|
Name |
Accession |
Description |
Interval |
E-value |
| YqdH |
COG1979 |
Alcohol dehydrogenase YqhD, Fe-dependent ADH family [Energy production and conversion]; |
1-390 |
0e+00 |
|
Alcohol dehydrogenase YqhD, Fe-dependent ADH family [Energy production and conversion];
Pssm-ID: 441582 [Multi-domain] Cd Length: 387 Bit Score: 688.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 1 MENFTYYNPTKLIFGKGQIDQLKKELKQYGKNVLLVYGGGSIKRNGLYDQVTGILKEEGATVHELAGVEPNPRLEMVNKG 80
Cdd:COG1979 1 MNNFTFYNPTKIIFGKGQIAKLGEEIPKYGKKVLLVYGGGSIKKNGLYDQVKAALKEAGIEVVEFGGVEPNPRLETVRKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 81 IELCRQHEIDFLLAVGGGSVIDCTKAIAAGAKYDGDAWDIYSKKVTAQDALPFGTVLTLAATGSEMNPDSVITNWETNEK 160
Cdd:COG1979 81 VELCKEEGIDFILAVGGGSVIDGAKAIAAGAKYDGDPWDILTGKAPVEKALPLGTVLTLPATGSEMNSGSVITNEETKEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 161 FVWGSNVTHPRFSILDPENTFSVPENQTVYGMVDMMSHVFEQYFHNVENTPLQDRMCFAVLQTVIETAPKLLEDLENYKH 240
Cdd:COG1979 161 LGFGSPLVFPKFSILDPELTYTLPKRQTANGIVDIFSHVMEQYFTYPVDAPLQDRFAEGLLRTLIEEGPKALKDPEDYDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 241 RETILYAGTIALNGTLQMGYFGDWASHTMEHAVSAVYDIPHAGGLAILFPNWMRYTLDTNVDRFKNLMLNMFDIDteGKT 320
Cdd:COG1979 241 RANLMWAATLALNGLIGAGVPQDWATHMIEHELSALYDIDHGAGLAIVLPAWMRYVLEEKPEKFAQYAERVWGIT--EGD 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 321 DKEIALEGIDKLSAFWTSLGAPSRLADYDIGEDKLELIADiAAKEMEYGGFGNFQKLNKDDVLAILKASL 390
Cdd:COG1979 319 DEERALEGIEATEEFFESLGLPTRLSEYGIDEEDIEEMAE-KATAHGMTALGEFKDLTPEDVREILELAL 387
|
|
| BDH |
cd08187 |
Butanol dehydrogenase catalyzes the conversion of butyraldehyde to butanol with the cofactor ... |
3-387 |
0e+00 |
|
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: 617.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 3 NFTYYNPTKLIFGKGQIDQLKKELKQYGKNVLLVYGGGSIKRNGLYDQVTGILKEEGATVHELAGVEPNPRLEMVNKGIE 82
Cdd:cd08187 1 NFTFYNPTKIIFGKGAIEELGEEIKKYGKKVLLVYGGGSIKKNGLYDRVVASLKEAGIEVVEFGGVEPNPRLETVREGIE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 83 LCRQHEIDFLLAVGGGSVIDCTKAIAAGAKYDGDAWDIYSKKVTAQDALPFGTVLTLAATGSEMNPDSVITNWETNEKFV 162
Cdd:cd08187 81 LAREENVDFILAVGGGSVIDAAKAIAAGAKYDGDVWDFFTGKAPPEKALPVGTVLTLAATGSEMNGGAVITNEETKEKLG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 163 WGSNVTHPRFSILDPENTFSVPENQTVYGMVDMMSHVFEQYFHNVENTPLQDRMCFAVLQTVIETAPKLLEDLENYKHRE 242
Cdd:cd08187 161 FGSPLLRPKFSILDPELTYTLPKYQTAAGIVDIFSHVLEQYFTGTEDAPLQDRLAEGLLRTVIENGPKALKDPDDYEARA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 243 TILYAGTIALNGTLQMGYFGDWASHTMEHAVSAVYDIPHAGGLAILFPNWMRYTLDTNVDRFKNLMLNMFDIDtEGKTDK 322
Cdd:cd08187 241 NLMWAATLALNGLLGAGRGGDWATHAIEHELSALYDITHGAGLAIVFPAWMRYVLKKKPERFAQFARRVFGID-PGGDDE 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2256122564 323 EIALEGIDKLSAFWTSLGAPSRLADYDIGEDKLELIADIAAKemEYGGFGNFQKLNKDDVLAILK 387
Cdd:cd08187 320 ETALEGIEALEEFFKSIGLPTTLSELGIDEEDIEEMAEKAVR--GGGLGGGFKPLTREDIEEILK 382
|
|
| Fe-ADH |
pfam00465 |
Iron-containing alcohol dehydrogenase; |
9-382 |
4.48e-125 |
|
Iron-containing alcohol dehydrogenase;
Pssm-ID: 425696 [Multi-domain] Cd Length: 362 Bit Score: 365.00 E-value: 4.48e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 9 PTKLIFGKGQIDQLKKELKQYGKNVLLVYGGGSIKrNGLYDQVTGILKEEGATVHELAGVEPNPRLEMVNKGIELCRQHE 88
Cdd:pfam00465 1 PTRIVFGAGALAELGEELKRLGARALIVTDPGSLK-SGLLDKVLASLEEAGIEVVVFDGVEPEPTLEEVDEAAALAREAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 89 IDFLLAVGGGSVIDCTKAIAAGAKYDGDAWDIYSKKVTAQDALPFGTVLTLAATGSEMNPDSVITNWETNEKFVWGSNVT 168
Cdd:pfam00465 80 ADVIIAVGGGSVIDTAKAIALLLTNPGDVWDYLGGKPLTKPALPLIAIPTTAGTGSEVTPLAVITDTETGEKLGIFSPKL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 169 HPRFSILDPENTFSVPENQTVYGMVDMMSHVFEQYFhNVENTPLQDRMCFAVLQTVIETAPKLLEDLENYKHRETILYAG 248
Cdd:pfam00465 160 LPDLAILDPELTLTLPPRLTAATGMDALAHAVEAYV-SKGANPLTDALALEAIRLIAENLPRAVADGEDLEARENMLLAS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 249 TIALNGtlqMGYFGDWASHTMEHAVSAVYDIPHAGGLAILFPNWMRYTLDTNVDRFKNLMLNMFdidteGKTDKEIALEG 328
Cdd:pfam00465 239 TLAGLA---FSNAGLGAAHALAHALGGRYGIPHGLANAILLPYVLRFNAPAAPEKLAQLARALG-----EDSDEEAAEEA 310
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 2256122564 329 IDKLSAFWTSLGAPSRLADYDIGEDKLELIADIAAKEMEYGgfGNFQKLNKDDV 382
Cdd:pfam00465 311 IEALRELLRELGLPTTLSELGVTEEDLDALAEAALRDRSLA--NNPRPLTAEDI 362
|
|
| Fe-ADH-like |
cd08185 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
6-387 |
1.78e-103 |
|
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: 310.58 E-value: 1.78e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 6 YYNPTKLIFGKGQIDQLKKELKQYGKNVLLVYGGGSIKRNGLYDQVTGILKEEGATVHELAGVEPNPRLEMVNKGIELCR 85
Cdd:cd08185 1 YYQPTRILFGAGKLNELGEEALRPGKKALIVTGKGSSKKTGLLDRVKKLLEKAGVEVVVFDKVEPNPLTTTVMEGAALAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 86 QHEIDFLLAVGGGSVIDCTKAIAAGAKYDGDAWDI----YSKKVTAQDALPFGTVLTLAATGSEMNPDSVITNWETNEKF 161
Cdd:cd08185 81 EEGCDFVIGLGGGSSMDAAKAIAFMATNPGDIWDYifggTGKGPPPEKALPIIAIPTTAGTGSEVDPWAVITNPETKEKK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 162 VWGSNVTHPRFSILDPENTFSVPENQTVY-GMvDMMSHVFEQYFHNVENtPLQDRMCFAVLQTVIETAPKLLEDLENYKH 240
Cdd:cd08185 161 GIGHPALFPKVSIVDPELMLTVPPRVTAYtGF-DALFHAFESYISKNAN-PFSDMLALEAIRLVAKYLPRAVKDGSDLEA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 241 RETILYAGT-----IALNGTLqmgyfgdwASHTMEHAVSAVY-DIPHAGGLAILFPNWMRYTLDTNVDRFKNLMLnmfdI 314
Cdd:cd08185 239 REKMAWASTlagivIANSGTT--------LPHGLEHPLSGYHpNIPHGAGLAALYPAYFEFTIEKAPEKFAFVAR----A 306
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2256122564 315 DTEGKTDKEIALEGIDKLSAFWTSLGAPSRLADYDIGEDKLELIADIAAKEMEYGGFGNFQKLNKDDVLAILK 387
Cdd:cd08185 307 EASGLSDAKAAEDFIEALRKLLKDIGLDDLLSDLGVTEEDIPWLAENAMETMGGLFANNPVELTEEDIVEIYE 379
|
|
| PRK15138 |
PRK15138 |
alcohol dehydrogenase; |
1-369 |
1.09e-98 |
|
alcohol dehydrogenase;
Pssm-ID: 185092 [Multi-domain] Cd Length: 387 Bit Score: 298.63 E-value: 1.09e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 1 MENFTYYNPTKLIFGKGQIDQLKKELKQyGKNVLLVYGGGSIKRNGLYDQVTGILKeeGATVHELAGVEPNPRLEMVNKG 80
Cdd:PRK15138 1 MNNFNLHTPTRILFGKGAIAGLREQIPA-DARVLITYGGGSVKKTGVLDQVLDALK--GMDVLEFGGIEPNPTYETLMKA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 81 IELCRQHEIDFLLAVGGGSVIDCTKAIAAGAKYDG--DAWDI---YSKKVTAqdALPFGTVLTLAATGSEMNPDSVITNW 155
Cdd:PRK15138 78 VKLVREEKITFLLAVGGGSVLDGTKFIAAAANYPEniDPWHIletGGKEIKS--AIPMGSVLTLPATGSESNAGAVISRK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 156 ETNEKFVWGSNVTHPRFSILDPENTFSVPENQTVYGMVDMMSHVFEQYFHNVENTPLQDRMCFAVLQTVIETAPKLLEDL 235
Cdd:PRK15138 156 TTGDKQAFHSPHVQPVFAVLDPVYTYTLPPRQVANGVVDAFVHTVEQYVTYPVDAKIQDRFAEGILLTLIEEGPKALKEP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 236 ENYKHRETILYAGTIALNGTLQMGYFGDWASHTMEHAVSAVYDIPHAGGLAILFPNWMRYTLDTNVDRFKNLMLNMFDId 315
Cdd:PRK15138 236 ENYDVRANVMWAATQALNGLIGAGVPQDWATHMLGHELTAMHGLDHAQTLAIVLPALWNEKRDTKRAKLLQYAERVWNI- 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 2256122564 316 TEGKTDKEIAlEGIDKLSAFWTSLGAPSRLADYDIGEDKlelIADIAAKEMEYG 369
Cdd:PRK15138 315 TEGSDDERID-AAIAATRNFFEQMGVPTRLSDYGLDGSS---IPALLKKLEEHG 364
|
|
| EutG |
COG1454 |
Alcohol dehydrogenase, class IV [Energy production and conversion]; |
4-390 |
5.52e-91 |
|
Alcohol dehydrogenase, class IV [Energy production and conversion];
Pssm-ID: 441063 [Multi-domain] Cd Length: 381 Bit Score: 278.54 E-value: 5.52e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 4 FTYYNPTKLIFGKGQIDQLKKELKQYG-KNVLLVyGGGSIKRNGLYDQVTGILKEEGATVHELAGVEPNPRLEMVNKGIE 82
Cdd:COG1454 3 FTFRLPTRIVFGAGALAELGEELKRLGaKRALIV-TDPGLAKLGLLDRVLDALEAAGIEVVVFDDVEPNPTVETVEAGAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 83 LCRQHEIDFLLAVGGGSVIDCTKAIAAGAKYDGDAWDIYSKKVTAQDALPFGTVLTLAATGSEMNPDSVITNWETNEKFV 162
Cdd:COG1454 82 AAREFGADVVIALGGGSAIDAAKAIALLATNPGDLEDYLGIKKVPGPPLPLIAIPTTAGTGSEVTPFAVITDPETGVKKG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 163 WGSNVTHPRFSILDPENTFSVPENQTVY-GMvDMMSHVFEQYFhNVENTPLQDRMCFAVLQTVIETAPKLLEDLENYKHR 241
Cdd:COG1454 162 IADPELLPDVAILDPELTLTLPPSLTAAtGM-DALTHAIEAYV-SKGANPLTDALALEAIRLIARNLPRAVADGDDLEAR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 242 ETILYAGTIAlnGT-LQMGYFGdwASHTMEHAVSAVYDIPHAGGLAILFPNWMRYTLDTNVDRFKNLmLNMFDIDTeGKT 320
Cdd:COG1454 240 EKMALASLLA--GMaFANAGLG--AVHALAHPLGGLFHVPHGLANAILLPHVLRFNAPAAPERYAEI-ARALGLDV-GLS 313
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2256122564 321 DKEIALEGIDKLSAFWTSLGAPSRLADYDIGEDKLELIADIAakeMEYGGFG-NFQKLNKDDVLAILKASL 390
Cdd:COG1454 314 DEEAAEALIEAIRELLRDLGIPTRLSELGVTEEDLPELAELA---LADRCLAnNPRPLTEEDIEAILRAAY 381
|
|
| Fe-ADH |
cd08551 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains large ... |
9-386 |
2.57e-87 |
|
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: 268.93 E-value: 2.57e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 9 PTKLIFGKGQIDQLKKELKQYG-KNVLLVYGGGsIKRNGLYDQVTGILKEEGATVHELAGVEPNPRLEMVNKGIELCRQH 87
Cdd:cd08551 1 PTRIVFGAGALARLGEELKALGgKKVLLVTDPG-LVKAGLLDKVLESLKAAGIEVEVFDDVEPNPTVETVEAAAELAREE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 88 EIDFLLAVGGGSVIDCTKAIAAGAKYDGDAWDIYSKKVTAQDALPFGTVLTLAATGSEMNPDSVITNWETNEKFVWGSNV 167
Cdd:cd08551 80 GADLVIAVGGGSVLDTAKAIAVLATNGGSIRDYEGIGKVPKPGLPLIAIPTTAGTGSEVTPNAVITDPETGRKMGIVSPY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 168 THPRFSILDPENTFSVPENQTVY-GMvDMMSHVFEQYFhNVENTPLQDRMCFAVLQTVIETAPKLLEDLENYKHRETILY 246
Cdd:cd08551 160 LLPDVAILDPELTLSLPPSVTAAtGM-DALTHAIEAYT-SKKANPISDALALEAIRLIGKNLRRAVADGSDLEAREAMLL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 247 AGT---IALNGTlqmgyfGDWASHTMEHAVSAVYDIPHAGGLAILFPNWMRYTLDTNVDRFKNlMLNMFDIDTEGKTDKE 323
Cdd:cd08551 238 ASLlagIAFGNA------GLGAVHALAYPLGGRYHIPHGVANAILLPYVMEFNLPACPEKYAE-IAEALGEDVEGLSDEE 310
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2256122564 324 IALEGIDKLSAFWTSLGAPSRLADYDIGEDKLELIADIAAKEMeYGGFGNFQKLNKDDVLAIL 386
Cdd:cd08551 311 AAEAAVEAVRELLRDLGIPTSLSELGVTEEDIPELAEDAMKSG-RLLSNNPRPLTEEDIREIY 372
|
|
| Fe-ADH-like |
cd14863 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
5-388 |
6.83e-76 |
|
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: 239.74 E-value: 6.83e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 5 TYYNPTKLIFGKGQIDQLKKELKQYG-KNVLLVYGGGsIKRNGLYDQVTGILKEEGATVHELAGVEPNPRLEMVNKGIEL 83
Cdd:cd14863 1 TYSQLTPVIFGAGAVEQIGELLKELGcKKVLLVTDKG-LKKAGIVDKIIDLLEEAGIEVVVFDDVEPDPPDEIVDEAAEI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 84 CRQHEIDFLLAVGGGSVIDCTKAIAAGAKYDGDAWDIYSKKVTAQD-ALPFGTVLTLAATGSEMNPDSVITNWETNEKFV 162
Cdd:cd14863 80 AREEGADGVIGIGGGSVLDTAKAIAVLLTNPGPIIDYALAGPPVPKpGIPLIAIPTTAGTGSEVTPIAVITDEENGVKKS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 163 WGSNVTHPRFSILDPENTFSVPENQTVY-GMvDMMSHVFEQYFHNvENTPLQDRMCFAVLQTVIETAPKLLEDLENYKHR 241
Cdd:cd14863 160 LLGPFLVPDLAILDPELTVGLPPSLTAAtGM-DALSHAIEAYTSK-LANPMTDALALQAIRLIVKNLPRAVKDGDNLEAR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 242 ETILYAGTIALNGtlqMGYFGDWASHTMEHAVSAVYDIPHAGGLAILFPNWMRYTLDTNVDRFKNLMLnMFDIDTEGKTD 321
Cdd:cd14863 238 ENMLLASNLAGIA---FNNAGTHIGHAIAHALGALYHIPHGLACALALPVVLEFNAEAYPEKVKKIAK-ALGVSFPGESD 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2256122564 322 KEIALEGIDKLSAFWTSLGAPSRLADYDIGEDKLELIADIAAKEMeyGGFGNFQKLNKDDVLAILKA 388
Cdd:cd14863 314 EELGEAVADAIREFMKELGIPSLFEDYGIDKEDLDKIAEAVLKDP--FAMFNPRPITEEEVAEILEA 378
|
|
| Fe-ADH-like |
cd08196 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
4-386 |
2.43e-66 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341475 [Multi-domain] Cd Length: 367 Bit Score: 214.75 E-value: 2.43e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 4 FTYYNPTKLIFGKGQIDQLKKELKQYG-KNVLLVyGGGSIKRNGLYDQVTGILKEEGATVHElaGVEPNPRLEMVNKGIE 82
Cdd:cd08196 1 WSYYQPVKIIFGEGILKELPDIIKELGgKRGLLV-TDPSFIKSGLAKRIVESLKGRIVAVFS--DVEPNPTVENVDKCAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 83 LCRQHEIDFLLAVGGGSVIDCTKAIAAGAKYDGDAWDIYSKKVT-AQDALPFGTVLTLAATGSEMNPDSVITNWETNEKF 161
Cdd:cd08196 78 LARENGADFVIAIGGGSVLDTAKAAACLAKTDGSIEDYLEGKKKiPKKGLPLIAIPTTAGTGSEVTPVAVLTDKEKGKKA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 162 VWGSNVTHPRFSILDPENTFSVPENQTV-YGMvDMMSHVFEQYFhNVENTPLQDRmcFAV--LQTVIETAPKLLEDLENY 238
Cdd:cd08196 158 PLVSPGFYPDIAIVDPELTYSMPPKVTAsTGI-DALCHAIEAYW-SINHQPISDA--LALeaAKLVLENLEKAYNNPNDK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 239 KHRETILYAGTIA-----LNGTLqmgyfgdwASHTMEHAVSAVYDIPHAGGLAILFPNWMRYTLDTNVDRFKNL--MLNM 311
Cdd:cd08196 234 EAREKMALASLLAglafsQTRTT--------ASHACSYPLTSHFGIPHGEACALTLPSFIRLNAEALPGRLDELakQLGF 305
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2256122564 312 FDIDtegktdkeialEGIDKLSAFWTSLGAPSRLADYDIGEDKLELIADIAAkEMEYGGfGNFQKLNKDDVLAIL 386
Cdd:cd08196 306 KDAE-----------ELADKIEELKKRIGLRTRLSELGITEEDLEEIVEESF-HPNRAN-NNPVEVTKEDLEKLL 367
|
|
| PDDH |
cd08188 |
1,3-Propanediol (1,3-PD) dehydrogenase; This family includes 1,3-propanediol (1,3-PD) ... |
4-387 |
4.88e-65 |
|
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: 211.60 E-value: 4.88e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 4 FTYYNPTKLIFGKGQIDQLKKELKQYG-KNVLLVYGGGSIKrNGLYDQVTGILKEEGATVHELAGVEPNPRLEMVNKGIE 82
Cdd:cd08188 1 FRFYIPPVNLFGPGCLKEIGDELKKLGgKKALIVTDKGLVK-LGLVKKVTDVLEEAGIEYVIFDGVQPNPTVTNVNEGLE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 83 LCRQHEIDFLLAVGGGSVIDCTKAIAAGAKYDGDAWDiY-----SKKvtaqDALPFGTVLTLAATGSEMNPDSVITNWET 157
Cdd:cd08188 80 LFKENGCDFIISVGGGSAHDCAKAIGILATNGGEIED-YegvdkSKK----PGLPLIAINTTAGTASEVTRFAVITDEER 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 158 NEKFV---WgsNVThPRFSILDPENTFSVPENQTVY-GMvDMMSHVFEQYFhNVENTPLQDRMCFAVLQTVIETAPKLLE 233
Cdd:cd08188 155 HVKMVivdW--NVT-PTIAVNDPELMLGMPPSLTAAtGM-DALTHAIEAYV-STGATPLTDALALEAIRLIAENLPKAVA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 234 DLENYKHRETILYAGTIA----LNGTLqmGYFgdwasHTMEHAVSAVYDIPHagGL--AILFPNWMRYTLDTNVDRFKNL 307
Cdd:cd08188 230 NGKDLEARENMAYAQFLAgmafNNAGL--GYV-----HAMAHQLGGFYNLPH--GVcnAILLPHVMEFNLPACPERFADI 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 308 MLNMFdIDTEGKTDKEIALEGIDKLSAFWTSLGAPSRLADYDIGEDKLELIADIAAKEMeyGGFGNFQKLNKDDVLAILK 387
Cdd:cd08188 301 ARALG-ENTEGLSDEEAAEAAIEAIRKLSRRVGIPSGLKELGVKEEDFPLLAENALKDA--CGPTNPRQATKEDVIAIYR 377
|
|
| Fe-ADH-like |
cd14865 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
4-390 |
2.57e-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: 341487 [Multi-domain] Cd Length: 383 Bit Score: 202.39 E-value: 2.57e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 4 FTYYNPTKLIFGKGQIDQLKKELKQYG-KNVLLVYGGGsIKRNGLYDQVTGILKEEGATVHELAGVEPNPRLEMVNKGIE 82
Cdd:cd14865 1 FEFFNPTKIVSGAGALENLPAELARLGaRRPLIVTDKG-LAAAGLLKKVEDALGDAIEIVGVFDDVPPDSSVAVVNEAAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 83 LCRQHEIDFLLAVGGGSVIDCTKAIAAGAKYDGDAWDIYS-KKVTAQDALPFGTVLTLAATGSEMNPDSVITNWETNEKF 161
Cdd:cd14865 80 RAREAGADGIIAVGGGSVIDTAKGVNILLSEGGDDLDDYGgANRLTRPLKPLIAIPTTAGTGSEVTLVAVIKDEEKKVKL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 162 VWGSNVTHPRFSILDPENTFSVPENQTVY-GMvDMMSHVFEQYfHNVENTPLQDRMCFAVLQTVIETAPKLLEDLENYKH 240
Cdd:cd14865 160 LFVSPFLLPDVAILDPRLTLSLPPKLTAAtGM-DALTHAIEAY-TSLQKNPISDALALQAIRLISENLPKAVKNGKDLEA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 241 RETILYAGTIAlnGTL----QMGyfgdwASHTMEHAVSAVYDIPHAGGLAILFPNWMRYTLDTNVDRFKNLMLNM-FDID 315
Cdd:cd14865 238 RLALAIAATMA--GIAfsnsMVG-----LVHAIAHAVGAVAGVPHGLANSILLPHVMRYNLDAAAERYAELALALaYGVT 310
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2256122564 316 TEGKTDKEIALEGIDKLSAFWTSLGAPSRLADYDIGEDKLELIADIAakeMEYGG-FGNFQKLNKDDVLAILKASL 390
Cdd:cd14865 311 PAGRRAEEAIEAAIDLVRRLHELCGLPTRLRDVGVPEEQLEAIAELA---LNDGAiLFNPREVDPEDILAILEAAY 383
|
|
| PPD-like |
cd08181 |
1,3-propanediol dehydrogenase-like (PPD); This family contains proteins similar to 1, ... |
6-387 |
3.15e-57 |
|
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: 190.87 E-value: 3.15e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 6 YYNPTKLIFGKGQIDQLKKELKQYGKNVLLVYGGGSIKRNGLYDQVTGILKEEGA--TVHElaGVEPNPRLEMVNKGIEL 83
Cdd:cd08181 1 FYMPTKVYFGKNCVEKHADELAALGKKALIVTGKHSAKKNGSLDDVTEALEENGIeyFIFD--EVEENPSIETVEKGAEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 84 CRQHEIDFLLAVGGGSVIDCTKAIAAGAKYDGDAWDIYSKKVTaQDALPFGTVLTLAATGSEMNPDSVITNWETNEKFVW 163
Cdd:cd08181 79 ARKEGADFVIGIGGGSPLDAAKAIALLAANKDGDEDLFQNGKY-NPPLPIVAIPTTAGTGSEVTPYSILTDHEKGTKKSF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 164 GSNVTHPRFSILDPENTFSVPENQTVYGMVDMMSHVFEQYFhNVENTPLQDRMCFAVLQTVIETAPKLLEDLENYKHRET 243
Cdd:cd08181 158 GNPLIFPKLALLDPKYTLSLPEELTIDTAVDALSHAIEGYL-SVKATPLSDALALEALRLIGECLPNLLGDELDEEDREK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 244 ILYAGT-----IALNGTLQMgyfgdwasHTMEHAVSAVYDIPHAGGLAILFPnwmRYtldtnvdrfknlmLNMFDIDTEG 318
Cdd:cd08181 237 LMYASTlagmvIAQTGTTLP--------HGLGYPLTYFKGIPHGRANGILLP---AY-------------LKLCEKQEPE 292
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2256122564 319 KTDKEIALEGIDKLSAFWTSLGAPSRLADYdIGEDKLELIADIA--AKEMEYGGFgnfqKLNKDDVLAILK 387
Cdd:cd08181 293 KVDKILKLLGFGSIEEFQKFLNRLLGKKEE-LSEEELEKYADEAmkAKNKKNTPG----NVTKEDILRIYR 358
|
|
| NADPH_BDH |
cd08179 |
NADPH-dependent butanol dehydrogenase involved in the butanol and ethanol formation pathway in ... |
6-362 |
7.01e-54 |
|
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: 182.77 E-value: 7.01e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 6 YYNPTKLIFGKGQIDQLKKeLKqyGKNVLLVYGGGSIKRNGLYDQVTGILKEEGATVHELAGVEPNPRLEMVNKGIELCR 85
Cdd:cd08179 2 FFVPRDIYFGEGALEYLKT-LK--GKRAFIVTGGGSMKRNGFLDKVEDYLKEAGMEVKVFEGVEPDPSVETVEKGAEAMR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 86 QHEIDFLLAVGGGSVIDCTKAIAAGAKYDGDAWDiyskkvtaqDALPFGTVLTL------------AATGSEMNPDSVIT 153
Cdd:cd08179 79 EFEPDWIIAIGGGSVIDAAKAMWVFYEYPELTFE---------DALVPFPLPELrkkarfiaipstSGTGSEVTRASVIT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 154 NWETNEKFVWGSNVTHPRFSILDPENTFSVPENQTVY-GMvDMMSHVFEQYFHNVeNTPLQDRMCFAVLQTVIETAPKLL 232
Cdd:cd08179 150 DTEKGIKYPLASFEITPDVAILDPELTMTMPPHVTANtGM-DALTHAIEAYVSTL-ANDFTDALALGAILDIFENLPKSY 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 233 EDLENYKHRETILYAGTIA----LNGTLQMgyfgdwaSHTMEHAVSAVYDIPHagGL--AILFPNWMRYTLDTNVDRFKN 306
Cdd:cd08179 228 NGGKDLEAREKMHNASCLAgmafSNSGLGI-------VHSMAHKGGAFFGIPH--GLanAILLPYVIEFNSKDPEARARY 298
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 307 LMLNMFDIDTEGKTDKEIALEGIDKlsafwtSLGAPSRLADYDIGED----KLELIADIA 362
Cdd:cd08179 299 AALLIGLTDEELVEDLIEAIEELNK------KLGIPLSFKEAGIDEDeffaKLDEMAENA 352
|
|
| LPO |
cd08176 |
Lactadehyde:propanediol oxidoreductase (LPO) catalyzes the interconversion between ... |
3-387 |
9.38e-54 |
|
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: 182.36 E-value: 9.38e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 3 NFTYYNPTkLIFGKGQIDQLKKELKQYG-KNVLLVYGGGSIKrNGLYDQVTGILKEEGATVHELAGVEPNPRLEMVNKGI 81
Cdd:cd08176 1 NRFVLNPT-SYFGWGAIEEIGEEAKKRGfKKALIVTDKGLVK-FGIVDKVTDVLKEAGIAYTVFDEVKPNPTIENVMAGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 82 ELCRQHEIDFLLAVGGGSVIDCTKAIAAGAKYDGDawDIYS--------KKVTAQDALPfgtvlTLAATGSEMNPDSVIT 153
Cdd:cd08176 79 AAYKESGADGIIAVGGGSSIDTAKAIGIIVANPGA--DVRSlegvaptkNPAVPIIAVP-----TTAGTGSEVTINYVIT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 154 NWETNEKFVWGSNVTHPRFSILDPENTFSVPENQTVY-GMvDMMSHVFEQYFHNVENtPLQDRMCFAVLQTVIETAPKLL 232
Cdd:cd08176 152 DTEKKRKFVCVDPHDIPTVAIVDPDLMSSMPKGLTAAtGM-DALTHAIEGYITKGAW-ELSDMLALKAIELIAKNLRKAV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 233 EDLENYKHRETILYAGTIAlngtlQMGYfgdwaS-------HTMEHAVSAVYDIPHagGL--AILFPNWMRYTLDTNVDR 303
Cdd:cd08176 230 ANPNNVEARENMALAQYIA-----GMAF-----SnvglgivHSMAHPLSAFYDTPH--GVanAILLPYVMEFNAPATGEK 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 304 FKNlMLNMFDIDTEGKTDKEIALEGIDKLSAFWTSLGAPSRLADYDIGEDKLELIADIAAKEMEYGgfGNFQKLNKDDVL 383
Cdd:cd08176 298 YRD-IARAMGVDTTGMSDEEAAEAAVDAVKKLSKDVGIPQKLSELGVKEEDIEALAEDALNDVCTP--GNPREATKEDII 374
|
....
gi 2256122564 384 AILK 387
Cdd:cd08176 375 ALYK 378
|
|
| Fe-ADH-like |
cd08189 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
7-365 |
1.21e-50 |
|
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: 174.19 E-value: 1.21e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 7 YNPTKLIFGKGQIDQLKKELKQYG-KNVLLVYGGGSIKRnGLYDQVTGILKEEGATVHELAGVEPNPRLEMVNKGIELCR 85
Cdd:cd08189 3 WPEPELFEGAGSLLQLPEALKKLGiKRVLIVTDKGLVKL-GLLDPLLDALKKAGIEYVVFDGVVPDPTIDNVEEGLALYK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 86 QHEIDFLLAVGGGSVIDCTKAIAAGAKYDGDawDIYS----KKVtAQDALPFGTVLTLAATGSEMNPDSVITNWETNEKF 161
Cdd:cd08189 82 ENGCDAIIAIGGGSVIDCAKVIAARAANPKK--SVRKlkglLKV-RKKLPPLIAVPTTAGTGSEATIAAVITDPETHEKY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 162 VWGSNVTHPRFSILDPENTFSVPENQTVY-GMvDMMSHVFEQYFhNVENTPLQDRMCFAVLQTVIETAPKLLEDLENYKH 240
Cdd:cd08189 159 AINDPKLIPDAAVLDPELTLGLPPAITAAtGM-DALTHAVEAYI-SRSATKETDEYALEAVKLIFENLPKAYEDGSDLEA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 241 RETIL----YAGtIALNGTLqMGYFgdwasHTMEHAVSAVYDIPHAGGLAILFPNWMRYTLDTNVDRFKNLMLnMFDIDT 316
Cdd:cd08189 237 RENMLlasyYAG-LAFTRAY-VGYV-----HAIAHQLGGLYGVPHGLANAVVLPHVLEFYGPAAEKRLAELAD-AAGLGD 308
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 2256122564 317 EGKTDKEIALEGIDKLSAFWTSLGAPSRLAdyDIGEDKLELIADIAAKE 365
Cdd:cd08189 309 SGESDSEKAEAFIAAIRELNRRMGIPTTLE--ELKEEDIPEIAKRALKE 355
|
|
| HEPD |
cd08182 |
Hydroxyethylphosphoate dehydrogenase (HEPD) catalyzes the reduction of phosphonoacetaldehyde ... |
9-386 |
3.74e-50 |
|
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: 172.79 E-value: 3.74e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 9 PTKLIFGKGQIDQLKKELKQYG-KNVLLVYGGGSIKRNGLYDQVTGILkeEGATVHELAGVEPNPRLEMVNKGIELCRQH 87
Cdd:cd08182 1 PVKIIFGPGALAELKDLLGGLGaRRVLLVTGPSAVRESGAADILDALG--GRIPVVVFSDFSPNPDLEDLERGIELFRES 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 88 EIDFLLAVGGGSVIDCTKAIAAGAKYDGDAWDIYSKKVTA--QDALPFGTVLTLAATGSEMNPDSVItnW--ETNEKFvw 163
Cdd:cd08182 79 GPDVIIAVGGGSVIDTAKAIAALLGSPGENLLLLRTGEKApeENALPLIAIPTTAGTGSEVTPFATI--WdeAEGKKY-- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 164 gSnVTH----PRFSILDPENTFSVPENQTVYGMVDMMSHVFEQYFhNVENTPLQDRMCFAVLQTVIETAPKLLEDLENYK 239
Cdd:cd08182 155 -S-LAHpslyPDAAILDPELTLSLPLYLTASTGLDALSHAIESIW-SVNANPESRAYALRAIRLILENLPLLLENLPNLE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 240 HRETI----LYAG-TIALNGTLqmgyfgdwASHTMEHAVSAVYDIPHagGLA--ILFPNWMRYTLDTNVDRFKN-----L 307
Cdd:cd08182 232 AREAMaeasLLAGlAISITKTT--------AAHAISYPLTSRYGVPH--GHAcaLTLPAVLRYNAGADDECDDDprgreI 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 308 MLNMFDIDTEgktdkeialEGIDKLSAFWTSLGAPSRLADYDIGEDKLELIADiaakEMEYGG-FGNFQ-KLNKDDVLAI 385
Cdd:cd08182 302 LLALGASDPA---------EAAERLRALLESLGLPTRLSEYGVTAEDLEALAA----SVNTPErLKNNPvRLSEEDLLRL 368
|
.
gi 2256122564 386 L 386
Cdd:cd08182 369 L 369
|
|
| Fe-ADH-like |
cd08194 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
9-365 |
1.31e-49 |
|
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: 171.56 E-value: 1.31e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 9 PTKLIFGKGQIDQLKKELKQ-YGKNVLLVyGGGSIKRNGLYDQVTGILKEEGATVHELAGVEPNPRLEMVNKGIELCRQH 87
Cdd:cd08194 1 PRTIIIGGGALEELGEEAASlGGKRALIV-TDKVMVKLGLVDKVTQLLAEAGIAYAVFDDVVSEPTDEMVEEGLALYKEG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 88 EIDFLLAVGGGSVIDCTKAIAAGAKYDGDAWDIYSKKVTAQDALPFGTVLTLAATGSEMNPDSVITNWETNEKFVWGSNV 167
Cdd:cd08194 80 GCDFIVALGGGSPIDTAKAIAVLATNGGPIRDYMGPRKVDKPGLPLIAIPTTAGTGSEVTRFTVITDTETDVKMLLKGPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 168 THPRFSILDPENTFSVPENQTVYGMVDMMSHVFEQYFhNVENTPLQDRMCFAVLQTVIETAPKLLEDLENYKHRETILYA 247
Cdd:cd08194 160 LLPAVAIVDPELTLSMPPRVTAATGIDALTHAIEAYV-SRKAQPLTDTLALSAIKLIGRNLRRAYADGDDLEAREAMMLA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 248 GT---IALNGtlqmgyfgdwAS----HTMEHAVSAVYDIPHagGL--AILFPNWMRYTLDTNVDRFKNLMLNMfDIDTEG 318
Cdd:cd08194 239 ALeagIAFSN----------SSvalvHGMSRPIGALFHVPH--GLsnAMLLPAVTEFSLPGAPERYAEIARAM-GIATEG 305
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 2256122564 319 KTDKEIALEGIDKLSAFWTSLGAPSrLADYDIGEDKLELIADIAAKE 365
Cdd:cd08194 306 DSDEEAAEKLVEALERLCADLEIPT-LREYGIDEEEFEAALDKMAED 351
|
|
| Fe-ADH-like |
cd08183 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
9-387 |
3.60e-49 |
|
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: 170.38 E-value: 3.60e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 9 PTKLIFGKGQIDQLKKELKQYGKNVLLVYGGGSIkRNGLYDQVTGILKEEGATVHELAGVEpNPRLEMVNKGIELCRQHE 88
Cdd:cd08183 1 PPRIVFGRGSLQELGELAAELGKRALLVTGRSSL-RSGRLARLLEALEAAGIEVALFSVSG-EPTVETVDAAVALAREAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 89 IDFLLAVGGGSVIDCTKAIAAGAKYDGDAWD----IYSKKVTAQDALPFGTVLTLAATGSEMNPDSVITNWETNEK---- 160
Cdd:cd08183 79 CDVVIAIGGGSVIDAAKAIAALLTNEGSVLDylevVGKGRPLTEPPLPFIAIPTTAGTGSEVTKNAVLSSPEHGVKvslr 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 161 ---FVwgsnvthPRFSILDPENTFSVPENQTVY-GMvDMMSHVFEQYfhnVEN--TPLQDRMCFAVLQTVIETAPKLLED 234
Cdd:cd08183 159 spsML-------PDVALVDPELTLSLPPEVTAAsGL-DALTQLIEPY---VSRkaNPLTDALAREGLRLAARSLRRAYED 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 235 LENYKHRETILYA---GTIAL-NGTLqmGyfgdwASHTMEHAVSAVYDIPHagGL--AILFPNWMRYTLDTNVDRF-KNL 307
Cdd:cd08183 228 GEDLEAREDMALAsllGGLALaNAGL--G-----AVHGLAGPLGGMFGAPH--GAicAALLPPVLEANLRALREREpDSP 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 308 MLNMFDIDTEGKTDKEIAL--EGIDKLSAFWTSLGAPsRLADYDIGEDKLELIADIAAK--EMEyggfGNFQKLNKDDVL 383
Cdd:cd08183 299 ALARYRELAGILTGDPDAAaeDGVEWLEELCEELGIP-RLSEYGLTEEDFPEIVEKARGssSMK----GNPIELSDEELL 373
|
....
gi 2256122564 384 AILK 387
Cdd:cd08183 374 EILE 377
|
|
| Fe-ADH-like |
cd14861 |
Iron-containing alcohol dehydrogenases-like; This family contains proteins similar to ... |
9-390 |
7.24e-48 |
|
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: 166.53 E-value: 7.24e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 9 PTKLIFGKGQIDQLKKELKQYG-KNVLLVYGGGsIKRNGLYDQVTGILKEEGATVHELAGVEPNPRLEMVNKGIELCRQH 87
Cdd:cd14861 3 PTRIRFGAGAIAELPEELKALGiRRPLLVTDPG-LAALGIVDRVLEALGAAGLSPAVFSDVPPNPTEADVEAGVAAYREG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 88 EIDFLLAVGGGSVIDCTKAIAAGAKYDGDAWD----IYSKKVTAQDALPFGTVLTLAATGSEMNPDSVITNWETNEKFVW 163
Cdd:cd14861 82 GCDGIIALGGGSAIDAAKAIALMATHPGPLWDyedgEGGPAAITPAVPPLIAIPTTAGTGSEVGRAAVITDDDTGRKKII 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 164 GSNVTHPRFSILDPENTFSVPENQTVY-GMvDMMSHVFEQYFHNVENtPLQDRMCFAVLQTVIETAPKLLEDLENYKHRE 242
Cdd:cd14861 162 FSPKLLPKVAICDPELTLGLPPRLTAAtGM-DALTHCIEAYLSPGFH-PMADGIALEGLRLISEWLPRAVADGSDLEARG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 243 TILYA---GTIAlngtLQMGyFGdwASHTMEHAVSAVYDIPHagGL--AILFPNWMRYTLDTNVDRFKNLMLNMFDIDTE 317
Cdd:cd14861 240 EMMMAalmGAVA----FQKG-LG--AVHALAHALGALYGLHH--GLlnAILLPYVLRFNRPAVEDKLARLARALGLGLGG 310
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2256122564 318 GKTdkeiALEGIDKLSAfwtSLGAPSRLADYDIGEDKLELIADIAAKEMEYGgfGNFQKLNKDDVLAILKASL 390
Cdd:cd14861 311 FDD----FIAWVEDLNE---RLGLPATLSELGVTEDDLDELAELALADPCHA--TNPRPVTAEDYRALLREAL 374
|
|
| Fe-ADH-like |
cd08186 |
Iron-containing alcohol dehydrogenase; This family contains iron-containing alcohol ... |
10-390 |
8.12e-48 |
|
Iron-containing alcohol dehydrogenase; This family contains iron-containing alcohol dehydrogenase (ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. The ADH of hyperthermophilic archaeon Thermococcus hydrothermalis oxidizes a series of primary aliphatic and aromatic alcohols, preferentially from C2 to C8, but is also active towards methanol and glycerol, and is stereospecific for monoterpenes. It has been suggested that the type III ADHs in microorganisms are involved in acetaldehyde detoxication rather than in alcohol turnover.
Pssm-ID: 341465 [Multi-domain] Cd Length: 380 Bit Score: 166.67 E-value: 8.12e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 10 TKLIFGKGQIDQLKKELKQYG-KNVLLVYGGGSIKRNGLYDQVTGILKEEGATVHELAGVEPNPRLEMVNKGIELCRQHE 88
Cdd:cd08186 2 TTLYFGVGAIAKIKDILKDLGiDKVIIVTGRSSYKKSGAWDDVEKALEENGIEYVVYDKVTPNPTVDQADEAAKLARDFG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 89 IDFLLAVGGGSVIDCTKAIAAGAKY-DGDAWDIYSKKVTAQDALPFGTVLTLAATGSEMNPDSVITNWETNEKFVWGSNV 167
Cdd:cd08186 82 ADAVIAIGGGSPIDTAKSVAVLLAYgGKTARDLYGFRFAPERALPLVAINLTHGTGSEVDRFAVATIPEKGYKPGIAYDC 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 168 THPRFSILDPENTFSVPENQTVYGMVDMMSHVFEQYFHNVENtPLQDRMCFAVLQTVIETAPKLLEDLENYKHRETILYA 247
Cdd:cd08186 162 IYPLYAIDDPRLTLTLPKEQTLYTSIDAFNHVYEAATTKVSS-PYVITLAKEAIRLIAEYLPRALANPKDLEARYWLLYA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 248 GTIA----LNGTLQMGyfgdwasHTMEHAVSAVY-DIPHAGGLAILFPNWMRYTL----DTNVDRFKNlmlnmfdIDTEG 318
Cdd:cd08186 241 SMIAgiaiDNGLLHLT-------HALEHPLSGLKpELPHGLGLALLGPAVVKYIYkavpETLADILRP-------IVPGL 306
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2256122564 319 KTDKEIALEGIDKLSAFWTSLGAPSRLADYDIGEDKLELIADIAAKEMEYGGFGNFQ--KLNKDDVLAILKASL 390
Cdd:cd08186 307 KGTPDEAEKAARGVEEFLFSVGFTEKLSDYGFTEDDVDRLVELAFTTPSLDLLLSLApvEVTEEVVREIYEESL 380
|
|
| Fe-ADH-like |
cd14862 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
5-367 |
5.33e-41 |
|
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: 148.53 E-value: 5.33e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 5 TYYNPTKLIFGKGQIDQLKKELkqyGKNVLLVYGGGsIKRNGLYDQVTGILKEEGATVHELAGVEPNPRLEMVNKGIELC 84
Cdd:cd14862 2 WYFSSPKIVFGEDALSHLEQLS---GKRALIVTDKV-LVKLGLLKKVLKRLLQAGFEVEVFDEVEPEPPLETVLKGAEAM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 85 RQHEIDFLLAVGGGSVIDCTKaiAAGAKYDGDawDIYSKKVTAQDALPFGTVLTLAA------TGSEMNPDSVITNWETN 158
Cdd:cd14862 78 REFEPDLIIALGGGSVMDAAK--AAWVLYERP--DLDPEDISPLDLLGLRKKAKLIAipttsgTGSEATWAIVLTDTEEP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 159 EKFVWGSNVTHPRFSILDPENTFSVPENQTVYGMVDMMSHVFEQY---FHNventPLQDRMCFAVLQTVIETAPKLLEDL 235
Cdd:cd14862 154 RKIAVANPELVPDVAILDPEFVLGMPPKLTAGTGLDALAHAVEAYlstWSN----DFSDALALKAIELIFKYLPRAYKDG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 236 ENYKHRETILYAGTIAlnGtlqMGyFGDWA---SHTMEHAVSAVYDIPHAGGLAILFPNWMRYTLDTNVDRFKNLMLnmf 312
Cdd:cd14862 230 DDLEAREKMHNAATIA--G---LA-FGNSQaglAHALGHSLGAVFHVPHGIAVGLFLPYVIEFYAKVTDERYDLLKL--- 300
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 2256122564 313 dIDTEGKTDKEIALEGIDKLSAFWTSLGAPSRLADYDIGEDK-LELIADIAAKEME 367
Cdd:cd14862 301 -LGIEARDEEEALKKLVEAIRELYKEVGQPLSIKDLGISEEEfEEKLDELVEYAME 355
|
|
| PRK09860 |
PRK09860 |
putative alcohol dehydrogenase; Provisional |
1-390 |
2.26e-40 |
|
putative alcohol dehydrogenase; Provisional
Pssm-ID: 182118 [Multi-domain] Cd Length: 383 Bit Score: 147.02 E-value: 2.26e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 1 MENFTYYNPTKLIFGKGQIDQLKKELKQYGKNVLLVYGGGSIKRNGLYDQVTGILKEEGATVHELAGVEPNPRLEMVNKG 80
Cdd:PRK09860 1 MAASTFFIPSVNVIGADSLTDAMNMMADYGFTRTLIVTDNMLTKLGMAGDVQKALEERNIFSVIYDGTQPNPTTENVAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 81 IELCRQHEIDFLLAVGGGSVIDCTKAIAAGAKYDGDAWDIYSKKVTAQDALPFGTVLTLAATGSEMNPDSVITNWETNEK 160
Cdd:PRK09860 81 LKLLKENNCDSVISLGGGSPHDCAKGIALVAANGGDIRDYEGVDRSAKPQLPMIAINTTAGTASEMTRFCIITDEARHIK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 161 FVWGSNVTHPRFSILDPENTFSVPENQTVYGMVDMMSHVFEQYFhNVENTPLQDRMCFAVLQTVIETAPKLLEDLENYKH 240
Cdd:PRK09860 161 MAIVDKHVTPLLSVNDSSLMIGMPKSLTAATGMDALTHAIEAYV-SIAATPITDACALKAVTMIAENLPLAVEDGSNAKA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 241 RETILYA---GTIALNGTlQMGYFgdwasHTMEHAVSAVYDIPHAGGLAILFPNWMRYTLDTNVDRFKNLMLNMfDIDTE 317
Cdd:PRK09860 240 REAMAYAqflAGMAFNNA-SLGYV-----HAMAHQLGGFYNLPHGVCNAVLLPHVQVFNSKVAAARLRDCAAAM-GVNVT 312
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2256122564 318 GKTDKEIALEGIDKLSAFWTSLGAPSRLADYDIGEDKLELIADIAAKEMeyGGFGNFQKLNKDDVLAILKASL 390
Cdd:PRK09860 313 GKNDAEGAEACINAIRELAKKVDIPAGLRDLNVKEEDFAVLATNALKDA--CGFTNPIQATHEEIVAIYRAAM 383
|
|
| Fe-ADH-like |
cd17814 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
13-364 |
2.99e-40 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341489 [Multi-domain] Cd Length: 374 Bit Score: 146.53 E-value: 2.99e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 13 IFGKGQIDQLKKELKQYG-KNVLLVYGGGSIKrNGLYDQVTGILKEEGATVHELAGVEPNPRLEMVNKGIELCRQHEIDF 91
Cdd:cd17814 8 IFGVGARKLAGRYAKNLGaRKVLVVTDPGVIK-AGWVDEVLDSLEAEGLEYVVFSDVTPNPRDFEVMEGAELYREEGCDG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 92 LLAVGGGSVIDCTKAIAAGAKYDGDAWDiYS--KKVTaQDALPFGTVLTLAATGSEMNPDSVITNWETNEKFVWGSNVTH 169
Cdd:cd17814 87 IVAVGGGSPIDCAKGIGIVVSNGGHILD-YEgvDKVR-RPLPPLICIPTTAGSSADVSQFAIITDTERRVKMAIISKTLV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 170 PRFSILDPENTFSVPENQTVYGMVDMMSHVFEQYFHNVeNTPLQDRMCFAVLQTVIETAPKLLEDLENYKHRETI----L 245
Cdd:cd17814 165 PDVSLIDPETLTTMDPELTACTGMDALTHAIEAYVSNA-SSPLTDLHALEAIRLISENLPKAVADPDDLEAREKMmlasL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 246 YAGTIALNGTLqmgyfGdwASHTMEHAVSAVYDIPHagGL--AILFPNWMRYTLDTNVDRFKNLMlNMFDIDTEGKTDKE 323
Cdd:cd17814 244 QAGLAFSNASL-----G--AVHAMAHSLGGLLDLPH--GEcnALLLPHVIRFNFPAAPERYRKIA-EAMGLDVDGLDDEE 313
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2256122564 324 IALEGIDKLSAFWTSLGAPSRLADYDIGEDKLELIADIAAK 364
Cdd:cd17814 314 VAERLIEAIRDLREDLGIPETLSELGVDEEDIPELAKRAMK 354
|
|
| Fe-ADH-like |
cd08191 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
9-390 |
3.72e-39 |
|
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: 143.91 E-value: 3.72e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 9 PTKLIFGKGQIDQLKKELKQYGKNVLLVyGGGSIKRNGLYDQVTGILKEEGATVHELAGVEPNPRLEMVNKGIELCRQHE 88
Cdd:cd08191 4 PSRLLFGPGARRALGRVAARLGSRVLIV-TDPRLASTPLVAELLAALTAAGVAVEVFDGGQPELPVSTVADAAAAARAFD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 89 IDFLLAVGGGSVIDCTKAIAAGAKYDGDAWDIYSKKVTAQDALPFGTVLTLAATGSEMNPDSVITNWETNEKFVWGSNVT 168
Cdd:cd08191 83 PDVVIGLGGGSNMDLAKVVALLLAHGGDPRDYYGEDRVPGPVLPLIAVPTTAGTGSEVTPVAVLTDPARGMKVGVSSPYL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 169 HPRFSILDPENTFSVPENQTVYGMVDMMSHVFEQYFHN--------------VENTPLQD-------RMCFAVLQTVIet 227
Cdd:cd08191 163 RPAVAIVDPELTLTCPPGVTADSGIDALTHAIESYTARdfppfprldpdpvyVGKNPLTDllaleaiRLIGRHLPRAV-- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 228 apkllEDLENYKHRETILYAgtiALNGTLQMGYFGDWASHTMEHAVSAVYDIPHAGGLAILFPNWMRYTLDTNVDRFKNL 307
Cdd:cd08191 241 -----RDGDDLEARSGMALA---ALLAGLAFGTAGTAAAHALQYPIGALTHTSHGVGNGLLLPYVMRFNRPARAAELAEI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 308 MlNMFDIDTEGKTDkEIALEGIDKLSAFWTSLGAPSRLADYDIGEDKLeliADIAAKemeygGFG-------NFQKLNKD 380
Cdd:cd08191 313 A-RALGVTTAGTSE-EAADRAIERVEELLARIGIPTTLADLGVTEADL---PGLAEK-----ALSvtrlianNPRPPTEE 382
|
410
....*....|
gi 2256122564 381 DVLAILKASL 390
Cdd:cd08191 383 DLLRILRAAF 392
|
|
| DHQ_Fe-ADH |
cd07766 |
Dehydroquinate synthase-like (DHQ-like) and iron-containing alcohol dehydrogenases (Fe-ADH); ... |
9-362 |
4.69e-38 |
|
Dehydroquinate synthase-like (DHQ-like) and iron-containing alcohol dehydrogenases (Fe-ADH); This superfamily consists of two subgroups: the dehydroquinate synthase (DHQS)-like, and a large metal-containing alcohol dehydrogenases (ADH), known as iron-containing alcohol dehydrogenases. Dehydroquinate synthase (DHQS) catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate-7-phosphate (DAHP) to dehydroquinate (DHQ) in the second step of the shikimate pathway. This pathway involves seven sequential enzymatic steps in the conversion of erythrose 4-phosphate and phosphoenolpyruvate into chorismate for subsequent synthesis of aromatic compounds. Dehydroquinate synthase-like group includes dehydroquinate synthase, 2-deoxy-scyllo-inosose synthase, and 2-epi-5-epi-valiolone synthase. The alcohol dehydrogenases (ADHs) in this superfamily contain a dehydroquinate synthase-like protein structural fold and mostly contain iron. They are distinct from other alcohol dehydrogenases which contains different protein domains. There are several distinct families of alcohol dehydrogenases: Zinc-containing long-chain alcohol dehydrogenases; insect-type, or short-chain alcohol dehydrogenases; iron-containing alcohol dehydrogenases, and others. The iron-containing family has a Rossmann fold-like topology that resembles the fold of the zinc-dependent alcohol dehydrogenases, but lacks sequence homology, and differs in strand arrangement. ADH catalyzes the reversible oxidation of alcohol to acetaldehyde with the simultaneous reduction of NAD(P)+ to NAD(P)H.
Pssm-ID: 341447 [Multi-domain] Cd Length: 271 Bit Score: 137.88 E-value: 4.69e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 9 PTKLIFGKGQIDQLKKELKQYGKNVLLVYGGGSIKrnGLYDQVTGILKEeGATVHELAGVEPNPRLEMVNKGIELCRQHE 88
Cdd:cd07766 1 PTRIVFGEGAIAKLGEIKRRGFDRALVVSDEGVVK--GVGEKVADSLKK-GLAVAIFDFVGENPTFEEVKNAVERARAAE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 89 IDFLLAVGGGSVIDCTKAIAAgakydgdawdiyskkvTAQDALPFGTVLTLAATGSEMNPDSVITNWETNEKFVwgsnVT 168
Cdd:cd07766 78 ADAVIAVGGGSTLDTAKAVAA----------------LLNRGIPFIIVPTTASTDSEVSPKSVITDKGGKNKQV----GP 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 169 H--PRFSILDPENTFSVPENQTVYGMVDMMSHVFEqyfhnventplqdrmcfavlqtvietapklledlenykhRETILY 246
Cdd:cd07766 138 HynPDVVFVDTDITKGLPPRQVASGGVDALAHAVE---------------------------------------LEKVVE 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 247 AGTIALNGTLQMGyfGDWASHTMEHAVSAVYDIPHAGGLAILFPNWMRYTLDTNVDRfknlmlnmfdidtegktdkEIAL 326
Cdd:cd07766 179 AATLAGMGLFESP--GLGLAHAIGHALTAFEGIPHGEAVAVGLPYVLKVANDMNPEP-------------------EAAI 237
|
330 340 350
....*....|....*....|....*....|....*.
gi 2256122564 327 EGIDKlsaFWTSLGAPSRLADYDIGEDKLELIADIA 362
Cdd:cd07766 238 EAVFK---FLEDLGLPTHLADLGVSKEDIPKLAEKA 270
|
|
| Fe-ADH-like |
cd14864 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
6-388 |
5.18e-36 |
|
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: 135.12 E-value: 5.18e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 6 YYNPTKLIFGKGQIDQLKKELKQYGKNVLLVYGGGSiKRNGLYDQVTGILKEEGATVHELAGVEPNPRLEMVNKGIELCR 85
Cdd:cd14864 1 FKIPPNIVFGADSLERIGEEVKEYGSRFLLITDPVL-KESGLADKIVSSLEKAGISVIVFDEIPASATSDTIDEAAELAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 86 QHEIDFLLAVGGGSVIDCTKAIAAGAKYDGDAWDIYSKKVTAQDALPFGTVLTLAATGSEMNPDSVITNWETNEKFVWGS 165
Cdd:cd14864 80 KAGADGIIAVGGGKVLDTAKAVAILANNDGGAYDFLEGAKPKKKPLPLIAVPTTPRSGFEFSDRFPVVDSRSREVKLLKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 166 NVTHPRFSILDPENTFSVPENQTVYGMVDMMSHVFEQYFHNvENTPLQDRMCFAVLQTVIETAPKLLEDLENYKHRETIL 245
Cdd:cd14864 160 QPGLPKAVIVDPNLMASLTGNQTAAMALAALALAVEAYLSK-KSNFFSDALALKAIELVSENLDGALADPKNTPAEELLA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 246 YAGTI----ALNGTLQMGYfgdwashTMEHAVSAVYDIPHAGGLAILFPNWMRYTLDTNVDRFKNlMLNMFDIDTEGKTD 321
Cdd:cd14864 239 QAGCLaglaASSSSPGLAT-------ALALAVNSRYKVSKSLVASILLPHVIEYAATSAPDKYAK-IARALGEDVEGASP 310
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2256122564 322 KEIALEGIDKLSAFWTSLGAPSRLADYDIGeDKLELIADIAAKEMEYGGFGNFqkLNKDDVLAILKA 388
Cdd:cd14864 311 EEAAIAAVEGVRRLIAQLNLPTRLKDLDLA-SSLEQLAAIAEDAPKLNGLPRS--MSSDDIFDILKA 374
|
|
| HOT |
cd08190 |
Hydroxyacid-oxoacid transhydrogenase (HOT) involved in gamma-hydroxybutyrate metabolism; This ... |
10-360 |
1.18e-34 |
|
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: 132.28 E-value: 1.18e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 10 TKLIFGKGQIDQLKKELKQYG-KNVLLVYGGGsIKRNGLYDQVTGILKEEGATVHELAGVEPNPRLEMVNKGIELCRQHE 88
Cdd:cd08190 2 SNIRFGPGATRELGMDLKRLGaKKVLVVTDPG-LAKLGLVERVLESLEKAGIEVVVYDGVRVEPTDESFEEAIEFAKEGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 89 IDFLLAVGGGSVIDCTKAIAAGAKYDGDAWDIY------SKKVTAQdALPFGTVLTLAATGSEMNPDSVITNWETNEKFV 162
Cdd:cd08190 81 FDAFVAVGGGSVIDTAKAANLYATHPGDFLDYVnapigkGKPVPGP-LKPLIAIPTTAGTGSETTGVAIFDLEELKVKTG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 163 WGSNVTHPRFSILDPENTFSVPENQTVY-GMvDMMSHVFEQY-------FHNVEN----------TPLQDRMCFAVLQTV 224
Cdd:cd08190 160 ISSRYLRPTLAIVDPLLTLTLPPRVTASsGF-DVLCHALESYtarpynaRPRPANpderpayqgsNPISDVWAEKAIELI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 225 IETAPKLLEDLENYKHRETILYAGTIAlnGtlqMGyFGD---WASHTMEHAVSAV-------------YDIPHAGGLAIL 288
Cdd:cd08190 239 GKYLRRAVNDGDDLEARSNMLLASTLA--G---IG-FGNagvHLPHAMAYPIAGLvkdyrppgypvdhPHVPHGLSVALT 312
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2256122564 289 FPNWMRYTLDTNVDRFKNLmLNMFDIDTEGKTDKEIALEGIDKLSAFWTSLGAPSRLADYDIGEDKLELIAD 360
Cdd:cd08190 313 APAVFRFTAPACPERHLEA-AELLGADTSGASDRDAGEVLADALIKLMRDIGIPNGLSALGYSEDDIPALVE 383
|
|
| MAR-like |
cd08192 |
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic ... |
9-388 |
1.96e-33 |
|
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: 128.13 E-value: 1.96e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 9 PTKLIFGKGQIDQLKKELKQYG-KNVLLVYGGgSIKRN-GLYDQVTGILKEEGATVHElaGVEPNPRLEMVNKGIELCRQ 86
Cdd:cd08192 1 LERVSYGPGAVEALLHELATLGaSRVFIVTSK-SLATKtDVIKRLEEALGDRHVGVFS--GVRQHTPREDVLEAARAVRE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 87 HEIDFLLAVGGGSVIDCTKAIA---AGAKYDGDAWDIY--SKKVTAQDALPFGTVL----TLAatGSEMNPDSVITNWET 157
Cdd:cd08192 78 AGADLLVSLGGGSPIDAAKAVAlalAEDVTDVDQLDALedGKRIDPNVTGPTLPHIaiptTLS--GAEFTAGAGATDDDT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 158 NEKFVWGSNVTHPRFSILDPENTFSVPEN---QTvyGM--VDmmsHVFEQYFHNvENTPLQDRMCFAVLQTVIETAPKLL 232
Cdd:cd08192 156 GHKQGFAHPELGPDAVILDPELTLHTPERlwlST--GIraVD---HAVETLCSP-QATPFVDALALKALRLLFEGLPRSK 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 233 EDLENYkhrETIL------YAGTIALNGTLQMGyfgdwASHTMEHAVSAVYDIPHagGLA--ILFPNWMRYTLDTNVDRF 304
Cdd:cd08192 230 ADPEDL---EARLkcqlaaWLSLFGLGSGVPMG-----ASHAIGHQLGPLYGVPH--GITscIMLPAVLRFNAPVNAERQ 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 305 KNLMLNMFDIDTEGKTDKEIALEGIDKLSAfwtSLGAPSRLADYDIGEDKLELIADIAAKEMEyGGFGNFQKLNKDDVLA 384
Cdd:cd08192 300 RLIARALGLVTGGLGREAADAADAIDALIR---ELGLPRTLRDVGVGRDQLEKIAENALTDVW-CRTNPRPITDKDDVLE 375
|
....
gi 2256122564 385 ILKA 388
Cdd:cd08192 376 ILES 379
|
|
| PRK10624 |
PRK10624 |
L-1,2-propanediol oxidoreductase; Provisional |
14-390 |
2.14e-33 |
|
L-1,2-propanediol oxidoreductase; Provisional
Pssm-ID: 182595 [Multi-domain] Cd Length: 382 Bit Score: 128.19 E-value: 2.14e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 14 FGKGQIDQLKKELKQYG-KNVLLVYGGGSIKrNGLYDQVTGILKEEGATVHELAGVEPNPRLEMVNKGIELCRQHEIDFL 92
Cdd:PRK10624 13 FGRGAIGALTDEVKRRGfKKALIVTDKTLVK-CGVVAKVTDVLDAAGLAYEIYDGVKPNPTIEVVKEGVEVFKASGADYL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 93 LAVGGGSVIDCTKAIAAgAKYDGDAWDIYSKK---VTAQDALPFGTVLTLAATGSEMNPDSVITNWETNEKFVWGSNVTH 169
Cdd:PRK10624 92 IAIGGGSPQDTCKAIGI-ISNNPEFADVRSLEgvaPTKKPSVPIIAIPTTAGTAAEVTINYVITDEEKRRKFVCVDPHDI 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 170 PRFSILDPENTFSVPENQTVYGMVDMMSHVFEQYFhnvenTPLQDRMCFAVLQTVIETAPKLLEDL--ENYKHRETILYA 247
Cdd:PRK10624 171 PQVAFVDADMMDSMPPGLKAATGVDALTHAIEGYI-----TRGAWALTDMLHLKAIEIIAGALRGAvaGDKEAGEGMALG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 248 GTIAlngtlQMGY--FGDWASHTMEHAVSAVYDIPHAGGLAILFPNWMRYTLDTNVDRFKNLMLNMfDIDTEGKTDKEIA 325
Cdd:PRK10624 246 QYIA-----GMGFsnVGLGLVHGMAHPLGAFYNTPHGVANAILLPHVMEYNADFTGEKYRDIARAM-GVKVEGMSLEEAR 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2256122564 326 LEGIDKLSAFWTSLGAPSRLADYDIGEDKLELIADIAAKEMEYGgfGNFQKLNKDDVLAILKASL 390
Cdd:PRK10624 320 NAAVEAVKALNRDVGIPPHLRDVGVKEEDIPALAQAAFDDVCTG--GNPREATLEDIVELYKKAW 382
|
|
| PDD |
cd08180 |
1,3-propanediol dehydrogenase (PPD) catalyzes the reduction of 3-hydroxypropionaldehyde (3-HPA) ... |
9-387 |
2.88e-31 |
|
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: 121.45 E-value: 2.88e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 9 PTKLIFGKGQIDQLKkELKqyGKNVLLVyGGGSIKRNGLYDQVTGILKEeGATVHELAGVEPNPRLEMVNKGIELCRQHE 88
Cdd:cd08180 4 KTKIYSGEDSLERLK-ELK--GKRVFIV-TDPFMVKSGMVDKVTDELDK-SNEVEIFSDVVPDPSIEVVAKGLAKILEFK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 89 IDFLLAVGGGSVIDCTKAIAAgakydgdawdIYSKKVTAQDALPFGTVLTLAATGSEMNPDSVITNWETNEKFVWGSNVT 168
Cdd:cd08180 79 PDTIIALGGGSAIDAAKAIIY----------FALKQKGNIKKPLFIAIPTTSGTGSEVTSFAVITDPEKGIKYPLVDDSM 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 169 HPRFSILDPENTFSVPENQTVY-GMvDMMSHVFEQYFhNVENTPLQDRMCFAVLQTVIETAPKLLEDLENYKHRETILYA 247
Cdd:cd08180 149 LPDIAILDPELVKSVPPKVTADtGM-DVLTHALEAYV-STNANDFTDALAEKAIKLVFENLPRAYRDGDDLEAREKMHNA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 248 GTIA----------LNgtlqmgyfgdwasHTMEHAVSAVYDIPHagGL--AILFPNWMRYtldtnvdrfknLMlnmfdid 315
Cdd:cd08180 227 SCMAgiafnnaglgIN-------------HSLAHALGGRFHIPH--GRanAILLPYVIEF-----------LI------- 273
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2256122564 316 tegktdkeialEGIDKLSAfwtSLGAPSRLADYDIGED----KLELIADIAAKEMEYGgfGNFQKLNKDDVLAILK 387
Cdd:cd08180 274 -----------AAIRRLNK---KLGIPSTLKELGIDEEefekAIDEMAEAALADRCTA--TNPRKPTAEDLIELLR 333
|
|
| HVD |
cd08193 |
5-hydroxyvalerate dehydrogenase (HVD) catalyzes the oxidation of 5-hydroxyvalerate to ... |
9-390 |
3.24e-31 |
|
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: 122.24 E-value: 3.24e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 9 PTKLIFGKGQIDQLKKELKQYG-KNVLLVYGGGsIKRNGLYDQVTGILKEEGATVHELAGVEPNPRLEMVNKGIELCRQH 87
Cdd:cd08193 4 VPRIICGAGAAARLGELLRELGaRRVLLVTDPG-LVKAGLADPALAALEAAGIAVTVFDDVVADPPEAVVEAAVEQAREA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 88 EIDFLLAVGGGSVIDCTKAIAAGAKYDGDAWDIYS-KKVTAQdALPFGTVLTLAATGSEMNPDSVITNWETNEKFVWgSN 166
Cdd:cd08193 83 GADGVIGFGGGSSMDVAKLVALLAGSDQPLDDIYGvGKATGP-RLPLILVPTTAGTGSEVTPISIVTTGETEKKGVV-SP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 167 VTHPRFSILDPENTFSVPENQTVYGMVDMMSHVFEQYFHNVENTPLQDRMCFAVLQTVIETAPKLLEDLENYKHRETILY 246
Cdd:cd08193 161 QLLPDVALLDAELTLGLPPHVTAATGIDAMVHAIEAYTSRHKKNPISDALAREALRLLGANLRRAVEDGSDLEAREAMLL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 247 AGTIA----LNGTLQmgyfgdwASHTMEHAVSAVYDIPHagGL--AILFPNWMRYTLDTNVDRFKNLMLNMFdIDTEGKT 320
Cdd:cd08193 241 GSMLAgqafANAPVA-------AVHALAYPLGGHFHVPH--GLsnALVLPHVLRFNLPAAEALYAELARALL-PGLAFGS 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 321 DKEIALEGIDKLSAFWTSLGAPSRLADYDIGEDKLELIADIAAK----------EMEYggfgnfqklnkDDVLAILKASL 390
Cdd:cd08193 311 DAAAAEAFIDALEELVEASGLPTRLRDVGVTEEDLPMLAEDAMKqtrllvnnprEVTE-----------EDALAIYQAAL 379
|
|
| AAD_C |
cd08178 |
C-terminal alcohol dehydrogenase domain of the acetaldehyde dehydrogenase-alcohol ... |
9-362 |
1.71e-28 |
|
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: 114.98 E-value: 1.71e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 9 PTKLIFGKGQIDQLKKELKQyGKNVLLVYGGGSIKrNGLYDQVTGILKEEGATVHELAGVEPNPRLEMVNKGIELCRQHE 88
Cdd:cd08178 3 PPKIYFEPGCLPYLLLELPG-VKRAFIVTDRVLYK-LGYVDKVLDVLEARGVETEVFSDVEPDPTLSTVRKGLEAMNAFK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 89 IDFLLAVGGGSVIDCTKAI------------AAGAKYDgdawDIySKKVTAQDALPFGTVL----TLAATGSEMNPDSVI 152
Cdd:cd08178 81 PDVIIALGGGSAMDAAKIMwlfyehpetkfeDLAQRFM----DI-RKRVYKFPKLGKKAKLvaipTTSGTGSEVTPFAVI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 153 TNWETNEKF-VWGSNVThPRFSILDPENTFSVPENQTVYGMVDMMSHVFEQYFhNVENTPLQDRMCFAVLQTVIETAPKL 231
Cdd:cd08178 156 TDDKTGKKYpLADYALT-PDMAIVDPELVMTMPKRLTADTGIDALTHAIEAYV-SVMASDYTDGLALQAIKLIFEYLPRS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 232 LEDLENYKHRETILYAGTIA----LNGTLQMGyfgdwasHTMEHAVSAVYDIPHagGL--AILFPNWMRYtlDTNVDRFK 305
Cdd:cd08178 234 YNNGNDIEAREKMHNAATIAgmafANAFLGIC-------HSLAHKLGAAFHIPH--GRanAILLPHVIRY--NATDPPTK 302
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2256122564 306 nlmLNMF-----------------DIDTEGKTDKEIALEGIDKLSAFWTSLGAPSRLADYDIGED----KLELIADIA 362
Cdd:cd08178 303 ---QAAFpqykyyvakeryaeiadLLGLGGKTPEEKVESLIKAIEDLKKDLGIPTSIREAGIDEAdflaAVDKLAEDA 377
|
|
| PRK13805 |
PRK13805 |
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional |
9-362 |
2.63e-24 |
|
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional
Pssm-ID: 237515 [Multi-domain] Cd Length: 862 Bit Score: 104.88 E-value: 2.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 9 PTKLIFGKGQIDQLKKELkqYGKN-VLLVYGGGSIKrNGLYDQVTGILK--EEGATVHELAGVEPNPRLEMVNKGIELCR 85
Cdd:PRK13805 460 PKKIYFERGSLPYLLDEL--DGKKrAFIVTDRFMVE-LGYVDKVTDVLKkrENGVEYEVFSEVEPDPTLSTVRKGAELMR 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 86 QHEIDFLLAVGGGSVIDCTKAIaagakydgdaWDIY-SKKVTAQD-ALPF-------------GT------VLTLAATGS 144
Cdd:PRK13805 537 SFKPDTIIALGGGSPMDAAKIM----------WLFYeHPETDFEDlAQKFmdirkriykfpklGKkaklvaIPTTSGTGS 606
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 145 EMNPDSVITNWETNEKFVWGSNVTHPRFSILDPENTFSVPENQTVYGMVDMMSHVFEQYFhNVENTPLQDRMCFAVLQTV 224
Cdd:PRK13805 607 EVTPFAVITDDKTGVKYPLADYELTPDVAIVDPNLVMTMPKSLTADTGIDALTHALEAYV-SVMASDYTDGLALQAIKLV 685
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 225 IETAPK-LLEDLENYKHRETILYAGTIA----LNGTLQMgyfgdwaSHTMEHAVSAVYDIPHagGL--AILFPNWMRY-- 295
Cdd:PRK13805 686 FEYLPRsYKNGAKDPEAREKMHNASTIAgmafANAFLGI-------CHSMAHKLGAEFHIPH--GRanAILLPHVIRYna 756
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 296 ------TLDTNVDRFKNL--------MLNMfdidtEGKTDKEIA---LEGIDKLSAfwtSLGAPSRLADYDIGED----K 354
Cdd:PRK13805 757 tdppkqAAFPQYEYPRADeryaeiarHLGL-----PGSTTEEKVeslIKAIEELKA---ELGIPMSIKEAGVDEAdflaK 828
|
....*...
gi 2256122564 355 LELIADIA 362
Cdd:PRK13805 829 LDELAELA 836
|
|
| Fe-ADH-like |
cd14866 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
7-388 |
3.04e-23 |
|
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: 100.00 E-value: 3.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 7 YNPTKLIFGKGQIDQLKKELKQYGKNVLLVYGGGSIKRNG-LYDQVTGILKEEGATVHelAGVEPNPRLEMVNKGIELCR 85
Cdd:cd14866 3 YPPLRLFSGRGALARLGRELDRLGARRALVVCGSSVGANPdLMDPVRAALGDRLAGVF--DGVRPHSPLETVEAAAEALR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 86 QHEIDFLLAVGGGSVIDCTKAIAAGAKYDGDAWDIY----------SKKVTAqDALPFGTVLTLAATGSEMNPdSVITNW 155
Cdd:cd14866 81 EADADAVVAVGGGSAIVTARAASILLAEDRDVRELCtrraedglmvSPRLDA-PKLPIFVVPTTPTTADVKAG-SAVTDP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 156 ETNEKFVWGSNVTHPRFSILDPENTFSVPENQTVYGMVDMMSHVFEQYFHNVENtPLQDRMCFAVLQTVIETAPKLLEDL 235
Cdd:cd14866 159 PAGQRLALFDPKTRPAAVFYDPELLATAPASLVAGAAMNGFDMAVEGLYSRHAD-PLADATLMHALRLLADGLPRLADDD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 236 ENYKHRETILYA-----GTIALNGTLqmgyfgdwaSHTMEHAVSAVYDIPHAGGLAILFPNWMRYTLDTnVDRFKNLMLN 310
Cdd:cd14866 238 DPAARADLVLAAvlagyGTDHTGGGV---------IHALGHAIGARYGVQNGVVHAILLPHVLRFNAPA-TDGRLDRLAE 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 311 MFDIDTEGktDKEIALEGIDKLSAFWTSLGAPSRLADYDIGEDKLELIADIAAKE--MEYGGFGNfqkLNKDDVLAILKA 388
Cdd:cd14866 308 ALGVADAG--DEASAAAVVDAVEALLDALGVPTRLRDLGVSREDLPAIAEAAMDDwfMDNNPRPV---PTAEELEALLEA 382
|
|
| MAR |
cd08177 |
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic ... |
9-388 |
3.30e-20 |
|
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: 90.64 E-value: 3.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 9 PTKLIFGKGQIDQLKKELKQYGKNVLLVYGGGSikRNGLYDQVTGILKEEGATVHELAgVEPNPRlEMVNKGIELCRQHE 88
Cdd:cd08177 1 PQRVVFGAGTLAELAEELERLGARRALVLSTPR--QRALAERVAALLGDRVAGVFDGA-VMHVPV-EVAERALAAAREAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 89 IDFLLAVGGGSVIDCTKAIAAGAKydgdawdiyskkvTAQDALPfgTvlTLAatGSEMNPdsvitNW-ETNEkfvwGSNV 167
Cdd:cd08177 77 ADGLVAIGGGSAIGLAKAIALRTG-------------LPIVAVP--T--TYA--GSEMTP-----IWgETED----GVKT 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 168 TH------PRFSILDPENTFSVPENQTVYGMVDMMSHVFEQ-YFHNVenTPLQDRMCFAVLQTVIETAPKLLEDLENYKH 240
Cdd:cd08177 129 TGrdprvlPRTVIYDPDLTLGLPAALSVASGLNALAHAVEAlYAPDA--NPITSLLAEEGIRALARALPRLVADPSDLEA 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 241 RETILY----AGTiALNGT---LQmgyfgdwasHTMEHAVSAVYDIPHAGGLAILFPnwmrYTLDTNVDRFKNLMLNMFD 313
Cdd:cd08177 207 RSDALYgawlAGV-VLGSVgmgLH---------HKLCHVLGGTFDLPHAETHAVVLP----HVLAYNAPAAPDAMARLAR 272
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2256122564 314 IDTEGKtdkeiALEGIDKLSAfwtSLGAPSRLADYDIGEDKLELIADIAAKEmeygGFGNFQKLNKDDVLAILKA 388
Cdd:cd08177 273 ALGGGD-----AAGGLYDLAR---RLGAPTSLRDLGMPEDDIDRAADLALAN----PYPNPRPVERDALRALLER 335
|
|
| PRK15454 |
PRK15454 |
ethanolamine utilization ethanol dehydrogenase EutG; |
85-347 |
3.85e-20 |
|
ethanolamine utilization ethanol dehydrogenase EutG;
Pssm-ID: 185351 [Multi-domain] Cd Length: 395 Bit Score: 91.24 E-value: 3.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 85 RQHEIDFLLAVGGGSVIDCTKAIAAGAKYDGDAWDIYSKKVTAQDALPFGTVLTLAATGSEMNPDSVITNWETNEKFVWG 164
Cdd:PRK15454 103 RESGCDGVIAFGGGSVLDAAKAVALLVTNPDSTLAEMSETSVLQPRLPLIAIPTTAGTGSETTNVTVIIDAVSGRKQVLA 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 165 SNVTHPRFSILDPENTFSVPENQTVYGMVDMMSHVFEQYfHNVENTPLQDRMCFAVLQTVIETAPKLLEDLENYKHRETI 244
Cdd:PRK15454 183 HASLMPDVAILDAALTEGVPSHVTAMTGIDALTHAIEAY-SALNATPFTDSLAIGAIAMIGKSLPKAVGYGHDLAARESM 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 245 LYAGTIAlngTLQMGYFGDWASHTMEHAVSAVYDIPHAGGLAILFPNWMRYTLDTNVDRFKNLMLNMfdidTEGKTDKEI 324
Cdd:PRK15454 262 LLASCMA---GMAFSSAGLGLCHAMAHQPGAALHIPHGLANAMLLPTVMEFNRMVCRERFSQIGRAL----RTKKSDDRD 334
|
250 260
....*....|....*....|...
gi 2256122564 325 ALEGIDKLSAfwtSLGAPSRLAD 347
Cdd:PRK15454 335 AINAVSELIA---EVGIGKRLGD 354
|
|
| GldA |
COG0371 |
Glycerol dehydrogenase or related enzyme, iron-containing ADH family [Energy production and ... |
9-388 |
2.68e-19 |
|
Glycerol dehydrogenase or related enzyme, iron-containing ADH family [Energy production and conversion]; Glycerol dehydrogenase or related enzyme, iron-containing ADH family is part of the Pathway/BioSystem: Isoprenoid biosynthesis
Pssm-ID: 440140 [Multi-domain] Cd Length: 355 Bit Score: 88.30 E-value: 2.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 9 PTKLIFGKGQIDQLKKELKQYGKNVLLVYGGGSIKRNGlyDQVTGILKEEGATVHeLAGVEPNPRLEMVNKGIELCRQHE 88
Cdd:COG0371 6 PRRYVQGEGALDELGEYLADLGKRALIITGPTALKAAG--DRLEESLEDAGIEVE-VEVFGGECSEEEIERLAEEAKEQG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 89 IDFLLAVGGGSVIDCTKAIAAGAKydgdawdiyskkvtaqdaLPFGTVLTLAATgsemnpD------SVITNweTNEKFV 162
Cdd:COG0371 83 ADVIIGVGGGKALDTAKAVAYRLG------------------LPVVSVPTIAST------DapasplSVIYT--EDGAFD 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 163 WGSNVTH-PRFSILDPENTFSVPENQTVYGMVDMMSHVFEQYFHNVENTPLQD-----------RMCfavLQTVIETAPK 230
Cdd:COG0371 137 GYSFLAKnPDLVLVDTDIIAKAPVRLLAAGIGDALAKWYEARDWSLAHRDLAGeyyteaavalaRLC---AETLLEYGEA 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 231 LLEDLENYKHRE--------TILYAGTIALNGTlqmGYFGDWASHTMEHAVSAVYDIPHAG-----GLAILFpnwmrytl 297
Cdd:COG0371 214 AIKAVEAGVVTPalervveaNLLLSGLAMGIGS---SRPGSGAAHAIHNGLTALPETHHALhgekvAFGTLV-------- 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 298 dtnvdrfknlMLNMFDIDTEgktdkeialegIDKLSAFWTSLGAPSRLADYDIGED---KLELIADIAAKEMEYGGFGNF 374
Cdd:COG0371 283 ----------QLVLEGRPEE-----------IEELLDFLRSVGLPTTLADLGLDDEteeELLTVAEAARPERYTILNLPF 341
|
410
....*....|....
gi 2256122564 375 qKLNKDDVLAILKA 388
Cdd:COG0371 342 -EVTPEAVEAAILA 354
|
|
| GlyDH |
cd08170 |
Glycerol dehydrogenases (GlyDH) catalyzes oxidation of glycerol to dihydroxyacetone in ... |
9-142 |
5.44e-11 |
|
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: 63.20 E-value: 5.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 9 PTKLIFGKGQIDQLKKELKQYGKNVLLVYGGGSIKRNGlyDQVTGILKEEGATVHELAGVEPNPRLEmVNKGIELCRQHE 88
Cdd:cd08170 1 PSRYVQGPGALDRLGEYLAPLGKKALVIADPFVLDLVG--ERLEESLEKAGLEVVFEVFGGECSREE-IERLAAIARANG 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2256122564 89 IDFLLAVGGGSVIDCTKAIAAGAKydgdawdiyskkvtaqdaLPFGTVLTLAAT 142
Cdd:cd08170 78 ADVVIGIGGGKTIDTAKAVADYLG------------------LPVVIVPTIAST 113
|
|
| Fe-ADH_2 |
pfam13685 |
Iron-containing alcohol dehydrogenase; |
13-109 |
2.17e-10 |
|
Iron-containing alcohol dehydrogenase;
Pssm-ID: 404557 [Multi-domain] Cd Length: 251 Bit Score: 60.39 E-value: 2.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 13 IFGKGQIDQLKKEL-KQYGKNVLLVYGGGSIKRNGlyDQVTGILKEEGATVHELAGVEPNPRLEMVNKGIELCRQHEIDF 91
Cdd:pfam13685 1 VIGPGALGRLGEYLaELGFRRVALVADANTYAAAG--RKVAESLKRAGIEVETRLEVAGNADMETAEKLVGALRERDADA 78
|
90
....*....|....*...
gi 2256122564 92 LLAVGGGSVIDCTKAIAA 109
Cdd:pfam13685 79 VVGVGGGTVIDLAKYAAF 96
|
|
| GlyDH-like |
cd08550 |
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins. ... |
9-388 |
9.55e-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: 59.47 E-value: 9.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 9 PTKLIFGKGQIDQLKKELKQYGKNVLLVYGGGSIKRNGlyDQVTGILKEEGATVH-ELAGVEPNprLEMVNKGIELCRQH 87
Cdd:cd08550 1 PGRYIQEPGILAKAGEYIAPLGKKALIIGGKTALEAVG--EKLEKSLEEAGIDYEvEVFGGECT--EENIERLAEKAKEE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 88 EIDFLLAVGGGSVIDCTKAIAAGAKydgdawdiyskkvtaqdaLPFGTVLTLAATGSEMNPDSVITNWETNEKFVWGSNV 167
Cdd:cd08550 77 GADVIIGIGGGKVLDTAKAVADRLG------------------LPVVTVPTIAATCAAWSALSVLYDEEGEFLGYSLLKR 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 168 ThPRFSILDPENTFSVPENQTVYGMVDMMSHVFEQYFH---NVENTPLQ-----DRMCFAVLqtvIETAPKLLEDLENyk 239
Cdd:cd08550 139 S-PDLVLVDTDIIAAAPVRYLAAGIGDTLAKWYEARPSsrgGPDDLALQaavqlAKLAYDLL---LEYGVQAVEDVRQ-- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 240 HRET----------ILYAGTIalnGTLQMGYFGDWASHTMEHAVSAVYDIPHAG-------GLAILfpnwmrytldtnvd 302
Cdd:cd08550 213 GKVTpaledvvdaiILLAGLV---GSLGGGGCRTAAAHAIHNGLTKLPETHGTLhgekvafGLLVQ-------------- 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 303 rfknLMLnmfdidtEGKTDKEialegIDKLSAFWTSLGAPSRLADYDIG--EDKLELIADiAAKEMEYGGFGNFQKLNKD 380
Cdd:cd08550 276 ----LAL-------EGRSEEE-----IEELIEFLRRLGLPVTLEDLGLEltEEELRKIAE-YACDPPDMAHMLPFPVTPE 338
|
....*....
gi 2256122564 381 DVL-AILKA 388
Cdd:cd08550 339 MLAeAILAA 347
|
|
| Fe-ADH_KdnB-like |
cd08184 |
Iron-containing alcohol dehydrogenase similar to Shewanella oneidensis KdnB required for Kdo8N ... |
9-208 |
2.52e-09 |
|
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: 58.05 E-value: 2.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 9 PTKLIFGKGQIDQLKKELKQY-----GKNVLLV----YGGGSIKR--NGLYDQVTGIlkeegATVHElagvepnPRLEMV 77
Cdd:cd08184 1 VPKYLFGRGSFDQLGELLAERrksnnDYVVFFIddvfKGKPLLDRlpLQNGDLLIFV-----DTTDE-------PKTDQI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 78 NKGIELCRQHEIDFLLAV---GGGSVIDCTKAIA-------AGAKYDGdaWDIYSKKVTAQDALPfgtvlTLAATGSEMN 147
Cdd:cd08184 69 DALRAQIRAENDKLPAAVvgiGGGSTMDIAKAVSnmltnpgSAADYQG--WDLVKNPGIYKIGVP-----TLSGTGAEAS 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2256122564 148 PDSVITNweTNEKFVWGSNVTHPRFSILDPENTFSVPENQTVYGMVDMmshvfeqYFHNVE 208
Cdd:cd08184 142 RTAVLTG--PEKKLGINSDYTVFDQVILDPELIATVPRDQYFYTGMDC-------YIHCVE 193
|
|
| egsA |
PRK00843 |
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed |
9-108 |
5.82e-09 |
|
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed
Pssm-ID: 179139 Cd Length: 350 Bit Score: 57.21 E-value: 5.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 9 PTKLIFGKGQIDQLK---KELKqYGKNVLLVYGGGSIKRNGlyDQVTGILKEEGaTVHELagVEPNPRLEMVNKGIELCR 85
Cdd:PRK00843 11 PRDVVVGHGVLDDIGdvcSDLK-LTGRALIVTGPTTKKIAG--DRVEENLEDAG-DVEVV--IVDEATMEEVEKVEEKAK 84
|
90 100
....*....|....*....|...
gi 2256122564 86 QHEIDFLLAVGGGSVIDCTKAIA 108
Cdd:PRK00843 85 DVNAGFLIGVGGGKVIDVAKLAA 107
|
|
| 4HBD_NAD |
cd14860 |
4-hydroxybutyrate dehydrogenase, also called gamma-hydroxybutyrate dehydrogenase, catalyzes ... |
69-388 |
1.87e-08 |
|
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: 55.69 E-value: 1.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 69 EPNPrlEMVNKGIELCRQHEIDFLLAVGGGSVIDCTKAIAagAKYDGDAWDIYSKKVTAQDALPFGTVLTLAATGSEMNP 148
Cdd:cd14860 61 EPSD--EMVEAIYKDIKKYGYKRVIAIGGGTVIDIAKLLA--LKGISPVLDLFDGKIPLIKEKELIIVPTTCGTGSEVTN 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 149 DSVITNWETNEKFVWGSNVTHPRFSILDPENTFSVPENQTVYGMVDMMSHVFEQYFhNVENTPLQDRMCFAVLQTVIETA 228
Cdd:cd14860 137 ISIVELTSLGTKKGLAVDELYADKAVLIPELLKGLPYKVFATSSIDALIHAIESYL-SPKATPYTEMFSYKAIEMILEGY 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 229 PKLLEDLENYkhRETIL--------YAGtIALngtlqmGYFGDWASHTMEHAVSAVYDIPHagG------LAILFPNWMR 294
Cdd:cd14860 216 QEIAEKGEEA--RFPLLgdfliasnYAG-IAF------GNAGCAAVHALSYPLGGKYHVPH--GeanyavFTGVLKNYQE 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 295 YTLDTNVDRFKNLMLNMFDIdtegktDKEIALEGIDKLsafwtsLG---APSRLADYDIGEDKLELIADIAAKEMEYGGF 371
Cdd:cd14860 285 KNPDGEIKKLNEFLAKILGC------DEEDVYDELEEL------LNkilPKKPLHEYGMKEEEIDEFADSVMENQQRLLA 352
|
330
....*....|....*..
gi 2256122564 372 GNFQKLNKDDVLAILKA 388
Cdd:cd14860 353 NNYVPLDREDVAEIYKE 369
|
|
| GlyDH-like |
cd08172 |
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins ... |
15-388 |
3.17e-08 |
|
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins that have yet to be characterized, but show sequence homology with glycerol dehydrogenase. Glycerol dehydrogenases (GlyDH) is a key enzyme in the glycerol dissimilation pathway. In anaerobic conditions, many microorganisms utilize glycerol as a source of carbon through coupled oxidative and reductive pathways. One of the pathways involves the oxidation of glycerol to dihydroxyacetone with the reduction of NAD+ to NADH catalyzed by glycerol dehydrogenases. Dihydroxyacetone is then phosphorylated by dihydroxyacetone kinase and enters the glycolytic pathway for further degradation. The activity of GlyDH is zinc-dependent; the zinc ion plays a role in stabilizing an alkoxide intermediate at the active site.
Pssm-ID: 341451 [Multi-domain] Cd Length: 346 Bit Score: 54.83 E-value: 3.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 15 GKGQIDQLKKELKQYG-KNVLLVYGGGSIK------RNGLYDQVTGILKEEGATVHELAgvepnpRLemvnkgIELCRQH 87
Cdd:cd08172 7 EEGALKELPELLSEFGiKRPLIIHGEKSWQaakpylPKLFEIEYPVLRYDGECSYEEID------RL------AEEAKEH 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 88 EIDFLLAVGGGSVIDCTKAIAAGAKydgdawdiyskkvtaqdaLPFGTVLTLAATGSEMNPDSVITNweTNEKFVwgSNV 167
Cdd:cd08172 75 QADVIIGIGGGKVLDTAKAVADKLN------------------IPLILIPTLASNCAAWTPLSVIYD--EDGEFI--GYD 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 168 THPR---FSILDPENTFSVPENQTVYGMVDMMSHVFEQ--YFHNVENTPLQDRM-------CFAVLQTVIETApklLEDL 235
Cdd:cd08172 133 YFPRsayLVLVDPRLLLDSPKDYFVAGIGDTLAKWYEAdaILRQLEELPAFLQLarqaaklCRDILLKDSEQA---LADL 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 236 ENYKHR-------ETIlyagtIALNGTLqmGYFGDW-----ASHTMEHAVSAVYDIPHA--G---GLAILFpnwmrytld 298
Cdd:cd08172 210 EAGKLTpafikvvETI-----IALAGMV--GGFGDEygrsaGAHAIHNGLTKLPETHHFlhGekvAYGILV--------- 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 299 tnvdrfkNLMLnmfdidtEGKTDKeialegIDKLSAFWTSLGAPSRLADYDIG---EDKLELIADIAAKEMEygGFGN-F 374
Cdd:cd08172 274 -------QLAL-------EGKWDE------IKKLLPFYRRLGLPTSLADLGLTddtEEALQKIAAFAASPEE--SIHLlP 331
|
410
....*....|....
gi 2256122564 375 QKLNKDDVLAILKA 388
Cdd:cd08172 332 PDVTAEEVLQAIEK 345
|
|
| Gro1PDH |
cd08173 |
Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) catalyzes the reversible conversion between ... |
9-108 |
4.58e-08 |
|
Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) catalyzes the reversible conversion between dihydroxyacetone phosphate and glycerol-1-phosphate using either NADH or NADPH as a coenzyme; Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH, EC 1.1.1.261) plays an important role in the formation of the enantiomeric configuration of the glycerophosphate backbone (sn-glycerol-1-phosphate) of archaeal ether lipids. It catalyzes the reversible conversion between dihydroxyacetone phosphate and glycerol-1-phosphate using either NADH or NADPH as a coenzyme. The activity is zinc-dependent. One characteristic feature of archaea is that their cellular membrane has an ether linkage between the glycerol backbone and the hydrocarbon residues. The polar lipids of the members of Archaea consist of di- and tetra-ethers of glycerol with isoprenoid alcohols bound at the sn-2 and sn-3 positions of the glycerol moiety. The archaeal polar lipids have the enantiomeric configuration of a glycerophosphate backbone [sn-glycerol-1-phosphate (G-1-P)] that is the mirror image structure of the bacterial or eukaryal counterpart [sn-glycerol- 3-phosphate (G-3-P)]. The absolute stereochemistry of the glycerol moiety in all archaeal polar lipids is opposite to that of glycerol ester lipids in bacteria and eukarya.
Pssm-ID: 341452 Cd Length: 343 Bit Score: 54.48 E-value: 4.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 9 PTKLIFGKGQIDQLKKELKQ--YGKNVLLVYGGGSIKRNGlyDQVTGILKEEGATVH--ELAGVEPNPRLEMVNKGIelc 84
Cdd:cd08173 2 PRNVVVGHGAINKIGEVLKKllLGKRALIITGPNTYKIAG--KRVEDLLESSGVEVVivDIATIEEAAEVEKVKKLI--- 76
|
90 100
....*....|....*....|....
gi 2256122564 85 RQHEIDFLLAVGGGSVIDCTKAIA 108
Cdd:cd08173 77 KESKADFIIGVGGGKVIDVAKYAA 100
|
|
| gldA |
PRK09423 |
glycerol dehydrogenase; Provisional |
9-112 |
1.23e-07 |
|
glycerol dehydrogenase; Provisional
Pssm-ID: 181843 Cd Length: 366 Bit Score: 52.89 E-value: 1.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 9 PTKLIFGKGQIDQLKKELKQYGKNVLLVYGGGSIKRNGlyDQVTGILKEEGATVHELA-GVEPNPrlEMVNKGIELCRQH 87
Cdd:PRK09423 8 PSKYVQGKGALARLGEYLKPLGKRALVIADEFVLGIVG--DRVEASLKEAGLTVVFEVfNGECSD--NEIDRLVAIAEEN 83
|
90 100
....*....|....*....|....*
gi 2256122564 88 EIDFLLAVGGGSVIDCTKAIAAGAK 112
Cdd:PRK09423 84 GCDVVIGIGGGKTLDTAKAVADYLG 108
|
|
| G1PDH-like |
cd08174 |
Glycerol-1-phosphate dehydrogenase-like; These glycerol-1-phosphate dehydrogenase-like ... |
9-112 |
1.91e-06 |
|
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: 49.06 E-value: 1.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 9 PTKLIFGKGQIDQLKKEL---KQYGKNVLLVYGGGSIKRngLYDQVTGILKEEGATVHELAGVEPNprLEMVNKgiELCR 85
Cdd:cd08174 1 PLILKIEEGALEHLGKYLadrNQGFGKVAIVTGEGIDEL--LGEDILESLEEAGEIVTVEENTDNS--AEELAE--KAFS 74
|
90 100
....*....|....*....|....*..
gi 2256122564 86 QHEIDFLLAVGGGSVIDCTKAIAAGAK 112
Cdd:cd08174 75 LPKVDAIVGIGGGKVLDVAKYAAFLSK 101
|
|
| GlyDH-like |
cd08171 |
Glycerol dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins ... |
15-108 |
1.42e-03 |
|
Glycerol dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins that have yet to be characterized, but show sequence homology with glycerol dehydrogenase. Glycerol dehydrogenases (GlyDH) is a key enzyme in the glycerol dissimilation pathway. In anaerobic conditions, many microorganisms utilize glycerol as a source of carbon through coupled oxidative and reductive pathways. One of the pathways involves the oxidation of glycerol to dihydroxyacetone with the reduction of NAD+ to NADH catalyzed by glycerol dehydrogenases. Dihydroxyacetone is then phosphorylated by dihydroxyacetone kinase and enters the glycolytic pathway for further degradation. The activity of GlyDH is zinc-dependent; the zinc ion plays a role in stabilizing an alkoxide intermediate at the active site.
Pssm-ID: 341450 Cd Length: 345 Bit Score: 40.20 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2256122564 15 GKGQIDQLKKELKQYGKNVLLVygGGSIKRNGLYDQVTGILKEEGATV--HELAGVEPNprLEMVNKGIELCRQHEIDFL 92
Cdd:cd08171 7 GEDAYDAIPKICSPYGKKVVVI--GGKKALAAAKPKLRAALEGSGLEItdFIWYGGEAT--YENVEKLKANPEVQEADMI 82
|
90
....*....|....*.
gi 2256122564 93 LAVGGGSVIDCTKAIA 108
Cdd:cd08171 83 FAVGGGKAIDTVKVLA 98
|
|
| |
