGAD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 90 YLIAIGGGSPQDTAKAIgiiinnpqyedvvSLEGvaptqnpAVPIIAIPTT-AGtaAEVTINYVITDNKlcRKFVCVDPH 168
Cdd:cd08177 79 GLVAIGGGSAIGLAKAI-------------ALRT-------GLPIVAVPTTyAG--SEMTPIWGETEDG--VKTTGRDPR 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 169 SIPIVAIIDPLMMASMPASLKAATGVDALTHAIEGYITKGAWALTDALHLKSIELISNSLRQSVkGDPQGVETMALAQY- 247
Cdd:cd08177 135 VLPRTVIYDPDLTLGLPAALSVASGLNALAHAVEALYAPDANPITSLLAEEGIRALARALPRLV-ADPSDLEARSDALYg 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 248 --MAGMGFSNVGLGLVHGMAHPLGAFYNTPHGVANAILLPHIMAYNANYTGEKYRDIARAMGVknidslplqearDTAIA 325
Cdd:cd08177 214 awLAGVVLGSVGMGLHHKLCHVLGGTFDLPHAETHAVVLPHVLAYNAPAAPDAMARLARALGG------------GDAAG 281
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 491051849 326 AVFALNKNVGIPEKLREIGMKPEDIPSLAQAAFDDVctGGNPRDATLEDIAELYQAIY 383
Cdd:cd08177 282 GLYDLARRLGAPTSLRDLGMPEDDIDRAADLALANP--YPNPRPVERDALRALLERAW 337
|
|
| YqdH |
COG1979 |
Alcohol dehydrogenase YqhD, Fe-dependent ADH family [Energy production and conversion]; |
12-381 |
3.48e-53 |
|
Alcohol dehydrogenase YqhD, Fe-dependent ADH family [Energy production and conversion];
Pssm-ID: 441582 [Multi-domain] Cd Length: 387 Bit Score: 180.65 E-value: 3.48e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 12 YFGEGAINHLVEEIqKRQFNKALIVTDADLVKFN-VVSKVTQLLDNAKLDYAIYDAVIPNPTIDTVQQGLKHFKQFNADY 90
Cdd:COG1979 13 IFGKGQIAKLGEEI-PKYGKKVLLVYGGGSIKKNgLYDQVKAALKEAGIEVVEFGGVEPNPRLETVRKGVELCKEEGIDF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 91 LIAIGGGSPQDTAKAIGIIINnpqYE----DVVslEGVAPTQNpAVPIIAIPTTAGTAAEVTINYVITDNKLCRKFVCVD 166
Cdd:COG1979 92 ILAVGGGSVIDGAKAIAAGAK---YDgdpwDIL--TGKAPVEK-ALPLGTVLTLPATGSEMNSGSVITNEETKEKLGFGS 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 167 PHSIPIVAIIDPLMMASMPASLKAATGVDALTHAIEGYITKGAWA-LTD----ALhLKSieLISNSLRqsVKGDPQGVET 241
Cdd:COG1979 166 PLVFPKFSILDPELTYTLPKRQTANGIVDIFSHVMEQYFTYPVDApLQDrfaeGL-LRT--LIEEGPK--ALKDPEDYDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 242 MA---LAQYMAGMGFsnVGLGL-----VHGMAHPLGAFYNTPHGVANAILLPHIMAYNANYTGEKYRDIARAmgVKNIDS 313
Cdd:COG1979 241 RAnlmWAATLALNGL--IGAGVpqdwaTHMIEHELSALYDIDHGAGLAIVLPAWMRYVLEEKPEKFAQYAER--VWGITE 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491051849 314 LPLQEARDTAIAAVFALNKNVGIPEKLREIGMKPEDIPSLAQAAFDDVCTG-GNPRDATLEDIAELYQA 381
Cdd:COG1979 317 GDDEERALEGIEATEEFFESLGLPTRLSEYGIDEEDIEEMAEKATAHGMTAlGEFKDLTPEDVREILEL 385
|
|
| MAR-like |
cd08192 |
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic ... |
12-374 |
5.56e-53 |
|
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: 180.14 E-value: 5.56e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 12 YFGEGAINHLVEEIQKRQFNKALIVTDADL-VKFNVVSKVTQLLDNAKLdyAIYDAVIPNPTIDTVQQGLKHFKQFNADY 90
Cdd:cd08192 5 SYGPGAVEALLHELATLGASRVFIVTSKSLaTKTDVIKRLEEALGDRHV--GVFSGVRQHTPREDVLEAARAVREAGADL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 91 LIAIGGGSPQDTAKAIGIIINN-----PQYEDVVSLEGVAPTQN-PAVPIIAIPTTAgTAAEVTINYVITDNKLCRKFVC 164
Cdd:cd08192 83 LVSLGGGSPIDAAKAVALALAEdvtdvDQLDALEDGKRIDPNVTgPTLPHIAIPTTL-SGAEFTAGAGATDDDTGHKQGF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 165 VDPHSIPIVAIIDPLMMASMPASLKAATGVDALTHAIEGYITKGAWALTDALHLKSIELISNSLRQSvKGDPQGVETMAL 244
Cdd:cd08192 162 AHPELGPDAVILDPELTLHTPERLWLSTGIRAVDHAVETLCSPQATPFVDALALKALRLLFEGLPRS-KADPEDLEARLK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 245 AQ---YMAGMGF-SNVGLGLVHGMAHPLGAFYNTPHGVANAILLPHIMAYNANYTGEKYRDIARAMGvknidSLPLQEAR 320
Cdd:cd08192 241 CQlaaWLSLFGLgSGVPMGASHAIGHQLGPLYGVPHGITSCIMLPAVLRFNAPVNAERQRLIARALG-----LVTGGLGR 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 491051849 321 DTAIAAVF--ALNKNVGIPEKLREIGMKPEDIPSLAQAAFDDVCTGGNPRDATLED 374
Cdd:cd08192 316 EAADAADAidALIRELGLPRTLRDVGVGRDQLEKIAENALTDVWCRTNPRPITDKD 371
|
|
| Fe-ADH-like |
cd08186 |
Iron-containing alcohol dehydrogenase; This family contains iron-containing alcohol ... |
10-379 |
4.48e-49 |
|
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: 169.75 E-value: 4.48e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 10 TSYFGEGAINHLVEEIQKRQFNKALIVTDADLVKFN-VVSKVTQLLDNAKLDYAIYDAVIPNPTIDTVQQGLKHFKQFNA 88
Cdd:cd08186 3 TLYFGVGAIAKIKDILKDLGIDKVIIVTGRSSYKKSgAWDDVEKALEENGIEYVVYDKVTPNPTVDQADEAAKLARDFGA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 89 DYLIAIGGGSPQDTAKAIGIIINNPQyEDVVSLEGVAPTQNPAVPIIAIPTTAGTAAEVTINYVITDNKLCRKFVCVDPH 168
Cdd:cd08186 83 DAVIAIGGGSPIDTAKSVAVLLAYGG-KTARDLYGFRFAPERALPLVAINLTHGTGSEVDRFAVATIPEKGYKPGIAYDC 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 169 SIPIVAIIDPLMMASMPASLKAATGVDALTHAIEGYITKGAWALTDALHLKSIELISNSLRQSVKgDPQGVET---MALA 245
Cdd:cd08186 162 IYPLYAIDDPRLTLTLPKEQTLYTSIDAFNHVYEAATTKVSSPYVITLAKEAIRLIAEYLPRALA-NPKDLEArywLLYA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 246 QYMAGMGFSNVGLGLVHGMAHPLGAFY-NTPHGVANAILLP----HIMAYNANYTGEKYRDIaramgVKNIDSLPlqEAR 320
Cdd:cd08186 241 SMIAGIAIDNGLLHLTHALEHPLSGLKpELPHGLGLALLGPavvkYIYKAVPETLADILRPI-----VPGLKGTP--DEA 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491051849 321 DTAIAAVFALNKNVGIPEKLREIGMKPEDIPSLAQAAFDDVCTGG----NPRDATLEDIAELY 379
Cdd:cd08186 314 EKAARGVEEFLFSVGFTEKLSDYGFTEDDVDRLVELAFTTPSLDLllslAPVEVTEEVVREIY 376
|
|
| 4HBD_NAD |
cd14860 |
4-hydroxybutyrate dehydrogenase, also called gamma-hydroxybutyrate dehydrogenase, catalyzes ... |
71-383 |
4.39e-34 |
|
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: 129.64 E-value: 4.39e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 71 PTIDTVQQGLKHFKQFNADYLIAIGGGSPQDTAKaigiiinnpqyedVVSLEGVAPTQN------PAV---PIIAIPTTA 141
Cdd:cd14860 62 PSDEMVEAIYKDIKKYGYKRVIAIGGGTVIDIAK-------------LLALKGISPVLDlfdgkiPLIkekELIIVPTTC 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 142 GTAAEVTiNYVITD-NKLCRKFVCVDPHSIPIVAIIDPLMMASMPASLKAATGVDALTHAIEGYITKGAWALTDALHLKS 220
Cdd:cd14860 129 GTGSEVT-NISIVElTSLGTKKGLAVDELYADKAVLIPELLKGLPYKVFATSSIDALIHAIESYLSPKATPYTEMFSYKA 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 221 IELISNSLRQSVKGDPQG----VETMALAQYMAGMGFSNVGLGLVHGMAHPLGAFYNTPHGVANAILLPHIMAYNA--NY 294
Cdd:cd14860 208 IEMILEGYQEIAEKGEEArfplLGDFLIASNYAGIAFGNAGCAAVHALSYPLGGKYHVPHGEANYAVFTGVLKNYQekNP 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 295 TGEKY---RDIARAMGVKNIDSLPlqeardtaiaavfALNK--NVGIPEK-LREIGMKPEDIPSLAqaafDDVCTG---- 364
Cdd:cd14860 288 DGEIKklnEFLAKILGCDEEDVYD-------------ELEEllNKILPKKpLHEYGMKEEEIDEFA----DSVMENqqrl 350
|
330 340
....*....|....*....|.
gi 491051849 365 --GNPRDATLEDIAELYQAIY 383
Cdd:cd14860 351 laNNYVPLDREDVAEIYKELY 371
|
|
| Fe-ADH_KdnB-like |
cd08184 |
Iron-containing alcohol dehydrogenase similar to Shewanella oneidensis KdnB required for Kdo8N ... |
13-315 |
2.08e-31 |
|
Iron-containing alcohol dehydrogenase similar to Shewanella oneidensis KdnB required for Kdo8N biosynthesis; This family contains iron-containing alcohol dehydrogenase-like proteins, many of which have not been characterized. Their specific function is unknown. The protein structure represents a dehydroquinate synthase-like fold and belongs to the iron-containing alcohol dehydrogenase-like superfamily. It is distinct from other alcohol dehydrogenases which contain different protein domains. Alcohol dehydrogenase catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron or zinc ions. This family also includes Shewanella oneidensis KdnB which is required for biosynthesis of 8-Amino-3,8-dideoxy-D-manno-octulosonic acid (Kdo8N), a unique amino sugar that has thus far only been observed on the lipopolysaccharides of marine bacteria belonging to the genus Shewanella, and thought to be important for the integrity of the bacterial cell outer membrane. KdnB requires NAD(P) and zinc ion for activity.
Pssm-ID: 341463 [Multi-domain] Cd Length: 348 Bit Score: 121.99 E-value: 2.08e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 13 FGEGAINHL---VEEIQKRQFNKALIVTDAdlvkfnvVSKVTQLLDNAKL---DYAIYDAVIPNPT---IDTVQQGLKHF 83
Cdd:cd08184 6 FGRGSFDQLgelLAERRKSNNDYVVFFIDD-------VFKGKPLLDRLPLqngDLLIFVDTTDEPKtdqIDALRAQIRAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 84 KQFNADYLIAIGGGSPQDTAKAIGIIINNP----QYE--DVVslegvaptQNPAVPIIAIPTTAGTAAEVTINYVITdNK 157
Cdd:cd08184 79 NDKLPAAVVGIGGGSTMDIAKAVSNMLTNPgsaaDYQgwDLV--------KNPGIYKIGVPTLSGTGAEASRTAVLT-GP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 158 LcRKFVCVDPHSIPIVAIIDPLMMASMPASLKAATGVDALTHAIEgyITKGAW--ALTDALHLKSIELISNSLRQSVKGD 235
Cdd:cd08184 150 E-KKLGINSDYTVFDQVILDPELIATVPRDQYFYTGMDCYIHCVE--SLNGTYrnAFGDAYAEKALELCRDVFLSDDMMS 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 236 PQGVETMALAQYMAGMGFSNVGLGLVHGMAHPLGAFYNTPHGVANAIllphIMAYNANYTGEKYRDIaRAMGVKNIDSLP 315
Cdd:cd08184 227 PENREKLMVASYLGGSSIANSQVGVCHALSYGLSVVLGTHHGVANCI----VFNVLEEFYPEGVKEF-REMLEKQNITLP 301
|
|
| PRK15138 |
PRK15138 |
alcohol dehydrogenase; |
13-381 |
5.72e-24 |
|
alcohol dehydrogenase;
Pssm-ID: 185092 [Multi-domain] Cd Length: 387 Bit Score: 101.79 E-value: 5.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 13 FGEGAINHLVEEIQkrQFNKALIVTDADLVKFN-VVSKVTQLLdnAKLDYAIYDAVIPNPTIDTVQQGLKHFKQFNADYL 91
Cdd:PRK15138 14 FGKGAIAGLREQIP--ADARVLITYGGGSVKKTgVLDQVLDAL--KGMDVLEFGGIEPNPTYETLMKAVKLVREEKITFL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 92 IAIGGGSPQDTAKAIGIIINNPQYEDVVS-LEGVAPTQNPAVPIIAIPTTAGTAAEVTINYVITDNKLCRKFVCVDPHSI 170
Cdd:PRK15138 90 LAVGGGSVLDGTKFIAAAANYPENIDPWHiLETGGKEIKSAIPMGSVLTLPATGSESNAGAVISRKTTGDKQAFHSPHVQ 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 171 PIVAIIDPLMMASMPASLKAATGVDALTHAIEGYITKGAWA-----LTDALHLKSIELISNSLRqsvkgDPQGVETMALA 245
Cdd:PRK15138 170 PVFAVLDPVYTYTLPPRQVANGVVDAFVHTVEQYVTYPVDAkiqdrFAEGILLTLIEEGPKALK-----EPENYDVRANV 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 246 QYMAGMGFSN-VGLGL-----VHGMAHPLGAFYNTPHGVANAILLPHIMayNANYTGEKYRDIARAMGVKNIDSLPLQEA 319
Cdd:PRK15138 245 MWAATQALNGlIGAGVpqdwaTHMLGHELTAMHGLDHAQTLAIVLPALW--NEKRDTKRAKLLQYAERVWNITEGSDDER 322
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491051849 320 RDTAIAAVFALNKNVGIPEKLREIGMKPEDIPSLAQAAFDDVCTG-GNPRDATLEDIAELYQA 381
Cdd:PRK15138 323 IDAAIAATRNFFEQMGVPTRLSDYGLDGSSIPALLKKLEEHGMTQlGEHHDITLDVSRRIYEA 385
|
|
| GldA |
COG0371 |
Glycerol dehydrogenase or related enzyme, iron-containing ADH family [Energy production and ... |
14-381 |
9.92e-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: 77.51 E-value: 9.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 14 GEGAINHLVEEIqKRQFNKALIVTDaDLVKFNVVSKVTQLLDNAKLDYAIYDaVIPNPTIDTVQQGLKHFKQFNADYLIA 93
Cdd:COG0371 12 GEGALDELGEYL-ADLGKRALIITG-PTALKAAGDRLEESLEDAGIEVEVEV-FGGECSEEEIERLAEEAKEQGADVIIG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 94 IGGGSPQDTAKAIGIIINnpqyedvvslegvaptqnpaVPIIAIPTTAGTAAEVTINYVITDNKlcRKFVCVDPH-SIPI 172
Cdd:COG0371 89 VGGGKALDTAKAVAYRLG--------------------LPVVSVPTIASTDAPASPLSVIYTED--GAFDGYSFLaKNPD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 173 VAIIDPLMMASMPASLKAAtGV-DAL-------------THAIEGYITKGAWALtdALHLKSIeLISNSLrQSVKGDPQG 238
Cdd:COG0371 147 LVLVDTDIIAKAPVRLLAA-GIgDALakwyeardwslahRDLAGEYYTEAAVAL--ARLCAET-LLEYGE-AAIKAVEAG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 239 VETMALAQ------YMAGMGF----SNVGLGLVHGMAHPLGAFYNTP---HG--VANAILlphIMAYnanytgekyrdia 303
Cdd:COG0371 222 VVTPALERvveanlLLSGLAMgigsSRPGSGAAHAIHNGLTALPETHhalHGekVAFGTL---VQLV------------- 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 304 ramgvknidslpLQEaRDTAIAAVFALNKNVGIPEKLREIGMKP---EDIPSLAQAAFDDVCT-GGNPRDATLEDIAELY 379
Cdd:COG0371 286 ------------LEG-RPEEIEELLDFLRSVGLPTTLADLGLDDeteEELLTVAEAARPERYTiLNLPFEVTPEAVEAAI 352
|
..
gi 491051849 380 QA 381
Cdd:COG0371 353 LA 354
|
|
| GlyDH-like |
cd08550 |
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins. ... |
14-383 |
5.03e-13 |
|
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: 69.49 E-value: 5.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 14 GEGAINHLVEEIqKRQFNKALIVTDADLVKfNVVSKVTQLLDNAKLDY--AIYDAVipnPTIDTVQQGLKHFKQFNADYL 91
Cdd:cd08550 7 EPGILAKAGEYI-APLGKKALIIGGKTALE-AVGEKLEKSLEEAGIDYevEVFGGE---CTEENIERLAEKAKEEGADVI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 92 IAIGGGSPQDTAKAIGIIINnpqyedvvslegvaptqnpaVPIIAIPTTAGTAAEVTINYVITDNKlcRKFVCVDPHSIP 171
Cdd:cd08550 82 IGIGGGKVLDTAKAVADRLG--------------------LPVVTVPTIAATCAAWSALSVLYDEE--GEFLGYSLLKRS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 172 IVAII-DPLMMASMPASLKAATGVDALTHAIEGYIT--------------KGAWALTDALHLKSIELIsnslrQSVKgdp 236
Cdd:cd08550 140 PDLVLvDTDIIAAAPVRYLAAGIGDTLAKWYEARPSsrggpddlalqaavQLAKLAYDLLLEYGVQAV-----EDVR--- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 237 QGVETMALAQ------YMAGMGfSNVGLGLVH-GMAHplgAFYN------TPHGVanaillphimaynanYTGEKYrdia 303
Cdd:cd08550 212 QGKVTPALEDvvdaiiLLAGLV-GSLGGGGCRtAAAH---AIHNgltklpETHGT---------------LHGEKV---- 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 304 rAMGvkNIDSLPLQEARDTAIAAVFALNKNVGIPEKLREIGMKP--EDIPSLAQAAFDDVCTGGNPRDATLEDiaELYQA 381
Cdd:cd08550 269 -AFG--LLVQLALEGRSEEEIEELIEFLRRLGLPVTLEDLGLELteEELRKIAEYACDPPDMAHMLPFPVTPE--MLAEA 343
|
..
gi 491051849 382 IY 383
Cdd:cd08550 344 IL 345
|
|
| GlyDH |
cd08170 |
Glycerol dehydrogenases (GlyDH) catalyzes oxidation of glycerol to dihydroxyacetone in ... |
14-382 |
5.16e-12 |
|
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: 66.28 E-value: 5.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 14 GEGAINHLVEEIqKRQFNKALIVTDADLVKfNVVSKVTQLLDNAKLDY--AIYDAVIPNPTIDTVQqglKHFKQFNADYL 91
Cdd:cd08170 7 GPGALDRLGEYL-APLGKKALVIADPFVLD-LVGERLEESLEKAGLEVvfEVFGGECSREEIERLA---AIARANGADVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 92 IAIGGGSPQDTAKAIGIIINnpqyedvvslegvaptqnpaVPIIAIPTTAGTAAEVTINYVI-TDNKlcrKFVCVD--PH 168
Cdd:cd08170 82 IGIGGGKTIDTAKAVADYLG--------------------LPVVIVPTIASTDAPCSALSVIyTEDG---EFDEYLflPR 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 169 SiPIVAIIDPLMMASMPASLKAAtGV-DALTHAIE--------------GYITKGAWALTdalhlksiELISNSLR---- 229
Cdd:cd08170 139 N-PDLVLVDTEIIAKAPVRFLVA-GMgDALATYFEaracarsgapnmagGRPTLAALALA--------ELCYDTLLeygv 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 230 ---QSVKgdpQGVETMALAQ------YMAGMGFSNVGLGLVHGMAHPLGAFYNTPHgvanailLPHimaynanytGEKYr 300
Cdd:cd08170 209 aakAAVE---AGVVTPALEAvieantLLSGLGFESGGLAAAHAIHNGLTALPETHH-------LLH---------GEKV- 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 301 diarAMGVknIDSLPLQEARDTAIAAVFALNKNVGIPEKLREIGMK---PEDIPSLAQAAFDDVCTGGN-PRDATLEDIa 376
Cdd:cd08170 269 ----AFGT--LVQLVLEGRPDEEIEEVIRFCRSVGLPVTLADLGLEdvtDEELRKVAEAACAPGETIHNmPFPVTPEDV- 341
|
....*.
gi 491051849 377 elYQAI 382
Cdd:cd08170 342 --VDAI 345
|
|
| Gro1PDH |
cd08173 |
Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) catalyzes the reversible conversion between ... |
12-141 |
1.10e-08 |
|
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: 56.02 E-value: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 12 YFGEGAINHLVEEIQKRQFNK-ALIVTDADLVKFnVVSKVTQLLDNAKLDYAIYDAVIPNpTIDTVQQGLKHFKQFNADY 90
Cdd:cd08173 6 VVGHGAINKIGEVLKKLLLGKrALIITGPNTYKI-AGKRVEDLLESSGVEVVIVDIATIE-EAAEVEKVKKLIKESKADF 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 491051849 91 LIAIGGGSPQDTAKAIGIIINnpqyedvvslegvaptqnpaVPIIAIPTTA 141
Cdd:cd08173 84 IIGVGGGKVIDVAKYAAYKLN--------------------LPFISIPTSA 114
|
|
| gldA |
PRK09423 |
glycerol dehydrogenase; Provisional |
14-382 |
1.41e-08 |
|
glycerol dehydrogenase; Provisional
Pssm-ID: 181843 Cd Length: 366 Bit Score: 55.98 E-value: 1.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 14 GEGAINHLVEEIqKRQFNKALIVTDADLVKFnVVSKVTQLLDNAKLDyAIYDAVIPNPTIDTVQQGLKHFKQFNADYLIA 93
Cdd:PRK09423 14 GKGALARLGEYL-KPLGKRALVIADEFVLGI-VGDRVEASLKEAGLT-VVFEVFNGECSDNEIDRLVAIAEENGCDVVIG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 94 IGGGSPQDTAKAIGIIINnpqyedvvslegvaptqnpaVPIIAIPTTAGTAAEVTINYVI-TDNKlcrKFVCVD--PHSi 170
Cdd:PRK09423 91 IGGGKTLDTAKAVADYLG--------------------VPVVIVPTIASTDAPTSALSVIyTEEG---EFERYLflPKN- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 171 PIVAIIDPLMMASMPASLKAATGVDALTHAIE--------------GYITKGAWALTdalhlksiELISNSLR------- 229
Cdd:PRK09423 147 PDLVLVDTAIIAKAPARFLAAGIGDALATWFEaracsrsggttmagGKPTLAALALA--------ELCYETLLedglkak 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 230 QSVKgdpQGVETMALAQ------YMAGMGFSNVGLGLVHGMAHPLGAfyntphgvanailLPHIMAYnanYTGEKYrdia 303
Cdd:PRK09423 219 LAVE---AKVVTPALENvieantLLSGLGFESGGLAAAHAIHNGLTA-------------LEDTHHL---THGEKV---- 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 304 rAMGVknIDSLPLQEARDTAIAAVFALNKNVGIPEKLREIGMK---PEDIPSLAQAAFDDVCTGGN-PRDATLEDIaelY 379
Cdd:PRK09423 276 -AFGT--LTQLVLENRPKEEIEEVIDFCHAVGLPTTLADLGLKedsDEELRKVAEAACAEGETIHNmPFKVTPEDV---A 349
|
...
gi 491051849 380 QAI 382
Cdd:PRK09423 350 AAI 352
|
|
| GlyDH-like |
cd08172 |
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins ... |
14-145 |
6.99e-08 |
|
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins that have yet to be characterized, but show sequence homology with glycerol dehydrogenase. Glycerol dehydrogenases (GlyDH) is a key enzyme in the glycerol dissimilation pathway. In anaerobic conditions, many microorganisms utilize glycerol as a source of carbon through coupled oxidative and reductive pathways. One of the pathways involves the oxidation of glycerol to dihydroxyacetone with the reduction of NAD+ to NADH catalyzed by glycerol dehydrogenases. Dihydroxyacetone is then phosphorylated by dihydroxyacetone kinase and enters the glycolytic pathway for further degradation. The activity of GlyDH is zinc-dependent; the zinc ion plays a role in stabilizing an alkoxide intermediate at the active site.
Pssm-ID: 341451 [Multi-domain] Cd Length: 346 Bit Score: 53.68 E-value: 6.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 14 GEGAINHLVEEIQKRQFNKALIVTDadlVK-FNVVSKVTQLLDNAKLDYAIYDAVIPNPTIDTVQQglkHFKQFNADYLI 92
Cdd:cd08172 7 EEGALKELPELLSEFGIKRPLIIHG---EKsWQAAKPYLPKLFEIEYPVLRYDGECSYEEIDRLAE---EAKEHQADVII 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 491051849 93 AIGGGSPQDTAKAIGIIINnpqyedvvslegvaptqnpaVPIIAIPTTAGTAA 145
Cdd:cd08172 81 GIGGGKVLDTAKAVADKLN--------------------IPLILIPTLASNCA 113
|
|
| egsA |
PRK00843 |
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed |
1-141 |
9.23e-07 |
|
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed
Pssm-ID: 179139 Cd Length: 350 Bit Score: 50.28 E-value: 9.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 1 MTHRMILNETSYFGEGAINHLVEEIQKRQF-NKALIVTdADLVKFNVVSKVTQLLDNAkldYAIYDAVIPNPTIDTVQQG 79
Cdd:PRK00843 4 KSHWIQLPRDVVVGHGVLDDIGDVCSDLKLtGRALIVT-GPTTKKIAGDRVEENLEDA---GDVEVVIVDEATMEEVEKV 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491051849 80 LKHFKQFNADYLIAIGGGSPQDTAKAIGIIINnpqyedvvslegvaptqnpaVPIIAIPTTA 141
Cdd:PRK00843 80 EEKAKDVNAGFLIGVGGGKVIDVAKLAAYRLG--------------------IPFISVPTAA 121
|
|
| DHQS |
cd08195 |
Dehydroquinate synthase (DHQS) catalyzes the conversion of DAHP to DHQ in shikimate pathway ... |
12-103 |
4.35e-06 |
|
Dehydroquinate synthase (DHQS) catalyzes the conversion of DAHP to DHQ in shikimate pathway for aromatic compounds synthesis; Dehydroquinate synthase (DHQS) catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate-7-phosphate (DAHP) to dehydroquinate (DHQ) in the second step of the shikimate pathway. This pathway, which involves seven sequential enzymatic steps in the conversion of erythrose 4-phosphate and phosphoenolpyruvate into chorismate for subsequent synthesis of aromatic compounds, is found in bacteria, microbial eukaryotes, and plants, but not in mammals. Therefore, enzymes of this pathway are attractive targets for the development of non-toxic antimicrobial compounds, herbicides and anti-parasitic agents. The activity of DHQS requires nicotinamide adenine dinucleotide (NAD) as cofactor. A single active site in DHQS catalyzes five sequential reactions involving alcohol oxidation, phosphate elimination, carbonyl reduction, ring opening, and intramolecular aldol condensation. The binding of substrates and ligands induces domain conformational changes. In some fungi and protozoa, this domain is fused with the other four domains in shikimate pathway and forms a penta-domain AROM protein, which catalyzes steps 2-6 in the shikimate pathway.
Pssm-ID: 341474 Cd Length: 343 Bit Score: 48.21 E-value: 4.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 12 YFGEGAINHLVEEIQKRQFNKALIVTDADLVKFNvVSKVTQLLDNAKLDYAIYdaVIP----NPTIDTVQQGLKHFKQFN 87
Cdd:cd08195 5 LIGSGLLDKLGELLELKKGSKVVIVTDENVAKLY-GELLLKSLEAAGFKVEVI--VIPagekSKSLETVERIYDFLLEAG 81
|
90
....*....|....*....
gi 491051849 88 A---DYLIAIGGGSPQDTA 103
Cdd:cd08195 82 LdrdSLLIALGGGVVGDLA 100
|
|
| G1PDH_related |
cd08549 |
Glycerol-1-phosphate dehydrogenase and related proteins; This family contains bacterial and ... |
9-350 |
4.91e-05 |
|
Glycerol-1-phosphate dehydrogenase and related proteins; This family contains bacterial and archeal glycerol-1-phosphate dehydrogenase-like oxidoreductases. These proteins have similarity with glycerol-1-phosphate dehydrogenase (G1PDH) which plays a role in the synthesis of phosphoglycerolipids in gram-positive bacterial species. It catalyzes the reversibly reduction of dihydroxyacetone phosphate (DHAP) to glycerol-1-phosphate (G1P) in a NADH-dependent manner. Its activity requires Ni++ ion. It also contains archaeal Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) that plays an important role in the formation of the enantiomeric configuration of the glycerophosphate backbone (sn-glycerol-1-phosphate) of archaeal ether lipids.
Pssm-ID: 341479 [Multi-domain] Cd Length: 331 Bit Score: 44.86 E-value: 4.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 9 ETSYFGEGAINHLVEEIQKRQFNKALIVTDadlvkfnvvskvtqllDNAKLDYA--IYDAVIPNPTIDTVQQGLKHFKQF 86
Cdd:cd08549 2 RYTIVGDGAINKIEEILKKLNLKRVLIITG----------------KNTKAKYCrfFYDQLKTVCDIVYYDNIDNLEDEL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 87 N----ADYLIAIGGGSPQDTAKAIGIIINnpqyedvvslegvaptqnpaVPIIAIPTTA---GTAAEVtINYVITDNKLC 159
Cdd:cd08549 66 KkytfYDCVIGIGGGRSIDTGKYLAYKLK--------------------IPFISVPTSAsndGIASPI-VSLRIPGVKKT 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 160 RkfvcvdPHSIPIVAIIDPLMMASMPASLKAATGVDALTHAIEGYITKGAWALTDA--------LHLKSI-ELISNSLRQ 230
Cdd:cd08549 125 F------MADAPIAIIADTEIIKKSPRRLLSAGIGDLVSNITAVLDWKLAHKEKGEkysefaaiLSKTSAkELVSYVLKA 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 231 SvkGDPQGVETM--ALAQ---YMAGMGFSNVGLGLVHGMAHPLGAFY------NTPHGVANAILLPhIMAYnanytgeky 299
Cdd:cd08549 199 S--DLEEYHRVLvkALVGsgiAMAIAGSSRPASGSEHLFSHALDKLKeeylniNVLHGEQVGVGTI-IMSY--------- 266
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 491051849 300 rdiarAMGVKNIDSLPLQEARDTAIaavfalnKNVGIPEKLREIGMKPEDI 350
Cdd:cd08549 267 -----LHEKENKKLSGLHERIKMIL-------KKVGAPTTAKQLGIDEDLI 305
|
|
| G1PDH-like |
cd08174 |
Glycerol-1-phosphate dehydrogenase-like; These glycerol-1-phosphate dehydrogenase-like ... |
14-141 |
3.03e-04 |
|
Glycerol-1-phosphate dehydrogenase-like; These glycerol-1-phosphate dehydrogenase-like proteins have not been characterized. The protein sequences have high similarity with that of glycerol-1-phosphate dehydrogenase (G1PDH) which plays a role in the synthesis of phosphoglycerolipids in Gram-positive bacterial species. It catalyzes the reversibly reduction of dihydroxyacetone phosphate (DHAP) to glycerol-1-phosphate (G1P) in a NADH-dependent manner. Its activity requires Ni++ ion.
Pssm-ID: 341453 [Multi-domain] Cd Length: 332 Bit Score: 42.51 E-value: 3.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 14 GEGAINHLVEEIQKR--QFNKALIVTDADLVKFnVVSKVTQLLDNAKLDYAIYDAVIPnpTIDTVQQGLKHFKQFNAdyL 91
Cdd:cd08174 7 EEGALEHLGKYLADRnqGFGKVAIVTGEGIDEL-LGEDILESLEEAGEIVTVEENTDN--SAEELAEKAFSLPKVDA--I 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 491051849 92 IAIGGGSPQDTAKAIGIIINnpqyedvvslegvaptqnpaVPIIAIPTTA 141
Cdd:cd08174 82 VGIGGGKVLDVAKYAAFLSK--------------------LPFISVPTSL 111
|
|
| GlyDH-like |
cd08171 |
Glycerol dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins ... |
87-383 |
4.81e-03 |
|
Glycerol dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins that have yet to be characterized, but show sequence homology with glycerol dehydrogenase. Glycerol dehydrogenases (GlyDH) is a key enzyme in the glycerol dissimilation pathway. In anaerobic conditions, many microorganisms utilize glycerol as a source of carbon through coupled oxidative and reductive pathways. One of the pathways involves the oxidation of glycerol to dihydroxyacetone with the reduction of NAD+ to NADH catalyzed by glycerol dehydrogenases. Dihydroxyacetone is then phosphorylated by dihydroxyacetone kinase and enters the glycolytic pathway for further degradation. The activity of GlyDH is zinc-dependent; the zinc ion plays a role in stabilizing an alkoxide intermediate at the active site.
Pssm-ID: 341450 Cd Length: 345 Bit Score: 38.66 E-value: 4.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 87 NADYLIAIGGGSPQDTAKAIGIIINnpqyedvvslegvaptqnpaVPIIAIPTTAGTAAEVT-INYVITDNKLCRKFVcv 165
Cdd:cd08171 78 EADMIFAVGGGKAIDTVKVLADRLN--------------------KPVFTFPTIASNCAAVTaVSVMYNPDGSFKEYY-- 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 166 DPHSIPIVAIIDPLMMASMPAS-LKAATGvDALTHAIEGYI-TKGA-WALTDALHLKSIELISNSLRQSvkgdpqGVEtm 242
Cdd:cd08171 136 FLKRPPVHTFIDTEIIAEAPEKyLWAGIG-DTLAKYYEVEFsARGDeLDHTNALGVAISKMCSEPLLKY------GVQ-- 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 243 ALAQYMAGM---GFSNVGL------GLVHGMAHPlgaFYNTphGVANAI-----LLPHImaynanytGEKYR--DIArAM 306
Cdd:cd08171 207 ALEDCRANKvsdALEQVVLdiivttGLVSNLVEP---DYNS--SLAHALyygltTLPQI--------EEEHLhgEVV-SY 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051849 307 GVknidsLPL------QEARDTaiaaVFALNKNVGIPEKLREIGMKPEDIPSLAQAAFDDVCTGGNPRDATLEdiaELYQ 380
Cdd:cd08171 273 GV-----LVLltvdgqFEELEK----VYAFNKSIGLPTCLADLGLTVEDLEKVLDKALKTKDLRHSPYPITKE---MFEE 340
|
...
gi 491051849 381 AIY 383
Cdd:cd08171 341 AIK 343
|
|
| |
