|
Name |
Accession |
Description |
Interval |
E-value |
| Fe-ADH-like |
cd17814 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
10-383 |
0e+00 |
|
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: 662.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 10 KFVSPEIIFGAGCRHSVGTCAGNFGARKVLVVSDPGVVKAGWVADVQASLARQGIEHCLFTDVSPNPRCEEVMLGAELYR 89
Cdd:cd17814 1 KFVAPEFIFGVGARKLAGRYAKNLGARKVLVVTDPGVIKAGWVDEVLDSLEAEGLEYVVFSDVTPNPRDFEVMEGAELYR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 90 SEGCNVIVAVGGGSPMDCAKGIGIVAAHGRHIYEFEGVDTLRVPSPPLILIPTTAGTSADVSQFVIISNQEERMKFSIVS 169
Cdd:cd17814 81 EEGCDGIVAVGGGSPIDCAKGIGIVVSNGGHILDYEGVDKVRRPLPPLICIPTTAGSSADVSQFAIITDTERRVKMAIIS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 170 KAAVPDVSLIDPETTLSMDPFLSACTGIDALVHAIEAFVSTGHGPLTDPHALEAMRLINGNLVQMIANPADIALREQIML 249
Cdd:cd17814 161 KTLVPDVSLIDPETLTTMDPELTACTGMDALTHAIEAYVSNASSPLTDLHALEAIRLISENLPKAVADPDDLEAREKMML 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 250 GSMQAGLAFSNAILGAVHAMSHSLGGYLDLPHGVCNAVLVEHVVAFNYDAAPDRYRIVAETLGIDSRGLSHRQVRERLVQ 329
Cdd:cd17814 241 ASLQAGLAFSNASLGAVHAMAHSLGGLLDLPHGECNALLLPHVIRFNFPAAPERYRKIAEAMGLDVDGLDDEEVAERLIE 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 515814333 330 HLIDLKQRIGFRETLSLHGVNLSDIPFLSQHAMQDPCILTNPRSSTQRDVEVVY 383
Cdd:cd17814 321 AIRDLREDLGIPETLSELGVDEEDIPELAKRAMKDPCLVTNPRRPTREDIEEIY 374
|
|
| EutG |
COG1454 |
Alcohol dehydrogenase, class IV [Energy production and conversion]; |
14-387 |
9.60e-166 |
|
Alcohol dehydrogenase, class IV [Energy production and conversion];
Pssm-ID: 441063 [Multi-domain] Cd Length: 381 Bit Score: 468.83 E-value: 9.60e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 14 PEIIFGAGCRHSVGTCAGNFGARKVLVVSDPGVVKAGWVADVQASLARQGIEHCLFTDVSPNPRCEEVMLGAELYRSEGC 93
Cdd:COG1454 9 TRIVFGAGALAELGEELKRLGAKRALIVTDPGLAKLGLLDRVLDALEAAGIEVVVFDDVEPNPTVETVEAGAAAAREFGA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 94 NVIVAVGGGSPMDCAKGIGIVAAHGRHIYEFEGVDTLRVPSPPLILIPTTAGTSADVSQFVIISNQEERMKFSIVSKAAV 173
Cdd:COG1454 89 DVVIALGGGSAIDAAKAIALLATNPGDLEDYLGIKKVPGPPLPLIAIPTTAGTGSEVTPFAVITDPETGVKKGIADPELL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 174 PDVSLIDPETTLSMDPFLSACTGIDALVHAIEAFVSTGHGPLTDPHALEAMRLINGNLVQMIANPADIALREQIMLGSMQ 253
Cdd:COG1454 169 PDVAILDPELTLTLPPSLTAATGMDALTHAIEAYVSKGANPLTDALALEAIRLIARNLPRAVADGDDLEAREKMALASLL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 254 AGLAFSNAILGAVHAMSHSLGGYLDLPHGVCNAVLVEHVVAFNYDAAPDRYRIVAETLGIDsRGLSHRQVRERLVQHLID 333
Cdd:COG1454 249 AGMAFANAGLGAVHALAHPLGGLFHVPHGLANAILLPHVLRFNAPAAPERYAEIARALGLD-VGLSDEEAAEALIEAIRE 327
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 515814333 334 LKQRIGFRETLSLHGVNLSDIPFLSQHAMQDPCILTNPRSSTQRDVEVVYAEAL 387
Cdd:COG1454 328 LLRDLGIPTRLSELGVTEEDLPELAELALADRCLANNPRPLTEEDIEAILRAAY 381
|
|
| Fe-ADH |
cd08551 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains large ... |
14-383 |
3.53e-157 |
|
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: 446.89 E-value: 3.53e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 14 PEIIFGAGCRHSVGTCAGNFGARKVLVVSDPGVVKAGWVADVQASLARQGIEHCLFTDVSPNPRCEEVMLGAELYRSEGC 93
Cdd:cd08551 2 TRIVFGAGALARLGEELKALGGKKVLLVTDPGLVKAGLLDKVLESLKAAGIEVEVFDDVEPNPTVETVEAAAELAREEGA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 94 NVIVAVGGGSPMDCAKGIGIVAAHGRHIYEFEGVDTLRVPSPPLILIPTTAGTSADVSQFVIISNQEERMKFSIVSKAAV 173
Cdd:cd08551 82 DLVIAVGGGSVLDTAKAIAVLATNGGSIRDYEGIGKVPKPGLPLIAIPTTAGTGSEVTPNAVITDPETGRKMGIVSPYLL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 174 PDVSLIDPETTLSMDPFLSACTGIDALVHAIEAFVSTGHGPLTDPHALEAMRLINGNLVQMIANPADIALREQIMLGSMQ 253
Cdd:cd08551 162 PDVAILDPELTLSLPPSVTAATGMDALTHAIEAYTSKKANPISDALALEAIRLIGKNLRRAVADGSDLEAREAMLLASLL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 254 AGLAFSNAILGAVHAMSHSLGGYLDLPHGVCNAVLVEHVVAFNYDAAPDRYRIVAETLGIDSRGLSHRQVRERLVQHLID 333
Cdd:cd08551 242 AGIAFGNAGLGAVHALAYPLGGRYHIPHGVANAILLPYVMEFNLPACPEKYAEIAEALGEDVEGLSDEEAAEAAVEAVRE 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 515814333 334 LKQRIGFRETLSLHGVNLSDIPFLSQHAMQDPCILTN-PRSSTQRDVEVVY 383
Cdd:cd08551 322 LLRDLGIPTSLSELGVTEEDIPELAEDAMKSGRLLSNnPRPLTEEDIREIY 372
|
|
| PDDH |
cd08188 |
1,3-Propanediol (1,3-PD) dehydrogenase; This family includes 1,3-propanediol (1,3-PD) ... |
9-383 |
9.62e-157 |
|
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: 445.81 E-value: 9.62e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 9 RKFVSPEI-IFGAGCRHSVGTCAGNFGARKVLVVSDPGVVKAGWVADVQASLARQGIEHCLFTDVSPNPRCEEVMLGAEL 87
Cdd:cd08188 1 FRFYIPPVnLFGPGCLKEIGDELKKLGGKKALIVTDKGLVKLGLVKKVTDVLEEAGIEYVIFDGVQPNPTVTNVNEGLEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 88 YRSEGCNVIVAVGGGSPMDCAKGIGIVAAHGRHIYEFEGVDTLRVPSPPLILIPTTAGTSADVSQFVIISNQEERMKFSI 167
Cdd:cd08188 81 FKENGCDFIISVGGGSAHDCAKAIGILATNGGEIEDYEGVDKSKKPGLPLIAINTTAGTASEVTRFAVITDEERHVKMVI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 168 VSKAAVPDVSLIDPETTLSMDPFLSACTGIDALVHAIEAFVSTGHGPLTDPHALEAMRLINGNLVQMIANPADIALREQI 247
Cdd:cd08188 161 VDWNVTPTIAVNDPELMLGMPPSLTAATGMDALTHAIEAYVSTGATPLTDALALEAIRLIAENLPKAVANGKDLEARENM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 248 MLGSMQAGLAFSNAILGAVHAMSHSLGGYLDLPHGVCNAVLVEHVVAFNYDAAPDRYRIVAETLGIDSRGLSHRQVRERL 327
Cdd:cd08188 241 AYAQFLAGMAFNNAGLGYVHAMAHQLGGFYNLPHGVCNAILLPHVMEFNLPACPERFADIARALGENTEGLSDEEAAEAA 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 515814333 328 VQHLIDLKQRIGFRETLSLHGVNLSDIPFLSQHAMQDPCILTNPRSSTQRDVEVVY 383
Cdd:cd08188 321 IEAIRKLSRRVGIPSGLKELGVKEEDFPLLAENALKDACGPTNPRQATKEDVIAIY 376
|
|
| Fe-ADH |
pfam00465 |
Iron-containing alcohol dehydrogenase; |
14-379 |
4.66e-141 |
|
Iron-containing alcohol dehydrogenase;
Pssm-ID: 425696 [Multi-domain] Cd Length: 362 Bit Score: 405.45 E-value: 4.66e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 14 PEIIFGAGCRHSVGTCAGNFGARkVLVVSDPGVVKAGWVADVQASLARQGIEHCLFTDVSPNPRCEEVMLGAELYRSEGC 93
Cdd:pfam00465 2 TRIVFGAGALAELGEELKRLGAR-ALIVTDPGSLKSGLLDKVLASLEEAGIEVVVFDGVEPEPTLEEVDEAAALAREAGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 94 NVIVAVGGGSPMDCAKGIGIVAAHGRHIYEFEGVDTLRVPSPPLILIPTTAGTSADVSQFVIISNQEERMKFSIVSKAAV 173
Cdd:pfam00465 81 DVIIAVGGGSVIDTAKAIALLLTNPGDVWDYLGGKPLTKPALPLIAIPTTAGTGSEVTPLAVITDTETGEKLGIFSPKLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 174 PDVSLIDPETTLSMDPFLSACTGIDALVHAIEAFVSTGHGPLTDPHALEAMRLINGNLVQMIANPADIALREQIMLGSMQ 253
Cdd:pfam00465 161 PDLAILDPELTLTLPPRLTAATGMDALAHAVEAYVSKGANPLTDALALEAIRLIAENLPRAVADGEDLEARENMLLASTL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 254 AGLAFSNAILGAVHAMSHSLGGYLDLPHGVCNAVLVEHVVAFNYDAAPDRYRIVAETLGIDSRglshRQVRERLVQHLID 333
Cdd:pfam00465 241 AGLAFSNAGLGAAHALAHALGGRYGIPHGLANAILLPYVLRFNAPAAPEKLAQLARALGEDSD----EEAAEEAIEALRE 316
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 515814333 334 LKQRIGFRETLSLHGVNLSDIPFLSQHAMQDPCILTNPRSSTQRDV 379
Cdd:pfam00465 317 LLRELGLPTTLSELGVTEEDLDALAEAALRDRSLANNPRPLTAEDI 362
|
|
| LPO |
cd08176 |
Lactadehyde:propanediol oxidoreductase (LPO) catalyzes the interconversion between ... |
14-383 |
1.49e-137 |
|
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: 397.30 E-value: 1.49e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 14 PEIIFGAGCRHSVGTCAGNFGARKVLVVSDPGVVKAGWVADVQASLARQGIEHCLFTDVSPNPRCEEVMLGAELYRSEGC 93
Cdd:cd08176 7 PTSYFGWGAIEEIGEEAKKRGFKKALIVTDKGLVKFGIVDKVTDVLKEAGIAYTVFDEVKPNPTIENVMAGVAAYKESGA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 94 NVIVAVGGGSPMDCAKGIGIVAAH-GRHIYEFEGVDTLRVPSPPLILIPTTAGTSADVSQFVIISNQEERMKFSIVSKAA 172
Cdd:cd08176 87 DGIIAVGGGSSIDTAKAIGIIVANpGADVRSLEGVAPTKNPAVPIIAVPTTAGTGSEVTINYVITDTEKKRKFVCVDPHD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 173 VPDVSLIDPETTLSMDPFLSACTGIDALVHAIEAFVSTGHGPLTDPHALEAMRLINGNLVQMIANPADIALREQIMLGSM 252
Cdd:cd08176 167 IPTVAIVDPDLMSSMPKGLTAATGMDALTHAIEGYITKGAWELSDMLALKAIELIAKNLRKAVANPNNVEARENMALAQY 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 253 QAGLAFSNAILGAVHAMSHSLGGYLDLPHGVCNAVLVEHVVAFNYDAAPDRYRIVAETLGIDSRGLSHRQVRERLVQHLI 332
Cdd:cd08176 247 IAGMAFSNVGLGIVHSMAHPLSAFYDTPHGVANAILLPYVMEFNAPATGEKYRDIARAMGVDTTGMSDEEAAEAAVDAVK 326
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 515814333 333 DLKQRIGFRETLSLHGVNLSDIPFLSQHAMQDPCILTNPRSSTQRDVEVVY 383
Cdd:cd08176 327 KLSKDVGIPQKLSELGVKEEDIEALAEDALNDVCTPGNPREATKEDIIALY 377
|
|
| Fe-ADH-like |
cd08194 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
14-386 |
1.96e-121 |
|
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: 356.07 E-value: 1.96e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 14 PEIIFGAGCRHSVGTCAGNFGARKVLVVSDPGVVKAGWVADVQASLARQGIEHCLFTDVSPNPRCEEVMLGAELYRSEGC 93
Cdd:cd08194 2 RTIIIGGGALEELGEEAASLGGKRALIVTDKVMVKLGLVDKVTQLLAEAGIAYAVFDDVVSEPTDEMVEEGLALYKEGGC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 94 NVIVAVGGGSPMDCAKGIGIVAAHGRHIYEFEGVDTLRVPSPPLILIPTTAGTSADVSQFVIISNQEERMKFSIVSKAAV 173
Cdd:cd08194 82 DFIVALGGGSPIDTAKAIAVLATNGGPIRDYMGPRKVDKPGLPLIAIPTTAGTGSEVTRFTVITDTETDVKMLLKGPALL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 174 PDVSLIDPETTLSMDPFLSACTGIDALVHAIEAFVSTGHGPLTDPHALEAMRLINGNLVQMIANPADIALREQIMLGSMQ 253
Cdd:cd08194 162 PAVAIVDPELTLSMPPRVTAATGIDALTHAIEAYVSRKAQPLTDTLALSAIKLIGRNLRRAYADGDDLEAREAMMLAALE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 254 AGLAFSNAILGAVHAMSHSLGGYLDLPHGVCNAVLVEHVVAFNYDAAPDRYRIVAETLGIDSRGLSHRQVRERLVQHLID 333
Cdd:cd08194 242 AGIAFSNSSVALVHGMSRPIGALFHVPHGLSNAMLLPAVTEFSLPGAPERYAEIARAMGIATEGDSDEEAAEKLVEALER 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 515814333 334 LKQRIGFrETLSLHGVN----LSDIPFLSQHAMQDPCILTNPRSSTQRDVEVVYAEA 386
Cdd:cd08194 322 LCADLEI-PTLREYGIDeeefEAALDKMAEDALASGSPANNPRVPTKEEIIELYREA 377
|
|
| Fe-ADH-like |
cd14863 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
14-387 |
7.99e-120 |
|
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: 352.22 E-value: 7.99e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 14 PEIIFGAGCRHSVGTCAGNFGARKVLVVSDPGVVKAGWVADVQASLARQGIEHCLFTDVSPNPRCEEVMLGAELYRSEGC 93
Cdd:cd14863 6 TPVIFGAGAVEQIGELLKELGCKKVLLVTDKGLKKAGIVDKIIDLLEEAGIEVVVFDDVEPDPPDEIVDEAAEIAREEGA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 94 NVIVAVGGGSPMDCAKGIGIVAAHGRHIYEFEG-VDTLRVPSPPLILIPTTAGTSADVSQFVIISNQEERMKFSIVSKAA 172
Cdd:cd14863 86 DGVIGIGGGSVLDTAKAIAVLLTNPGPIIDYALaGPPVPKPGIPLIAIPTTAGTGSEVTPIAVITDEENGVKKSLLGPFL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 173 VPDVSLIDPETTLSMDPFLSACTGIDALVHAIEAFVSTGHGPLTDPHALEAMRLINGNLVQMIANPADIALREQIMLGSM 252
Cdd:cd14863 166 VPDLAILDPELTVGLPPSLTAATGMDALSHAIEAYTSKLANPMTDALALQAIRLIVKNLPRAVKDGDNLEARENMLLASN 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 253 QAGLAFSNAILGAVHAMSHSLGGYLDLPHGVCNAVLVEHVVAFNYDAAPDRYRIVAETLGIDSRGLSHRQVRERLVQHLI 332
Cdd:cd14863 246 LAGIAFNNAGTHIGHAIAHALGALYHIPHGLACALALPVVLEFNAEAYPEKVKKIAKALGVSFPGESDEELGEAVADAIR 325
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 515814333 333 DLKQRIGFRETLSLHGVNLSDIPFLSQHAMQDPCILTNPRSSTQRDVEVVYAEAL 387
Cdd:cd14863 326 EFMKELGIPSLFEDYGIDKEDLDKIAEAVLKDPFAMFNPRPITEEEVAEILEAIY 380
|
|
| Fe-ADH-like |
cd14861 |
Iron-containing alcohol dehydrogenases-like; This family contains proteins similar to ... |
14-387 |
8.23e-119 |
|
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: 349.50 E-value: 8.23e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 14 PEIIFGAGCRHSVGTCAGNFGARKVLVVSDPGVVKAGWVADVQASLARQGIEHCLFTDVSPNPRCEEVMLGAELYRSEGC 93
Cdd:cd14861 4 TRIRFGAGAIAELPEELKALGIRRPLLVTDPGLAALGIVDRVLEALGAAGLSPAVFSDVPPNPTEADVEAGVAAYREGGC 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 94 NVIVAVGGGSPMDCAKGIGIVAAHGRHI--YEFEGVDTLRVPS--PPLILIPTTAGTSADVSQFVIISNQEERMKFSIVS 169
Cdd:cd14861 84 DGIIALGGGSAIDAAKAIALMATHPGPLwdYEDGEGGPAAITPavPPLIAIPTTAGTGSEVGRAAVITDDDTGRKKIIFS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 170 KAAVPDVSLIDPETTLSMDPFLSACTGIDALVHAIEAFVSTGHGPLTDPHALEAMRLINGNLVQMIANPADIALREQIML 249
Cdd:cd14861 164 PKLLPKVAICDPELTLGLPPRLTAATGMDALTHCIEAYLSPGFHPMADGIALEGLRLISEWLPRAVADGSDLEARGEMMM 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 250 GSMQAGLAFSNAiLGAVHAMSHSLGGYLDLPHGVCNAVLVEHVVAFNYDAAPDRYRIVAETLGIDSRGlshrqvRERLVQ 329
Cdd:cd14861 244 AALMGAVAFQKG-LGAVHALAHALGALYGLHHGLLNAILLPYVLRFNRPAVEDKLARLARALGLGLGG------FDDFIA 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 515814333 330 HLIDLKQRIGFRETLSLHGVNLSDIPFLSQHAMQDPCILTNPRSSTQRDVEVVYAEAL 387
Cdd:cd14861 317 WVEDLNERLGLPATLSELGVTEDDLDELAELALADPCHATNPRPVTAEDYRALLREAL 374
|
|
| lactal_redase |
TIGR02638 |
lactaldehyde reductase; This clade of genes encoding iron-containing alcohol dehydrogenase ... |
10-383 |
5.18e-116 |
|
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: 342.49 E-value: 5.18e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 10 KFVSPEI-IFGAGCRHSVGTCAGNFGARKVLVVSDPGVVKAGWVADVQASLARQGIEHCLFTDVSPNPRCEEVMLGAELY 88
Cdd:TIGR02638 3 RLILNETsYFGAGAIEDIVDEVKRRGFKKALVVTDKDLIKFGVADKVTDLLDEAGIAYELFDEVKPNPTITVVKAGVAAF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 89 RSEGCNVIVAVGGGSPMDCAKGIGIVAAHGR--HIYEFEGVDTLRVPSPPLILIPTTAGTSADVSQFVIISNQEERMKFS 166
Cdd:TIGR02638 83 KASGADYLIAIGGGSPIDTAKAIGIISNNPEfaDVRSLEGVAPTKKPGVPIIAIPTTAGTAAEVTINYVITDEENKRKFV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 167 IVSKAAVPDVSLIDPETTLSMDPFLSACTGIDALVHAIEAFVSTGHGPLTDPHALEAMRLINGNLVQMIANPADIALREQ 246
Cdd:TIGR02638 163 CVDPHDIPDVAVIDAEMMYSMPKSLTAATGMDALTHAIEGYITKGAWELTDMLHLKAIEIIARWLRSAVEGGKDLEAREQ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 247 IMLGSMQAGLAFSNAILGAVHAMSHSLGGYLDLPHGVCNAVLVEHVVAFNYDAAPDRYRIVAETLGIDSRGLSHRQVRER 326
Cdd:TIGR02638 243 MALGQYVAGMGFSNVGLGLVHGMAHPLGAFYNTPHGVANAILLPHVMEFNAEFTGEKYREIAKAMGVKTEGMSDEEARDA 322
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 515814333 327 LVQHLIDLKQRIGFRETLSLHGVNLSDIPFLSQHAMQDPCILTNPRSSTQRDVEVVY 383
Cdd:TIGR02638 323 AVEAVKTLSKRVGIPEGLSELGVKEEDIPALAEAALADVCTGGNPRETTVEEIEELY 379
|
|
| Fe-ADH-like |
cd14865 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
11-387 |
1.01e-111 |
|
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: 331.81 E-value: 1.01e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 11 FVSPEIIFGAGCRHSVGTCAGNFGARKVLVVSDPGVVKAGWVADVQASLARQGIEHCLFTDVSPNPRCEEVMLGAELYRS 90
Cdd:cd14865 4 FNPTKIVSGAGALENLPAELARLGARRPLIVTDKGLAAAGLLKKVEDALGDAIEIVGVFDDVPPDSSVAVVNEAAARARE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 91 EGCNVIVAVGGGSPMDCAKGIGIVAAHG-RHIYEFEGVDTLRVPSPPLILIPTTAGTSADVSQFVIISNQEERMKFSIVS 169
Cdd:cd14865 84 AGADGIIAVGGGSVIDTAKGVNILLSEGgDDLDDYGGANRLTRPLKPLIAIPTTAGTGSEVTLVAVIKDEEKKVKLLFVS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 170 KAAVPDVSLIDPETTLSMDPFLSACTGIDALVHAIEAFVSTGHGPLTDPHALEAMRLINGNLVQMIANPADIALREQIML 249
Cdd:cd14865 164 PFLLPDVAILDPRLTLSLPPKLTAATGMDALTHAIEAYTSLQKNPISDALALQAIRLISENLPKAVKNGKDLEARLALAI 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 250 GSMQAGLAFSNAILGAVHAMSHSLGGYLDLPHGVCNAVLVEHVVAFNYDAAPDRYRIVAETL--GIDSRGLSHRQVRERL 327
Cdd:cd14865 244 AATMAGIAFSNSMVGLVHAIAHAVGAVAGVPHGLANSILLPHVMRYNLDAAAERYAELALALayGVTPAGRRAEEAIEAA 323
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 328 VQHLIDLKQRIGFRETLSLHGVNLSDIPFLSQHAMQDPCILTNPRSSTQRDVEVVYAEAL 387
Cdd:cd14865 324 IDLVRRLHELCGLPTRLRDVGVPEEQLEAIAELALNDGAILFNPREVDPEDILAILEAAY 383
|
|
| Fe-ADH-like |
cd08185 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
11-383 |
7.08e-110 |
|
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: 326.76 E-value: 7.08e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 11 FVSPEIIFGAGCRHSVGTCAGNFGaRKVLVVSDPGVVK-AGWVADVQASLARQGIEHCLFTDVSPNPRCEEVMLGAELYR 89
Cdd:cd08185 2 YQPTRILFGAGKLNELGEEALRPG-KKALIVTGKGSSKkTGLLDRVKKLLEKAGVEVVVFDKVEPNPLTTTVMEGAALAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 90 SEGCNVIVAVGGGSPMDCAKGIGIVAAHGRHI--YEFEGVDTLRVPSP--PLILIPTTAGTSADVSQFVIISNQEERMKF 165
Cdd:cd08185 81 EEGCDFVIGLGGGSSMDAAKAIAFMATNPGDIwdYIFGGTGKGPPPEKalPIIAIPTTAGTGSEVDPWAVITNPETKEKK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 166 SIVSKAAVPDVSLIDPETTLSMDPFLSACTGIDALVHAIEAFVSTGHGPLTDPHALEAMRLINGNLVQMIANPADIALRE 245
Cdd:cd08185 161 GIGHPALFPKVSIVDPELMLTVPPRVTAYTGFDALFHAFESYISKNANPFSDMLALEAIRLVAKYLPRAVKDGSDLEARE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 246 QIMLGSMQAGLAFSNAILGAVHAMSHSLGGYL-DLPHGVCNAVLVEHVVAFNYDAAPDRYRIVAEtlgIDSRGLSHRQVR 324
Cdd:cd08185 241 KMAWASTLAGIVIANSGTTLPHGLEHPLSGYHpNIPHGAGLAALYPAYFEFTIEKAPEKFAFVAR---AEASGLSDAKAA 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515814333 325 ERLVQHLIDLKQRIGFRETLSLHGVNLSDIPFLSQHAM--QDPCILTNPRSSTQRDVEVVY 383
Cdd:cd08185 318 EDFIEALRKLLKDIGLDDLLSDLGVTEEDIPWLAENAMetMGGLFANNPVELTEEDIVEIY 378
|
|
| Fe-ADH-like |
cd08189 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
14-363 |
9.48e-107 |
|
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: 318.64 E-value: 9.48e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 14 PEIIFGAGCRHSVGTCAGNFGARKVLVVSDPGVVKAGWVADVQASLARQGIEHCLFTDVSPNPRCEEVMLGAELYRSEGC 93
Cdd:cd08189 6 PELFEGAGSLLQLPEALKKLGIKRVLIVTDKGLVKLGLLDPLLDALKKAGIEYVVFDGVVPDPTIDNVEEGLALYKENGC 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 94 NVIVAVGGGSPMDCAKGIGIVAAHGRH-IYEFEGVDTLRVPSPPLILIPTTAGTSADVSQFVIISNQEERMKFSIVSKAA 172
Cdd:cd08189 86 DAIIAIGGGSVIDCAKVIAARAANPKKsVRKLKGLLKVRKKLPPLIAVPTTAGTGSEATIAAVITDPETHEKYAINDPKL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 173 VPDVSLIDPETTLSMDPFLSACTGIDALVHAIEAFVSTGHGPLTDPHALEAMRLINGNLVQMIANPADIALREQIMLGSM 252
Cdd:cd08189 166 IPDAAVLDPELTLGLPPAITAATGMDALTHAVEAYISRSATKETDEYALEAVKLIFENLPKAYEDGSDLEARENMLLASY 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 253 QAGLAFSNAILGAVHAMSHSLGGYLDLPHGVCNAVLVEHVVAFNYDAAPDRYRIVAETLGIDSRGLSHRQVRERLVQHLI 332
Cdd:cd08189 246 YAGLAFTRAYVGYVHAIAHQLGGLYGVPHGLANAVVLPHVLEFYGPAAEKRLAELADAAGLGDSGESDSEKAEAFIAAIR 325
|
330 340 350
....*....|....*....|....*....|.
gi 515814333 333 DLKQRIGFRETLSlhGVNLSDIPFLSQHAMQ 363
Cdd:cd08189 326 ELNRRMGIPTTLE--ELKEEDIPEIAKRALK 354
|
|
| PRK10624 |
PRK10624 |
L-1,2-propanediol oxidoreductase; Provisional |
18-387 |
9.10e-104 |
|
L-1,2-propanediol oxidoreductase; Provisional
Pssm-ID: 182595 [Multi-domain] Cd Length: 382 Bit Score: 311.16 E-value: 9.10e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 18 FGAGCRHSVGTCAGNFGARKVLVVSDPGVVKAGWVADVQASLARQGIEHCLFTDVSPNPRCEEVMLGAELYRSEGCNVIV 97
Cdd:PRK10624 13 FGRGAIGALTDEVKRRGFKKALIVTDKTLVKCGVVAKVTDVLDAAGLAYEIYDGVKPNPTIEVVKEGVEVFKASGADYLI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 98 AVGGGSPMDCAKGIGIVAAHGrhiyEF------EGVDTLRVPSPPLILIPTTAGTSADVSQFVIISNQEERMKFSIVSKA 171
Cdd:PRK10624 93 AIGGGSPQDTCKAIGIISNNP----EFadvrslEGVAPTKKPSVPIIAIPTTAGTAAEVTINYVITDEEKRRKFVCVDPH 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 172 AVPDVSLIDPETTLSMDPFLSACTGIDALVHAIEAFVSTGHGPLTDPHALEAMRLINGNLVQMIANPADIalREQIMLGS 251
Cdd:PRK10624 169 DIPQVAFVDADMMDSMPPGLKAATGVDALTHAIEGYITRGAWALTDMLHLKAIEIIAGALRGAVAGDKEA--GEGMALGQ 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 252 MQAGLAFSNAILGAVHAMSHSLGGYLDLPHGVCNAVLVEHVVAFNYDAAPDRYRIVAETLGIDSRGLSHRQVRERLVQHL 331
Cdd:PRK10624 247 YIAGMGFSNVGLGLVHGMAHPLGAFYNTPHGVANAILLPHVMEYNADFTGEKYRDIARAMGVKVEGMSLEEARNAAVEAV 326
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 515814333 332 IDLKQRIGFRETLSLHGVNLSDIPFLSQHAMQDPCILTNPRSSTQRDVEVVYAEAL 387
Cdd:PRK10624 327 KALNRDVGIPPHLRDVGVKEEDIPALAQAAFDDVCTGGNPREATLEDIVELYKKAW 382
|
|
| HOT |
cd08190 |
Hydroxyacid-oxoacid transhydrogenase (HOT) involved in gamma-hydroxybutyrate metabolism; This ... |
13-387 |
2.87e-101 |
|
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: 306.01 E-value: 2.87e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 13 SPEIIFGAGCRHSVGTCAGNFGARKVLVVSDPGVVKAGWVADVQASLARQGIEHCLFTDVSPNPRCEEVMLGAELYRSEG 92
Cdd:cd08190 1 ASNIRFGPGATRELGMDLKRLGAKKVLVVTDPGLAKLGLVERVLESLEKAGIEVVVYDGVRVEPTDESFEEAIEFAKEGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 93 CNVIVAVGGGSPMDCAKGIGIVAAHGRHIYEF------EGvdtLRVPSP--PLILIPTTAGTSADVSQFVIISNQEERMK 164
Cdd:cd08190 81 FDAFVAVGGGSVIDTAKAANLYATHPGDFLDYvnapigKG---KPVPGPlkPLIAIPTTAGTGSETTGVAIFDLEELKVK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 165 FSIVSKAAVPDVSLIDPETTLSMDPFLSACTGIDALVHAIEAF------------------VSTGHGPLTDPHALEAMRL 226
Cdd:cd08190 158 TGISSRYLRPTLAIVDPLLTLTLPPRVTASSGFDVLCHALESYtarpynarprpanpderpAYQGSNPISDVWAEKAIEL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 227 INGNLVQMIANPADIALREQIMLGSMQAGLAFSNAILGAVHAMSHSLGG---------YLD----LPHGVCNAVLVEHVV 293
Cdd:cd08190 238 IGKYLRRAVNDGDDLEARSNMLLASTLAGIGFGNAGVHLPHAMAYPIAGlvkdyrppgYPVdhphVPHGLSVALTAPAVF 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 294 AFNYDAAPDRYRIVAETLGIDSRGLSHRQVRERLVQHLIDLKQRIGFRETLSLHGVNLSDIPFLSQHAM-QDPCILTNPR 372
Cdd:cd08190 318 RFTAPACPERHLEAAELLGADTSGASDRDAGEVLADALIKLMRDIGIPNGLSALGYSEDDIPALVEGTLpQQRLLKLNPR 397
|
410
....*....|....*
gi 515814333 373 SSTQRDVEVVYAEAL 387
Cdd:cd08190 398 PVTEEDLEEIFEDAL 412
|
|
| HVD |
cd08193 |
5-hydroxyvalerate dehydrogenase (HVD) catalyzes the oxidation of 5-hydroxyvalerate to ... |
14-387 |
8.78e-101 |
|
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: 303.66 E-value: 8.78e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 14 PEIIFGAGCRHSVGTCAGNFGARKVLVVSDPGVVKAGWVADVQASLARQGIEHCLFTDVSPNPRCEEVMLGAELYRSEGC 93
Cdd:cd08193 5 PRIICGAGAAARLGELLRELGARRVLLVTDPGLVKAGLADPALAALEAAGIAVTVFDDVVADPPEAVVEAAVEQAREAGA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 94 NVIVAVGGGSPMDCAKGIGIVAAHGRHIYEFEGVDTLRVPSPPLILIPTTAGTSADVSQFVIISNQEERmKFSIVSKAAV 173
Cdd:cd08193 85 DGVIGFGGGSSMDVAKLVALLAGSDQPLDDIYGVGKATGPRLPLILVPTTAGTGSEVTPISIVTTGETE-KKGVVSPQLL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 174 PDVSLIDPETTLSMDPFLSACTGIDALVHAIEAFVS-TGHGPLTDPHALEAMRLINGNLVQMIANPADIALREQIMLGSM 252
Cdd:cd08193 164 PDVALLDAELTLGLPPHVTAATGIDAMVHAIEAYTSrHKKNPISDALAREALRLLGANLRRAVEDGSDLEAREAMLLGSM 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 253 QAGLAFSNAILGAVHAMSHSLGGYLDLPHGVCNAVLVEHVVAFNYDAAPDRYRIVAETLGIDSRGLSHRQVRERLVQHLI 332
Cdd:cd08193 244 LAGQAFANAPVAAVHALAYPLGGHFHVPHGLSNALVLPHVLRFNLPAAEALYAELARALLPGLAFGSDAAAAEAFIDALE 323
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 515814333 333 DLKQRIGFRETLSLHGVNLSDIPFLSQHAM-QDPCILTNPRSSTQRDVEVVYAEAL 387
Cdd:cd08193 324 ELVEASGLPTRLRDVGVTEEDLPMLAEDAMkQTRLLVNNPREVTEEDALAIYQAAL 379
|
|
| PRK09860 |
PRK09860 |
putative alcohol dehydrogenase; Provisional |
11-387 |
1.41e-99 |
|
putative alcohol dehydrogenase; Provisional
Pssm-ID: 182118 [Multi-domain] Cd Length: 383 Bit Score: 300.72 E-value: 1.41e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 11 FVSPEIIFGAGCRHSVGTCAGNFGARKVLVVSDPGVVKAGWVADVQASLARQGIEHCLFTDVSPNPRCEEVMLGAELYRS 90
Cdd:PRK09860 7 FIPSVNVIGADSLTDAMNMMADYGFTRTLIVTDNMLTKLGMAGDVQKALEERNIFSVIYDGTQPNPTTENVAAGLKLLKE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 91 EGCNVIVAVGGGSPMDCAKGIGIVAAHGRHIYEFEGVDTLRVPSPPLILIPTTAGTSADVSQFVIISNQEERMKFSIVSK 170
Cdd:PRK09860 87 NNCDSVISLGGGSPHDCAKGIALVAANGGDIRDYEGVDRSAKPQLPMIAINTTAGTASEMTRFCIITDEARHIKMAIVDK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 171 AAVPDVSLIDPETTLSMDPFLSACTGIDALVHAIEAFVSTGHGPLTDPHALEAMRLINGNLVQMIANPADIALREQIMLG 250
Cdd:PRK09860 167 HVTPLLSVNDSSLMIGMPKSLTAATGMDALTHAIEAYVSIAATPITDACALKAVTMIAENLPLAVEDGSNAKAREAMAYA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 251 SMQAGLAFSNAILGAVHAMSHSLGGYLDLPHGVCNAVLVEHVVAFNYDAAPDRYRIVAETLGIDSRGLSHRQVRERLVQH 330
Cdd:PRK09860 247 QFLAGMAFNNASLGYVHAMAHQLGGFYNLPHGVCNAVLLPHVQVFNSKVAAARLRDCAAAMGVNVTGKNDAEGAEACINA 326
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 515814333 331 LIDLKQRIGFRETLSLHGVNLSDIPFLSQHAMQDPCILTNPRSSTQRDVEVVYAEAL 387
Cdd:PRK09860 327 IRELAKKVDIPAGLRDLNVKEEDFAVLATNALKDACGFTNPIQATHEEIVAIYRAAM 383
|
|
| Fe-ADH-like |
cd08191 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
11-387 |
6.26e-94 |
|
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: 286.43 E-value: 6.26e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 11 FVSPEIIFGAGCRHSVGTCAGNFGARkVLVVSDPGVVKAGWVADVQASLARQGIEHCLFTDVSPNPRCEEVMLGAELYRS 90
Cdd:cd08191 2 RSPSRLLFGPGARRALGRVAARLGSR-VLIVTDPRLASTPLVAELLAALTAAGVAVEVFDGGQPELPVSTVADAAAAARA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 91 EGCNVIVAVGGGSPMDCAKGIGIVAAHGRHIYEFEGVDtlRVPSP--PLILIPTTAGTSADVSQFVIISNQEERMKFSIV 168
Cdd:cd08191 81 FDPDVVIGLGGGSNMDLAKVVALLLAHGGDPRDYYGED--RVPGPvlPLIAVPTTAGTGSEVTPVAVLTDPARGMKVGVS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 169 SKAAVPDVSLIDPETTLSMDPFLSACTGIDALVHAIEAFVST---------------GHGPLTDPHALEAMRLINGNLVQ 233
Cdd:cd08191 159 SPYLRPAVAIVDPELTLTCPPGVTADSGIDALTHAIESYTARdfppfprldpdpvyvGKNPLTDLLALEAIRLIGRHLPR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 234 MIANPADIALREQIMLGSMQAGLAFSNAILGAVHAMSHSLGGYLDLPHGVCNAVLVEHVVAFNYDAAPDRYRIVAETLGI 313
Cdd:cd08191 239 AVRDGDDLEARSGMALAALLAGLAFGTAGTAAAHALQYPIGALTHTSHGVGNGLLLPYVMRFNRPARAAELAEIARALGV 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515814333 314 DSRGLSHRQVReRLVQHLIDLKQRIGFRETLSLHGVNLSDIPFLSQHAMQ-DPCILTNPRSSTQRDVEVVYAEAL 387
Cdd:cd08191 319 TTAGTSEEAAD-RAIERVEELLARIGIPTTLADLGVTEADLPGLAEKALSvTRLIANNPRPPTEEDLLRILRAAF 392
|
|
| Fe-ADH-like |
cd14862 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
11-380 |
2.45e-92 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341484 [Multi-domain] Cd Length: 375 Bit Score: 281.81 E-value: 2.45e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 11 FVSPEIIFGAGcrhsVGTCAGNFGARKVLVVSDPGVVKAGWVADVQASLARQGIEHCLFTDVSPNPRCEEVMLGAELYRS 90
Cdd:cd14862 4 FSSPKIVFGED----ALSHLEQLSGKRALIVTDKVLVKLGLLKKVLKRLLQAGFEVEVFDEVEPEPPLETVLKGAEAMRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 91 EGCNVIVAVGGGSPMDCAKGIGIvaahgrhIYEFEGVDTLRVPSPP---------LILIPTTAGTSADVSQFVIISNQEE 161
Cdd:cd14862 80 FEPDLIIALGGGSVMDAAKAAWV-------LYERPDLDPEDISPLDllglrkkakLIAIPTTSGTGSEATWAIVLTDTEE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 162 RMKFSIVSKAAVPDVSLIDPETTLSMDPFLSACTGIDALVHAIEAFVSTGHGPLTDPHALEAMRLINGNLVQMIANPADI 241
Cdd:cd14862 153 PRKIAVANPELVPDVAILDPEFVLGMPPKLTAGTGLDALAHAVEAYLSTWSNDFSDALALKAIELIFKYLPRAYKDGDDL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 242 ALREQIMLGSMQAGLAFSNAILGAVHAMSHSLGGYLDLPHGVCNAVLVEHVVAFNYDAAPDRYRIVAEtlgIDSRGLSHR 321
Cdd:cd14862 233 EAREKMHNAATIAGLAFGNSQAGLAHALGHSLGAVFHVPHGIAVGLFLPYVIEFYAKVTDERYDLLKL---LGIEARDEE 309
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515814333 322 QVRERLVQHLIDLKQRIGFRETLSLHGVNLSD----IPFLSQHAMQDPCILTNPRSSTQRDVE 380
Cdd:cd14862 310 EALKKLVEAIRELYKEVGQPLSIKDLGISEEEfeekLDELVEYAMEDSCTITSPRPPSEEDLK 372
|
|
| NADPH_BDH |
cd08179 |
NADPH-dependent butanol dehydrogenase involved in the butanol and ethanol formation pathway in ... |
9-383 |
8.30e-92 |
|
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: 280.62 E-value: 8.30e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 9 RKFVSPEIIFGAGCRHSVGTCAGnfgaRKVLVVSDPGVVKA-GWVADVQASLARQGIEHCLFTDVSPNPRCEEVMLGAEL 87
Cdd:cd08179 1 RFFVPRDIYFGEGALEYLKTLKG----KRAFIVTGGGSMKRnGFLDKVEDYLKEAGMEVKVFEGVEPDPSVETVEKGAEA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 88 YRSEGCNVIVAVGGGSPMDCAKGIGIVaahgrhiYE-----FEgvDTLRVPSPP-------LILIPTTAGTSADVSQFVI 155
Cdd:cd08179 77 MREFEPDWIIAIGGGSVIDAAKAMWVF-------YEypeltFE--DALVPFPLPelrkkarFIAIPSTSGTGSEVTRASV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 156 ISNQEERMKFSIVSKAAVPDVSLIDPETTLSMDPFLSACTGIDALVHAIEAFVSTGHGPLTDPHALEAMRLINGNLVQMI 235
Cdd:cd08179 148 ITDTEKGIKYPLASFEITPDVAILDPELTMTMPPHVTANTGMDALTHAIEAYVSTLANDFTDALALGAILDIFENLPKSY 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 236 ANPADIALREQIMLGSMQAGLAFSNAILGAVHAMSHSLGGYLDLPHGVCNAVLVEHVVAFNYDAAPDRYRIVAETLGIDS 315
Cdd:cd08179 228 NGGKDLEAREKMHNASCLAGMAFSNSGLGIVHSMAHKGGAFFGIPHGLANAILLPYVIEFNSKDPEARARYAALLIGLTD 307
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515814333 316 RGLShrqvrERLVQHLIDLKQRIGFRETLSLHGVN----LSDIPFLSQHAMQDPCILTNPRSSTQRDVEVVY 383
Cdd:cd08179 308 EELV-----EDLIEAIEELNKKLGIPLSFKEAGIDedefFAKLDEMAENAMNDACTGTNPRKPTVEEMKELL 374
|
|
| Fe-ADH-like |
cd08183 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
14-372 |
4.84e-90 |
|
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: 275.92 E-value: 4.84e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 14 PEIIFGAGCRHSVGTCAGNFGaRKVLVVSDPGVVKAGWVADVQASLARQGIEHCLFtDVSPNPRCEEVMLGAELYRSEGC 93
Cdd:cd08183 2 PRIVFGRGSLQELGELAAELG-KRALLVTGRSSLRSGRLARLLEALEAAGIEVALF-SVSGEPTVETVDAAVALAREAGC 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 94 NVIVAVGGGSPMDCAKGIGIVAAHGRHIYEF-EGVDT---LRVPSPPLILIPTTAGTSADVSQFVIISNQEERMKFSIVS 169
Cdd:cd08183 80 DVVIAIGGGSVIDAAKAIAALLTNEGSVLDYlEVVGKgrpLTEPPLPFIAIPTTAGTGSEVTKNAVLSSPEHGVKVSLRS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 170 KAAVPDVSLIDPETTLSMDPFLSACTGIDALVHAIEAFVSTGHGPLTDPHALEAMRLINGNLVQMIANPADIALREQIML 249
Cdd:cd08183 160 PSMLPDVALVDPELTLSLPPEVTAASGLDALTQLIEPYVSRKANPLTDALAREGLRLAARSLRRAYEDGEDLEAREDMAL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 250 GSMQAGLAFSNAILGAVHAMSHSLGGYLDLPHG-VCnAVLVEHVVAFNYDA---------APDRYRIVAETLGIDsrgls 319
Cdd:cd08183 240 ASLLGGLALANAGLGAVHGLAGPLGGMFGAPHGaIC-AALLPPVLEANLRAlrerepdspALARYRELAGILTGD----- 313
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 515814333 320 HRQVRERLVQHLIDLKQRIGFReTLSLHGVNLSDIPFLSQHAMQDPCILTNPR 372
Cdd:cd08183 314 PDAAAEDGVEWLEELCEELGIP-RLSEYGLTEEDFPEIVEKARGSSSMKGNPI 365
|
|
| AAD_C |
cd08178 |
C-terminal alcohol dehydrogenase domain of the acetaldehyde dehydrogenase-alcohol ... |
12-372 |
6.97e-89 |
|
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: 273.68 E-value: 6.97e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 12 VSPEIIFGAGC-RHSVGTcagNFGARKVLVVSDPGVVKAGWVADVQASLARQGIEHCLFTDVSPNPRCEEVMLGAELYRS 90
Cdd:cd08178 2 VPPKIYFEPGClPYLLLE---LPGVKRAFIVTDRVLYKLGYVDKVLDVLEARGVETEVFSDVEPDPTLSTVRKGLEAMNA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 91 EGCNVIVAVGGGSPMDCAKGIGIvaahgrhIYE-----FEGVDTL------RVPSPP-------LILIPTTAGTSADVSQ 152
Cdd:cd08178 79 FKPDVIIALGGGSAMDAAKIMWL-------FYEhpetkFEDLAQRfmdirkRVYKFPklgkkakLVAIPTTSGTGSEVTP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 153 FVIISNQEERMKFSIVSKAAVPDVSLIDPETTLSMDPFLSACTGIDALVHAIEAFVSTGHGPLTDPHALEAMRLINGNLV 232
Cdd:cd08178 152 FAVITDDKTGKKYPLADYALTPDMAIVDPELVMTMPKRLTADTGIDALTHAIEAYVSVMASDYTDGLALQAIKLIFEYLP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 233 QMIANPADIALREQIMLGSMQAGLAFSNAILGAVHAMSHSLGGYLDLPHGVCNAVLVEHVVAFN---------------Y 297
Cdd:cd08178 232 RSYNNGNDIEAREKMHNAATIAGMAFANAFLGICHSLAHKLGAAFHIPHGRANAILLPHVIRYNatdpptkqaafpqykY 311
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515814333 298 DAAPDRYRIVAETLGIdsRGLSHRQVRERLVQHLIDLKQRIGFRETLSLHGVNLSD----IPFLSQHAMQDPCILTNPR 372
Cdd:cd08178 312 YVAKERYAEIADLLGL--GGKTPEEKVESLIKAIEDLKKDLGIPTSIREAGIDEADflaaVDKLAEDAFDDQCTGANPR 388
|
|
| Fe-ADH-like |
cd08196 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
10-383 |
3.54e-88 |
|
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: 270.99 E-value: 3.54e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 10 KFVSP-EIIFGAGCRHSVGTCAGNFGARKVLVVSDPGVVKAGWVADVQASLARQGIEhcLFTDVSPNPRCEEVMLGAELY 88
Cdd:cd08196 2 SYYQPvKIIFGEGILKELPDIIKELGGKRGLLVTDPSFIKSGLAKRIVESLKGRIVA--VFSDVEPNPTVENVDKCARLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 89 RSEGCNVIVAVGGGSPMDCAKGIGIVAAHGRHIYEF-EGVDTLRVPSPPLILIPTTAGTSADVSQFVIISNQEERMKFSI 167
Cdd:cd08196 80 RENGADFVIAIGGGSVLDTAKAAACLAKTDGSIEDYlEGKKKIPKKGLPLIAIPTTAGTGSEVTPVAVLTDKEKGKKAPL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 168 VSKAAVPDVSLIDPETTLSMDPFLSACTGIDALVHAIEAFVSTGHGPLTDPHALEAMRLINGNLVQMIANPADIALREQI 247
Cdd:cd08196 160 VSPGFYPDIAIVDPELTYSMPPKVTASTGIDALCHAIEAYWSINHQPISDALALEAAKLVLENLEKAYNNPNDKEAREKM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 248 MLGSMQAGLAFSNAILGAVHAMSHSLGGYLDLPHGVCNAVLVEHVVAFNYDAAPDRYRIVAETLGIDSrglshrqvRERL 327
Cdd:cd08196 240 ALASLLAGLAFSQTRTTASHACSYPLTSHFGIPHGEACALTLPSFIRLNAEALPGRLDELAKQLGFKD--------AEEL 311
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 515814333 328 VQHLIDLKQRIGFRETLSLHGVNLSDIPFLSQHAMQDPCILTNPRSSTQRDVEVVY 383
Cdd:cd08196 312 ADKIEELKKRIGLRTRLSELGITEEDLEEIVEESFHPNRANNNPVEVTKEDLEKLL 367
|
|
| PDD |
cd08180 |
1,3-propanediol dehydrogenase (PPD) catalyzes the reduction of 3-hydroxypropionaldehyde (3-HPA) ... |
11-383 |
1.35e-78 |
|
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: 245.10 E-value: 1.35e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 11 FVSPEIIFGAGCRHSVGTCAGnfgaRKVLVVSDPGVVKAGWVADVQASLaRQGIEHCLFTDVSPNPRCEEVMLGAELYRS 90
Cdd:cd08180 2 SLKTKIYSGEDSLERLKELKG----KRVFIVTDPFMVKSGMVDKVTDEL-DKSNEVEIFSDVVPDPSIEVVAKGLAKILE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 91 EGCNVIVAVGGGSPMDCAKGIGIVAAHGRHIYEFegvdtlrvpsPPLILIPTTAGTSADVSQFVIISNQEERMKFSIVSK 170
Cdd:cd08180 77 FKPDTIIALGGGSAIDAAKAIIYFALKQKGNIKK----------PLFIAIPTTSGTGSEVTSFAVITDPEKGIKYPLVDD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 171 AAVPDVSLIDPETTLSMDPFLSACTGIDALVHAIEAFVSTGHGPLTDPHALEAMRLINGNLVQMIANPADIALREQIMLG 250
Cdd:cd08180 147 SMLPDIAILDPELVKSVPPKVTADTGMDVLTHALEAYVSTNANDFTDALAEKAIKLVFENLPRAYRDGDDLEAREKMHNA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 251 SMQAGLAFSNAILGAVHAMSHSLGGYLDLPHGVCNAVLVEHVVAFnydaapdryrivaetlgidsrglshrqvrerLVQH 330
Cdd:cd08180 227 SCMAGIAFNNAGLGINHSLAHALGGRFHIPHGRANAILLPYVIEF-------------------------------LIAA 275
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 515814333 331 LIDLKQRIGFRETLSLHGVNLSD----IPFLSQHAMQDPCILTNPRSSTQRDVEVVY 383
Cdd:cd08180 276 IRRLNKKLGIPSTLKELGIDEEEfekaIDEMAEAALADRCTATNPRKPTAEDLIELL 332
|
|
| HEPD |
cd08182 |
Hydroxyethylphosphoate dehydrogenase (HEPD) catalyzes the reduction of phosphonoacetaldehyde ... |
15-380 |
1.85e-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: 243.29 E-value: 1.85e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 15 EIIFGAGCRHSVGTCAGNFGARKVLVVSDPGVVKAGWVADVQASLArQGIEHCLFTDVSPNPRCEEVMLGAELYRSEGCN 94
Cdd:cd08182 3 KIIFGPGALAELKDLLGGLGARRVLLVTGPSAVRESGAADILDALG-GRIPVVVFSDFSPNPDLEDLERGIELFRESGPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 95 VIVAVGGGSPMDCAKGIGIVAAHGRHIYEF--EGVDTLRVPSPPLILIPTTAGTSADVSQFVIISNQEERMKFSIVSKAA 172
Cdd:cd08182 82 VIIAVGGGSVIDTAKAIAALLGSPGENLLLlrTGEKAPEENALPLIAIPTTAGTGSEVTPFATIWDEAEGKKYSLAHPSL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 173 VPDVSLIDPETTLSMDPFLSACTGIDALVHAIEAFVSTGHGPLTDPHALEAMRLINGNLVQMIANPADIALREQIMLGSM 252
Cdd:cd08182 162 YPDAAILDPELTLSLPLYLTASTGLDALSHAIESIWSVNANPESRAYALRAIRLILENLPLLLENLPNLEAREAMAEASL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 253 QAGLAFSNAILGAVHAMSHSLGGYLDLPHGVCNAVLVEHVVAFNYDAAPDryRIVAETLGIDSRGLSHRQVRErLVQHLI 332
Cdd:cd08182 242 LAGLAISITKTTAAHAISYPLTSRYGVPHGHACALTLPAVLRYNAGADDE--CDDDPRGREILLALGASDPAE-AAERLR 318
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 515814333 333 DLKQRIGFRETLSLHGVNLSDIPFLSQHAMQDPCILTNPRSSTQRDVE 380
Cdd:cd08182 319 ALLESLGLPTRLSEYGVTAEDLEALAASVNTPERLKNNPVRLSEEDLL 366
|
|
| PRK13805 |
PRK13805 |
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional |
34-372 |
3.98e-77 |
|
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional
Pssm-ID: 237515 [Multi-domain] Cd Length: 862 Bit Score: 254.72 E-value: 3.98e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 34 GARKVLVVSDPGVVKAGWVADV--QASLARQGIEHCLFTDVSPNPRCEEVMLGAELYRSEGCNVIVAVGGGSPMDCAKGI 111
Cdd:PRK13805 479 GKKRAFIVTDRFMVELGYVDKVtdVLKKRENGVEYEVFSEVEPDPTLSTVRKGAELMRSFKPDTIIALGGGSPMDAAKIM 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 112 givaahgRHIYE-----FEGV-----D----TLRVPSPP----LILIPTTAGTSADVSQFVIISNQEERMKFSIVSKAAV 173
Cdd:PRK13805 559 -------WLFYEhpetdFEDLaqkfmDirkrIYKFPKLGkkakLVAIPTTSGTGSEVTPFAVITDDKTGVKYPLADYELT 631
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 174 PDVSLIDPETTLSMDPFLSACTGIDALVHAIEAFVSTGHGPLTDPHALEAMRLINGNLVQMIANPA-DIALREQIMLGSM 252
Cdd:PRK13805 632 PDVAIVDPNLVMTMPKSLTADTGIDALTHALEAYVSVMASDYTDGLALQAIKLVFEYLPRSYKNGAkDPEAREKMHNAST 711
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 253 QAGLAFSNAILGAVHAMSHSLGGYLDLPHGVCNAVLVEHVVAFN------------YDA--APDRYRIVAETLGIdsRGL 318
Cdd:PRK13805 712 IAGMAFANAFLGICHSMAHKLGAEFHIPHGRANAILLPHVIRYNatdppkqaafpqYEYprADERYAEIARHLGL--PGS 789
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 515814333 319 SHRQVRERLVQHLIDLKQRIGFRETLSLHGVN----LSDIPFLSQHAMQDPCILTNPR 372
Cdd:PRK13805 790 TTEEKVESLIKAIEELKAELGIPMSIKEAGVDeadfLAKLDELAELAFDDQCTGANPR 847
|
|
| PPD-like |
cd08181 |
1,3-propanediol dehydrogenase-like (PPD); This family contains proteins similar to 1, ... |
11-384 |
5.00e-69 |
|
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: 221.31 E-value: 5.00e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 11 FVSP-EIIFGAGCRHSVGTCAGNFGaRKVLVVSdpGVV---KAGWVADVQASLARQGIEHCLFTDVSPNPRCEEVMLGAE 86
Cdd:cd08181 1 FYMPtKVYFGKNCVEKHADELAALG-KKALIVT--GKHsakKNGSLDDVTEALEENGIEYFIFDEVEENPSIETVEKGAE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 87 LYRSEGCNVIVAVGGGSPMDCAKGIGIVAAHGRHIYE-FEGVDTLrvPSPPLILIPTTAGTSADVSQFVIISNQEERMKF 165
Cdd:cd08181 78 LARKEGADFVIGIGGGSPLDAAKAIALLAANKDGDEDlFQNGKYN--PPLPIVAIPTTAGTGSEVTPYSILTDHEKGTKK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 166 SIVSKAAVPDVSLIDPETTLSMDPFLSACTGIDALVHAIEAFVSTGHGPLTDPHALEAMRLINGNLVQMIANPADIALRE 245
Cdd:cd08181 156 SFGNPLIFPKLALLDPKYTLSLPEELTIDTAVDALSHAIEGYLSVKATPLSDALALEALRLIGECLPNLLGDELDEEDRE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 246 QIMLGSMQAGLAFSNAILGAVHAMSHSLGGYLDLPHGVCNAVLVEHVVAFNYDAAPDRYRIVAETLGIDSRGlshrqvre 325
Cdd:cd08181 236 KLMYASTLAGMVIAQTGTTLPHGLGYPLTYFKGIPHGRANGILLPAYLKLCEKQEPEKVDKILKLLGFGSIE-------- 307
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 515814333 326 rlvQHLIDLKQRIGFRETLSlhgvnLSDIPFLSQHAMQDPCILTNPRSSTQRDVEVVYA 384
Cdd:cd08181 308 ---EFQKFLNRLLGKKEELS-----EEELEKYADEAMKAKNKKNTPGNVTKEDILRIYR 358
|
|
| BDH |
cd08187 |
Butanol dehydrogenase catalyzes the conversion of butyraldehyde to butanol with the cofactor ... |
15-383 |
4.79e-66 |
|
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: 214.22 E-value: 4.79e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 15 EIIFGAGCRHSVGTCAGNFGaRKVLVVSDPG-VVKAGWVADVQASLARQGIEHCLFTDVSPNPRCEEVMLGAELYRSEGC 93
Cdd:cd08187 9 KIIFGKGAIEELGEEIKKYG-KKVLLVYGGGsIKKNGLYDRVVASLKEAGIEVVEFGGVEPNPRLETVREGIELAREENV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 94 NVIVAVGGGSPMDCAKGIGIVAAHGRHIYEFegVDTLRVPSP--PLILIPTTAGTSADVSQFVIISNQEERMKFSIVSKA 171
Cdd:cd08187 88 DFILAVGGGSVIDAAKAIAAGAKYDGDVWDF--FTGKAPPEKalPVGTVLTLAATGSEMNGGAVITNEETKEKLGFGSPL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 172 AVPDVSLIDPETTLSMDPFLSACTGIDALVHAIEA-FVSTGHGPLTDPHALEAMRLINGNLVQMIANPADIALREQIMLG 250
Cdd:cd08187 166 LRPKFSILDPELTYTLPKYQTAAGIVDIFSHVLEQyFTGTEDAPLQDRLAEGLLRTVIENGPKALKDPDDYEARANLMWA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 251 SMQAgLafsNAILG-------AVHAMSHSLGGYLDLPHGVCNAVLVEHVVAFNYDAAPDRYRIVAETL-GIDSrGLSHRQ 322
Cdd:cd08187 246 ATLA-L---NGLLGagrggdwATHAIEHELSALYDITHGAGLAIVFPAWMRYVLKKKPERFAQFARRVfGIDP-GGDDEE 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515814333 323 VRERLVQHLIDLKQRIGFRETLSLHGVNLSDIPFLSQHAMQDPCILTNPRSSTQRDVEVVY 383
Cdd:cd08187 321 TALEGIEALEEFFKSIGLPTTLSELGIDEEDIEEMAEKAVRGGGLGGGFKPLTREDIEEIL 381
|
|
| Fe-ADH-like |
cd08186 |
Iron-containing alcohol dehydrogenase; This family contains iron-containing alcohol ... |
18-365 |
5.81e-62 |
|
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: 203.65 E-value: 5.81e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 18 FGAGCRHSVGTCAGNFGARKVLVVSDPGVVKA-GWVADVQASLARQGIEHCLFTDVSPNPRCEEVMLGAELYRSEGCNVI 96
Cdd:cd08186 6 FGVGAIAKIKDILKDLGIDKVIIVTGRSSYKKsGAWDDVEKALEENGIEYVVYDKVTPNPTVDQADEAAKLARDFGADAV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 97 VAVGGGSPMDCAKGIGIVAAHG----RHIYEFEgvdtlRVP--SPPLILIPTTAGTSADVSQFVIISNQEERMKFSIVSK 170
Cdd:cd08186 86 IAIGGGSPIDTAKSVAVLLAYGgktaRDLYGFR-----FAPerALPLVAINLTHGTGSEVDRFAVATIPEKGYKPGIAYD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 171 AAVPDVSLIDPETTLSMDPFLSACTGIDALVHAIEAFVSTGHGPLTDPHALEAMRLINGNLVQMIANPADIALREQIMLG 250
Cdd:cd08186 161 CIYPLYAIDDPRLTLTLPKEQTLYTSIDAFNHVYEAATTKVSSPYVITLAKEAIRLIAEYLPRALANPKDLEARYWLLYA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 251 SMQAGLAFSNAILGAVHAMSHSLGGYL-DLPHGVCNAVLVEHVVAFNYDAAPDryrIVAETLG-IDSRGLSHRQVRERLV 328
Cdd:cd08186 241 SMIAGIAIDNGLLHLTHALEHPLSGLKpELPHGLGLALLGPAVVKYIYKAVPE---TLADILRpIVPGLKGTPDEAEKAA 317
|
330 340 350
....*....|....*....|....*....|....*..
gi 515814333 329 QHLIDLKQRIGFRETLSLHGVNLSDIPFLSQHAMQDP 365
Cdd:cd08186 318 RGVEEFLFSVGFTEKLSDYGFTEDDVDRLVELAFTTP 354
|
|
| Fe-ADH-like |
cd14864 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
13-380 |
3.78e-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: 341486 [Multi-domain] Cd Length: 376 Bit Score: 201.38 E-value: 3.78e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 13 SPEIIFGAGCRHSVGTCAGNFGARkVLVVSDPGVVKAGWVADVQASLARQGIEHCLFTDVSPNPRCEEVMLGAELYRSEG 92
Cdd:cd14864 4 PPNIVFGADSLERIGEEVKEYGSR-FLLITDPVLKESGLADKIVSSLEKAGISVIVFDEIPASATSDTIDEAAELARKAG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 93 CNVIVAVGGGSPMDCAKGIGIVAAHGRHIYEFEGVDTLRVPSPPLILIPTTAGTSADVSQFVIISNQEERMKFSIVSKAA 172
Cdd:cd14864 83 ADGIIAVGGGKVLDTAKAVAILANNDGGAYDFLEGAKPKKKPLPLIAVPTTPRSGFEFSDRFPVVDSRSREVKLLKAQPG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 173 VPDVSLIDPETTLSMDPFLSACTGIDALVHAIEAFVSTGHGPLTDPHALEAMRLINGNLVQMIANPADIALREQIMLGSM 252
Cdd:cd14864 163 LPKAVIVDPNLMASLTGNQTAAMALAALALAVEAYLSKKSNFFSDALALKAIELVSENLDGALADPKNTPAEELLAQAGC 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 253 QAGLAFSNAILGAVHAMSHSLGGYLDLPHGVCNAVLVEHVVAFNYDAAPDRYRIVAETLGIDSRGLSHRQVRERLVQHLI 332
Cdd:cd14864 243 LAGLAASSSSPGLATALALAVNSRYKVSKSLVASILLPHVIEYAATSAPDKYAKIARALGEDVEGASPEEAAIAAVEGVR 322
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 515814333 333 DLKQRIGFRETLSLHGVNlSDIPFLSQHAMQDPCILTNPRSSTQRDVE 380
Cdd:cd14864 323 RLIAQLNLPTRLKDLDLA-SSLEQLAAIAEDAPKLNGLPRSMSSDDIF 369
|
|
| PRK15454 |
PRK15454 |
ethanolamine utilization ethanol dehydrogenase EutG; |
12-386 |
1.85e-57 |
|
ethanolamine utilization ethanol dehydrogenase EutG;
Pssm-ID: 185351 [Multi-domain] Cd Length: 395 Bit Score: 192.55 E-value: 1.85e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 12 VSPEIIFGAGCRHSVGTCAGNFGARKVLVVSDPGVVKAGWVADVQASLARQGIEHCLFTDVSPNPRCEEVMLGAELYRSE 91
Cdd:PRK15454 26 VPPVTLCGPGAVSSCGQQAQTRGLKHLFVMADSFLHQAGMTAGLTRSLAVKGIAMTLWPCPVGEPCITDVCAAVAQLRES 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 92 GCNVIVAVGGGSPMDCAKGIGIVAAH-GRHIYEFEGVDTLRvPSPPLILIPTTAGTSADVSQFVIISNQEERMKFSIVSK 170
Cdd:PRK15454 106 GCDGVIAFGGGSVLDAAKAVALLVTNpDSTLAEMSETSVLQ-PRLPLIAIPTTAGTGSETTNVTVIIDAVSGRKQVLAHA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 171 AAVPDVSLIDPETTLSMDPFLSACTGIDALVHAIEAFVSTGHGPLTDPHALEAMRLINGNLVQMIANPADIALREQIMLG 250
Cdd:PRK15454 185 SLMPDVAILDAALTEGVPSHVTAMTGIDALTHAIEAYSALNATPFTDSLAIGAIAMIGKSLPKAVGYGHDLAARESMLLA 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 251 SMQAGLAFSNAILGAVHAMSHSLGGYLDLPHGVCNAVLVEHVVAFNYDAAPDRYRIVAetlgidsRGLSHRQVRER-LVQ 329
Cdd:PRK15454 265 SCMAGMAFSSAGLGLCHAMAHQPGAALHIPHGLANAMLLPTVMEFNRMVCRERFSQIG-------RALRTKKSDDRdAIN 337
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 515814333 330 HLIDLKQRIGFRETLSLHGVNLSDIPFLSQHAMQDPCILTNPRSSTQRDVEVVYAEA 386
Cdd:PRK15454 338 AVSELIAEVGIGKRLGDVGATSAHYGAWAQAALEDICLRSNPRTASLEQIVGLYAAA 394
|
|
| MAR-like |
cd08192 |
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic ... |
14-378 |
1.85e-54 |
|
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: 183.99 E-value: 1.85e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 14 PEIIFGAGCRHSVGTCAGNFGARKVLVVsdpgvvkagwvadVQASLARQG-----IEHCL-------FTDVSPN-PRcEE 80
Cdd:cd08192 2 ERVSYGPGAVEALLHELATLGASRVFIV-------------TSKSLATKTdvikrLEEALgdrhvgvFSGVRQHtPR-ED 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 81 VMLGAELYRSEGCNVIVAVGGGSPMDCAKGIGIVAAHgrHIYEFEGVDTLRV----------PSPPLILIPTT-AGtsAD 149
Cdd:cd08192 68 VLEAARAVREAGADLLVSLGGGSPIDAAKAVALALAE--DVTDVDQLDALEDgkridpnvtgPTLPHIAIPTTlSG--AE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 150 VSQFVIISNQEERMKFSIVSKAAVPDVSLIDPETTLSMDPFLSACTGIDALVHAIEAFVSTGHGPLTDPHALEAMRLING 229
Cdd:cd08192 144 FTAGAGATDDDTGHKQGFAHPELGPDAVILDPELTLHTPERLWLSTGIRAVDHAVETLCSPQATPFVDALALKALRLLFE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 230 NLVQMIANPADIALREQIMLGSMQAGLAF-SNAILGAVHAMSHSLGGYLDLPHGVCNAVLVEHVVAFNYDAAPDRYRIVA 308
Cdd:cd08192 224 GLPRSKADPEDLEARLKCQLAAWLSLFGLgSGVPMGASHAIGHQLGPLYGVPHGITSCIMLPAVLRFNAPVNAERQRLIA 303
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 309 ETLGIDSRGLSHRQvrERLVQHLIDLKQRIGFRETLSLHGVNLSDIPFLSQHAMQDPCILTNPRSSTQRD 378
Cdd:cd08192 304 RALGLVTGGLGREA--ADAADAIDALIRELGLPRTLRDVGVGRDQLEKIAENALTDVWCRTNPRPITDKD 371
|
|
| YqdH |
COG1979 |
Alcohol dehydrogenase YqhD, Fe-dependent ADH family [Energy production and conversion]; |
11-363 |
8.07e-50 |
|
Alcohol dehydrogenase YqhD, Fe-dependent ADH family [Energy production and conversion];
Pssm-ID: 441582 [Multi-domain] Cd Length: 387 Bit Score: 172.18 E-value: 8.07e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 11 FVSP-EIIFGAGCRHSVGTCAGNFGArKVLVVSDPG-VVKAGWVADVQASLARQGIEHCLFTDVSPNPRCEEVMLGAELY 88
Cdd:COG1979 6 FYNPtKIIFGKGQIAKLGEEIPKYGK-KVLLVYGGGsIKKNGLYDQVKAALKEAGIEVVEFGGVEPNPRLETVRKGVELC 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 89 RSEGCNVIVAVGGGSPMDCAKGIGIVAAhgrhiYEFEGVDTLRVPSP-----PLILIPTTAGTSADVSQFVIISNQEERM 163
Cdd:COG1979 85 KEEGIDFILAVGGGSVIDGAKAIAAGAK-----YDGDPWDILTGKAPvekalPLGTVLTLPATGSEMNSGSVITNEETKE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 164 KFSIVSKAAVPDVSLIDPETTLSMDPFLSACTGIDALVHAIEA-FVSTGHGPLTDPHAlEA-MR-LINgNLVQMIANPAD 240
Cdd:COG1979 160 KLGFGSPLVFPKFSILDPELTYTLPKRQTANGIVDIFSHVMEQyFTYPVDAPLQDRFA-EGlLRtLIE-EGPKALKDPED 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 241 IALREQIMLGSMQAgLafsNAILG-------AVHAMSHSLGGYLDLPHGVCNAVLVEHVVAFNYDAAPDRYRIVAETL-G 312
Cdd:COG1979 238 YDARANLMWAATLA-L---NGLIGagvpqdwATHMIEHELSALYDIDHGAGLAIVLPAWMRYVLEEKPEKFAQYAERVwG 313
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 515814333 313 IDsrGLSHRQVRERLVQHLIDLKQRIGFRETLSLHGVNLSDIPFLSQHAMQ 363
Cdd:COG1979 314 IT--EGDDEERALEGIEATEEFFESLGLPTRLSEYGIDEEDIEEMAEKATA 362
|
|
| MAR |
cd08177 |
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic ... |
13-379 |
1.49e-46 |
|
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: 162.29 E-value: 1.49e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 13 SPEIIFGAGCRHSVGTCAGNFGARKVLVVSDPGvvKAGWVADVQASLARQGIEHclFTDVSPN-PRcEEVMLGAELYRSE 91
Cdd:cd08177 1 PQRVVFGAGTLAELAEELERLGARRALVLSTPR--QRALAERVAALLGDRVAGV--FDGAVMHvPV-EVAERALAAAREA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 92 GCNVIVAVGGGSPMDCAKGIgivAAHGrhiyefeGVdtlrvpspPLILIPTT-AG---TSadvsqfvIISNQEERMKFSI 167
Cdd:cd08177 76 GADGLVAIGGGSAIGLAKAI---ALRT-------GL--------PIVAVPTTyAGsemTP-------IWGETEDGVKTTG 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 168 VSKAAVPDVSLIDPETTLSMDPFLSACTGIDALVHAIEAFVSTGHGPLTDPHALEAMRLINGNLVQMIANPADIALREQI 247
Cdd:cd08177 131 RDPRVLPRTVIYDPDLTLGLPAALSVASGLNALAHAVEALYAPDANPITSLLAEEGIRALARALPRLVADPSDLEARSDA 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 248 MLGSMQAGLAFSNAILGAVHAMSHSLGGYLDLPHGVCNAVLVEHVVAFNYDAAPDRYRIVAETLGidsrglshrqvRERL 327
Cdd:cd08177 211 LYGAWLAGVVLGSVGMGLHHKLCHVLGGTFDLPHAETHAVVLPHVLAYNAPAAPDAMARLARALG-----------GGDA 279
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 515814333 328 VQHLIDLKQRIGFRETLSLHGVNLSDIPFLSQHAMQDPciLTNPRSSTQRDV 379
Cdd:cd08177 280 AGGLYDLARRLGAPTSLRDLGMPEDDIDRAADLALANP--YPNPRPVERDAL 329
|
|
| Fe-ADH-like |
cd14866 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
13-378 |
3.01e-46 |
|
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: 162.79 E-value: 3.01e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 13 SPEIIFGAGCRHSVGTCAGNFGARKVLVVSDPGVVK-AGWVADVQASLARQ--GIehclFTDVSPNPRCEEVMLGAELYR 89
Cdd:cd14866 5 PLRLFSGRGALARLGRELDRLGARRALVVCGSSVGAnPDLMDPVRAALGDRlaGV----FDGVRPHSPLETVEAAAEALR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 90 SEGCNVIVAVGGGSPMDCAKGIGIVAAHGR-------HIYEFEGVDTLRVPSP--PLILIPTTAgTSADVSQFVIISNQE 160
Cdd:cd14866 81 EADADAVVAVGGGSAIVTARAASILLAEDRdvrelctRRAEDGLMVSPRLDAPklPIFVVPTTP-TTADVKAGSAVTDPP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 161 ERMKFSIVSKAAVPDVSLIDPETTLSMDPFLSACTGIDALVHAIEAFVSTGHGPLTDPHALEAMRLINGNLVQMiANPAD 240
Cdd:cd14866 160 AGQRLALFDPKTRPAAVFYDPELLATAPASLVAGAAMNGFDMAVEGLYSRHADPLADATLMHALRLLADGLPRL-ADDDD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 241 IALREQIMLGSMQAGLAFSNAILGAVHAMSHSLGGYLDLPHGVCNAVLVEHVVAFNYDAAPDRYRIVAETLGIDSRGlsH 320
Cdd:cd14866 239 PAARADLVLAAVLAGYGTDHTGGGVIHALGHAIGARYGVQNGVVHAILLPHVLRFNAPATDGRLDRLAEALGVADAG--D 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 515814333 321 RQVRERLVQHLIDLKQRIGFRETLSLHGVNLSDIPFLSQHAMQDPCILTNPRSSTQRD 378
Cdd:cd14866 317 EASAAAVVDAVEALLDALGVPTRLRDLGVSREDLPAIAEAAMDDWFMDNNPRPVPTAE 374
|
|
| 4HBD_NAD |
cd14860 |
4-hydroxybutyrate dehydrogenase, also called gamma-hydroxybutyrate dehydrogenase, catalyzes ... |
92-385 |
1.90e-37 |
|
4-hydroxybutyrate dehydrogenase, also called gamma-hydroxybutyrate dehydrogenase, catalyzes the reduction of succinic simialdehyde to 4-hydroxybutyrate in the succinic degradation pathway; 4-hydroxybutyrate dehydrogenase (4HBD) is an iron-containing (type III) NAD-dependent alcohol dehydrogenase. It plays a role in the succinate metabolism biochemical pathway. It catalyzes the reduction of succinic simialdehide to 4-hydroxybutyrate in the succinate degradation pathway This succinate degradation pathway is present in some bacteria which can use succinate as sole carbon source.
Pssm-ID: 341482 Cd Length: 371 Bit Score: 138.89 E-value: 1.90e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 92 GCNVIVAVGGGSPMDCAKgigIVA-AHGRHIYE-FEGVDTLRvPSPPLILIPTTAGTSADVSQFVIISNQEERMKFSIVS 169
Cdd:cd14860 78 GYKRVIAIGGGTVIDIAK---LLAlKGISPVLDlFDGKIPLI-KEKELIIVPTTCGTGSEVTNISIVELTSLGTKKGLAV 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 170 KAAVPDVSLIDPE--TTLSMDPFlsACTGIDALVHAIEAFVSTGHGPLTDPHALEAMRLINGNLVQMIANPAD--IALRE 245
Cdd:cd14860 154 DELYADKAVLIPEllKGLPYKVF--ATSSIDALIHAIESYLSPKATPYTEMFSYKAIEMILEGYQEIAEKGEEarFPLLG 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 246 QIMLGSMQAGLAFSNAILGAVHAMSHSLGGYLDLPHGVCNAVLVEHVVAFNYDAAPDRY-----RIVAETLGIDS----R 316
Cdd:cd14860 232 DFLIASNYAGIAFGNAGCAAVHALSYPLGGKYHVPHGEANYAVFTGVLKNYQEKNPDGEikklnEFLAKILGCDEedvyD 311
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515814333 317 GLshrqvrERLVQHLIDLKQrigfretLSLHGVNLSDIPFLSQHAM--QDPCILTNPRSSTQRDVEVVYAE 385
Cdd:cd14860 312 EL------EELLNKILPKKP-------LHEYGMKEEEIDEFADSVMenQQRLLANNYVPLDREDVAEIYKE 369
|
|
| DHQ_Fe-ADH |
cd07766 |
Dehydroquinate synthase-like (DHQ-like) and iron-containing alcohol dehydrogenases (Fe-ADH); ... |
16-361 |
5.69e-36 |
|
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: 132.49 E-value: 5.69e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 16 IIFGAGCRHSVGTCAGNFGARkVLVVSDPGVVKaGWVADVQASLARQGIEHcLFTDVSPNPRCEEVMLGAELYRSEGCNV 95
Cdd:cd07766 4 IVFGEGAIAKLGEIKRRGFDR-ALVVSDEGVVK-GVGEKVADSLKKGLAVA-IFDFVGENPTFEEVKNAVERARAAEADA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 96 IVAVGGGSPMDCAKGIGIvaahgrhiyefegvdtLRVPSPPLILIPTTAGTSADVSQFVIISnqEERMKFSIVSKAAVPD 175
Cdd:cd07766 81 VIAVGGGSTLDTAKAVAA----------------LLNRGIPFIIVPTTASTDSEVSPKSVIT--DKGGKNKQVGPHYNPD 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 176 VSLIDPETTLSMDPFLSACTGIDALVHAIEafvstghgpltdphaleamrlingnlvqmianpadialREQIMLGSMQAG 255
Cdd:cd07766 143 VVFVDTDITKGLPPRQVASGGVDALAHAVE--------------------------------------LEKVVEAATLAG 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 256 LAFSNA-ILGAVHAMSHSLGGYLDLPHGVCNAVLVEHVVAFNYDAAPDryrivaetlgidsrglshrqvRERLVQHLIDL 334
Cdd:cd07766 185 MGLFESpGLGLAHAIGHALTAFEGIPHGEAVAVGLPYVLKVANDMNPE---------------------PEAAIEAVFKF 243
|
330 340
....*....|....*....|....*..
gi 515814333 335 KQRIGFRETLSLHGVNLSDIPFLSQHA 361
Cdd:cd07766 244 LEDLGLPTHLADLGVSKEDIPKLAEKA 270
|
|
| Fe-ADH_KdnB-like |
cd08184 |
Iron-containing alcohol dehydrogenase similar to Shewanella oneidensis KdnB required for Kdo8N ... |
95-285 |
2.33e-24 |
|
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: 102.35 E-value: 2.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 95 VIVAVGGGSPMDCAKGIGIVAAHGRHIYEFEGVDTLRVPSPPLILIPTTAGTSADVSQFVIISNQEerMKFSIVSKAAVP 174
Cdd:cd08184 85 AVVGIGGGSTMDIAKAVSNMLTNPGSAADYQGWDLVKNPGIYKIGVPTLSGTGAEASRTAVLTGPE--KKLGINSDYTVF 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 175 DVSLIDPETTLSMDPFLSACTGIDALVHAIEAFVSTGHGPLTDPHALEAMRLINGNLVQMIANPADiaLREQIMLGSMQA 254
Cdd:cd08184 163 DQVILDPELIATVPRDQYFYTGMDCYIHCVESLNGTYRNAFGDAYAEKALELCRDVFLSDDMMSPE--NREKLMVASYLG 240
|
170 180 190
....*....|....*....|....*....|.
gi 515814333 255 GLAFSNAILGAVHAMSHSLGGYLDLPHGVCN 285
Cdd:cd08184 241 GSSIANSQVGVCHALSYGLSVVLGTHHGVAN 271
|
|
| GldA |
COG0371 |
Glycerol dehydrogenase or related enzyme, iron-containing ADH family [Energy production and ... |
9-273 |
1.19e-14 |
|
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: 74.43 E-value: 1.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 9 RKFVSP-EIIFGAGCRHSVGTCAGNFGaRKVLVVSDPGVVKAgWVADVQASLARQGIEHCLFTdVSPNPRCEEVMLGAEL 87
Cdd:COG0371 1 RVIILPrRYVQGEGALDELGEYLADLG-KRALIITGPTALKA-AGDRLEESLEDAGIEVEVEV-FGGECSEEEIERLAEE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 88 YRSEGCNVIVAVGGGSPMDCAKgigiVAAHGRHIyefegvdtlrvpspPLILIPTTAGTSADVSQF-VIISNQEERMKFS 166
Cdd:COG0371 78 AKEQGADVIIGVGGGKALDTAK----AVAYRLGL--------------PVVSVPTIASTDAPASPLsVIYTEDGAFDGYS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 167 IVSKAavPDVSLIDPETTLSMDP-FLSActGI-DALVHAIEA-FVSTGHGPLTDPHALEAMRlingNLVQMIANP----A 239
Cdd:COG0371 140 FLAKN--PDLVLVDTDIIAKAPVrLLAA--GIgDALAKWYEArDWSLAHRDLAGEYYTEAAV----ALARLCAETlleyG 211
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 515814333 240 DIALR---------------EQIMLGSmqaGLAF----SNAILGAVHAMSHSL 273
Cdd:COG0371 212 EAAIKaveagvvtpalervvEANLLLS---GLAMgigsSRPGSGAAHAIHNGL 261
|
|
| Fe-ADH_2 |
pfam13685 |
Iron-containing alcohol dehydrogenase; |
34-273 |
1.36e-14 |
|
Iron-containing alcohol dehydrogenase;
Pssm-ID: 404557 [Multi-domain] Cd Length: 251 Bit Score: 72.72 E-value: 1.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 34 GARKVLVVSDPGVVKAGwVADVQASLARQGIEHCLFTDVSPNPRCEEVMLGAELYRSEGCNVIVAVGGGSPMDCAKgigi 113
Cdd:pfam13685 18 GFRRVALVADANTYAAA-GRKVAESLKRAGIEVETRLEVAGNADMETAEKLVGALRERDADAVVGVGGGTVIDLAK---- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 114 VAAHGRHIyefegvdtlrvpspPLILIPTTAG----TSADVSqfvIISNQEermKFSIvsKAAVPDVSLIDPETTLSMDP 189
Cdd:pfam13685 93 YAAFKLGK--------------PFISVPTAASndgfASPGAS---LTVDGK---KRSI--PAAAPFGVIADTDVIAAAPR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 190 FLSAcTGIDALVHAIEAFV---STGHGPLTDPHALEAMRLINGNLVQMIANPADIALREQIMLGSMQAGLAFSNAILGAV 266
Cdd:pfam13685 151 RLLA-SGVGDLLAKITAVAdweLAHAEEVAAPLALLSAAMVMNFADRPLRDPGDIEALAELLSALAMGGAGSSRPASGSE 229
|
....*..
gi 515814333 267 HAMSHSL 273
Cdd:pfam13685 230 HLISHAL 236
|
|
| PRK15138 |
PRK15138 |
alcohol dehydrogenase; |
37-289 |
3.51e-12 |
|
alcohol dehydrogenase;
Pssm-ID: 185092 [Multi-domain] Cd Length: 387 Bit Score: 67.13 E-value: 3.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 37 KVLVVSDPGVVKAGWVADvQASLARQGIEHCLFTDVSPNPRCEEVMLGAELYRSEGCNVIVAVGGGSPMDCAKGIGIVAA 116
Cdd:PRK15138 31 RVLITYGGGSVKKTGVLD-QVLDALKGMDVLEFGGIEPNPTYETLMKAVKLVREEKITFLLAVGGGSVLDGTKFIAAAAN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 117 HGR-----HIYEFEGVDTLRvpSPPLILIPTTAGTSADVSQFVIISNQEERMKFSIVSKAAVPDVSLIDPETTLSMDPFL 191
Cdd:PRK15138 110 YPEnidpwHILETGGKEIKS--AIPMGSVLTLPATGSESNAGAVISRKTTGDKQAFHSPHVQPVFAVLDPVYTYTLPPRQ 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 192 SACTGIDALVHAIEAFVSTG-HGPLTDphaleamRLINGNLVQMI-------ANPADIALREQIMLGSMQAglafSNAIL 263
Cdd:PRK15138 188 VANGVVDAFVHTVEQYVTYPvDAKIQD-------RFAEGILLTLIeegpkalKEPENYDVRANVMWAATQA----LNGLI 256
|
250 260 270
....*....|....*....|....*....|...
gi 515814333 264 GA-------VHAMSHSLGGYLDLPHGVCNAVLV 289
Cdd:PRK15138 257 GAgvpqdwaTHMLGHELTAMHGLDHAQTLAIVL 289
|
|
| GlyDH-like |
cd08550 |
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins. ... |
19-214 |
5.71e-10 |
|
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: 60.24 E-value: 5.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 19 GAGCRHSVGTCAGNFGaRKVLVVSDPGVVKAgWVADVQASLARQGI--EHCLFT-DVSPnprcEEVMLGAELYRSEGCNV 95
Cdd:cd08550 7 EPGILAKAGEYIAPLG-KKALIIGGKTALEA-VGEKLEKSLEEAGIdyEVEVFGgECTE----ENIERLAEKAKEEGADV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 96 IVAVGGGSPMDCAKgigiVAAHGRHIyefegvdtlrvpspPLILIPTTAGTSADVSQFVIISNQEERMKFSIVSKAAvPD 175
Cdd:cd08550 81 IIGIGGGKVLDTAK----AVADRLGL--------------PVVTVPTIAATCAAWSALSVLYDEEGEFLGYSLLKRS-PD 141
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 515814333 176 VSLIDPETTLSMDP-FLSActGI-DALVHAIEAFVSTGHGP 214
Cdd:cd08550 142 LVLVDTDIIAAAPVrYLAA--GIgDTLAKWYEARPSSRGGP 180
|
|
| GlyDH |
cd08170 |
Glycerol dehydrogenases (GlyDH) catalyzes oxidation of glycerol to dihydroxyacetone in ... |
19-151 |
2.81e-09 |
|
Glycerol dehydrogenases (GlyDH) catalyzes oxidation of glycerol to dihydroxyacetone in glycerol dissmilation; Glycerol dehydrogenases (GlyDH) is a key enzyme in the glycerol dissimilation pathway. In anaerobic conditions, many microorganisms utilize glycerol as a source of carbon through coupled oxidative and reductive pathways. One of the pathways involves the oxidation of glycerol to dihydroxyacetone with the reduction of NAD+ to NADH catalyzed by glycerol dehydrogenases. Dihydroxyacetone is then phosphorylated by dihydroxyacetone kinase and enters the glycolytic pathway for further degradation. The activity of GlyDH is zinc-dependent; the zinc ion plays a role in stabilizing an alkoxide intermediate at the active site.
Pssm-ID: 341449 [Multi-domain] Cd Length: 351 Bit Score: 58.19 E-value: 2.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 19 GAGCRHSVGTCAGNFGaRKVLVVSDPGVVKAgwVAD-VQASLARQGIEHCL--FT-DVSPnprcEEVMLGAELYRSEGCN 94
Cdd:cd08170 7 GPGALDRLGEYLAPLG-KKALVIADPFVLDL--VGErLEESLEKAGLEVVFevFGgECSR----EEIERLAAIARANGAD 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 515814333 95 VIVAVGGGSPMDCAKGIgivaAHGRHIyefegvdtlrvpspPLILIPTTAGTSADVS 151
Cdd:cd08170 80 VVIGIGGGKTIDTAKAV----ADYLGL--------------PVVIVPTIASTDAPCS 118
|
|
| gldA |
PRK09423 |
glycerol dehydrogenase; Provisional |
9-156 |
1.14e-05 |
|
glycerol dehydrogenase; Provisional
Pssm-ID: 181843 Cd Length: 366 Bit Score: 47.12 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 9 RKFVSP-EIIFGAGCRHSVGTCAGNFGaRKVLVVSDPGVVKAGWvADVQASLARQGIEhclFTDVSPNPRC--EEVMLGA 85
Cdd:PRK09423 3 RIFISPsKYVQGKGALARLGEYLKPLG-KRALVIADEFVLGIVG-DRVEASLKEAGLT---VVFEVFNGECsdNEIDRLV 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515814333 86 ELYRSEGCNVIVAVGGGSPMDCAKGIGivaahgrhiyEFEGVdtlrvpspPLILIPTTAGTSADVSQFVII 156
Cdd:PRK09423 78 AIAEENGCDVVIGIGGGKTLDTAKAVA----------DYLGV--------PVVIVPTIASTDAPTSALSVI 130
|
|
| GlyDH-like |
cd08172 |
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins ... |
85-182 |
3.53e-05 |
|
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: 45.20 E-value: 3.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 85 AELYRSEGCNVIVAVGGGSPMDCAKGigivAAHGRHIyefegvdtlrvpspPLILIPTTAGTSADVSQFVIISNQEERMK 164
Cdd:cd08172 68 AEEAKEHQADVIIGIGGGKVLDTAKA----VADKLNI--------------PLILIPTLASNCAAWTPLSVIYDEDGEFI 129
|
90
....*....|....*....
gi 515814333 165 -FSIVSKAAvpDVSLIDPE 182
Cdd:cd08172 130 gYDYFPRSA--YLVLVDPR 146
|
|
| DHQS |
cd08195 |
Dehydroquinate synthase (DHQS) catalyzes the conversion of DAHP to DHQ in shikimate pathway ... |
15-143 |
1.50e-04 |
|
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: 43.20 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 15 EIIFGAGCRHSVGTCAGNFGARKVLVVSDPGVVKAgWVADVQASLARQGIEHCLFTdVSPN---------PRCEEVMLGA 85
Cdd:cd08195 3 PILIGSGLLDKLGELLELKKGSKVVIVTDENVAKL-YGELLLKSLEAAGFKVEVIV-IPAGeksksletvERIYDFLLEA 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 515814333 86 ELYRSegcNVIVAVGGGSPMDCAkgiGIVAAhgrhIYefegvdtLR-VpspPLILIPTT 143
Cdd:cd08195 81 GLDRD---SLLIALGGGVVGDLA---GFVAS----TY-------MRgI---PFIQVPTT 119
|
|
| Gro1PDH |
cd08173 |
Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) catalyzes the reversible conversion between ... |
15-179 |
8.87e-04 |
|
Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) catalyzes the reversible conversion between dihydroxyacetone phosphate and glycerol-1-phosphate using either NADH or NADPH as a coenzyme; Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH, EC 1.1.1.261) plays an important role in the formation of the enantiomeric configuration of the glycerophosphate backbone (sn-glycerol-1-phosphate) of archaeal ether lipids. It catalyzes the reversible conversion between dihydroxyacetone phosphate and glycerol-1-phosphate using either NADH or NADPH as a coenzyme. The activity is zinc-dependent. One characteristic feature of archaea is that their cellular membrane has an ether linkage between the glycerol backbone and the hydrocarbon residues. The polar lipids of the members of Archaea consist of di- and tetra-ethers of glycerol with isoprenoid alcohols bound at the sn-2 and sn-3 positions of the glycerol moiety. The archaeal polar lipids have the enantiomeric configuration of a glycerophosphate backbone [sn-glycerol-1-phosphate (G-1-P)] that is the mirror image structure of the bacterial or eukaryal counterpart [sn-glycerol- 3-phosphate (G-3-P)]. The absolute stereochemistry of the glycerol moiety in all archaeal polar lipids is opposite to that of glycerol ester lipids in bacteria and eukarya.
Pssm-ID: 341452 Cd Length: 343 Bit Score: 41.00 E-value: 8.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 15 EIIFGAGCRHSVGT-CAGNFGARKVLVVSDPGVVK-AGwvADVQASLARQGIEHCL--FTDVSPNPRCEEVmlgAELYRS 90
Cdd:cd08173 4 NVVVGHGAINKIGEvLKKLLLGKRALIITGPNTYKiAG--KRVEDLLESSGVEVVIvdIATIEEAAEVEKV---KKLIKE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 91 EGCNVIVAVGGGSPMDCAKgigiVAAHGRHIyefegvdtlrvpspPLILIPTTAGTSADVSQFVIISNQEERMKFSIVSK 170
Cdd:cd08173 79 SKADFIIGVGGGKVIDVAK----YAAYKLNL--------------PFISIPTSASHDGIASPFASIKGGDKPYSIKAKAP 140
|
170
....*....|
gi 515814333 171 AAV-PDVSLI 179
Cdd:cd08173 141 IAIiADTEII 150
|
|
| G1PDH-like |
cd08174 |
Glycerol-1-phosphate dehydrogenase-like; These glycerol-1-phosphate dehydrogenase-like ... |
32-180 |
3.53e-03 |
|
Glycerol-1-phosphate dehydrogenase-like; These glycerol-1-phosphate dehydrogenase-like proteins have not been characterized. The protein sequences have high similarity with that of glycerol-1-phosphate dehydrogenase (G1PDH) which plays a role in the synthesis of phosphoglycerolipids in Gram-positive bacterial species. It catalyzes the reversibly reduction of dihydroxyacetone phosphate (DHAP) to glycerol-1-phosphate (G1P) in a NADH-dependent manner. Its activity requires Ni++ ion.
Pssm-ID: 341453 [Multi-domain] Cd Length: 332 Bit Score: 39.04 E-value: 3.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 32 NFGARKVLVVSDPGVvKAGWVADVQASLARQGiEHCLFTDVSPNprcEEVMLGAELYRSEGCNVIVAVGGGSPMDCAKgi 111
Cdd:cd08174 22 NQGFGKVAIVTGEGI-DELLGEDILESLEEAG-EIVTVEENTDN---SAEELAEKAFSLPKVDAIVGIGGGKVLDVAK-- 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515814333 112 giVAAHGRHIyefegvdtlrvpspPLILIPTTagTSAD--VSQFVIISNQEERMKFsivsKAAVPDVSLID 180
Cdd:cd08174 95 --YAAFLSKL--------------PFISVPTS--LSNDgiASPVAVLKVDGKRKSL----GAKMPYGVIVD 143
|
|
| G1PDH |
cd08175 |
Glycerol-1-phosphate dehydrogenase (G1PDH) catalyzes the reversible reduction of ... |
15-109 |
6.88e-03 |
|
Glycerol-1-phosphate dehydrogenase (G1PDH) catalyzes the reversible reduction of dihydroxyacetone phosphate (DHAP) to glycerol-1-phosphate (G1P) in an NADH-dependent manner; Glycerol-1-phosphate dehydrogenase (G1PDH) plays a role in the synthesis of phosphoglycerolipids in Gram-positive bacterial species. It catalyzes the reversibly reduction of dihydroxyacetone phosphate (DHAP) to glycerol-1-phosphate (G1P) in a NADH-dependent manner. Its activity requires a Ni++ ion. In Bacillus subtilis, it has been described as AraM gene in L-arabinose (ara) operon. AraM protein forms homodimer.
Pssm-ID: 341454 Cd Length: 340 Bit Score: 38.26 E-value: 6.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515814333 15 EIIFGAGCRHSVG-TCAGNFGARKVLVVSDPGVVK-AGwvADVQASLARQGIEHCLFT-DVSPNPRCEEVMLGAELYRSE 91
Cdd:cd08175 3 EIVIGEGALKKLPeYLKELFGGKKVLVVADENTYAaAG--EEVEAALEEAGVTVCLLIfPGEGDLIADEAAVGKVLLELE 80
|
90
....*....|....*....
gi 515814333 92 GCN-VIVAVGGGSPMDCAK 109
Cdd:cd08175 81 KDTdLIIAVGSGTINDLTK 99
|
|
| |
