|
Name |
Accession |
Description |
Interval |
E-value |
| NDMA_methanol |
TIGR04266 |
NDMA-dependent methanol dehydrogenase; Members of this family belong to the iron-dependent ... |
10-424 |
0e+00 |
|
NDMA-dependent methanol dehydrogenase; Members of this family belong to the iron-dependent alcohol dehydrogenase family (see pfam00465). The NADP(H) cofactor is bound too tightly for exchange (although non-convalently), so enzymatic activity depends on a second substrate or electron carrier. The radical SAM-modified natural product mycofactocin is proposed to fill this role. In Rhodococcus erythropolis N9T-4, a role was shown for this protein in CO2 fixation during extreme oligotrophic (or possibly chemoautotrophic) growth.
Pssm-ID: 211989 Cd Length: 420 Bit Score: 629.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 10 FPLKEFHPFPRALMGPGAHEMIGPEALKLGFRKPLVMTSGLRGTDIVHNIVESLKYHGLDPVLYDEVESNPKDYNTMDSV 89
Cdd:TIGR04266 8 FPIKEFHPFPRALLGVGAHDIIGVEAKNLGFKRTLLMTTGLRGSGIIEELKGKIEYQGVEVVLYDKVESNPKDYNVMEAA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 90 ALYQENSCDSFISIGGGSSHDACKGARVSVAHDGRNVNEFEGFNKSENPNNPPHIAVSTTAGTGSETSWAYVITDTTtDP 169
Cdd:TIGR04266 88 ALYQSEKCDSIISIGGGSSHDAAKGARVVIAHDGRNINEFEGFAKSTNKQNPPHIAVSTTAGTGSETSWAYVITDTS-DM 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 170 DNPHKYVAFDDACVASLAIDDPVLYYDCPVDYTAQCGFDVLAHASEPYVSRINFEPSLGNALRAIKLTAENLRQATWNGQ 249
Cdd:TIGR04266 167 DQPHKWVGFDEATIVTLAIDDPLLYYTCPQHFTAYCGFDVLAHGSEPYVSRLDFAPSLGNALYSVELVAKHLREAVFEPR 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 250 DLPGREGMMYAQYIAAQAFNSGGLGVIHSISHAVSAFYDTHHGLNNAIALPRVWAFNMPVAYKRFAEMAEAMGVNTRGMN 329
Cdd:TIGR04266 247 NLKAREGMMNAQYIAGQAFNSGGLGIVHSISHAVSAFFDSHHGLNNAIALPRVWEYNLPSRYERYAQLATAMGVDTRNMT 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 330 DVQAADAALNAAIRLLRDVGITERFVDITKDTYSKNRLGEGptKFYERRTQIKGDAEDVDAITKHVLGDACTPGNPKECT 409
Cdd:TIGR04266 327 TVQAADAAVEAAIRLSKDVGIPDNFGQVRKDSYDKNRMNTG--KYSGRGPVIKGDDKTVRAISEHIQGDWCTPGNPREVT 404
|
410
....*....|....*
gi 1433560031 410 FDTVRPVVEHCMTGS 424
Cdd:TIGR04266 405 VESMIPVVSHAINKS 419
|
|
| LPO |
cd08176 |
Lactadehyde:propanediol oxidoreductase (LPO) catalyzes the interconversion between ... |
13-418 |
0e+00 |
|
Lactadehyde:propanediol oxidoreductase (LPO) catalyzes the interconversion between L-lactaldehyde and L-1,2-propanediol in Escherichia coli and other enterobacteria; Lactadehyde:propanediol oxidoreductase (LPO) is a member of the group III iron-activated dehydrogenases which catalyze the interconversion between L-lactaldehyde and L-1,2-propanediol in Escherichia coli and other enterobacteria. L-fucose and L-rhamnose are used by Escherichia coli through an inducible pathway mediated by the fucose regulon comprising four linked operons fucO, fucA, fucPIK, and fucR. The fucA-encoded aldolase catalyzes the formation of dihydroxyacetone phosphate and L-lactaldehyde. Under anaerobic conditions, with NADH as a cofactor, lactaldehyde is converted by a fucO-encoded lactadehyde:propanediol oxidoreductase (LPO) to L-1,2-propanediol, which is excreted as a fermentation product. In mutant strains, E. coli adapted to grow on L-1,2-propanediol, FucO catalyzes the oxidation of the polyol to L-lactaldehyde. FucO is induced regardless of the respiratory conditions of the culture, remains fully active in the absence of oxygen. In the presence of oxygen, this enzyme becomes oxidatively inactivated by a metal-catalyzed oxidation mechanism. FucO is an iron-dependent metalloenzyme that is inactivated by other metals, such as zinc, copper, or cadmium. This enzyme can also reduce glycol aldehyde with similar efficiency. Beside L-1,2-propanediol, the enzyme is also able to oxidize methanol as an alternative substrate.
Pssm-ID: 341455 [Multi-domain] Cd Length: 378 Bit Score: 530.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 13 KEFHPFPRALMGPGAHEMIGPEALKLGFRKPLVMTSGLRG-TDIVHNIVESLKYHGLDPVLYDEVESNPKDYNTMDSVAL 91
Cdd:cd08176 1 NRFVLNPTSYFGWGAIEEIGEEAKKRGFKKALIVTDKGLVkFGIVDKVTDVLKEAGIAYTVFDEVKPNPTIENVMAGVAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 92 YQENSCDSFISIGGGSSHDACKGARVSVAHDGRNVNEFEGFNKSENPNnPPHIAVSTTAGTGSETSWAYVITDTttdpDN 171
Cdd:cd08176 81 YKESGADGIIAVGGGSSIDTAKAIGIIVANPGADVRSLEGVAPTKNPA-VPIIAVPTTAGTGSEVTINYVITDT----EK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 172 PHKYVAFDDACVASLAIDDPVLYYDCPVDYTAQCGFDVLAHASEPYVSRINFEPSLGNALRAIKLTAENLRQATWNGQDL 251
Cdd:cd08176 156 KRKFVCVDPHDIPTVAIVDPDLMSSMPKGLTAATGMDALTHAIEGYITKGAWELSDMLALKAIELIAKNLRKAVANPNNV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 252 PGREGMMYAQYIAAQAFNSGGLGVIHSISHAVSAFYDTHHGLNNAIALPRVWAFNMPVAYKRFAEMAEAMGVNTRGMNDV 331
Cdd:cd08176 236 EARENMALAQYIAGMAFSNVGLGIVHSMAHPLSAFYDTPHGVANAILLPYVMEFNAPATGEKYRDIARAMGVDTTGMSDE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 332 QAADAALNAAIRLLRDVGITERFvditkdtysknrlgegptkfyerrTQIKGDAEDVDAITKHVLGDACTPGNPKECTFD 411
Cdd:cd08176 316 EAAEAAVDAVKKLSKDVGIPQKL------------------------SELGVKEEDIEALAEDALNDVCTPGNPREATKE 371
|
....*..
gi 1433560031 412 TVRPVVE 418
Cdd:cd08176 372 DIIALYK 378
|
|
| EutG |
COG1454 |
Alcohol dehydrogenase, class IV [Energy production and conversion]; |
14-421 |
4.75e-127 |
|
Alcohol dehydrogenase, class IV [Energy production and conversion];
Pssm-ID: 441063 [Multi-domain] Cd Length: 381 Bit Score: 372.15 E-value: 4.75e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 14 EFHPFPRALMGPGAHEMIGPEALKLGFRKPLVMT-SGLRGTDIVHNIVESLKYHGLDPVLYDEVESNPKDYNTMDSVALY 92
Cdd:COG1454 4 TFRLPTRIVFGAGALAELGEELKRLGAKRALIVTdPGLAKLGLLDRVLDALEAAGIEVVVFDDVEPNPTVETVEAGAAAA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 93 QENSCDSFISIGGGSSHDACKGARVSVAHDGrNVNEFEGFNKSENPNnPPHIAVSTTAGTGSETSWAYVITDtttdPDNP 172
Cdd:COG1454 84 REFGADVVIALGGGSAIDAAKAIALLATNPG-DLEDYLGIKKVPGPP-LPLIAIPTTAGTGSEVTPFAVITD----PETG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 173 HKYVAFDDACVASLAIDDPVLYYDCPVDYTAQCGFDVLAHASEPYVSRINFEPSLGNALRAIKLTAENLRQATWNGQDLP 252
Cdd:COG1454 158 VKKGIADPELLPDVAILDPELTLTLPPSLTAATGMDALTHAIEAYVSKGANPLTDALALEAIRLIARNLPRAVADGDDLE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 253 GREGMMYAQYIAAQAFNSGGLGVIHSISHAVSAFYDTHHGLNNAIALPRVWAFNMPVAYKRFAEMAEAMGVNTrGMNDVQ 332
Cdd:COG1454 238 AREKMALASLLAGMAFANAGLGAVHALAHPLGGLFHVPHGLANAILLPHVLRFNAPAAPERYAEIARALGLDV-GLSDEE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 333 AADAALNAAIRLLRDVGITERFVDItkdtysknrlgeGPTKfyerrtqikgdaEDVDAITKHVLGDACTPGNPKECTFDT 412
Cdd:COG1454 317 AAEALIEAIRELLRDLGIPTRLSEL------------GVTE------------EDLPELAELALADRCLANNPRPLTEED 372
|
....*....
gi 1433560031 413 VRPVVEHCM 421
Cdd:COG1454 373 IEAILRAAY 381
|
|
| PDDH |
cd08188 |
1,3-Propanediol (1,3-PD) dehydrogenase; This family includes 1,3-propanediol (1,3-PD) ... |
13-409 |
1.38e-124 |
|
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: 365.68 E-value: 1.38e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 13 KEFHPFPRALMGPGAHEMIGPEALKLGFRKPLVMTS-GLRGTDIVHNIVESLKYHGLDPVLYDEVESNPKDYNTMDSVAL 91
Cdd:cd08188 1 FRFYIPPVNLFGPGCLKEIGDELKKLGGKKALIVTDkGLVKLGLVKKVTDVLEEAGIEYVIFDGVQPNPTVTNVNEGLEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 92 YQENSCDSFISIGGGSSHDACKGARVSVAHDGrNVNEFEGFNKSENPNnPPHIAVSTTAGTGSETSWAYVITDTTTdpdn 171
Cdd:cd08188 81 FKENGCDFIISVGGGSAHDCAKAIGILATNGG-EIEDYEGVDKSKKPG-LPLIAINTTAGTASEVTRFAVITDEER---- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 172 pH-KYVAFDDACVASLAIDDPVLYYDCPVDYTAQCGFDVLAHASEPYVSRINFEPSLGNALRAIKLTAENLRQATWNGQD 250
Cdd:cd08188 155 -HvKMVIVDWNVTPTIAVNDPELMLGMPPSLTAATGMDALTHAIEAYVSTGATPLTDALALEAIRLIAENLPKAVANGKD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 251 LPGREGMMYAQYIAAQAFNSGGLGVIHSISHAVSAFYDTHHGLNNAIALPRVWAFNMPVAYKRFAEMAEAMGVNTRGMND 330
Cdd:cd08188 234 LEARENMAYAQFLAGMAFNNAGLGYVHAMAHQLGGFYNLPHGVCNAILLPHVMEFNLPACPERFADIARALGENTEGLSD 313
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1433560031 331 VQAADAALNAAIRLLRDVGITERFVDitkdtysknrLGegptkfyerrtqIKgdAEDVDAITKHVLGDACTPGNPKECT 409
Cdd:cd08188 314 EEAAEAAIEAIRKLSRRVGIPSGLKE----------LG------------VK--EEDFPLLAENALKDACGPTNPRQAT 368
|
|
| Fe-ADH |
cd08551 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains large ... |
19-414 |
9.27e-105 |
|
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: 315.16 E-value: 9.27e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 19 PRALMGPGAHEMIGPEALKLGFRKPLVMT-SGLRGTDIVHNIVESLKYHGLDPVLYDEVESNPKDYNTMDSVALYQENSC 97
Cdd:cd08551 2 TRIVFGAGALARLGEELKALGGKKVLLVTdPGLVKAGLLDKVLESLKAAGIEVEVFDDVEPNPTVETVEAAAELAREEGA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 98 DSFISIGGGSSHDACKGARVSVAHDGRnVNEFEGFNKSENPNnPPHIAVSTTAGTGSETSWAYVITDTTTDpdnpHKYVA 177
Cdd:cd08551 82 DLVIAVGGGSVLDTAKAIAVLATNGGS-IRDYEGIGKVPKPG-LPLIAIPTTAGTGSEVTPNAVITDPETG----RKMGI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 178 FDDACVASLAIDDPVLYYDCPVDYTAQCGFDVLAHASEPYVSRINFEPSLGNALRAIKLTAENLRQATWNGQDLPGREGM 257
Cdd:cd08551 156 VSPYLLPDVAILDPELTLSLPPSVTAATGMDALTHAIEAYTSKKANPISDALALEAIRLIGKNLRRAVADGSDLEAREAM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 258 MYAQYIAAQAFNSGGLGVIHSISHAVSAFYDTHHGLNNAIALPRVWAFNMPVAYKRFAEMAEAMGVNTRGMNDVQAADAA 337
Cdd:cd08551 236 LLASLLAGIAFGNAGLGAVHALAYPLGGRYHIPHGVANAILLPYVMEFNLPACPEKYAEIAEALGEDVEGLSDEEAAEAA 315
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1433560031 338 LNAAIRLLRDVGIterfvditkdtysknrlgegPTKFyerrTQIKGDAEDVDAITKHVLGDACTPGN-PKECTFDTVR 414
Cdd:cd08551 316 VEAVRELLRDLGI--------------------PTSL----SELGVTEEDIPELAEDAMKSGRLLSNnPRPLTEEDIR 369
|
|
| Fe-ADH |
pfam00465 |
Iron-containing alcohol dehydrogenase; |
19-413 |
8.77e-100 |
|
Iron-containing alcohol dehydrogenase;
Pssm-ID: 425696 [Multi-domain] Cd Length: 362 Bit Score: 301.83 E-value: 8.77e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 19 PRALMGPGAHEMIGPEALKLGFRkPLVMTS-GLRGTDIVHNIVESLKYHGLDPVLYDEVESNPKDYNTMDSVALYQENSC 97
Cdd:pfam00465 2 TRIVFGAGALAELGEELKRLGAR-ALIVTDpGSLKSGLLDKVLASLEEAGIEVVVFDGVEPEPTLEEVDEAAALAREAGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 98 DSFISIGGGSSHDACKGARVSVAHDGRNVNEFEGFNKSENPnnPPHIAVSTTAGTGSETSWAYVITDtttdPDNPHKYVA 177
Cdd:pfam00465 81 DVIIAVGGGSVIDTAKAIALLLTNPGDVWDYLGGKPLTKPA--LPLIAIPTTAGTGSEVTPLAVITD----TETGEKLGI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 178 FDDACVASLAIDDPVLYYDCPVDYTAQCGFDVLAHASEPYVSRINFEPSLGNALRAIKLTAENLRQATWNGQDLPGREGM 257
Cdd:pfam00465 155 FSPKLLPDLAILDPELTLTLPPRLTAATGMDALAHAVEAYVSKGANPLTDALALEAIRLIAENLPRAVADGEDLEARENM 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 258 MYAQYIAAQAFNSGGLGVIHSISHAVSAFYDTHHGLNNAIALPRVWAFNMPVAYKRFAEMAEAMGVNTrgmnDVQAADAA 337
Cdd:pfam00465 235 LLASTLAGLAFSNAGLGAAHALAHALGGRYGIPHGLANAILLPYVLRFNAPAAPEKLAQLARALGEDS----DEEAAEEA 310
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1433560031 338 LNAAIRLLRDVGIterfvditkdtysknrlgegPTKFyerrTQIKGDAEDVDAITKHVLGDACTPGNPKECTFDTV 413
Cdd:pfam00465 311 IEALRELLRELGL--------------------PTTL----SELGVTEEDLDALAEAALRDRSLANNPRPLTAEDI 362
|
|
| Fe-ADH-like |
cd14863 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
14-414 |
9.86e-91 |
|
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: 279.42 E-value: 9.86e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 14 EFHPFPRALMGPGAHEMIGPEALKLGFRKPLVMT-SGLRGTDIVHNIVESLKYHGLDPVLYDEVESNPKDYNTMDSVALY 92
Cdd:cd14863 1 TYSQLTPVIFGAGAVEQIGELLKELGCKKVLLVTdKGLKKAGIVDKIIDLLEEAGIEVVVFDDVEPDPPDEIVDEAAEIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 93 QENSCDSFISIGGGSSHDACKGARVsVAHDGRNVNEFEGFNKSENPNNPPHIAVSTTAGTGSETSWAYVITDTTTDpdnp 172
Cdd:cd14863 81 REEGADGVIGIGGGSVLDTAKAIAV-LLTNPGPIIDYALAGPPVPKPGIPLIAIPTTAGTGSEVTPIAVITDEENG---- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 173 HKYVAFDDACVASLAIDDPVLYYDCPVDYTAQCGFDVLAHASEPYVSRINFEPSLGNALRAIKLTAENLRQATWNGQDLP 252
Cdd:cd14863 156 VKKSLLGPFLVPDLAILDPELTVGLPPSLTAATGMDALSHAIEAYTSKLANPMTDALALQAIRLIVKNLPRAVKDGDNLE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 253 GREGMMYAQYIAAQAFNSGGLGVIHSISHAVSAFYDTHHGLNNAIALPRVWAFNMPVAYKRFAEMAEAMGVNTRGMNDVQ 332
Cdd:cd14863 236 ARENMLLASNLAGIAFNNAGTHIGHAIAHALGALYHIPHGLACALALPVVLEFNAEAYPEKVKKIAKALGVSFPGESDEE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 333 AADAALNAAIRLLRDVGIterfvditkdtysknrlgegPTKFyerrTQIKGDAEDVDAITKHVLGDACTPGNPKECTFDT 412
Cdd:cd14863 316 LGEAVADAIREFMKELGI--------------------PSLF----EDYGIDKEDLDKIAEAVLKDPFAMFNPRPITEEE 371
|
..
gi 1433560031 413 VR 414
Cdd:cd14863 372 VA 373
|
|
| lactal_redase |
TIGR02638 |
lactaldehyde reductase; This clade of genes encoding iron-containing alcohol dehydrogenase ... |
21-414 |
2.13e-89 |
|
lactaldehyde reductase; This clade of genes encoding iron-containing alcohol dehydrogenase (pfam00465) proteins is generally found in apparent operons for the catabolism of rhamnose or fucose. Catabolism of both of these monosaccharides results in lactaldehyde which is reduced by this enzyme to 1,2 propanediol. This protein is alternatively known by the name 1,2 propanediol oxidoreductase. This enzyme is active under anaerobic conditions in E. coli while being inactivated by reactive oxygen species under aerobic conditions. Under aerobic conditions the lactaldehyde product of rhamnose and fucose catabolism is believed to be oxidized to lactate by a separate enzyme, lactaldehyde dehydrogenase. [Energy metabolism, Sugars]
Pssm-ID: 131686 [Multi-domain] Cd Length: 379 Bit Score: 275.85 E-value: 2.13e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 21 ALMGPGAHEMIGPEALKLGFRKPLVMTSG-LRGTDIVHNIVESLKYHGLDPVLYDEVESNPKDYNTMDSVALYQENSCDS 99
Cdd:TIGR02638 10 SYFGAGAIEDIVDEVKRRGFKKALVVTDKdLIKFGVADKVTDLLDEAGIAYELFDEVKPNPTITVVKAGVAAFKASGADY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 100 FISIGGGSSHDACKGARVSVAHDGRN-VNEFEGFNKSENPNNPPhIAVSTTAGTGSETSWAYVITDTttdpDNPHKYVAF 178
Cdd:TIGR02638 90 LIAIGGGSPIDTAKAIGIISNNPEFAdVRSLEGVAPTKKPGVPI-IAIPTTAGTAAEVTINYVITDE----ENKRKFVCV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 179 DDACVASLAIDDPVLYYDCPVDYTAQCGFDVLAHASEPYVSRINFEPSLGNALRAIKLTAENLRQATWNGQDLPGREGMM 258
Cdd:TIGR02638 165 DPHDIPDVAVIDAEMMYSMPKSLTAATGMDALTHAIEGYITKGAWELTDMLHLKAIEIIARWLRSAVEGGKDLEAREQMA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 259 YAQYIAAQAFNSGGLGVIHSISHAVSAFYDTHHGLNNAIALPRVWAFNMPVAYKRFAEMAEAMGVNTRGMNDVQAADAAL 338
Cdd:TIGR02638 245 LGQYVAGMGFSNVGLGLVHGMAHPLGAFYNTPHGVANAILLPHVMEFNAEFTGEKYREIAKAMGVKTEGMSDEEARDAAV 324
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1433560031 339 NAAIRLLRDVGITERFVDItkdtysknrlgeGPTKfyerrtqikgdaEDVDAITKHVLGDACTPGNPKECTFDTVR 414
Cdd:TIGR02638 325 EAVKTLSKRVGIPEGLSEL------------GVKE------------EDIPALAEAALADVCTGGNPRETTVEEIE 376
|
|
| Fe-ADH-like |
cd08189 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
17-396 |
4.48e-89 |
|
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: 275.12 E-value: 4.48e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 17 PFPRALMGPGAHEMIgPEALK-LGFRKPLVMT-SGLRGTDIVHNIVESLKYHGLDPVLYDEVESNPKDYNTMDSVALYQE 94
Cdd:cd08189 4 PEPELFEGAGSLLQL-PEALKkLGIKRVLIVTdKGLVKLGLLDPLLDALKKAGIEYVVFDGVVPDPTIDNVEEGLALYKE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 95 NSCDSFISIGGGSSHDACKGARVSVAHDGRNVNEFEGFNKSENPNnPPHIAVSTTAGTGSETSWAYVITDTTTdpdnpHK 174
Cdd:cd08189 83 NGCDAIIAIGGGSVIDCAKVIAARAANPKKSVRKLKGLLKVRKKL-PPLIAVPTTAGTGSEATIAAVITDPET-----HE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 175 YVAFDDAC-VASLAIDDPVLYYDCPVDYTAQCGFDVLAHASEPYVSRINFEPSLGNALRAIKLTAENLRQATWNGQDLPG 253
Cdd:cd08189 157 KYAINDPKlIPDAAVLDPELTLGLPPAITAATGMDALTHAVEAYISRSATKETDEYALEAVKLIFENLPKAYEDGSDLEA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 254 REGMMYAQYIAAQAFNSGGLGVIHSISHAVSAFYDTHHGLNNAIALPRVWAFNMPVAYKRFAEMAEAMGVNTRGMNDVQA 333
Cdd:cd08189 237 RENMLLASYYAGLAFTRAYVGYVHAIAHQLGGLYGVPHGLANAVVLPHVLEFYGPAAEKRLAELADAAGLGDSGESDSEK 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1433560031 334 ADAALNAAIRLLRDVGIterfvditkdtysknrlgegPTKFyerrTQIKgdAEDVDAITKHVL 396
Cdd:cd08189 317 AEAFIAAIRELNRRMGI--------------------PTTL----EELK--EEDIPEIAKRAL 353
|
|
| Fe-ADH-like |
cd17814 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
24-406 |
1.65e-86 |
|
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: 268.26 E-value: 1.65e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 24 GPGAHEMIGPEALKLGFRKPLVMT-SGLRGTDIVHNIVESLKYHGLDPVLYDEVESNPKDYNTMDSVALYQENSCDSFIS 102
Cdd:cd17814 10 GVGARKLAGRYAKNLGARKVLVVTdPGVIKAGWVDEVLDSLEAEGLEYVVFSDVTPNPRDFEVMEGAELYREEGCDGIVA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 103 IGGGSSHDACKGARVSVAHdGRNVNEFEGFNKSENPNnPPHIAVSTTAGTGSETSWAYVITDTTTDpdnpHKYVAFDDAC 182
Cdd:cd17814 90 VGGGSPIDCAKGIGIVVSN-GGHILDYEGVDKVRRPL-PPLICIPTTAGSSADVSQFAIITDTERR----VKMAIISKTL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 183 VASLAIDDPVLYYDCPVDYTAQCGFDVLAHASEPYVSRINFEPSLGNALRAIKLTAENLRQATWNGQDLPGREGMMYAQY 262
Cdd:cd17814 164 VPDVSLIDPETLTTMDPELTACTGMDALTHAIEAYVSNASSPLTDLHALEAIRLISENLPKAVADPDDLEAREKMMLASL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 263 IAAQAFNSGGLGVIHSISHAVSAFYDTHHGLNNAIALPRVWAFNMPVAYKRFAEMAEAMGVNTRGMNDVQAADAALNAAI 342
Cdd:cd17814 244 QAGLAFSNASLGAVHAMAHSLGGLLDLPHGECNALLLPHVIRFNFPAAPERYRKIAEAMGLDVDGLDDEEVAERLIEAIR 323
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1433560031 343 RLLRDVGITERFVDItkdtysknrlgeGPTKfyerrtqikgdaEDVDAITKHVLGDACTPGNPK 406
Cdd:cd17814 324 DLREDLGIPETLSEL------------GVDE------------EDIPELAKRAMKDPCLVTNPR 363
|
|
| Fe-ADH-like |
cd08194 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
19-365 |
6.02e-85 |
|
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: 264.39 E-value: 6.02e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 19 PRALMGPGAHEMIGPEALKLGFRKPLVMT-SGLRGTDIVHNIVESLKYHGLDPVLYDEVESNPKDYNTMDSVALYQENSC 97
Cdd:cd08194 2 RTIIIGGGALEELGEEAASLGGKRALIVTdKVMVKLGLVDKVTQLLAEAGIAYAVFDDVVSEPTDEMVEEGLALYKEGGC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 98 DSFISIGGGSSHDACKGARVSVAHDGrNVNEFEGFNKSENPNnPPHIAVSTTAGTGSETSWAYVITDTTTDpdnpHKYVA 177
Cdd:cd08194 82 DFIVALGGGSPIDTAKAIAVLATNGG-PIRDYMGPRKVDKPG-LPLIAIPTTAGTGSEVTRFTVITDTETD----VKMLL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 178 FDDACVASLAIDDPVLYYDCPVDYTAQCGFDVLAHASEPYVSRINFEPSLGNALRAIKLTAENLRQATWNGQDLPGREGM 257
Cdd:cd08194 156 KGPALLPAVAIVDPELTLSMPPRVTAATGIDALTHAIEAYVSRKAQPLTDTLALSAIKLIGRNLRRAYADGDDLEAREAM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 258 MYAQYIAAQAFNSGGLGVIHSISHAVSAFYDTHHGLNNAIALPRVWAFNMPVAYKRFAEMAEAMGVNTRGMNDVQAADAA 337
Cdd:cd08194 236 MLAALEAGIAFSNSSVALVHGMSRPIGALFHVPHGLSNAMLLPAVTEFSLPGAPERYAEIARAMGIATEGDSDEEAAEKL 315
|
330 340
....*....|....*....|....*....
gi 1433560031 338 LNAAIRLLRDVGI-TERFVDITKDTYSKN 365
Cdd:cd08194 316 VEALERLCADLEIpTLREYGIDEEEFEAA 344
|
|
| Fe-ADH-like |
cd14861 |
Iron-containing alcohol dehydrogenases-like; This family contains proteins similar to ... |
18-421 |
3.81e-83 |
|
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: 259.75 E-value: 3.81e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 18 FPRALMGPGA-HEMigPEALK-LGFRKPLVMTS-GLRGTDIVHNIVESLKYHGLDPVLYDEVESNPKDYNTMDSVALYQE 94
Cdd:cd14861 3 PTRIRFGAGAiAEL--PEELKaLGIRRPLLVTDpGLAALGIVDRVLEALGAAGLSPAVFSDVPPNPTEADVEAGVAAYRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 95 NSCDSFISIGGGSSHDACKGARVSVAHDGRnVNEFE---GFNKSENPNNPPHIAVSTTAGTGSETSWAYVITDTTTDPdn 171
Cdd:cd14861 81 GGCDGIIALGGGSAIDAAKAIALMATHPGP-LWDYEdgeGGPAAITPAVPPLIAIPTTAGTGSEVGRAAVITDDDTGR-- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 172 phKYVAFDDACVASLAIDDPVLYYDCPVDYTAQCGFDVLAHASEPYVSRINFEPSLGNALRAIKLTAENLRQATWNGQDL 251
Cdd:cd14861 158 --KKIIFSPKLLPKVAICDPELTLGLPPRLTAATGMDALTHCIEAYLSPGFHPMADGIALEGLRLISEWLPRAVADGSDL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 252 PGREGMMYAQYIAAQAFnSGGLGVIHSISHAVSAFYDTHHGLNNAIALPRVWAFNMPVAYKRFAEMAEAMGVNTRGMNDV 331
Cdd:cd14861 236 EARGEMMMAALMGAVAF-QKGLGAVHALAHALGALYGLHHGLLNAILLPYVLRFNRPAVEDKLARLARALGLGLGGFDDF 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 332 qaadaaLNAAIRLLRDVGITerfvditkdtyskNRLGEgptkfyerrtqIKGDAEDVDAITKHVLGDACTPGNPKECTFD 411
Cdd:cd14861 315 ------IAWVEDLNERLGLP-------------ATLSE-----------LGVTEDDLDELAELALADPCHATNPRPVTAE 364
|
410
....*....|
gi 1433560031 412 TVRPVVEHCM 421
Cdd:cd14861 365 DYRALLREAL 374
|
|
| PRK10624 |
PRK10624 |
L-1,2-propanediol oxidoreductase; Provisional |
24-409 |
6.63e-78 |
|
L-1,2-propanediol oxidoreductase; Provisional
Pssm-ID: 182595 [Multi-domain] Cd Length: 382 Bit Score: 246.45 E-value: 6.63e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 24 GPGAHEMIGPEALKLGFRKPLVMT-SGLRGTDIVHNIVESLKYHGLDPVLYDEVESNPKDYNTMDSVALYQENSCDSFIS 102
Cdd:PRK10624 14 GRGAIGALTDEVKRRGFKKALIVTdKTLVKCGVVAKVTDVLDAAGLAYEIYDGVKPNPTIEVVKEGVEVFKASGADYLIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 103 IGGGSSHDACKGARVSVAH-DGRNVNEFEGFNKSENPNNPPhIAVSTTAGTGSETSWAYVITDtttdPDNPHKYVAFDDA 181
Cdd:PRK10624 94 IGGGSPQDTCKAIGIISNNpEFADVRSLEGVAPTKKPSVPI-IAIPTTAGTAAEVTINYVITD----EEKRRKFVCVDPH 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 182 CVASLAIDDPVLYYDCPVDYTAQCGFDVLAHASEPYVSRINFEPSLGNALRAIKLTAENLRQATWNgqDLPGREGMMYAQ 261
Cdd:PRK10624 169 DIPQVAFVDADMMDSMPPGLKAATGVDALTHAIEGYITRGAWALTDMLHLKAIEIIAGALRGAVAG--DKEAGEGMALGQ 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 262 YIAAQAFNSGGLGVIHSISHAVSAFYDTHHGLNNAIALPRVWAFNMPVAYKRFAEMAEAMGVNTRGMNDVQAADAALNAA 341
Cdd:PRK10624 247 YIAGMGFSNVGLGLVHGMAHPLGAFYNTPHGVANAILLPHVMEYNADFTGEKYRDIARAMGVKVEGMSLEEARNAAVEAV 326
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1433560031 342 IRLLRDVGIterfvditkdtysknrlgegPTKFYErrtqIKGDAEDVDAITKHVLGDACTPGNPKECT 409
Cdd:PRK10624 327 KALNRDVGI--------------------PPHLRD----VGVKEEDIPALAQAAFDDVCTGGNPREAT 370
|
|
| Fe-ADH-like |
cd14865 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
14-418 |
3.70e-77 |
|
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: 244.76 E-value: 3.70e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 14 EFHPFPRALMGPGAHEMIGPEALKLGFRKPLVMTS-GLRGTDIVHNIVESLKYHGLDPVLYDEVESNPkDYNTMDSVA-L 91
Cdd:cd14865 2 EFFNPTKIVSGAGALENLPAELARLGARRPLIVTDkGLAAAGLLKKVEDALGDAIEIVGVFDDVPPDS-SVAVVNEAAaR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 92 YQENSCDSFISIGGGSSHDACKGARVSVAHDGRNVNEFEGFNKSENPNnPPHIAVSTTAGTGSETSWAYVITDTTTdpdn 171
Cdd:cd14865 81 AREAGADGIIAVGGGSVIDTAKGVNILLSEGGDDLDDYGGANRLTRPL-KPLIAIPTTAGTGSEVTLVAVIKDEEK---- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 172 pHKYVAF-DDACVASLAIDDPVLYYDCPVDYTAQCGFDVLAHASEPYVSrINFEP-SLGNALRAIKLTAENLRQATWNGQ 249
Cdd:cd14865 156 -KVKLLFvSPFLLPDVAILDPRLTLSLPPKLTAATGMDALTHAIEAYTS-LQKNPiSDALALQAIRLISENLPKAVKNGK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 250 DLPGREGMMYAQYIAAQAFNSGGLGVIHSISHAVSAFYDTHHGLNNAIALPRVWAFNMPVAYKRFAEMAEAM--GVNTRG 327
Cdd:cd14865 234 DLEARLALAIAATMAGIAFSNSMVGLVHAIAHAVGAVAGVPHGLANSILLPHVMRYNLDAAAERYAELALALayGVTPAG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 328 MNDVQAADAALNAAIRLLRDVGIterfvditkdtysknrlgegPTKFyeRRTQIKgdAEDVDAITKHVLGDACTPGNPKE 407
Cdd:cd14865 314 RRAEEAIEAAIDLVRRLHELCGL--------------------PTRL--RDVGVP--EEQLEAIAELALNDGAILFNPRE 369
|
410
....*....|.
gi 1433560031 408 CTFDTVRPVVE 418
Cdd:cd14865 370 VDPEDILAILE 380
|
|
| HOT |
cd08190 |
Hydroxyacid-oxoacid transhydrogenase (HOT) involved in gamma-hydroxybutyrate metabolism; This ... |
24-351 |
2.24e-67 |
|
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: 220.11 E-value: 2.24e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 24 GPGAHEMIGPEALKLGFRKPLVMT-SGLRGTDIVHNIVESLKYHGLDPVLYDEVESNPKDYNTMDSVALYQENSCDSFIS 102
Cdd:cd08190 7 GPGATRELGMDLKRLGAKKVLVVTdPGLAKLGLVERVLESLEKAGIEVVVYDGVRVEPTDESFEEAIEFAKEGDFDAFVA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 103 IGGGSSHDACKGARVSVAHDGRN---VNEFEGfnKSENPNNP--PHIAVSTTAGTGSETSWAYVItdttTDPDNPHKYVA 177
Cdd:cd08190 87 VGGGSVIDTAKAANLYATHPGDFldyVNAPIG--KGKPVPGPlkPLIAIPTTAGTGSETTGVAIF----DLEELKVKTGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 178 FDDACVASLAIDDPVLYYDCPVDYTAQCGFDVLAHASE-----PYVSRINFEPSLGN-------------ALRAIKLTAE 239
Cdd:cd08190 161 SSRYLRPTLAIVDPLLTLTLPPRVTASSGFDVLCHALEsytarPYNARPRPANPDERpayqgsnpisdvwAEKAIELIGK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 240 NLRQATWNGQDLPGREGMMYAQYIAAQAFNSGGLGVIHSISHAVS--------AFYDTH-----HGLNNAIALPRVWAFN 306
Cdd:cd08190 241 YLRRAVNDGDDLEARSNMLLASTLAGIGFGNAGVHLPHAMAYPIAglvkdyrpPGYPVDhphvpHGLSVALTAPAVFRFT 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1433560031 307 MPVAYKRFAEMAEAMGVNTRGMNDVQAADAALNAAIRLLRDVGIT 351
Cdd:cd08190 321 APACPERHLEAAELLGADTSGASDRDAGEVLADALIKLMRDIGIP 365
|
|
| PRK09860 |
PRK09860 |
putative alcohol dehydrogenase; Provisional |
30-421 |
2.31e-67 |
|
putative alcohol dehydrogenase; Provisional
Pssm-ID: 182118 [Multi-domain] Cd Length: 383 Bit Score: 219.44 E-value: 2.31e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 30 MIGPEALK--------LGFRKPLVMTSG-LRGTDIVHNIVESLKYHGLDPVLYDEVESNPKDYNTMDSVALYQENSCDSF 100
Cdd:PRK09860 13 VIGADSLTdamnmmadYGFTRTLIVTDNmLTKLGMAGDVQKALEERNIFSVIYDGTQPNPTTENVAAGLKLLKENNCDSV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 101 ISIGGGSSHDACKGARVsVAHDGRNVNEFEGFNKSENPNnPPHIAVSTTAGTGSETSWAYVITDTTTdpdnpHKYVAFDD 180
Cdd:PRK09860 93 ISLGGGSPHDCAKGIAL-VAANGGDIRDYEGVDRSAKPQ-LPMIAINTTAGTASEMTRFCIITDEAR-----HIKMAIVD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 181 ACVAS-LAIDDPVLYYDCPVDYTAQCGFDVLAHASEPYVSRINFEPSLGNALRAIKLTAENLRQATWNGQDLPGREGMMY 259
Cdd:PRK09860 166 KHVTPlLSVNDSSLMIGMPKSLTAATGMDALTHAIEAYVSIAATPITDACALKAVTMIAENLPLAVEDGSNAKAREAMAY 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 260 AQYIAAQAFNSGGLGVIHSISHAVSAFYDTHHGLNNAIALPRVWAFNMPVAYKRFAEMAEAMGVNTRGMNDVQAADAALN 339
Cdd:PRK09860 246 AQFLAGMAFNNASLGYVHAMAHQLGGFYNLPHGVCNAVLLPHVQVFNSKVAAARLRDCAAAMGVNVTGKNDAEGAEACIN 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 340 AAIRLLRDVGIterfvditkdtysknrlgegPTKFYERRTQikgdAEDVDAITKHVLGDACTPGNPKECTFDTVRPVVEH 419
Cdd:PRK09860 326 AIRELAKKVDI--------------------PAGLRDLNVK----EEDFAVLATNALKDACGFTNPIQATHEEIVAIYRA 381
|
..
gi 1433560031 420 CM 421
Cdd:PRK09860 382 AM 383
|
|
| Fe-ADH-like |
cd08185 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
20-414 |
9.92e-66 |
|
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: 214.67 E-value: 9.92e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 20 RALMGPGAHEMIGPEALKLGfRKPLVMTSG--LRGTDIVHNIVESLKYHGLDPVLYDEVESNPKDYNTMDSVALYQENSC 97
Cdd:cd08185 6 RILFGAGKLNELGEEALRPG-KKALIVTGKgsSKKTGLLDRVKKLLEKAGVEVVVFDKVEPNPLTTTVMEGAALAKEEGC 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 98 DSFISIGGGSSHDACKGARVSVAHDGrNVNE--FEGFNKSENPNNP-PHIAVSTTAGTGSETSWAYVITDtttdPDNPHK 174
Cdd:cd08185 85 DFVIGLGGGSSMDAAKAIAFMATNPG-DIWDyiFGGTGKGPPPEKAlPIIAIPTTAGTGSEVDPWAVITN----PETKEK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 175 YVAFDDACVASLAIDDPVLYYDCPVDYTAQCGFDVLAHASEPYVSRINFEPSLGNALRAIKLTAENLRQATWNGQDLPGR 254
Cdd:cd08185 160 KGIGHPALFPKVSIVDPELMLTVPPRVTAYTGFDALFHAFESYISKNANPFSDMLALEAIRLVAKYLPRAVKDGSDLEAR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 255 EGMMYAQYIAAQAFNSGGLGVIHSISHAVSAFY-DTHHGLNNAIALPRVWAFNMPVAYKRFAEMAEAmgvNTRGMNDVQA 333
Cdd:cd08185 240 EKMAWASTLAGIVIANSGTTLPHGLEHPLSGYHpNIPHGAGLAALYPAYFEFTIEKAPEKFAFVARA---EASGLSDAKA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 334 ADAALNAAIRLLRDVGiterfVDITKDTYsknrlgeGPTKfyerrtqikgdaEDVDAITKHVLGdacTPG-----NPKEC 408
Cdd:cd08185 317 AEDFIEALRKLLKDIG-----LDDLLSDL-------GVTE------------EDIPWLAENAME---TMGglfanNPVEL 369
|
....*.
gi 1433560031 409 TFDTVR 414
Cdd:cd08185 370 TEEDIV 375
|
|
| Fe-ADH-like |
cd08191 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
19-357 |
8.54e-57 |
|
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: 192.06 E-value: 8.54e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 19 PRALMGPGAHEMIGPEALKLGFRKPLVMTSGLRGTDIVHNIVESLKYHGLDPVLYDEVESNPKDYNTMDSVALYQENSCD 98
Cdd:cd08191 5 SRLLFGPGARRALGRVAARLGSRVLIVTDPRLASTPLVAELLAALTAAGVAVEVFDGGQPELPVSTVADAAAAARAFDPD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 99 SFISIGGGSSHDACKGARVSVAHDGrNVNEFEGFNKSENPNNPPhIAVSTTAGTGSETSWAYVITDtttdPDNPHKYVAF 178
Cdd:cd08191 85 VVIGLGGGSNMDLAKVVALLLAHGG-DPRDYYGEDRVPGPVLPL-IAVPTTAGTGSEVTPVAVLTD----PARGMKVGVS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 179 DDACVASLAIDDPVLYYDCPVDYTAQCGFDVLAHASEPYVSRiNFEPSLGN----------------ALRAIKLTAENLR 242
Cdd:cd08191 159 SPYLRPAVAIVDPELTLTCPPGVTADSGIDALTHAIESYTAR-DFPPFPRLdpdpvyvgknpltdllALEAIRLIGRHLP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 243 QATWNGQDLPGREGMMYAQYIAAQAFNSGGLGVIHSISHAVSAFYDTHHGLNNAIALPRVWAFNMPVAYKRFAEMAEAMG 322
Cdd:cd08191 238 RAVRDGDDLEARSGMALAALLAGLAFGTAGTAAAHALQYPIGALTHTSHGVGNGLLLPYVMRFNRPARAAELAEIARALG 317
|
330 340 350
....*....|....*....|....*....|....*
gi 1433560031 323 VNTRGMNDvQAADAALNAAIRLLRDVGITERFVDI 357
Cdd:cd08191 318 VTTAGTSE-EAADRAIERVEELLARIGIPTTLADL 351
|
|
| NADPH_BDH |
cd08179 |
NADPH-dependent butanol dehydrogenase involved in the butanol and ethanol formation pathway in ... |
19-420 |
3.88e-53 |
|
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: 182.00 E-value: 3.88e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 19 PRAL-MGPGAHEmigpeALK-LGFRKPLVMTSG--LRGTDIVHNIVESLKYHGLDPVLYDEVESNPkdynTMDSV----A 90
Cdd:cd08179 5 PRDIyFGEGALE-----YLKtLKGKRAFIVTGGgsMKRNGFLDKVEDYLKEAGMEVKVFEGVEPDP----SVETVekgaE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 91 LYQENSCDSFISIGGGSSHDACKGARVSVAHDGRNVNE-FEGFNKSENPNNPPHIAVSTTAGTGSETSWAYVITDTttdp 169
Cdd:cd08179 76 AMREFEPDWIIAIGGGSVIDAAKAMWVFYEYPELTFEDaLVPFPLPELRKKARFIAIPSTSGTGSEVTRASVITDT---- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 170 DNPHKYVAFDDACVASLAIDDPVLYYDCPVDYTAQCGFDVLAHASEPYVSRIN--FEPSLgnALRAIKLTAENLRQATWN 247
Cdd:cd08179 152 EKGIKYPLASFEITPDVAILDPELTMTMPPHVTANTGMDALTHAIEAYVSTLAndFTDAL--ALGAILDIFENLPKSYNG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 248 GQDLPGREGMMYAQYIAAQAFNSGGLGVIHSISHAVSAFYDTHHGLNNAIALPRVWAFNMP------VAYKRFAEMAEAM 321
Cdd:cd08179 230 GKDLEAREKMHNASCLAGMAFSNSGLGIVHSMAHKGGAFFGIPHGLANAILLPYVIEFNSKdpearaRYAALLIGLTDEE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 322 GVNT-----RGMNDvqaadaalnaaiRL-----LRDVGITErfvditkDTYSKNrlgegptkfyerrtqikgdaedVDAI 391
Cdd:cd08179 310 LVEDlieaiEELNK------------KLgiplsFKEAGIDE-------DEFFAK----------------------LDEM 348
|
410 420
....*....|....*....|....*....
gi 1433560031 392 TKHVLGDACTPGNPKECTFDTVRPVVEHC 420
Cdd:cd08179 349 AENAMNDACTGTNPRKPTVEEMKELLKAA 377
|
|
| Fe-ADH-like |
cd14862 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
18-405 |
3.13e-52 |
|
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: 179.34 E-value: 3.13e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 18 FPRALMGPGAhemiGPEALKLGFRKPLVMT-SGLRGTDIVHNIVESLKYHGLDPVLYDEVESNPKDYNTMDSVALYQENS 96
Cdd:cd14862 6 SPKIVFGEDA----LSHLEQLSGKRALIVTdKVLVKLGLLKKVLKRLLQAGFEVEVFDEVEPEPPLETVLKGAEAMREFE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 97 CDSFISIGGGSSHDACKGARVsvahdgrnvnefegfnKSENPNNPPH----------------IAVSTTAGTGSETSWAY 160
Cdd:cd14862 82 PDLIIALGGGSVMDAAKAAWV----------------LYERPDLDPEdispldllglrkkaklIAIPTTSGTGSEATWAI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 161 VITDTTtdpdNPHKYVAFDDACVASLAIDDPVLYYDCPVDYTAQCGFDVLAHASEPYVSRINFEPSLGNALRAIKLTAEN 240
Cdd:cd14862 146 VLTDTE----EPRKIAVANPELVPDVAILDPEFVLGMPPKLTAGTGLDALAHAVEAYLSTWSNDFSDALALKAIELIFKY 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 241 LRQATWNGQDLPGREGMMYAQYIAAQAFNSGGLGVIHSISHAVSAFYDTHHGLNNAIALPRVWAFNMPVAYKRFAEMAEA 320
Cdd:cd14862 222 LPRAYKDGDDLEAREKMHNAATIAGLAFGNSQAGLAHALGHSLGAVFHVPHGIAVGLFLPYVIEFYAKVTDERYDLLKLL 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 321 mGVNTRgmnDVQAADAALNAAIR-LLRDVGITERFVD--ITKDTYSKNrlgegptkfyerrtqikgdaedVDAITKHVLG 397
Cdd:cd14862 302 -GIEAR---DEEEALKKLVEAIReLYKEVGQPLSIKDlgISEEEFEEK----------------------LDELVEYAME 355
|
....*...
gi 1433560031 398 DACTPGNP 405
Cdd:cd14862 356 DSCTITSP 363
|
|
| AAD_C |
cd08178 |
C-terminal alcohol dehydrogenase domain of the acetaldehyde dehydrogenase-alcohol ... |
33-406 |
5.77e-52 |
|
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: 179.30 E-value: 5.77e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 33 PEALK--LGFRKPLVMTS-GLRGTDIVHNIVESLKYHGLDPVLYDEVESNPKDYNTMDSVALYQENSCDSFISIGGGSSH 109
Cdd:cd08178 14 PYLLLelPGVKRAFIVTDrVLYKLGYVDKVLDVLEARGVETEVFSDVEPDPTLSTVRKGLEAMNAFKPDVIIALGGGSAM 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 110 DACKGARVSVAHDGRNVNEFEG--FNKSENPNNPPH-------IAVSTTAGTGSE-TSWAyVITDTTTdpdnPHKYVAFD 179
Cdd:cd08178 94 DAAKIMWLFYEHPETKFEDLAQrfMDIRKRVYKFPKlgkkaklVAIPTTSGTGSEvTPFA-VITDDKT----GKKYPLAD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 180 DACVASLAIDDPVLYYDCPVDYTAQCGFDVLAHASEPYVSRINFEPSLGNALRAIKLTAENLRQATWNGQDLPGREGMMY 259
Cdd:cd08178 169 YALTPDMAIVDPELVMTMPKRLTADTGIDALTHAIEAYVSVMASDYTDGLALQAIKLIFEYLPRSYNNGNDIEAREKMHN 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 260 AQYIAAQAFNSGGLGVIHSISHAVSAFYDTHHGLNNAIALPRVWAFNM---------------PVAYKRFAEMAEAMGVn 324
Cdd:cd08178 249 AATIAGMAFANAFLGICHSLAHKLGAAFHIPHGRANAILLPHVIRYNAtdpptkqaafpqykyYVAKERYAEIADLLGL- 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 325 tRGMNDVQAADAALNAAIRLLRDVGITERFVD--ITKDTYSKNrlgegptkfyerrtqikgdaedVDAITKHVLGDACTP 402
Cdd:cd08178 328 -GGKTPEEKVESLIKAIEDLKKDLGIPTSIREagIDEADFLAA----------------------VDKLAEDAFDDQCTG 384
|
....
gi 1433560031 403 GNPK 406
Cdd:cd08178 385 ANPR 388
|
|
| HVD |
cd08193 |
5-hydroxyvalerate dehydrogenase (HVD) catalyzes the oxidation of 5-hydroxyvalerate to ... |
15-360 |
2.09e-51 |
|
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: 177.32 E-value: 2.09e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 15 FHPFPRALMGPGAHEMIGPEALKLGFRKPLVMT-SGLRGTDIVHNIVESLKYHGLDPVLYDEVESNPKDYNTMDSVALYQ 93
Cdd:cd08193 1 FQTVPRIICGAGAAARLGELLRELGARRVLLVTdPGLVKAGLADPALAALEAAGIAVTVFDDVVADPPEAVVEAAVEQAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 94 ENSCDSFISIGGGSSHDACKGARVsVAHDGRNVNEFEGFNKSENPNnPPHIAVSTTAGTGSETSWAYVITDTTTDpdnph 173
Cdd:cd08193 81 EAGADGVIGFGGGSSMDVAKLVAL-LAGSDQPLDDIYGVGKATGPR-LPLILVPTTAGTGSEVTPISIVTTGETE----- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 174 KYVAFDDACVASLAIDDPVLYYDCPVDYTAQCGFDVLAHASEPYVSRINFEP-SLGNALRAIKLTAENLRQATWNGQDLP 252
Cdd:cd08193 154 KKGVVSPQLLPDVALLDAELTLGLPPHVTAATGIDAMVHAIEAYTSRHKKNPiSDALAREALRLLGANLRRAVEDGSDLE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 253 GREGMMYAQYIAAQAFNSGGLGVIHSISHAVSAFYDTHHGLNNAIALPRVWAFNMPVAYKRFAEMAEAMGVNTRGMNDVQ 332
Cdd:cd08193 234 AREAMLLGSMLAGQAFANAPVAAVHALAYPLGGHFHVPHGLSNALVLPHVLRFNLPAAEALYAELARALLPGLAFGSDAA 313
|
330 340 350
....*....|....*....|....*....|
gi 1433560031 333 AADAALNAAIRLLRDVGITERF--VDITKD 360
Cdd:cd08193 314 AAEAFIDALEELVEASGLPTRLrdVGVTEE 343
|
|
| Fe-ADH-like |
cd08196 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
24-371 |
1.95e-50 |
|
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: 174.30 E-value: 1.95e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 24 GPGAHEMIGPEALKLGFRKPLVMTSG-LRGTDIVHNIVESLKyhGLDPVLYDEVESNPKDYNTMDSVALYQENSCDSFIS 102
Cdd:cd08196 12 GEGILKELPDIIKELGGKRGLLVTDPsFIKSGLAKRIVESLK--GRIVAVFSDVEPNPTVENVDKCARLARENGADFVIA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 103 IGGGSSHDACKGARVSVAHDGrNVNEFEGfNKSENPNNP-PHIAVSTTAGTGSE-TSWAyVITDTttdpDNPHKYVAFDD 180
Cdd:cd08196 90 IGGGSVLDTAKAAACLAKTDG-SIEDYLE-GKKKIPKKGlPLIAIPTTAGTGSEvTPVA-VLTDK----EKGKKAPLVSP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 181 ACVASLAIDDPVLYYDCPVDYTAQCGFDVLAHASEPYVSrINFEP-SLGNALRAIKLTAENLRQATWNGQDLPGREGMMY 259
Cdd:cd08196 163 GFYPDIAIVDPELTYSMPPKVTASTGIDALCHAIEAYWS-INHQPiSDALALEAAKLVLENLEKAYNNPNDKEAREKMAL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 260 AQYIAAQAFNSGGLGVIHSISHAVSAFYDTHHGLNNAIALPRVWAFNMPVAYKRFAEMAEAMGVNTrgMNDVQAADAALN 339
Cdd:cd08196 242 ASLLAGLAFSQTRTTASHACSYPLTSHFGIPHGEACALTLPSFIRLNAEALPGRLDELAKQLGFKD--AEELADKIEELK 319
|
330 340 350
....*....|....*....|....*....|....*.
gi 1433560031 340 AAIRL---LRDVGITERFVD-ITKDTYSKNRLGEGP 371
Cdd:cd08196 320 KRIGLrtrLSELGITEEDLEeIVEESFHPNRANNNP 355
|
|
| Fe-ADH-like |
cd08183 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
19-320 |
3.68e-47 |
|
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: 166.14 E-value: 3.68e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 19 PRALMGPGAHEMIGPEALKLGfRKPLVMT-SGLRGTDIVHNIVESLKYHGLDPVLYDeVESNPKDYNTMDSVALYQENSC 97
Cdd:cd08183 2 PRIVFGRGSLQELGELAAELG-KRALLVTgRSSLRSGRLARLLEALEAAGIEVALFS-VSGEPTVETVDAAVALAREAGC 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 98 DSFISIGGGSSHDACKGARVSVAHDGRNVNEFEGFNKSENPNNP--PHIAVSTTAGTGSE-TSWAyVITDtttdPDNPHK 174
Cdd:cd08183 80 DVVIAIGGGSVIDAAKAIAALLTNEGSVLDYLEVVGKGRPLTEPplPFIAIPTTAGTGSEvTKNA-VLSS----PEHGVK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 175 yVAF-DDACVASLAIDDPVLYYDCPVDYTAQCGFDVLAHASEPYVSRinfepsLGN------ALRAIKLTAENLRQATWN 247
Cdd:cd08183 155 -VSLrSPSMLPDVALVDPELTLSLPPEVTAASGLDALTQLIEPYVSR------KANpltdalAREGLRLAARSLRRAYED 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 248 GQDLPGREGMMYAQYIAAQAFNSGGLGVIHSISHAVSAFYDTHHGLNNAIALPRVWAFNMPV---------AYKRFAEMA 318
Cdd:cd08183 228 GEDLEAREDMALASLLGGLALANAGLGAVHGLAGPLGGMFGAPHGAICAALLPPVLEANLRAlrerepdspALARYRELA 307
|
..
gi 1433560031 319 EA 320
Cdd:cd08183 308 GI 309
|
|
| PRK15454 |
PRK15454 |
ethanolamine utilization ethanol dehydrogenase EutG; |
12-357 |
1.11e-44 |
|
ethanolamine utilization ethanol dehydrogenase EutG;
Pssm-ID: 185351 [Multi-domain] Cd Length: 395 Bit Score: 159.81 E-value: 1.11e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 12 LKEFHPFPRALMGPGAHEMIGPEALKLGFRKPLVMT-SGLRGTDIVHNIVESLKYHGLDPVLYDEVESNPKDYNTMDSVA 90
Cdd:PRK15454 21 VKTFSVPPVTLCGPGAVSSCGQQAQTRGLKHLFVMAdSFLHQAGMTAGLTRSLAVKGIAMTLWPCPVGEPCITDVCAAVA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 91 LYQENSCDSFISIGGGSSHDACKGARVSVAHDGRNVNEFEgfNKSENPNNPPHIAVSTTAGTGSETSWAYVITDTTTDpd 170
Cdd:PRK15454 101 QLRESGCDGVIAFGGGSVLDAAKAVALLVTNPDSTLAEMS--ETSVLQPRLPLIAIPTTAGTGSETTNVTVIIDAVSG-- 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 171 npHKYVAFDDACVASLAIDDPVLYYDCPVDYTAQCGFDVLAHASEPYVSR--INFEPSLgnALRAIKLTAENLRQATWNG 248
Cdd:PRK15454 177 --RKQVLAHASLMPDVAILDAALTEGVPSHVTAMTGIDALTHAIEAYSALnaTPFTDSL--AIGAIAMIGKSLPKAVGYG 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 249 QDLPGREGMMYAQYIAAQAFNSGGLGVIHSISHAVSAFYDTHHGLNNAIALPRVWAFNMPVAYKRFAEMAEAMgvNTRGM 328
Cdd:PRK15454 253 HDLAARESMLLASCMAGMAFSSAGLGLCHAMAHQPGAALHIPHGLANAMLLPTVMEFNRMVCRERFSQIGRAL--RTKKS 330
|
330 340
....*....|....*....|....*....
gi 1433560031 329 NDVQAADAALnaaiRLLRDVGITERFVDI 357
Cdd:PRK15454 331 DDRDAINAVS----ELIAEVGIGKRLGDV 355
|
|
| PDD |
cd08180 |
1,3-propanediol dehydrogenase (PPD) catalyzes the reduction of 3-hydroxypropionaldehyde (3-HPA) ... |
19-409 |
1.25e-44 |
|
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: 158.04 E-value: 1.25e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 19 PRALMGPGAHEMIGpealKLGFRKPLVMT-SGLRGTDIVHNIVESL----KYHgldpvLYDEVESNPKDYNTMDSVALYQ 93
Cdd:cd08180 5 TKIYSGEDSLERLK----ELKGKRVFIVTdPFMVKSGMVDKVTDELdksnEVE-----IFSDVVPDPSIEVVAKGLAKIL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 94 ENSCDSFISIGGGSSHDACKGARvsvahdgrnvneFEGFNKSENPNNPPHIAVSTTAGTGSE-TSWAyVITDtttdPDNP 172
Cdd:cd08180 76 EFKPDTIIALGGGSAIDAAKAII------------YFALKQKGNIKKPLFIAIPTTSGTGSEvTSFA-VITD----PEKG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 173 HKYVAFDDACVASLAIDDPVLYYDCPVDYTAQCGFDVLAHASEPYVSRI--NFEPSLgnALRAIKLTAENLRQATWNGQD 250
Cdd:cd08180 139 IKYPLVDDSMLPDIAILDPELVKSVPPKVTADTGMDVLTHALEAYVSTNanDFTDAL--AEKAIKLVFENLPRAYRDGDD 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 251 LPGREGMMYAQYIAAQAFNSGGLGVIHSISHAVSAFYDTHHGLNNAIALPRVWAFnMPVAYKRfaeMAEAMGVNTRgmnd 330
Cdd:cd08180 217 LEAREKMHNASCMAGIAFNNAGLGINHSLAHALGGRFHIPHGRANAILLPYVIEF-LIAAIRR---LNKKLGIPST---- 288
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1433560031 331 vqaadaalnaairlLRDVGITErfvditkDTYsknrlgegptkfyerrtqikgdAEDVDAITKHVLGDACTPGNPKECT 409
Cdd:cd08180 289 --------------LKELGIDE-------EEF----------------------EKAIDEMAEAALADRCTATNPRKPT 324
|
|
| HEPD |
cd08182 |
Hydroxyethylphosphoate dehydrogenase (HEPD) catalyzes the reduction of phosphonoacetaldehyde ... |
20-325 |
5.87e-43 |
|
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: 154.69 E-value: 5.87e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 20 RALMGPGAHEMIGPEALKLGFRKP-LVMTSGLRGTDIVHNIVESLKyHGLDPVLYDEVESNPkDYNTMDS-VALYQENSC 97
Cdd:cd08182 3 KIIFGPGALAELKDLLGGLGARRVlLVTGPSAVRESGAADILDALG-GRIPVVVFSDFSPNP-DLEDLERgIELFRESGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 98 DSFISIGGGSSHDACKGARVSVAHDGRNVNEFEGFNKSENPNNPPHIAVSTTAGTGSE-TSWAyVITDTTTDpdnpHKY- 175
Cdd:cd08182 81 DVIIAVGGGSVIDTAKAIAALLGSPGENLLLLRTGEKAPEENALPLIAIPTTAGTGSEvTPFA-TIWDEAEG----KKYs 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 176 VAfDDACVASLAIDDPVLYYDCPVDYTAQCGFDVLAHASEPYVSRINFEPSLGNALRAIKLTAENLRQATWNGQDLPGRE 255
Cdd:cd08182 156 LA-HPSLYPDAAILDPELTLSLPLYLTASTGLDALSHAIESIWSVNANPESRAYALRAIRLILENLPLLLENLPNLEARE 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1433560031 256 GMMYAQYIAAQAFNSGGLGVIHSISHAVSAFYDTHHGLNNAIALPRVWAFNMPV-----AYKRFAEMAEAMGVNT 325
Cdd:cd08182 235 AMAEASLLAGLAISITKTTAAHAISYPLTSRYGVPHGHACALTLPAVLRYNAGAddecdDDPRGREILLALGASD 309
|
|
| PRK13805 |
PRK13805 |
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional |
56-407 |
2.14e-41 |
|
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional
Pssm-ID: 237515 [Multi-domain] Cd Length: 862 Bit Score: 156.50 E-value: 2.14e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 56 VHNIVESLKYHGLDPV--LYDEVESNPKDYNTMDSVALYQENSCDSFISIGGGSSHDACKGARVSVAHDGRnvnEFEG-- 131
Cdd:PRK13805 497 VDKVTDVLKKRENGVEyeVFSEVEPDPTLSTVRKGAELMRSFKPDTIIALGGGSPMDAAKIMWLFYEHPET---DFEDla 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 132 ----------FNKSENPNNPPHIAVSTTAGTGSE-TSWAyVITDTTTDpdnpHKYVAFDDACVASLAIDDPVLYYDCPVD 200
Cdd:PRK13805 574 qkfmdirkriYKFPKLGKKAKLVAIPTTSGTGSEvTPFA-VITDDKTG----VKYPLADYELTPDVAIVDPNLVMTMPKS 648
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 201 YTAQCGFDVLAHASEPYVSRINFEPSLGNALRAIKLTAENLRQATWNG-QDLPGREGMMYAQYIAAQAFNSGGLGVIHSI 279
Cdd:PRK13805 649 LTADTGIDALTHALEAYVSVMASDYTDGLALQAIKLVFEYLPRSYKNGaKDPEAREKMHNASTIAGMAFANAFLGICHSM 728
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 280 SHAVSAFYDTHHGLNNAIALPRVWAFN--------------MPVAYKRFAEMAEAMGVntRGMNDVQAADAALNAAIRLL 345
Cdd:PRK13805 729 AHKLGAEFHIPHGRANAILLPHVIRYNatdppkqaafpqyeYPRADERYAEIARHLGL--PGSTTEEKVESLIKAIEELK 806
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1433560031 346 RDVGITERFVDitkdtysknrLGEGPTKFYERrtqikgdaedVDAITKHVLGDACTPGNPKE 407
Cdd:PRK13805 807 AELGIPMSIKE----------AGVDEADFLAK----------LDELAELAFDDQCTGANPRY 848
|
|
| BDH |
cd08187 |
Butanol dehydrogenase catalyzes the conversion of butyraldehyde to butanol with the cofactor ... |
24-414 |
2.46e-41 |
|
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: 150.66 E-value: 2.46e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 24 GPGAHEMIGPEALKLGfRKPLVMTSGlrgTDIVHN-----IVESLKYHGLDPVLYDEVESNPKdYNTMDS-VALYQENSC 97
Cdd:cd08187 13 GKGAIEELGEEIKKYG-KKVLLVYGG---GSIKKNglydrVVASLKEAGIEVVEFGGVEPNPR-LETVREgIELAREENV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 98 DSFISIGGGSSHDACKGARVSVAHDGrNVNEFegFNKSENPNNP-PHIAVSTTAGTGSETSWAYVITDTTTDpdnpHKYV 176
Cdd:cd08187 88 DFILAVGGGSVIDAAKAIAAGAKYDG-DVWDF--FTGKAPPEKAlPVGTVLTLAATGSEMNGGAVITNEETK----EKLG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 177 AFDDACVASLAIDDPVLYYDCPVDYTAQCGFDVLAHASEPYVSRINFEP-------SLgnaLRAIKltaENLRQATWNGQ 249
Cdd:cd08187 161 FGSPLLRPKFSILDPELTYTLPKYQTAAGIVDIFSHVLEQYFTGTEDAPlqdrlaeGL---LRTVI---ENGPKALKDPD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 250 DLPGREGMMYAqyiAAQAFNsG--GLGV-----IHSISHAVSAFYDTHHGLNNAIALPRVWAFNMPVAYKRFAEMAEA-M 321
Cdd:cd08187 235 DYEARANLMWA---ATLALN-GllGAGRggdwaTHAIEHELSALYDITHGAGLAIVFPAWMRYVLKKKPERFAQFARRvF 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 322 GVnTRGMNDVQAAdaalnaairllrDVGItERFVDITKDtysknrLGeGPTKFyerrTQIKGDAEDVDAITKHVLGDACT 401
Cdd:cd08187 311 GI-DPGGDDEETA------------LEGI-EALEEFFKS------IG-LPTTL----SELGIDEEDIEEMAEKAVRGGGL 365
|
410
....*....|...
gi 1433560031 402 PGNPKECTFDTVR 414
Cdd:cd08187 366 GGGFKPLTREDIE 378
|
|
| Fe-ADH-like |
cd14864 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
15-332 |
1.59e-39 |
|
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: 145.52 E-value: 1.59e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 15 FHPFPRALMGPGAHEMIGPEALKLGFRKPLVMTSGLRGTDIVHNIVESLKYHGLDPVLYDEVESNPkDYNTMDSVA-LYQ 93
Cdd:cd14864 1 FKIPPNIVFGADSLERIGEEVKEYGSRFLLITDPVLKESGLADKIVSSLEKAGISVIVFDEIPASA-TSDTIDEAAeLAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 94 ENSCDSFISIGGGSSHDACKGARVSVAHDGRNVNEFEGFNKSENPNnpPHIAVSTTAGTGSETSWAYVITDTTTDpdNPH 173
Cdd:cd14864 80 KAGADGIIAVGGGKVLDTAKAVAILANNDGGAYDFLEGAKPKKKPL--PLIAVPTTPRSGFEFSDRFPVVDSRSR--EVK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 174 KYVAFDDACVAslAIDDPVLYYDCPVDYTAQCGFDVLAHASEPYVSRINFEPSLGNALRAIKLTAENLRQATWNGQDLPG 253
Cdd:cd14864 156 LLKAQPGLPKA--VIVDPNLMASLTGNQTAAMALAALALAVEAYLSKKSNFFSDALALKAIELVSENLDGALADPKNTPA 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1433560031 254 REGMMYAQYIAAQAFNSGGLGVIHSISHAVSAFYDTHHGLNNAIALPRVWAFNMPVAYKRFAEMAEAMGVNTRGMNDVQ 332
Cdd:cd14864 234 EELLAQAGCLAGLAASSSSPGLATALALAVNSRYKVSKSLVASILLPHVIEYAATSAPDKYAKIARALGEDVEGASPEE 312
|
|
| Fe-ADH-like |
cd08186 |
Iron-containing alcohol dehydrogenase; This family contains iron-containing alcohol ... |
24-316 |
4.50e-34 |
|
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: 130.85 E-value: 4.50e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 24 GPGAHEMIGPEALKLGFRKPLVMTSGL--RGTDIVHNIVESLKYHGLDPVLYDEVESNPKDYNTMDSVALYQENSCDSFI 101
Cdd:cd08186 7 GVGAIAKIKDILKDLGIDKVIIVTGRSsyKKSGAWDDVEKALEENGIEYVVYDKVTPNPTVDQADEAAKLARDFGADAVI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 102 SIGGGSSHDACKGARVSVAHDGRNVNEFEGFNKSENpNNPPHIAVSTTAGTGSETSWAYVItdttTDPDNPHKYVAFDDA 181
Cdd:cd08186 87 AIGGGSPIDTAKSVAVLLAYGGKTARDLYGFRFAPE-RALPLVAINLTHGTGSEVDRFAVA----TIPEKGYKPGIAYDC 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 182 CVASLAIDDPVLYYDCPVDYTAQCGFDVLAHASEPYVSRINFEPSLGNALRAIKLTAENLRQATWNGQDLPGREGMMYAQ 261
Cdd:cd08186 162 IYPLYAIDDPRLTLTLPKEQTLYTSIDAFNHVYEAATTKVSSPYVITLAKEAIRLIAEYLPRALANPKDLEARYWLLYAS 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1433560031 262 YIAAQAFNSGGLGVIHSISHAVSAFY-DTHHGLNNAIALPRVwafnMPVAYKRFAE 316
Cdd:cd08186 242 MIAGIAIDNGLLHLTHALEHPLSGLKpELPHGLGLALLGPAV----VKYIYKAVPE 293
|
|
| PPD-like |
cd08181 |
1,3-propanediol dehydrogenase-like (PPD); This family contains proteins similar to 1, ... |
15-302 |
7.98e-34 |
|
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: 129.63 E-value: 7.98e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 15 FHPFPRALMGPGAHEMIGPEALKLGfRKPLVMT--SGLRGTDIVHNIVESLKYHGLDPVLYDEVESNPkDYNT-MDSVAL 91
Cdd:cd08181 1 FYMPTKVYFGKNCVEKHADELAALG-KKALIVTgkHSAKKNGSLDDVTEALEENGIEYFIFDEVEENP-SIETvEKGAEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 92 YQENSCDSFISIGGGSSHDACKgarvSVAHDGRNVNEFEGFNKSENPNNP-PHIAVSTTAGTGSETSWAYVItdttTDPD 170
Cdd:cd08181 79 ARKEGADFVIGIGGGSPLDAAK----AIALLAANKDGDEDLFQNGKYNPPlPIVAIPTTAGTGSEVTPYSIL----TDHE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 171 NPHKYVAFDDACVASLAIDDPVLYYDCPVDYTAQCGFDVLAHASEPYVS-RINFEPSL--GNALRAIKLTAENLRQATWN 247
Cdd:cd08181 151 KGTKKSFGNPLIFPKLALLDPKYTLSLPEELTIDTAVDALSHAIEGYLSvKATPLSDAlaLEALRLIGECLPNLLGDELD 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1433560031 248 GQDlpgREGMMYAQYIAAQAFNSGGLGVIHSISHAVSAFYDTHHGLNNAIALPRV 302
Cdd:cd08181 231 EED---REKLMYASTLAGMVIAQTGTTLPHGLGYPLTYFKGIPHGRANGILLPAY 282
|
|
| Fe-ADH-like |
cd14866 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
20-406 |
5.46e-29 |
|
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: 116.95 E-value: 5.46e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 20 RALMGPGAHEMIGPEALKLGFRKPLVMT-SGLRGTDIVHNIVESlkyhGLDPVL---YDEVESNpKDYNT-MDSVALYQE 94
Cdd:cd14866 7 RLFSGRGALARLGRELDRLGARRALVVCgSSVGANPDLMDPVRA----ALGDRLagvFDGVRPH-SPLETvEAAAEALRE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 95 NSCDSFISIGGGSSHDACKGARVSVAHDG-----RNVNEFEGFNKSENPNNP--PHIAVSTTAGTGSETSWAYVitdttT 167
Cdd:cd14866 82 ADADAVVAVGGGSAIVTARAASILLAEDRdvrelCTRRAEDGLMVSPRLDAPklPIFVVPTTPTTADVKAGSAV-----T 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 168 DPDNPHKYVAFDDACVASLAIDDPVLYYDCPVDYTAQCGFDVLAHASEPYVSRiNFEP-SLGNALRAIKLTAENLRQATw 246
Cdd:cd14866 157 DPPAGQRLALFDPKTRPAAVFYDPELLATAPASLVAGAAMNGFDMAVEGLYSR-HADPlADATLMHALRLLADGLPRLA- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 247 NGQDLPGREGMMYAQYIAAQAFNSGGLGVIHSISHAVSAFYDTHHGLNNAIALPRVWAFNMPVAYKRFAEMAEAMGVNTR 326
Cdd:cd14866 235 DDDDPAARADLVLAAVLAGYGTDHTGGGVIHALGHAIGARYGVQNGVVHAILLPHVLRFNAPATDGRLDRLAEALGVADA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 327 GmnDVQAADAALNAAIRLLRDVGITERFVDItkdtysknrlgeGPTKfyerrtqikgdaEDVDAITKHVLGDACTPGNPK 406
Cdd:cd14866 315 G--DEASAAAVVDAVEALLDALGVPTRLRDL------------GVSR------------EDLPAIAEAAMDDWFMDNNPR 368
|
|
| MAR-like |
cd08192 |
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic ... |
19-418 |
5.66e-29 |
|
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: 116.58 E-value: 5.66e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 19 PRALMGPGAHEMIGPEALKLGFRKPLVMTSG--LRGTDIVHNIVESL------KYHGLDP-VLYDEVEsnpkdyntmDSV 89
Cdd:cd08192 2 ERVSYGPGAVEALLHELATLGASRVFIVTSKslATKTDVIKRLEEALgdrhvgVFSGVRQhTPREDVL---------EAA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 90 ALYQENSCDSFISIGGGSSHDACKGARVSVAHDGRNVNEFEGFN------KSENPNNPPHIAVSTTAgTGSETSwAYVit 163
Cdd:cd08192 73 RAVREAGADLLVSLGGGSPIDAAKAVALALAEDVTDVDQLDALEdgkridPNVTGPTLPHIAIPTTL-SGAEFT-AGA-- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 164 dTTTDPDNPHKYVAFDDACVASLAIDDPVLYYDCPVDYTAQCGFDVLAHASEPYVSRINFEPSLGNALRAIKLTAENLRQ 243
Cdd:cd08192 149 -GATDDDTGHKQGFAHPELGPDAVILDPELTLHTPERLWLSTGIRAVDHAVETLCSPQATPFVDALALKALRLLFEGLPR 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 244 ATWNGQDLPGREGMMYAQYIAAQAF-NSGGLGVIHSISHAVSAFYDTHHGLNNAIALPRVWAFNMPVAYKRFAEMAEAMG 322
Cdd:cd08192 228 SKADPEDLEARLKCQLAAWLSLFGLgSGVPMGASHAIGHQLGPLYGVPHGITSCIMLPAVLRFNAPVNAERQRLIARALG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 323 VNTRGMNDVQAADAALNAAI-------RLLRDVGITErfvditkdtysknrlgegptkfyerrtqikgdaEDVDAITKHV 395
Cdd:cd08192 308 LVTGGLGREAADAADAIDALirelglpRTLRDVGVGR---------------------------------DQLEKIAENA 354
|
410 420
....*....|....*....|....
gi 1433560031 396 LGDACTPGNPKECT-FDTVRPVVE 418
Cdd:cd08192 355 LTDVWCRTNPRPITdKDDVLEILE 378
|
|
| MAR |
cd08177 |
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic ... |
19-325 |
8.95e-25 |
|
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: 104.12 E-value: 8.95e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 19 PRALMGPGAHEMIGPEALKLGFRKPLVMTSGlRGTDIVHNIVESLkyHGLDPVLYDEVESN-PKDyNTMDSVALYQENSC 97
Cdd:cd08177 2 QRVVFGAGTLAELAEELERLGARRALVLSTP-RQRALAERVAALL--GDRVAGVFDGAVMHvPVE-VAERALAAAREAGA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 98 DSFISIGGGSSHDACKGarVSVAHDGrnvnefegfnksenpnnpPHIAVSTT-AgtGSETSWAYVITD----TTTDpdnp 172
Cdd:cd08177 78 DGLVAIGGGSAIGLAKA--IALRTGL------------------PIVAVPTTyA--GSEMTPIWGETEdgvkTTGR---- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 173 hkyvafDDACVASLAIDDPVLYYDCPVDYTAQCGFDVLAHASEP-YVSRINFEPSLgNALRAIKLTAENLRQATWNGQDL 251
Cdd:cd08177 132 ------DPRVLPRTVIYDPDLTLGLPAALSVASGLNALAHAVEAlYAPDANPITSL-LAEEGIRALARALPRLVADPSDL 204
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1433560031 252 PGREGMMYAQYIAAQAFNSGGLGVIHSISHAVSAFYDTHHGLNNAIALPRVWAFNMPVAYKRFAEMAEAMGVNT 325
Cdd:cd08177 205 EARSDALYGAWLAGVVLGSVGMGLHHKLCHVLGGTFDLPHAETHAVVLPHVLAYNAPAAPDAMARLARALGGGD 278
|
|
| YqdH |
COG1979 |
Alcohol dehydrogenase YqhD, Fe-dependent ADH family [Energy production and conversion]; |
14-319 |
1.98e-22 |
|
Alcohol dehydrogenase YqhD, Fe-dependent ADH family [Energy production and conversion];
Pssm-ID: 441582 [Multi-domain] Cd Length: 387 Bit Score: 98.22 E-value: 1.98e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 14 EFHpFP-RALMGPGAHEMIGPEALKLGfRKPLVMTsGlrGTDIVHN-----IVESLKYHGLDPVLYDEVESNPKdYNT-M 86
Cdd:COG1979 5 TFY-NPtKIIFGKGQIAKLGEEIPKYG-KKVLLVY-G--GGSIKKNglydqVKAALKEAGIEVVEFGGVEPNPR-LETvR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 87 DSVALYQENSCDSFISIGGGSSHDACKGARVSVAHDGrNVNEFegFNKSENPNNP-PHIAVSTTAGTGSETSWAYVITDT 165
Cdd:COG1979 79 KGVELCKEEGIDFILAVGGGSVIDGAKAIAAGAKYDG-DPWDI--LTGKAPVEKAlPLGTVLTLPATGSEMNSGSVITNE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 166 TTDpdnpHKYVAFDDACVASLAIDDPVLYYDCPVDYTAQCGFDVLAHASEPYVSRINfepslgNA----------LRAIK 235
Cdd:COG1979 156 ETK----EKLGFGSPLVFPKFSILDPELTYTLPKRQTANGIVDIFSHVMEQYFTYPV------DAplqdrfaeglLRTLI 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 236 ltaENLRQATWNGQDLPGREGMMYAqyiAAQAFNsG--GLGV-----IHSISHAVSAFYDTHHGLNNAIALPRVWAFNMP 308
Cdd:COG1979 226 ---EEGPKALKDPEDYDARANLMWA---ATLALN-GliGAGVpqdwaTHMIEHELSALYDIDHGAGLAIVLPAWMRYVLE 298
|
330
....*....|.
gi 1433560031 309 VAYKRFAEMAE 319
Cdd:COG1979 299 EKPEKFAQYAE 309
|
|
| Fe-ADH_KdnB-like |
cd08184 |
Iron-containing alcohol dehydrogenase similar to Shewanella oneidensis KdnB required for Kdo8N ... |
57-323 |
7.13e-13 |
|
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: 69.22 E-value: 7.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 57 HNIVESLKYHGLDPVLYDEVESNPK----DYNTMDSVALYQENSCdSFISIGGGSSHDACKGARVSVAHDGRNvNEFEGF 132
Cdd:cd08184 40 KPLLDRLPLQNGDLLIFVDTTDEPKtdqiDALRAQIRAENDKLPA-AVVGIGGGSTMDIAKAVSNMLTNPGSA-ADYQGW 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 133 NKSENPNnPPHIAVSTTAGTGSETSWAYVITdtttdpdNPHK-------YVAFDdacvasLAIDDPVLYYDCPVD---YT 202
Cdd:cd08184 118 DLVKNPG-IYKIGVPTLSGTGAEASRTAVLT-------GPEKklginsdYTVFD------QVILDPELIATVPRDqyfYT 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 203 aqcGFDVLAHASEPYVSRINFEPSLGNALRAIKLTAENLRQatwngqDLPG----REGMMYAQYIAAQAFNSGGLGVIHS 278
Cdd:cd08184 184 ---GMDCYIHCVESLNGTYRNAFGDAYAEKALELCRDVFLS------DDMMspenREKLMVASYLGGSSIANSQVGVCHA 254
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1433560031 279 ISHAVSAFYDTHHGLNNAIalprvwAFNM-----PVAYKRFAEMAEAMGV 323
Cdd:cd08184 255 LSYGLSVVLGTHHGVANCI------VFNVleefyPEGVKEFREMLEKQNI 298
|
|
| 4HBD_NAD |
cd14860 |
4-hydroxybutyrate dehydrogenase, also called gamma-hydroxybutyrate dehydrogenase, catalyzes ... |
90-295 |
5.48e-10 |
|
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: 60.69 E-value: 5.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 90 ALYQENSCDSF---ISIGGGSSHDACKgaRVSVAHDGRNVNEFEGfnKSENPNNPPHIAVSTTAGTGSE-TSWAYV-ITD 164
Cdd:cd14860 69 AIYKDIKKYGYkrvIAIGGGTVIDIAK--LLALKGISPVLDLFDG--KIPLIKEKELIIVPTTCGTGSEvTNISIVeLTS 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 165 TTTdpdnphKYVAFDDACVASLAIDDPVLYYDCPVDYTAQCGFDVLAHASEPYVSRINFEPSLGNALRAIKLTAENLRQA 244
Cdd:cd14860 145 LGT------KKGLAVDELYADKAVLIPELLKGLPYKVFATSSIDALIHAIESYLSPKATPYTEMFSYKAIEMILEGYQEI 218
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1433560031 245 TWNGQDlpGREGMMYAQYIAAQ----AFNSGGLGVIHSISHAVSAFYDTHHGLNN 295
Cdd:cd14860 219 AEKGEE--ARFPLLGDFLIASNyagiAFGNAGCAAVHALSYPLGGKYHVPHGEAN 271
|
|
| PRK15138 |
PRK15138 |
alcohol dehydrogenase; |
66-303 |
4.27e-07 |
|
alcohol dehydrogenase;
Pssm-ID: 185092 [Multi-domain] Cd Length: 387 Bit Score: 51.72 E-value: 4.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 66 HGLDPVLYDEVESNPKDYNTMDSVALYQENSCDSFISIGGGSSHDACK----GARVSVAHDGRNVNEFEGfnkSENPNNP 141
Cdd:PRK15138 55 KGMDVLEFGGIEPNPTYETLMKAVKLVREEKITFLLAVGGGSVLDGTKfiaaAANYPENIDPWHILETGG---KEIKSAI 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 142 PHIAVSTTAGTGSETSWAYVITDTTTDPDnphkyVAFDDACVASL-AIDDPVLYYDCPVDYTAQCGFDVLAHASEPYVS- 219
Cdd:PRK15138 132 PMGSVLTLPATGSESNAGAVISRKTTGDK-----QAFHSPHVQPVfAVLDPVYTYTLPPRQVANGVVDAFVHTVEQYVTy 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1433560031 220 ----RINFEPSLGNALRAIKLTAENLRQAtwngQDLPGREGMMYAqyiAAQAFNSG-GLGV-----IHSISHAVSAFYDT 289
Cdd:PRK15138 207 pvdaKIQDRFAEGILLTLIEEGPKALKEP----ENYDVRANVMWA---ATQALNGLiGAGVpqdwaTHMLGHELTAMHGL 279
|
250
....*....|....
gi 1433560031 290 HHGLNNAIALPRVW 303
Cdd:PRK15138 280 DHAQTLAIVLPALW 293
|
|
| |
