|
Name |
Accession |
Description |
Interval |
E-value |
| HOT |
cd08190 |
Hydroxyacid-oxoacid transhydrogenase (HOT) involved in gamma-hydroxybutyrate metabolism; This ... |
49-462 |
0e+00 |
|
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: 726.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 49 VSNIRYGAGVTKEVGMDLQNMGAKNVCLMTDKNLSQLPPVQIVMDSLSKNGISFQVYDDVRVEPTDGSFMDAIEFAKKGA 128
Cdd:cd08190 1 ASNIRFGPGATRELGMDLKRLGAKKVLVVTDPGLAKLGLVERVLESLEKAGIEVVVYDGVRVEPTDESFEEAIEFAKEGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 129 FDAYVAVGGGSTMDTCKAANLYASSPhSEFLDYVNAPIGKGKPVTVPLKPLIAVPTTSGTGSETTGVAIFDYEHLKVKTG 208
Cdd:cd08190 81 FDAFVAVGGGSVIDTAKAANLYATHP-GDFLDYVNAPIGKGKPVPGPLKPLIAIPTTAGTGSETTGVAIFDLEELKVKTG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 209 IASRAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTAIPYSMRsPCPSNPIQRPAYQGSNPISDIWAVHALQIV 288
Cdd:cd08190 160 ISSRYLRPTLAIVDPLLTLTLPPRVTASSGFDVLCHALESYTARPYNAR-PRPANPDERPAYQGSNPISDVWAEKAIELI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 289 AKYLKRAVRNPDDLEARSKMHLASAFAGIGFGNAGVHLCHGMSYPISGLVKTYKAKEYNVDHPLVPHGLSVVLTSPAVFT 368
Cdd:cd08190 239 GKYLRRAVNDGDDLEARSNMLLASTLAGIGFGNAGVHLPHAMAYPIAGLVKDYRPPGYPVDHPHVPHGLSVALTAPAVFR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 369 FTAQMFPERHLETAGILGANIRTARIQDAGLVLADALRKFLFDLNVDDGLAALGYSKDDIPSLVKGTLPQERVTKLAPRA 448
Cdd:cd08190 319 FTAPACPERHLEAAELLGADTSGASDRDAGEVLADALIKLMRDIGIPNGLSALGYSEDDIPALVEGTLPQQRLLKLNPRP 398
|
410
....*....|....
gi 30424876 449 QSEEDLSALFEASM 462
Cdd:cd08190 399 VTEEDLEEIFEDAL 412
|
|
| EutG |
COG1454 |
Alcohol dehydrogenase, class IV [Energy production and conversion]; |
52-462 |
8.88e-109 |
|
Alcohol dehydrogenase, class IV [Energy production and conversion];
Pssm-ID: 441063 [Multi-domain] Cd Length: 381 Bit Score: 327.08 E-value: 8.88e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 52 IRYGAGVTKEVGMDLQNMGAKNVCLMTDKNLSQLPPVQIVMDSLSKNGISFQVYDDVRVEPTDGSFMDAIEFAKKGAFDA 131
Cdd:COG1454 11 IVFGAGALAELGEELKRLGAKRALIVTDPGLAKLGLLDRVLDALEAAGIEVVVFDDVEPNPTVETVEAGAAAAREFGADV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 132 YVAVGGGSTMDTCKAANLYASSPHSeFLDYVNApigkgKPVTVPLKPLIAVPttsgtgsettGVAIFDYEHLKVKTGIAS 211
Cdd:COG1454 91 VIALGGGSAIDAAKAIALLATNPGD-LEDYLGI-----KKVPGPPLPLIAIPttagtgsevtPFAVITDPETGVKKGIAD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 212 RAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTAIpysmrspcpsnpiqrpayqGSNPISDIWAVHALQIVAKY 291
Cdd:COG1454 165 PELLPDVAILDPELTLTLPPSLTAATGMDALTHAIEAYVSK-------------------GANPLTDALALEAIRLIARN 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 292 LKRAVRNPDDLEARSKMHLASAFAGIGFGNAGVHLCHGMSYPISGLvktykakeYNvdhplVPHGLSVVLTSPAVFTFTA 371
Cdd:COG1454 226 LPRAVADGDDLEAREKMALASLLAGMAFANAGLGAVHALAHPLGGL--------FH-----VPHGLANAILLPHVLRFNA 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 372 QMFPERHLETAGILGANIrTARIQDAGLVLADALRKFLFDLNVDDGLAALGYSKDDIPSLVKGTLpQERVTKLAPRAQSE 451
Cdd:COG1454 293 PAAPERYAEIARALGLDV-GLSDEEAAEALIEAIRELLRDLGIPTRLSELGVTEEDLPELAELAL-ADRCLANNPRPLTE 370
|
410
....*....|.
gi 30424876 452 EDLSALFEASM 462
Cdd:COG1454 371 EDIEAILRAAY 381
|
|
| Fe-ADH |
cd08551 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains large ... |
50-458 |
1.58e-104 |
|
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: 315.93 E-value: 1.58e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 50 SNIRYGAGVTKEVGMDLQNMGAKNVCLMTDKNLSQLPPVQIVMDSLSKNGISFQVYDDVRVEPTDGSFMDAIEFAKKGAF 129
Cdd:cd08551 2 TRIVFGAGALARLGEELKALGGKKVLLVTDPGLVKAGLLDKVLESLKAAGIEVEVFDDVEPNPTVETVEAAAELAREEGA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 130 DAYVAVGGGSTMDTCKAANLYASSPHSeFLDYVNapigkGKPVTVPLKPLIAVPttsgtgsettGVAIFDYEHLKVKTGI 209
Cdd:cd08551 82 DLVIAVGGGSVLDTAKAIAVLATNGGS-IRDYEG-----IGKVPKPGLPLIAIPttagtgsevtPNAVITDPETGRKMGI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 210 ASRAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTAIPysmrspcpsnpiqrpayqgSNPISDIWAVHALQIVA 289
Cdd:cd08551 156 VSPYLLPDVAILDPELTLSLPPSVTAATGMDALTHAIEAYTSKK-------------------ANPISDALALEAIRLIG 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 290 KYLKRAVRNPDDLEARSKMHLASAFAGIGFGNAGVHLCHGMSYPISGlvktykakEYNvdhplVPHGLSVVLTSPAVFTF 369
Cdd:cd08551 217 KNLRRAVADGSDLEAREAMLLASLLAGIAFGNAGLGAVHALAYPLGG--------RYH-----IPHGVANAILLPYVMEF 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 370 TAQMFPERHLETAGILGANIRTARIQDAGLVLADALRKFLFDLNVDDGLAALGYSKDDIPSLVKGTLPQERVTKLAPRAQ 449
Cdd:cd08551 284 NLPACPEKYAEIAEALGEDVEGLSDEEAAEAAVEAVRELLRDLGIPTSLSELGVTEEDIPELAEDAMKSGRLLSNNPRPL 363
|
....*....
gi 30424876 450 SEEDLSALF 458
Cdd:cd08551 364 TEEDIREIY 372
|
|
| Fe-ADH |
pfam00465 |
Iron-containing alcohol dehydrogenase; |
50-454 |
2.50e-93 |
|
Iron-containing alcohol dehydrogenase;
Pssm-ID: 425696 [Multi-domain] Cd Length: 362 Bit Score: 286.81 E-value: 2.50e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 50 SNIRYGAGVTKEVGMDLQNMGAKnVCLMTDKNLSQLPPVQIVMDSLSKNGISFQVYDDVRVEPTDGSFMDAIEFAKKGAF 129
Cdd:pfam00465 2 TRIVFGAGALAELGEELKRLGAR-ALIVTDPGSLKSGLLDKVLASLEEAGIEVVVFDGVEPEPTLEEVDEAAALAREAGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 130 DAYVAVGGGSTMDTCKAANLYASSPHSEFLDYvnapigKGKPVTVPLKPLIAVPTTSGTGSETTGVAIFDYEHLKVKTGI 209
Cdd:pfam00465 81 DVIIAVGGGSVIDTAKAIALLLTNPGDVWDYL------GGKPLTKPALPLIAIPTTAGTGSEVTPLAVITDTETGEKLGI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 210 ASRAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTAipysmrspcpsnpiqrpayQGSNPISDIWAVHALQIVA 289
Cdd:pfam00465 155 FSPKLLPDLAILDPELTLTLPPRLTAATGMDALAHAVEAYVS-------------------KGANPLTDALALEAIRLIA 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 290 KYLKRAVRNPDDLEARSKMHLASAFAGIGFGNAGVHLCHGMSYPISGLVKtykakeynvdhplVPHGLSVVLTSPAVFTF 369
Cdd:pfam00465 216 ENLPRAVADGEDLEARENMLLASTLAGLAFSNAGLGAAHALAHALGGRYG-------------IPHGLANAILLPYVLRF 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 370 TAQMFPERHLETAGILGANIRTARIQDAglvlADALRKFLFDLNVDDGLAALGYSKDDIPSLVKGTLpQERVTKLAPRAQ 449
Cdd:pfam00465 283 NAPAAPEKLAQLARALGEDSDEEAAEEA----IEALRELLRELGLPTTLSELGVTEEDLDALAEAAL-RDRSLANNPRPL 357
|
....*
gi 30424876 450 SEEDL 454
Cdd:pfam00465 358 TAEDI 362
|
|
| Fe-ADH-like |
cd14863 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
52-460 |
3.81e-83 |
|
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: 260.93 E-value: 3.81e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 52 IRYGAGVTKEVGMDLQNMGAKNVCLMTDKNLSQLPPVQIVMDSLSKNGISFQVYDDVRVEPTDGSFMDAIEFAKKGAFDA 131
Cdd:cd14863 8 VIFGAGAVEQIGELLKELGCKKVLLVTDKGLKKAGIVDKIIDLLEEAGIEVVVFDDVEPDPPDEIVDEAAEIAREEGADG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 132 YVAVGGGSTMDTCKAANLYASSPHsEFLDYvnapIGKGKPVTVPLKPLIAVPTTSGTGSETTGVAIFDYEHLKVKTGIAS 211
Cdd:cd14863 88 VIGIGGGSVLDTAKAIAVLLTNPG-PIIDY----ALAGPPVPKPGIPLIAIPTTAGTGSEVTPIAVITDEENGVKKSLLG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 212 RAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTAipysmrspcpsnpiqrpayQGSNPISDIWAVHALQIVAKY 291
Cdd:cd14863 163 PFLVPDLAILDPELTVGLPPSLTAATGMDALSHAIEAYTS-------------------KLANPMTDALALQAIRLIVKN 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 292 LKRAVRNPDDLEARSKMHLASAFAGIGFGNAGVHLCHGMSYPISGLvktykakeYNvdhplVPHGLSVVLTSPAVFTFTA 371
Cdd:cd14863 224 LPRAVKDGDNLEARENMLLASNLAGIAFNNAGTHIGHAIAHALGAL--------YH-----IPHGLACALALPVVLEFNA 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 372 QMFPERHLETAGILGANIRTARIQDAGLVLADALRKFLFDLNVDDGLAALGYSKDDIPSLVKGTLpQERVTKLAPRAQSE 451
Cdd:cd14863 291 EAYPEKVKKIAKALGVSFPGESDEELGEAVADAIREFMKELGIPSLFEDYGIDKEDLDKIAEAVL-KDPFAMFNPRPITE 369
|
....*....
gi 30424876 452 EDLSALFEA 460
Cdd:cd14863 370 EEVAEILEA 378
|
|
| Fe-ADH-like |
cd08185 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
51-459 |
3.05e-75 |
|
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: 240.48 E-value: 3.05e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 51 NIRYGAGVTKEVGmDLQNMGAKNVCLMTDKNLSQLPPV-QIVMDSLSKNGISFQVYDDVRVEPTDGSFMDAIEFAKKGAF 129
Cdd:cd08185 6 RILFGAGKLNELG-EEALRPGKKALIVTGKGSSKKTGLlDRVKKLLEKAGVEVVVFDKVEPNPLTTTVMEGAALAKEEGC 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 130 DAYVAVGGGSTMDTCKAANLYASSPHSEFlDYVNAPIGKGKPVTVPLkPLIAVPTTSGTGSETTGVAIFDYEHLKVKTGI 209
Cdd:cd08185 85 DFVIGLGGGSSMDAAKAIAFMATNPGDIW-DYIFGGTGKGPPPEKAL-PIIAIPTTAGTGSEVDPWAVITNPETKEKKGI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 210 ASRAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTAIpysmrspcpsnpiqrpayqGSNPISDIWAVHALQIVA 289
Cdd:cd08185 163 GHPALFPKVSIVDPELMLTVPPRVTAYTGFDALFHAFESYISK-------------------NANPFSDMLALEAIRLVA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 290 KYLKRAVRNPDDLEARSKMHLASAFAGIGFGNAGVHLCHGMSYPISGLvktykakeynvdHPLVPHGLSVVLTSPAVFTF 369
Cdd:cd08185 224 KYLPRAVKDGSDLEAREKMAWASTLAGIVIANSGTTLPHGLEHPLSGY------------HPNIPHGAGLAALYPAYFEF 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 370 TAQMFPERhleTAGILGANIRTARIQDAGLVLADALRKFLFDLNVDDGLAALGYSKDDIPSLVkgtlpqERVTKLA---- 445
Cdd:cd08185 292 TIEKAPEK---FAFVARAEASGLSDAKAAEDFIEALRKLLKDIGLDDLLSDLGVTEEDIPWLA------ENAMETMgglf 362
|
410
....*....|....*..
gi 30424876 446 ---PRAQSEEDLSALFE 459
Cdd:cd08185 363 annPVELTEEDIVEIYE 379
|
|
| Fe-ADH-like |
cd08191 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
50-462 |
1.19e-73 |
|
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: 236.74 E-value: 1.19e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 50 SNIRYGAGVTKEVGMDLQNMGAKnVCLMTDKNLSQLPPVQIVMDSLSKNGISFQVYDDVRVEPTDGSFMDAIEFAKKGAF 129
Cdd:cd08191 5 SRLLFGPGARRALGRVAARLGSR-VLIVTDPRLASTPLVAELLAALTAAGVAVEVFDGGQPELPVSTVADAAAAARAFDP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 130 DAYVAVGGGSTMDTCKAANLYASSPhSEFLDYvnapIGKGKpVTVPLKPLIAVPTTSGTGSETTGVAIFDYEHLKVKTGI 209
Cdd:cd08191 84 DVVIGLGGGSNMDLAKVVALLLAHG-GDPRDY----YGEDR-VPGPVLPLIAVPTTAGTGSEVTPVAVLTDPARGMKVGV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 210 ASRAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTAIPysmRSPCPSNPiQRPAYQGSNPISDIWAVHALQIVA 289
Cdd:cd08191 158 SSPYLRPAVAIVDPELTLTCPPGVTADSGIDALTHAIESYTARD---FPPFPRLD-PDPVYVGKNPLTDLLALEAIRLIG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 290 KYLKRAVRNPDDLEARSKMHLASAFAGIGFGNAGVHLCHGMSYPISGLVKTykakeynvdhplvPHGLSVVLTSPAVFTF 369
Cdd:cd08191 234 RHLPRAVRDGDDLEARSGMALAALLAGLAFGTAGTAAAHALQYPIGALTHT-------------SHGVGNGLLLPYVMRF 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 370 TAQMFPERHLETAGILGANiRTARIQDAGLVLADALRKFLFDLNVDDGLAALGYSKDDIPSLVKGTLPQERVTKLAPRAQ 449
Cdd:cd08191 301 NRPARAAELAEIARALGVT-TAGTSEEAADRAIERVEELLARIGIPTTLADLGVTEADLPGLAEKALSVTRLIANNPRPP 379
|
410
....*....|...
gi 30424876 450 SEEDLSALFEASM 462
Cdd:cd08191 380 TEEDLLRILRAAF 392
|
|
| Fe-ADH-like |
cd08196 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
43-458 |
5.13e-73 |
|
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: 234.40 E-value: 5.13e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 43 YAFEMAVsNIRYGAGVTKEVGMDLQNMGAKNVCLMTDKNLSQLPPVQIVMDSLSKNGISfqVYDDVRVEPTDGSFMDAIE 122
Cdd:cd08196 1 WSYYQPV-KIIFGEGILKELPDIIKELGGKRGLLVTDPSFIKSGLAKRIVESLKGRIVA--VFSDVEPNPTVENVDKCAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 123 FAKKGAFDAYVAVGGGSTMDTCKAANLYASSPHSeFLDYvnapIGKGKPVTVPLKPLIAVPTTSGTGSETTGVAIFDYEH 202
Cdd:cd08196 78 LARENGADFVIAIGGGSVLDTAKAAACLAKTDGS-IEDY----LEGKKKIPKKGLPLIAIPTTAGTGSEVTPVAVLTDKE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 203 LKVKTGIASRAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTAIpysmrspcpsnpiqrpayqGSNPISDIWAV 282
Cdd:cd08196 153 KGKKAPLVSPGFYPDIAIVDPELTYSMPPKVTASTGIDALCHAIEAYWSI-------------------NHQPISDALAL 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 283 HALQIVAKYLKRAVRNPDDLEARSKMHLASAFAGIGFGNAGVHLCHGMSYPISglvktykaKEYNvdhplVPHGLSVVLT 362
Cdd:cd08196 214 EAAKLVLENLEKAYNNPNDKEAREKMALASLLAGLAFSQTRTTASHACSYPLT--------SHFG-----IPHGEACALT 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 363 SPAVFTFTAQMFPERHLETAGILGANirtariqDAGLvLADALRKFLFDLNVDDGLAALGYSKDDIPSLVKGTLPQERVt 442
Cdd:cd08196 281 LPSFIRLNAEALPGRLDELAKQLGFK-------DAEE-LADKIEELKKRIGLRTRLSELGITEEDLEEIVEESFHPNRA- 351
|
410
....*....|....*.
gi 30424876 443 KLAPRAQSEEDLSALF 458
Cdd:cd08196 352 NNNPVEVTKEDLEKLL 367
|
|
| Fe-ADH-like |
cd08194 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
50-460 |
4.82e-71 |
|
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: 229.73 E-value: 4.82e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 50 SNIRYGAGVTKEVGMDLQNMGAKNVCLMTDKNLSQLPPVQIVMDSLSKNGISFQVYDDVRVEPTDGSFMDAIEFAKKGAF 129
Cdd:cd08194 2 RTIIIGGGALEELGEEAASLGGKRALIVTDKVMVKLGLVDKVTQLLAEAGIAYAVFDDVVSEPTDEMVEEGLALYKEGGC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 130 DAYVAVGGGSTMDTCKAANLYASSPhSEFLDYVNAPIGKGKPVtvplkPLIAVPTTSGTGSETTGVAIFDYEHLKVKTGI 209
Cdd:cd08194 82 DFIVALGGGSPIDTAKAIAVLATNG-GPIRDYMGPRKVDKPGL-----PLIAIPTTAGTGSEVTRFTVITDTETDVKMLL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 210 ASRAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTaipySMRspcpsnpiqrpayqgSNPISDIWAVHALQIVA 289
Cdd:cd08194 156 KGPALLPAVAIVDPELTLSMPPRVTAATGIDALTHAIEAYV----SRK---------------AQPLTDTLALSAIKLIG 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 290 KYLKRAVRNPDDLEARSKMHLASAFAGIGFGNAGVHLCHGMSYPISGLVktykakeynvdHplVPHGLSVVLTSPAVFTF 369
Cdd:cd08194 217 RNLRRAYADGDDLEAREAMMLAALEAGIAFSNSSVALVHGMSRPIGALF-----------H--VPHGLSNAMLLPAVTEF 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 370 TAQMFPERHLETAGILGANIRTARIQDAGLVLADALRKFLFDLNVdDGLAALGYSKDD----IPSLVKGTL----PQerv 441
Cdd:cd08194 284 SLPGAPERYAEIARAMGIATEGDSDEEAAEKLVEALERLCADLEI-PTLREYGIDEEEfeaaLDKMAEDALasgsPA--- 359
|
410
....*....|....*....
gi 30424876 442 tkLAPRAQSEEDLSALFEA 460
Cdd:cd08194 360 --NNPRVPTKEEIIELYRE 376
|
|
| Fe-ADH-like |
cd17814 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
54-436 |
6.53e-68 |
|
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: 221.26 E-value: 6.53e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 54 YGAGVTKEVGMDLQNMGAKNVCLMTDKNLSQLPPVQIVMDSLSKNGISFQVYDDVRVEPTDGSFMDAIE-FAKKGAfDAY 132
Cdd:cd17814 9 FGVGARKLAGRYAKNLGARKVLVVTDPGVIKAGWVDEVLDSLEAEGLEYVVFSDVTPNPRDFEVMEGAElYREEGC-DGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 133 VAVGGGSTMDTCKAANLYASSpHSEFLDYvnapIGKGKpVTVPLKPLIAVPTTSGTGSETTGVAIFDYEHLKVKTGIASR 212
Cdd:cd17814 88 VAVGGGSPIDCAKGIGIVVSN-GGHILDY----EGVDK-VRRPLPPLICIPTTAGSSADVSQFAIITDTERRVKMAIISK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 213 AIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTaipysmrspcpSNpiqrpayqGSNPISDIWAVHALQIVAKYL 292
Cdd:cd17814 162 TLVPDVSLIDPETLTTMDPELTACTGMDALTHAIEAYV-----------SN--------ASSPLTDLHALEAIRLISENL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 293 KRAVRNPDDLEARSKMHLASAFAGIGFGNAGVHLCHGMSYPISGLvktykakeynVDhplVPHGLSVVLTSPAVFTFTAQ 372
Cdd:cd17814 223 PKAVADPDDLEAREKMMLASLQAGLAFSNASLGAVHAMAHSLGGL----------LD---LPHGECNALLLPHVIRFNFP 289
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30424876 373 MFPERHLETAGILGANIRTARIQDAGLVLADALRKFLFDLNVDDGLAALGYSKDDIPSLVKGTL 436
Cdd:cd17814 290 AAPERYRKIAEAMGLDVDGLDDEEVAERLIEAIRDLREDLGIPETLSELGVDEEDIPELAKRAM 353
|
|
| LPO |
cd08176 |
Lactadehyde:propanediol oxidoreductase (LPO) catalyzes the interconversion between ... |
54-459 |
1.86e-64 |
|
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: 212.41 E-value: 1.86e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 54 YGAGVTKEVGMDLQNMGAKNVCLMTDKNLSQLPPVQIVMDSLSKNGISFQVYDDVRVEPTDGSFMDAIEFAKKGAFDAYV 133
Cdd:cd08176 11 FGWGAIEEIGEEAKKRGFKKALIVTDKGLVKFGIVDKVTDVLKEAGIAYTVFDEVKPNPTIENVMAGVAAYKESGADGII 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 134 AVGGGSTMDTCKAANLYASSPhseFLDyVNAPIGKgKPVTVPLKPLIAVPTTSGTGSETTGVA-IFDYEHlKVKTGIASR 212
Cdd:cd08176 91 AVGGGSSIDTAKAIGIIVANP---GAD-VRSLEGV-APTKNPAVPIIAVPTTAGTGSEVTINYvITDTEK-KRKFVCVDP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 213 AIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTAipysmrspcpsnpiqrpayQGSNPISDIWAVHALQIVAKYL 292
Cdd:cd08176 165 HDIPTVAIVDPDLMSSMPKGLTAATGMDALTHAIEGYIT-------------------KGAWELSDMLALKAIELIAKNL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 293 KRAVRNPDDLEARSKMHLASAFAGIGFGNAGVHLCHGMSYPISGLvktykakeYNvdhplVPHGLSVVLTSPAVFTFTAQ 372
Cdd:cd08176 226 RKAVANPNNVEARENMALAQYIAGMAFSNVGLGIVHSMAHPLSAF--------YD-----TPHGVANAILLPYVMEFNAP 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 373 MFPERHLETAGILGANIRTARIQDAGLVLADALRKFLFDLNVDDGLAALGYSKDDIPSLVKGTLpQERVTKLAPRAQSEE 452
Cdd:cd08176 293 ATGEKYRDIARAMGVDTTGMSDEEAAEAAVDAVKKLSKDVGIPQKLSELGVKEEDIEALAEDAL-NDVCTPGNPREATKE 371
|
....*..
gi 30424876 453 DLSALFE 459
Cdd:cd08176 372 DIIALYK 378
|
|
| Fe-ADH-like |
cd14862 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
66-458 |
2.81e-62 |
|
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: 206.69 E-value: 2.81e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 66 LQNMGAKNVCLMTDKNLSQLPPVQIVMDSLSKNGISFQVYDDVRVEPTDGSFMDAIEFAKKGAFDAYVAVGGGSTMDTCK 145
Cdd:cd14862 19 LEQLSGKRALIVTDKVLVKLGLLKKVLKRLLQAGFEVEVFDEVEPEPPLETVLKGAEAMREFEPDLIIALGGGSVMDAAK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 146 AANLYASSPHSEFLDYV-NAPIGKGKpvtvplKP-LIAVPTTSGTGSETTGVAIFDYEHLKVKTGIASRAIKPTLGLVDP 223
Cdd:cd14862 99 AAWVLYERPDLDPEDISpLDLLGLRK------KAkLIAIPTTSGTGSEATWAIVLTDTEEPRKIAVANPELVPDVAILDP 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 224 LHTLHMPCQVVANSGFDVLCHALESYTAipysmrspcpsnpiqrpayQGSNPISDIWAVHALQIVAKYLKRAVRNPDDLE 303
Cdd:cd14862 173 EFVLGMPPKLTAGTGLDALAHAVEAYLS-------------------TWSNDFSDALALKAIELIFKYLPRAYKDGDDLE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 304 ARSKMHLASAFAGIGFGNAGVHLCHGMSYPISGLVKtykakeynvdhplVPHGLSVVLTSPAVFTFTAQmFPERHLETAG 383
Cdd:cd14862 234 AREKMHNAATIAGLAFGNSQAGLAHALGHSLGAVFH-------------VPHGIAVGLFLPYVIEFYAK-VTDERYDLLK 299
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30424876 384 ILGANIRTAriQDAGLVLADALRKFLFDLNVDDGLAALGYSKDD----IPSLVKGTLpQERVTKLAPRAQSEEDLSALF 458
Cdd:cd14862 300 LLGIEARDE--EEALKKLVEAIRELYKEVGQPLSIKDLGISEEEfeekLDELVEYAM-EDSCTITSPRPPSEEDLKKLF 375
|
|
| PDDH |
cd08188 |
1,3-Propanediol (1,3-PD) dehydrogenase; This family includes 1,3-propanediol (1,3-PD) ... |
55-459 |
6.82e-61 |
|
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: 203.13 E-value: 6.82e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 55 GAGVTKEVGMDLQNMGAKNVCLMTDKNLSQLPPVQIVMDSLSKNGISFQVYDDVRVEPTDGSFMDAIEFAKKGAFDAYVA 134
Cdd:cd08188 12 GPGCLKEIGDELKKLGGKKALIVTDKGLVKLGLVKKVTDVLEEAGIEYVIFDGVQPNPTVTNVNEGLELFKENGCDFIIS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 135 VGGGSTMDTCKAANLYASSPhSEFLDYVNapIGKgkpVTVPLKPLIAVPTTSGTGSETTGVAIFDYEHLKVKTGIASRAI 214
Cdd:cd08188 92 VGGGSAHDCAKAIGILATNG-GEIEDYEG--VDK---SKKPGLPLIAINTTAGTASEVTRFAVITDEERHVKMVIVDWNV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 215 KPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTAIpysmrspcpsnpiqrpayqGSNPISDIWAVHALQIVAKYLKR 294
Cdd:cd08188 166 TPTIAVNDPELMLGMPPSLTAATGMDALTHAIEAYVST-------------------GATPLTDALALEAIRLIAENLPK 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 295 AVRNPDDLEARSKMHLASAFAGIGFGNAGVHLCHGMSYPISGLvktykakeYNvdhplVPHGL--SVVLtsPAVFTFTAQ 372
Cdd:cd08188 227 AVANGKDLEARENMAYAQFLAGMAFNNAGLGYVHAMAHQLGGF--------YN-----LPHGVcnAILL--PHVMEFNLP 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 373 MFPERHLETAGILGANIRTARIQDAGLVLADALRKFLFDLNVDDGLAALGYSKDDIPSLVKGTLpQERVTKLAPRAQSEE 452
Cdd:cd08188 292 ACPERFADIARALGENTEGLSDEEAAEAAIEAIRKLSRRVGIPSGLKELGVKEEDFPLLAENAL-KDACGPTNPRQATKE 370
|
....*..
gi 30424876 453 DLSALFE 459
Cdd:cd08188 371 DVIAIYR 377
|
|
| Fe-ADH-like |
cd14865 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
52-462 |
1.00e-59 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341487 [Multi-domain] Cd Length: 383 Bit Score: 200.46 E-value: 1.00e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 52 IRYGAGVTKEVGMDLQNMGAKNVCLMTDKNLSQLPPVQIVMDSLSKNGISFQVYDDVrvePTDGSF---MDAIEFAKKGA 128
Cdd:cd14865 9 IVSGAGALENLPAELARLGARRPLIVTDKGLAAAGLLKKVEDALGDAIEIVGVFDDV---PPDSSVavvNEAAARAREAG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 129 FDAYVAVGGGSTMDTCKAANLYASSPHSEFLDYVNAPIgkgkpVTVPLKPLIAVPTTSGTGSETTGVAIFDYEHLKVKTG 208
Cdd:cd14865 86 ADGIIAVGGGSVIDTAKGVNILLSEGGDDLDDYGGANR-----LTRPLKPLIAIPTTAGTGSEVTLVAVIKDEEKKVKLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 209 IASRAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTAIpysmrspcpsnpiqrpayqGSNPISDIWAVHALQIV 288
Cdd:cd14865 161 FVSPFLLPDVAILDPRLTLSLPPKLTAATGMDALTHAIEAYTSL-------------------QKNPISDALALQAIRLI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 289 AKYLKRAVRNPDDLEARSKMHLASAFAGIGFGNAGVHLCHGMSYPISGLVKtykakeynvdhplVPHGL--SVVLtsPAV 366
Cdd:cd14865 222 SENLPKAVKNGKDLEARLALAIAATMAGIAFSNSMVGLVHAIAHAVGAVAG-------------VPHGLanSILL--PHV 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 367 FTFTAQMFPERHLETAGIL--GANIRTARIQDAGLVLADALRKFLFDLNVDDGLAALGYSKDDIPSLVKGTLpQERVTKL 444
Cdd:cd14865 287 MRYNLDAAAERYAELALALayGVTPAGRRAEEAIEAAIDLVRRLHELCGLPTRLRDVGVPEEQLEAIAELAL-NDGAILF 365
|
410
....*....|....*...
gi 30424876 445 APRAQSEEDLSALFEASM 462
Cdd:cd14865 366 NPREVDPEDILAILEAAY 383
|
|
| HVD |
cd08193 |
5-hydroxyvalerate dehydrogenase (HVD) catalyzes the oxidation of 5-hydroxyvalerate to ... |
49-460 |
1.92e-56 |
|
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: 191.57 E-value: 1.92e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 49 VSNIRYGAGVTKEVGMDLQNMGAKNVCLMTDKNLSQLPPVQIVMDSLSKNGISFQVYDDVRVEPTDGSFMDAIEFAKKGA 128
Cdd:cd08193 4 VPRIICGAGAAARLGELLRELGARRVLLVTDPGLVKAGLADPALAALEAAGIAVTVFDDVVADPPEAVVEAAVEQAREAG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 129 FDAYVAVGGGSTMDTCKAANLYASSPHSefldyVNAPIGKGKpVTVPLKPLIAVPTTSGTGSETTGVAIF-DYEHlkVKT 207
Cdd:cd08193 84 ADGVIGFGGGSSMDVAKLVALLAGSDQP-----LDDIYGVGK-ATGPRLPLILVPTTAGTGSEVTPISIVtTGET--EKK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 208 GIASRAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTAipysmRSpcpsnpiqrpayqGSNPISDIWAVHALQI 287
Cdd:cd08193 156 GVVSPQLLPDVALLDAELTLGLPPHVTAATGIDAMVHAIEAYTS-----RH-------------KKNPISDALAREALRL 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 288 VAKYLKRAVRNPDDLEARSKMHLASAFAGIGFGNAGVHLCHGMSYPISGLVKtykakeynvdhplVPHGLSVVLTSPAVF 367
Cdd:cd08193 218 LGANLRRAVEDGSDLEAREAMLLGSMLAGQAFANAPVAAVHALAYPLGGHFH-------------VPHGLSNALVLPHVL 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 368 TFTAQMFPERHLETAGILGANIRTARIQDAGLVLADALRKFLFDLNVDDGLAALGYSKDDIPSLVKGTLPQERVTKLAPR 447
Cdd:cd08193 285 RFNLPAAEALYAELARALLPGLAFGSDAAAAEAFIDALEELVEASGLPTRLRDVGVTEEDLPMLAEDAMKQTRLLVNNPR 364
|
410
....*....|...
gi 30424876 448 AQSEEDLSALFEA 460
Cdd:cd08193 365 EVTEEDALAIYQA 377
|
|
| Fe-ADH-like |
cd14861 |
Iron-containing alcohol dehydrogenases-like; This family contains proteins similar to ... |
52-462 |
2.07e-55 |
|
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: 188.87 E-value: 2.07e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 52 IRYGAGVTKEVGMDLQNMGAKNVCLMTDKNLSQLPPVQIVMDSLSKNGISFQVYDDVRVEPTDGSFMDAIEFAKKGAFDA 131
Cdd:cd14861 6 IRFGAGAIAELPEELKALGIRRPLLVTDPGLAALGIVDRVLEALGAAGLSPAVFSDVPPNPTEADVEAGVAAYREGGCDG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 132 YVAVGGGSTMDTCKAANLYASSPHSEFlDYVNAPIGkGKPVTVPLKPLIAVPTTSGTGSETTGVAIFDYEHLKVKTGIAS 211
Cdd:cd14861 86 IIALGGGSAIDAAKAIALMATHPGPLW-DYEDGEGG-PAAITPAVPPLIAIPTTAGTGSEVGRAAVITDDDTGRKKIIFS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 212 RAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTAIPYsmrspcpsnpiqrpayqgsNPISDIWAVHALQIVAKY 291
Cdd:cd14861 164 PKLLPKVAICDPELTLGLPPRLTAATGMDALTHCIEAYLSPGF-------------------HPMADGIALEGLRLISEW 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 292 LKRAVRNPDDLEARSKMHLASAFAGIGFGNaGVHLCHGMSYPISGLVKTykakeynvdhplvPHGLSVVLTSPAVFTFTA 371
Cdd:cd14861 225 LPRAVADGSDLEARGEMMMAALMGAVAFQK-GLGAVHALAHALGALYGL-------------HHGLLNAILLPYVLRFNR 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 372 QMFPERHLETAGILGANIRTAriqDAglvLADALRKFLFDLNVDDGLAALGYSKDDIPSLVKGTLpQERVTKLAPRAQSE 451
Cdd:cd14861 291 PAVEDKLARLARALGLGLGGF---DD---FIAWVEDLNERLGLPATLSELGVTEDDLDELAELAL-ADPCHATNPRPVTA 363
|
410
....*....|.
gi 30424876 452 EDLSALFEASM 462
Cdd:cd14861 364 EDYRALLREAL 374
|
|
| Fe-ADH-like |
cd08183 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
52-459 |
2.07e-54 |
|
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: 186.17 E-value: 2.07e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 52 IRYGAGVTKEVGMDLQNMGaKNVCLMTDKNLSQLPPVQIVMDSLSKNGISFQVYDDVRvEPTDGSFMDAIEFAKKGAFDA 131
Cdd:cd08183 4 IVFGRGSLQELGELAAELG-KRALLVTGRSSLRSGRLARLLEALEAAGIEVALFSVSG-EPTVETVDAAVALAREAGCDV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 132 YVAVGGGSTMDTCKAANLYASSPHS--EFLDYVnapiGKGKPVTVPLKPLIAVPTtsgtgsettgVA-----------IF 198
Cdd:cd08183 82 VIAIGGGSVIDAAKAIAALLTNEGSvlDYLEVV----GKGRPLTEPPLPFIAIPT----------TAgtgsevtknavLS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 199 DYEHlKVKTGIASRAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTAIpysmrspcpsnpiqrpayqGSNPISD 278
Cdd:cd08183 148 SPEH-GVKVSLRSPSMLPDVALVDPELTLSLPPEVTAASGLDALTQLIEPYVSR-------------------KANPLTD 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 279 IWAVHALQIVAKYLKRAVRNPDDLEARSKMHLASAFAGIGFGNAGVHLCHGMSYPISGLVKtykakeynvdhplVPHGL- 357
Cdd:cd08183 208 ALAREGLRLAARSLRRAYEDGEDLEAREDMALASLLGGLALANAGLGAVHGLAGPLGGMFG-------------APHGAi 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 358 -SVVLtsPAVFTFTAQM----FPERHLETAGILGANIRTARIQDAGLVLADALRKFLFDLNVdDGLAALGYSKDDIPSLV 432
Cdd:cd08183 275 cAALL--PPVLEANLRAlrerEPDSPALARYRELAGILTGDPDAAAEDGVEWLEELCEELGI-PRLSEYGLTEEDFPEIV 351
|
410 420
....*....|....*....|....*..
gi 30424876 433 KGTLpQERVTKLAPRAQSEEDLSALFE 459
Cdd:cd08183 352 EKAR-GSSSMKGNPIELSDEELLEILE 377
|
|
| NADPH_BDH |
cd08179 |
NADPH-dependent butanol dehydrogenase involved in the butanol and ethanol formation pathway in ... |
66-460 |
1.65e-50 |
|
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: 175.84 E-value: 1.65e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 66 LQNMGAKNVCLMTDKN-LSQLPPVQIVMDSLSKNGISFQVYDDVRVEPTDGSFMDAIEFAKKGAFDAYVAVGGGSTMDTC 144
Cdd:cd08179 18 LKTLKGKRAFIVTGGGsMKRNGFLDKVEDYLKEAGMEVKVFEGVEPDPSVETVEKGAEAMREFEPDWIIAIGGGSVIDAA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 145 KAANLYASSPHSEFLDYVnapigkgKPVTVPLKP----LIAVPTTSGTGSETTGVAIF-DYEHlKVKTGIASRAIKPTLG 219
Cdd:cd08179 98 KAMWVFYEYPELTFEDAL-------VPFPLPELRkkarFIAIPSTSGTGSEVTRASVItDTEK-GIKYPLASFEITPDVA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 220 LVDPLHTLHMPCQVVANSGFDVLCHALESYTAIPysmrspcpsnpiqrpayqgSNPISDIWAVHALQIVAKYLKRAVRNP 299
Cdd:cd08179 170 ILDPELTMTMPPHVTANTGMDALTHAIEAYVSTL-------------------ANDFTDALALGAILDIFENLPKSYNGG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 300 DDLEARSKMHLASAFAGIGFGNAGVHLCHGMSYPISGlvktykakEYNvdhplVPHGL--SVVLtsPAVFTFTAQMFPER 377
Cdd:cd08179 231 KDLEAREKMHNASCLAGMAFSNSGLGIVHSMAHKGGA--------FFG-----IPHGLanAILL--PYVIEFNSKDPEAR 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 378 HLETAGILGANirtariqdaGLVLADALRKFLFDLN----VDDGLAALGYSKDD----IPSLVKGTLpQERVTKLAPRAQ 449
Cdd:cd08179 296 ARYAALLIGLT---------DEELVEDLIEAIEELNkklgIPLSFKEAGIDEDEffakLDEMAENAM-NDACTGTNPRKP 365
|
410
....*....|.
gi 30424876 450 SEEDLSALFEA 460
Cdd:cd08179 366 TVEEMKELLKA 376
|
|
| HEPD |
cd08182 |
Hydroxyethylphosphoate dehydrogenase (HEPD) catalyzes the reduction of phosphonoacetaldehyde ... |
50-459 |
3.63e-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: 174.72 E-value: 3.63e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 50 SNIRYGAGVTKEVGMDLQNMGAKNVCLMTDKNLSQLPPVQIVMDSLsKNGISFQVYDDVRVEPTDGSFMDAIEFAKKGAF 129
Cdd:cd08182 2 VKIIFGPGALAELKDLLGGLGARRVLLVTGPSAVRESGAADILDAL-GGRIPVVVFSDFSPNPDLEDLERGIELFRESGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 130 DAYVAVGGGSTMDTCKAANLYASSPHSEFLdyvnAPIGKGKPVTVPLKPLIAVPTTsgtgsettgvA-----------IF 198
Cdd:cd08182 81 DVIIAVGGGSVIDTAKAIAALLGSPGENLL----LLRTGEKAPEENALPLIAIPTT----------AgtgsevtpfatIW 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 199 DyEHLKVKTGIASRAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTAIpysmrspcpsnpiqrpayqGSNPISD 278
Cdd:cd08182 147 D-EAEGKKYSLAHPSLYPDAAILDPELTLSLPLYLTASTGLDALSHAIESIWSV-------------------NANPESR 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 279 IWAVHALQIVAKYLKRAVRNPDDLEARSKMHLASAFAGIGFGNAGVHLCHGMSYPISglvktykaKEYNvdhplVPHGLS 358
Cdd:cd08182 207 AYALRAIRLILENLPLLLENLPNLEAREAMAEASLLAGLAISITKTTAAHAISYPLT--------SRYG-----VPHGHA 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 359 VVLTSPAVFTFTAQMFPERHletagilgANIRTARIQDAGLV-----LADALRKFLFDLNVDDGLAALGYSKDDIPSLVK 433
Cdd:cd08182 274 CALTLPAVLRYNAGADDECD--------DDPRGREILLALGAsdpaeAAERLRALLESLGLPTRLSEYGVTAEDLEALAA 345
|
410 420
....*....|....*....|....*.
gi 30424876 434 GTLPQERVtKLAPRAQSEEDLSALFE 459
Cdd:cd08182 346 SVNTPERL-KNNPVRLSEEDLLRLLE 370
|
|
| PDD |
cd08180 |
1,3-propanediol dehydrogenase (PPD) catalyzes the reduction of 3-hydroxypropionaldehyde (3-HPA) ... |
66-459 |
1.02e-46 |
|
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: 164.59 E-value: 1.02e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 66 LQNMGAKNVCLMTDKNLSQLPPVQIVMDSLSKNgISFQVYDDVRVEPTDGSFMDAIEFAKKGAFDAYVAVGGGSTMDTCK 145
Cdd:cd08180 17 LKELKGKRVFIVTDPFMVKSGMVDKVTDELDKS-NEVEIFSDVVPDPSIEVVAKGLAKILEFKPDTIIALGGGSAIDAAK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 146 AANLYassphsefldYVNAPIGKGKPvtvplkPLIAVPTTSGTGSETTGVA-IFDYEHlKVKTGIASRAIKPTLGLVDPL 224
Cdd:cd08180 96 AIIYF----------ALKQKGNIKKP------LFIAIPTTSGTGSEVTSFAvITDPEK-GIKYPLVDDSMLPDIAILDPE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 225 HTLHMPCQVVANSGFDVLCHALESYTAIpysmrspcpsnpiqrpayqGSNPISDIWAVHALQIVAKYLKRAVRNPDDLEA 304
Cdd:cd08180 159 LVKSVPPKVTADTGMDVLTHALEAYVST-------------------NANDFTDALAEKAIKLVFENLPRAYRDGDDLEA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 305 RSKMHLASAFAGIGFGNAGVHLCHGMSYPISGLVKtykakeynvdhplVPHGLSVVLTSPAVFTFtaqmfperhletagi 384
Cdd:cd08180 220 REKMHNASCMAGIAFNNAGLGINHSLAHALGGRFH-------------IPHGRANAILLPYVIEF--------------- 271
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30424876 385 lganirtariqdaglvLADALRKFLFDLNVDDGLAALGYSKDD----IPSLVKGTLpQERVTKLAPRAQSEEDLSALFE 459
Cdd:cd08180 272 ----------------LIAAIRRLNKKLGIPSTLKELGIDEEEfekaIDEMAEAAL-ADRCTATNPRKPTAEDLIELLR 333
|
|
| PPD-like |
cd08181 |
1,3-propanediol dehydrogenase-like (PPD); This family contains proteins similar to 1, ... |
45-459 |
1.56e-44 |
|
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: 159.29 E-value: 1.56e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 45 FEMAVsNIRYGAGVTKEVGMDLQNMGaKNVCLMT-----DKNLSQlppvQIVMDSLSKNGISFQVYDDVRVEPTDGSFMD 119
Cdd:cd08181 1 FYMPT-KVYFGKNCVEKHADELAALG-KKALIVTgkhsaKKNGSL----DDVTEALEENGIEYFIFDEVEENPSIETVEK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 120 AIEFAKKGAFDAYVAVGGGSTMDTCKAANLYASSP-HSEFLDYVNAPigkGKPVtvplkPLIAVPTTSGTGSETTGVAIF 198
Cdd:cd08181 75 GAELARKEGADFVIGIGGGSPLDAAKAIALLAANKdGDEDLFQNGKY---NPPL-----PIVAIPTTAGTGSEVTPYSIL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 199 DYEHLKVKTGIASRAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYtaipYSMRspcpsnpiqrpayqgSNPISD 278
Cdd:cd08181 147 TDHEKGTKKSFGNPLIFPKLALLDPKYTLSLPEELTIDTAVDALSHAIEGY----LSVK---------------ATPLSD 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 279 IWAVHALQIVAKYLKRAVRNPDDLEARSKMHLASAFAGIGFGNAGVHLCHGMSYPIsglvkTYkakEYNvdhplVPHGLS 358
Cdd:cd08181 208 ALALEALRLIGECLPNLLGDELDEEDREKLMYASTLAGMVIAQTGTTLPHGLGYPL-----TY---FKG-----IPHGRA 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 359 VVLTSPAVFTFTAQMFPERHLETAGILganirtariqdaGLVLADALRKFLFDLNVDDGLaalgYSKDDIPSLVKGTLPQ 438
Cdd:cd08181 275 NGILLPAYLKLCEKQEPEKVDKILKLL------------GFGSIEEFQKFLNRLLGKKEE----LSEEELEKYADEAMKA 338
|
410 420
....*....|....*....|.
gi 30424876 439 ERVtKLAPRAQSEEDLSALFE 459
Cdd:cd08181 339 KNK-KNTPGNVTKEDILRIYR 358
|
|
| AAD_C |
cd08178 |
C-terminal alcohol dehydrogenase domain of the acetaldehyde dehydrogenase-alcohol ... |
69-427 |
2.45e-41 |
|
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: 151.96 E-value: 2.45e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 69 MGAKNVCLMTDKNLSQLPPVQIVMDSLSKNGISFQVYDDVRVEPTDGSFMDAIEFAKkgAF--DAYVAVGGGSTMDTCKA 146
Cdd:cd08178 21 PGVKRAFIVTDRVLYKLGYVDKVLDVLEARGVETEVFSDVEPDPTLSTVRKGLEAMN--AFkpDVIIALGGGSAMDAAKI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 147 ANLYASSPHSEFLD------------YVNAPIGKGKPvtvplkpLIAVPTTSGTGSETTGVA-IFDyEHLKVKTGIASRA 213
Cdd:cd08178 99 MWLFYEHPETKFEDlaqrfmdirkrvYKFPKLGKKAK-------LVAIPTTSGTGSEVTPFAvITD-DKTGKKYPLADYA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 214 IKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTAIPysmrspcpsnpiqrpayqgSNPISDIWAVHALQIVAKYLK 293
Cdd:cd08178 171 LTPDMAIVDPELVMTMPKRLTADTGIDALTHAIEAYVSVM-------------------ASDYTDGLALQAIKLIFEYLP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 294 RAVRNPDDLEARSKMHLASAFAGIGFGNAGVHLCHGMSYPISGlvktykakEYNvdhplVPHGLSVVLTSPAVFTFTAQ- 372
Cdd:cd08178 232 RSYNNGNDIEAREKMHNAATIAGMAFANAFLGICHSLAHKLGA--------AFH-----IPHGRANAILLPHVIRYNATd 298
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30424876 373 ------MFP--------ERHLETAGILGANIRTariqDAGLV--LADALRKFLFDLNVDDGLAALGYSKDD 427
Cdd:cd08178 299 pptkqaAFPqykyyvakERYAEIADLLGLGGKT----PEEKVesLIKAIEDLKKDLGIPTSIREAGIDEAD 365
|
|
| Fe-ADH-like |
cd08189 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
55-433 |
7.33e-41 |
|
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: 149.93 E-value: 7.33e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 55 GAGVTKEVGMDLQNMGAKNVCLMTDKNLSQLPPVQIVMDSLSKNGISFQVYDDVRVEPTDGSFMDAIEFAKKGAFDAYVA 134
Cdd:cd08189 11 GAGSLLQLPEALKKLGIKRVLIVTDKGLVKLGLLDPLLDALKKAGIEYVVFDGVVPDPTIDNVEEGLALYKENGCDAIIA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 135 VGGGSTMDTCKAANLYASSPHSEFLDYVnapiGKGKpVTVPLKPLIAVPTTSGTGSETTGVA-IFDYEHlKVKTGIASRA 213
Cdd:cd08189 91 IGGGSVIDCAKVIAARAANPKKSVRKLK----GLLK-VRKKLPPLIAVPTTAGTGSEATIAAvITDPET-HEKYAINDPK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 214 IKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTAIPYsmrspcpsnpiqrpayqgsNPISDIWAVHALQIVAKYLK 293
Cdd:cd08189 165 LIPDAAVLDPELTLGLPPAITAATGMDALTHAVEAYISRSA-------------------TKETDEYALEAVKLIFENLP 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 294 RAVRNPDDLEARSKMHLASAFAGIGFGNAGVHLCHGMSYPISGLvktykakeYNvdhplVPHGL--SVVLtsPAVFTFTA 371
Cdd:cd08189 226 KAYEDGSDLEARENMLLASYYAGLAFTRAYVGYVHAIAHQLGGL--------YG-----VPHGLanAVVL--PHVLEFYG 290
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30424876 372 QMFPERHLETAGILGANIRTARIQDAGLVLADALRKFLFDLNVDDGLAALgySKDDIPSLVK 433
Cdd:cd08189 291 PAAEKRLAELADAAGLGDSGESDSEKAEAFIAAIRELNRRMGIPTTLEEL--KEEDIPEIAK 350
|
|
| PRK10624 |
PRK10624 |
L-1,2-propanediol oxidoreductase; Provisional |
54-462 |
9.58e-41 |
|
L-1,2-propanediol oxidoreductase; Provisional
Pssm-ID: 182595 [Multi-domain] Cd Length: 382 Bit Score: 149.76 E-value: 9.58e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 54 YGAGVTKEVGMDLQNMGAKNVCLMTDKNLSQLPPVQIVMDSLSKNGISFQVYDDVRVEPTDGSFMDAIE-FAKKGAfDAY 132
Cdd:PRK10624 13 FGRGAIGALTDEVKRRGFKKALIVTDKTLVKCGVVAKVTDVLDAAGLAYEIYDGVKPNPTIEVVKEGVEvFKASGA-DYL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 133 VAVGGGSTMDTCKAANLYASSPhsEFLDYVN----APIGKgkpvtvPLKPLIAVPTTS-GTGSETTGVAIFDYEHLKVKT 207
Cdd:PRK10624 92 IAIGGGSPQDTCKAIGIISNNP--EFADVRSlegvAPTKK------PSVPIIAIPTTAgTAAEVTINYVITDEEKRRKFV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 208 GIASRAIkPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTAipysmrspcpsnpiqrpayQGSNPISDIWAVHALQI 287
Cdd:PRK10624 164 CVDPHDI-PQVAFVDADMMDSMPPGLKAATGVDALTHAIEGYIT-------------------RGAWALTDMLHLKAIEI 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 288 VAKYLKRAVRNpdDLEARSKMHLASAFAGIGFGNAGVHLCHGMSYPISGLvktykakeYNvdhplVPHGLSVVLTSPAVF 367
Cdd:PRK10624 224 IAGALRGAVAG--DKEAGEGMALGQYIAGMGFSNVGLGLVHGMAHPLGAF--------YN-----TPHGVANAILLPHVM 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 368 TFTAQMFPERHLETAGILGANIRTARIQDAGLVLADALRKFLFDLNVDDGLAALGYSKDDIPSLVKGTLpQERVTKLAPR 447
Cdd:PRK10624 289 EYNADFTGEKYRDIARAMGVKVEGMSLEEARNAAVEAVKALNRDVGIPPHLRDVGVKEEDIPALAQAAF-DDVCTGGNPR 367
|
410
....*....|....*
gi 30424876 448 AQSEEDLSALFEASM 462
Cdd:PRK10624 368 EATLEDIVELYKKAW 382
|
|
| Fe-ADH-like |
cd08186 |
Iron-containing alcohol dehydrogenase; This family contains iron-containing alcohol ... |
54-462 |
1.23e-40 |
|
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: 149.34 E-value: 1.23e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 54 YGAGVTKEVGMDLQNMGAKNVCLMTDKNLSQLPPV-QIVMDSLSKNGISFQVYDDVRVEPTDGSFMDAIEFAKKGAFDAY 132
Cdd:cd08186 6 FGVGAIAKIKDILKDLGIDKVIIVTGRSSYKKSGAwDDVEKALEENGIEYVVYDKVTPNPTVDQADEAAKLARDFGADAV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 133 VAVGGGSTMDTCKAANLYASSPHS---EFLDYVNAPIGKgkpvtvplKPLIAVPTTSGTGSETTGVAIFDYEHLKVKTGI 209
Cdd:cd08186 86 IAIGGGSPIDTAKSVAVLLAYGGKtarDLYGFRFAPERA--------LPLVAINLTHGTGSEVDRFAVATIPEKGYKPGI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 210 ASRAIKPTLGLVDPLHTLHMPC-QVVANSgFDVLCHALESYTAipysmrspcpsnpiqrpayQGSNPISDIWAVHALQIV 288
Cdd:cd08186 158 AYDCIYPLYAIDDPRLTLTLPKeQTLYTS-IDAFNHVYEAATT-------------------KVSSPYVITLAKEAIRLI 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 289 AKYLKRAVRNPDDLEARSKMHLASAFAGIGFGNAGVHLCHGMSYPISGLVktykakeynvdhPLVPHGLSVVLTSPAVFT 368
Cdd:cd08186 218 AEYLPRALANPKDLEARYWLLYASMIAGIAIDNGLLHLTHALEHPLSGLK------------PELPHGLGLALLGPAVVK 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 369 FTAQMFPErhlETAGILganirtaRIQDAGLV--------LADALRKFLFDLNVDDGLAALGYSKDDIPSLVK---GTLP 437
Cdd:cd08186 286 YIYKAVPE---TLADIL-------RPIVPGLKgtpdeaekAARGVEEFLFSVGFTEKLSDYGFTEDDVDRLVElafTTPS 355
|
410 420
....*....|....*....|....*
gi 30424876 438 QERVTKLAPRAQSEEDLSALFEASM 462
Cdd:cd08186 356 LDLLLSLAPVEVTEEVVREIYEESL 380
|
|
| Fe-ADH-like |
cd14864 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
50-460 |
4.49e-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: 341486 [Multi-domain] Cd Length: 376 Bit Score: 147.83 E-value: 4.49e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 50 SNIRYGAGVTKEVGMDLQNMGAKNVcLMTDKNLSQLPPVQIVMDSLSKNGISFQVYDDVRVEPTDGSFMDAIEFAKKGAF 129
Cdd:cd14864 5 PNIVFGADSLERIGEEVKEYGSRFL-LITDPVLKESGLADKIVSSLEKAGISVIVFDEIPASATSDTIDEAAELARKAGA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 130 DAYVAVGGGSTMDTCKAANLYASSPHsEFLDYVNAPIGKGKPVtvplkPLIAVPTTSGTGSETTGVAIF-DYEHLKVKTg 208
Cdd:cd14864 84 DGIIAVGGGKVLDTAKAVAILANNDG-GAYDFLEGAKPKKKPL-----PLIAVPTTPRSGFEFSDRFPVvDSRSREVKL- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 209 IASRAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTAipysmrspcpsnpiqrpayQGSNPISDIWAVHALQIV 288
Cdd:cd14864 157 LKAQPGLPKAVIVDPNLMASLTGNQTAAMALAALALAVEAYLS-------------------KKSNFFSDALALKAIELV 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 289 AKYLKRAVRNPDDLEARSKMHLASAFAGIGFGNAGVHLCHGMSYPISGLvktykakeYNVDHPLVphgLSVVLtsPAVFT 368
Cdd:cd14864 218 SENLDGALADPKNTPAEELLAQAGCLAGLAASSSSPGLATALALAVNSR--------YKVSKSLV---ASILL--PHVIE 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 369 FTAQMFPERHLETAGILGANIRTARIQDAGLVLADALRKFLFDLNVDDGLAALG--YSKDDIPSLVKgtlpQERVTKLAP 446
Cdd:cd14864 285 YAATSAPDKYAKIARALGEDVEGASPEEAAIAAVEGVRRLIAQLNLPTRLKDLDlaSSLEQLAAIAE----DAPKLNGLP 360
|
410
....*....|....
gi 30424876 447 RAQSEEDLSALFEA 460
Cdd:cd14864 361 RSMSSDDIFDILKA 374
|
|
| PRK13805 |
PRK13805 |
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional |
69-427 |
2.77e-36 |
|
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional
Pssm-ID: 237515 [Multi-domain] Cd Length: 862 Bit Score: 142.63 E-value: 2.77e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 69 MGAKNVCLMTDKNLSQLPPVQIVMDSLSK--NGISFQVYDDVRVEPTdgsfmdaIEFAKKGA-----F--DAYVAVGGGS 139
Cdd:PRK13805 478 DGKKRAFIVTDRFMVELGYVDKVTDVLKKreNGVEYEVFSEVEPDPT-------LSTVRKGAelmrsFkpDTIIALGGGS 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 140 TMDTCKAANLYASSPHSEFLD------------YVNAPIG-KGKPVTVP--------LKPlIAVpttsgtgsettgvaIF 198
Cdd:PRK13805 551 PMDAAKIMWLFYEHPETDFEDlaqkfmdirkriYKFPKLGkKAKLVAIPttsgtgseVTP-FAV--------------IT 615
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 199 DyEHLKVKTGIASRAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTAIpysMrspcpsnpiqrpayqgSNPISD 278
Cdd:PRK13805 616 D-DKTGVKYPLADYELTPDVAIVDPNLVMTMPKSLTADTGIDALTHALEAYVSV---M----------------ASDYTD 675
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 279 IWAVHALQIVAKYLKRAVRN-PDDLEARSKMHLASAFAGIGFGNAGVHLCHGMSYPISGlvktykakEYNvdhplVPHGL 357
Cdd:PRK13805 676 GLALQAIKLVFEYLPRSYKNgAKDPEAREKMHNASTIAGMAFANAFLGICHSMAHKLGA--------EFH-----IPHGR 742
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 358 SVVLTSPAVFTFTAQ------MFP--------ERHLETAGILGANIRTariqDAGLV--LADALRKFLFDLNVDDGLAAL 421
Cdd:PRK13805 743 ANAILLPHVIRYNATdppkqaAFPqyeypradERYAEIARHLGLPGST----TEEKVesLIKAIEELKAELGIPMSIKEA 818
|
....*.
gi 30424876 422 GYSKDD 427
Cdd:PRK13805 819 GVDEAD 824
|
|
| BDH |
cd08187 |
Butanol dehydrogenase catalyzes the conversion of butyraldehyde to butanol with the cofactor ... |
52-433 |
1.05e-32 |
|
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: 127.55 E-value: 1.05e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 52 IRYGAGVTKEVGMDLQNMGaKNVCLMTDKN-------LSQlppvqiVMDSLSKNGISFQVYDDVRVEPTDGSFMDAIEFA 124
Cdd:cd08187 10 IIFGKGAIEELGEEIKKYG-KKVLLVYGGGsikknglYDR------VVASLKEAGIEVVEFGGVEPNPRLETVREGIELA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 125 KKGAFDAYVAVGGGSTMDTCKAANLYASSPHsEFLDYVNapigKGKPVTVPLkPLIAVPTTSGTGSETTGVAIFDYEHLK 204
Cdd:cd08187 83 REENVDFILAVGGGSVIDAAKAIAAGAKYDG-DVWDFFT----GKAPPEKAL-PVGTVLTLAATGSEMNGGAVITNEETK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 205 VKTGIASRAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESY-TaipysmrspcpsnpiqrpaYQGSNPISDIWAVH 283
Cdd:cd08187 157 EKLGFGSPLLRPKFSILDPELTYTLPKYQTAAGIVDIFSHVLEQYfT-------------------GTEDAPLQDRLAEG 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 284 ALQIVAKYLKRAVRNPDDLEARSKMHLASAFA--GI-GFGNAGVHLCHGMSYPISGLvktykakeYNVDHplvPHGLSVV 360
Cdd:cd08187 218 LLRTVIENGPKALKDPDDYEARANLMWAATLAlnGLlGAGRGGDWATHAIEHELSAL--------YDITH---GAGLAIV 286
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30424876 361 LtsPAVFTFTAQMFPERHLETA----GILGANIRTARIQDAglvlADALRKFLFDLNVDDGLAALGYSKDDIPSLVK 433
Cdd:cd08187 287 F--PAWMRYVLKKKPERFAQFArrvfGIDPGGDDEETALEG----IEALEEFFKSIGLPTTLSELGIDEEDIEEMAE 357
|
|
| PRK09860 |
PRK09860 |
putative alcohol dehydrogenase; Provisional |
55-462 |
6.13e-31 |
|
putative alcohol dehydrogenase; Provisional
Pssm-ID: 182118 [Multi-domain] Cd Length: 383 Bit Score: 122.76 E-value: 6.13e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 55 GAGVTKEVGMDLQNMGAKNVCLMTDKNLSQLPPVQIVMDSLSKNGISFQVYDDVRVEPTDGSFMDAIEFAKKGAFDAYVA 134
Cdd:PRK09860 15 GADSLTDAMNMMADYGFTRTLIVTDNMLTKLGMAGDVQKALEERNIFSVIYDGTQPNPTTENVAAGLKLLKENNCDSVIS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 135 VGGGSTMDTCKAANLYASSpHSEFLDYVNAPIGKGkpvtvPLKPLIAVPTTSGTGSETTGVAIFDYEHLKVKTGIASRAI 214
Cdd:PRK09860 95 LGGGSPHDCAKGIALVAAN-GGDIRDYEGVDRSAK-----PQLPMIAINTTAGTASEMTRFCIITDEARHIKMAIVDKHV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 215 KPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTAIpysmrspcpsnpiqrpayqGSNPISDIWAVHALQIVAKYLKR 294
Cdd:PRK09860 169 TPLLSVNDSSLMIGMPKSLTAATGMDALTHAIEAYVSI-------------------AATPITDACALKAVTMIAENLPL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 295 AVRNPDDLEARSKMHLASAFAGIGFGNAGVHLCHGMSYPISGLvktykakeYNvdhplVPHGLSVVLTSPAVFTFTAQMF 374
Cdd:PRK09860 230 AVEDGSNAKAREAMAYAQFLAGMAFNNASLGYVHAMAHQLGGF--------YN-----LPHGVCNAVLLPHVQVFNSKVA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 375 PERHLETAGILGANIRTARIQDAGLVLADALRKFLFDLNVDDGLAALGYSKDDIPSLVKGTLpQERVTKLAPRAQSEEDL 454
Cdd:PRK09860 297 AARLRDCAAAMGVNVTGKNDAEGAEACINAIRELAKKVDIPAGLRDLNVKEEDFAVLATNAL-KDACGFTNPIQATHEEI 375
|
....*...
gi 30424876 455 SALFEASM 462
Cdd:PRK09860 376 VAIYRAAM 383
|
|
| PRK15454 |
PRK15454 |
ethanolamine utilization ethanol dehydrogenase EutG; |
55-461 |
1.61e-29 |
|
ethanolamine utilization ethanol dehydrogenase EutG;
Pssm-ID: 185351 [Multi-domain] Cd Length: 395 Bit Score: 119.36 E-value: 1.61e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 55 GAGVTKEVGMDLQNMGAKNVCLMTDKNLSQLPPVQIVMDSLSKNGISFQVYDDVRVEPTDGSFMDAIEFAKKGAFDAYVA 134
Cdd:PRK15454 33 GPGAVSSCGQQAQTRGLKHLFVMADSFLHQAGMTAGLTRSLAVKGIAMTLWPCPVGEPCITDVCAAVAQLRESGCDGVIA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 135 VGGGSTMDTCKAANLYASSPHSEFLDYVNapigkgKPVTVPLKPLIAVPTTSGTGSETTGVAIFDYEHLKVKTGIASRAI 214
Cdd:PRK15454 113 FGGGSVLDAAKAVALLVTNPDSTLAEMSE------TSVLQPRLPLIAIPTTAGTGSETTNVTVIIDAVSGRKQVLAHASL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 215 KPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTAIpysmrspcpsnpiqrpayqGSNPISDIWAVHALQIVAKYLKR 294
Cdd:PRK15454 187 MPDVAILDAALTEGVPSHVTAMTGIDALTHAIEAYSAL-------------------NATPFTDSLAIGAIAMIGKSLPK 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 295 AVRNPDDLEARSKMHLASAFAGIGFGNAGVHLCHGMSY-PISGLvktykakeynvdHplVPHGLSVVLTSPAVFTFTAQM 373
Cdd:PRK15454 248 AVGYGHDLAARESMLLASCMAGMAFSSAGLGLCHAMAHqPGAAL------------H--IPHGLANAMLLPTVMEFNRMV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 374 FPERHLEtagiLGANIRTARIQDAGLVlaDALRKFLFDLNVDDGLAALGYSKDDIPSLVKGTLpQERVTKLAPRAQSEED 453
Cdd:PRK15454 314 CRERFSQ----IGRALRTKKSDDRDAI--NAVSELIAEVGIGKRLGDVGATSAHYGAWAQAAL-EDICLRSNPRTASLEQ 386
|
....*...
gi 30424876 454 LSALFEAS 461
Cdd:PRK15454 387 IVGLYAAA 394
|
|
| 4HBD_NAD |
cd14860 |
4-hydroxybutyrate dehydrogenase, also called gamma-hydroxybutyrate dehydrogenase, catalyzes ... |
111-465 |
3.71e-25 |
|
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: 106.15 E-value: 3.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 111 EPTDGSFMDAIEFAKKGAFDAYVAVGGGSTMDTCKAANLYASSPHSEFLDYvNAPIGKGKPvtvplkpLIAVPTTSGTGS 190
Cdd:cd14860 61 EPSDEMVEAIYKDIKKYGYKRVIAIGGGTVIDIAKLLALKGISPVLDLFDG-KIPLIKEKE-------LIIVPTTCGTGS 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 191 ETTGVAIFDYEHLKVKTGIASRAIKPTLGLVDP--LHTLhmPCQVVANSGFDVLCHALESYTaipysmrSPcpsnpiqrp 268
Cdd:cd14860 133 EVTNISIVELTSLGTKKGLAVDELYADKAVLIPelLKGL--PYKVFATSSIDALIHAIESYL-------SP--------- 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 269 ayqGSNPISDIWAVHALQ-IVAKYLKRAVRNPDDL-EARSKMHLASAFAGIGFGNAGVHLCHGMSYPISGlvkTYKakey 346
Cdd:cd14860 195 ---KATPYTEMFSYKAIEmILEGYQEIAEKGEEARfPLLGDFLIASNYAGIAFGNAGCAAVHALSYPLGG---KYH---- 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 347 nvdhplVPHGLS--VVLTspAVFTFTAQMFPERHLET-----AGILGAnirtariqDAGLVLaDALRKFLFDLNVDDGLA 419
Cdd:cd14860 265 ------VPHGEAnyAVFT--GVLKNYQEKNPDGEIKKlneflAKILGC--------DEEDVY-DELEELLNKILPKKPLH 327
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 30424876 420 ALGYSKDDIPSLVKGTLP-QERVTKLAPRAQSEEDLSALFeasMKLY 465
Cdd:cd14860 328 EYGMKEEEIDEFADSVMEnQQRLLANNYVPLDREDVAEIY---KELY 371
|
|
| MAR-like |
cd08192 |
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic ... |
52-460 |
5.06e-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 (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: 106.18 E-value: 5.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 52 IRYGAGVTKEVGMDLQNMGAKNVCLMTDKNLSQLPPVqiVMDSLSKNGISF-QVYDDVRVEPTDGSFMDAIEFAKKGAFD 130
Cdd:cd08192 4 VSYGPGAVEALLHELATLGASRVFIVTSKSLATKTDV--IKRLEEALGDRHvGVFSGVRQHTPREDVLEAARAVREAGAD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 131 AYVAVGGGSTMDTCKAANL-YASSPH-SEFLDYVNAPIGKGKPVTVPLKPLIAVPTTSGTGSETTGVAIFDyEHLKVKTG 208
Cdd:cd08192 82 LLVSLGGGSPIDAAKAVALaLAEDVTdVDQLDALEDGKRIDPNVTGPTLPHIAIPTTLSGAEFTAGAGATD-DDTGHKQG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 209 IASRAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYtaipYSMRSpcpsnpiqrpayqgsNPISDIWAVHALQIV 288
Cdd:cd08192 161 FAHPELGPDAVILDPELTLHTPERLWLSTGIRAVDHAVETL----CSPQA---------------TPFVDALALKALRLL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 289 AKYLKRAVRNPDDLEARSKMHLASAFAGIGFGN-AGVHLCHGMSYPISGLvktykakeYNvdhplVPHGLSVVLTSPAVF 367
Cdd:cd08192 222 FEGLPRSKADPEDLEARLKCQLAAWLSLFGLGSgVPMGASHAIGHQLGPL--------YG-----VPHGITSCIMLPAVL 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 368 TFTAQMFPERHLETAGILGANIRTARIQDAGlvLADALRKFLFDLNVDDGLAALGYSKDDIPSLVKGTLPQERVTKLAPR 447
Cdd:cd08192 289 RFNAPVNAERQRLIARALGLVTGGLGREAAD--AADAIDALIRELGLPRTLRDVGVGRDQLEKIAENALTDVWCRTNPRP 366
|
410
....*....|...
gi 30424876 448 AQSEEDLSALFEA 460
Cdd:cd08192 367 ITDKDDVLEILES 379
|
|
| Fe-ADH-like |
cd14866 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
45-460 |
7.47e-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: 99.61 E-value: 7.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 45 FEMAVSNIRYGAGVTKEVGMDLQNMGAKNVCLMTDKNLSQLPPVqivMDSLsKNGIS---FQVYDDVRVEPTDGSFMDAI 121
Cdd:cd14866 1 HDYPPLRLFSGRGALARLGRELDRLGARRALVVCGSSVGANPDL---MDPV-RAALGdrlAGVFDGVRPHSPLETVEAAA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 122 EFAKKGAFDAYVAVGGGSTMDTCKAANLYASSPHSeFLDYVNAPIGKGKPVT----VPLKPLIAVPTTSGTGSETTGVAI 197
Cdd:cd14866 77 EALREADADAVVAVGGGSAIVTARAASILLAEDRD-VRELCTRRAEDGLMVSprldAPKLPIFVVPTTPTTADVKAGSAV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 198 FDYEHLKvKTGIASRAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESytaiPYSMRspcpsnpiqrpayqgSNPIS 277
Cdd:cd14866 156 TDPPAGQ-RLALFDPKTRPAAVFYDPELLATAPASLVAGAAMNGFDMAVEG----LYSRH---------------ADPLA 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 278 DIWAVHALQIVAKYLKRAVrNPDDLEARSKMHLASAFAGIGFGNAGVHLCHGMSYPISGlvktykakEYNVDHPLVpHgl 357
Cdd:cd14866 216 DATLMHALRLLADGLPRLA-DDDDPAARADLVLAAVLAGYGTDHTGGGVIHALGHAIGA--------RYGVQNGVV-H-- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 358 SVVLtsPAVFTFTAQMFPERHLETAGILGAniRTARIQDAGLVLADALRKFLFDLNVDDGLAALGYSKDDIPSLVKGTLP 437
Cdd:cd14866 284 AILL--PHVLRFNAPATDGRLDRLAEALGV--ADAGDEASAAAVVDAVEALLDALGVPTRLRDLGVSREDLPAIAEAAMD 359
|
410 420
....*....|....*....|...
gi 30424876 438 QERVTKLAPRAQSEEDLSALFEA 460
Cdd:cd14866 360 DWFMDNNPRPVPTAEELEALLEA 382
|
|
| YqdH |
COG1979 |
Alcohol dehydrogenase YqhD, Fe-dependent ADH family [Energy production and conversion]; |
91-462 |
4.71e-19 |
|
Alcohol dehydrogenase YqhD, Fe-dependent ADH family [Energy production and conversion];
Pssm-ID: 441582 [Multi-domain] Cd Length: 387 Bit Score: 88.59 E-value: 4.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 91 VMDSLSKNGISFQVYDDVRVEPTDGSFMDAIEFAKKGAFDAYVAVGGGSTMDTCK---AANLYASSPHseflDYVNapig 167
Cdd:COG1979 51 VKAALKEAGIEVVEFGGVEPNPRLETVRKGVELCKEEGIDFILAVGGGSVIDGAKaiaAGAKYDGDPW----DILT---- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 168 KGKPVTVPLkPLIAVPTTSGTGSETTGVAIFDYEHLKVKTGIASRAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALE 247
Cdd:COG1979 123 GKAPVEKAL-PLGTVLTLPATGSEMNSGSVITNEETKEKLGFGSPLVFPKFSILDPELTYTLPKRQTANGIVDIFSHVME 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 248 SYTaipysmrspcpSNPIQrpayqgsNPISDIWAVHALQIVAKYLKRAVRNPDDLEARSKMHLASAFAGIGFGNAGVH-- 325
Cdd:COG1979 202 QYF-----------TYPVD-------APLQDRFAEGLLRTLIEEGPKALKDPEDYDARANLMWAATLALNGLIGAGVPqd 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 326 -LCHGMSYPISGLvktykakeYNVDHplvPHGLSVVLtsPAVFTFTAQMFPERHLETA----GILGANIRtARIQDAglv 400
Cdd:COG1979 264 wATHMIEHELSAL--------YDIDH---GAGLAIVL--PAWMRYVLEEKPEKFAQYAervwGITEGDDE-ERALEG--- 326
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30424876 401 lADALRKFLFDLNVDDGLAALGYSKDDIPSLVKGTLPQERVTKLAPRAQSEEDLSALFEASM 462
Cdd:COG1979 327 -IEATEEFFESLGLPTRLSEYGIDEEDIEEMAEKATAHGMTALGEFKDLTPEDVREILELAL 387
|
|
| MAR |
cd08177 |
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic ... |
52-460 |
2.78e-17 |
|
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: 82.55 E-value: 2.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 52 IRYGAGVTKEVGMDLQNMGAKNVCLMTDKnlSQLPPVQIVMDSLSKNGISfqVYDDVR----VEPTDgsfmDAIEFAKKG 127
Cdd:cd08177 4 VVFGAGTLAELAEELERLGARRALVLSTP--RQRALAERVAALLGDRVAG--VFDGAVmhvpVEVAE----RALAAAREA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 128 AFDAYVAVGGGSTmdtckaanlyassphsefldyvnapIGKGKPVTVPLK-PLIAVPTTSgtgsettgvA------IFDY 200
Cdd:cd08177 76 GADGLVAIGGGSA-------------------------IGLAKAIALRTGlPIVAVPTTY---------AgsemtpIWGE 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 201 EHLKVKTGIASRAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTAipysmrspcpsnpiqrpayQGSNPISDIW 280
Cdd:cd08177 122 TEDGVKTTGRDPRVLPRTVIYDPDLTLGLPAALSVASGLNALAHAVEALYA-------------------PDANPITSLL 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 281 AVHALQIVAKYLKRAVRNPDDLEARSKMHLASAFAGIGFGNAG--VH--LCH--GMSYpisGLvktykakeynvdhplvP 354
Cdd:cd08177 183 AEEGIRALARALPRLVADPSDLEARSDALYGAWLAGVVLGSVGmgLHhkLCHvlGGTF---DL----------------P 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 355 HGL--SVVLtsPAVFTFTAQMFPErhletagilganiRTARIQDAGLV--LADALRKFLFDLNVDDGLAALGYSKDDIPS 430
Cdd:cd08177 244 HAEthAVVL--PHVLAYNAPAAPD-------------AMARLARALGGgdAAGGLYDLARRLGAPTSLRDLGMPEDDIDR 308
|
410 420 430
....*....|....*....|....*....|...
gi 30424876 431 LVkgtlpqERVTKLA---PRAQSEEDLSALFEA 460
Cdd:cd08177 309 AA------DLALANPypnPRPVERDALRALLER 335
|
|
| DHQ_Fe-ADH |
cd07766 |
Dehydroquinate synthase-like (DHQ-like) and iron-containing alcohol dehydrogenases (Fe-ADH); ... |
51-433 |
4.79e-09 |
|
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: 56.99 E-value: 4.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 51 NIRYGAGVTKEVGMDLQNMGAKnVCLMTDKNLSQLPpVQIVMDSLSKnGISFQVYDDVRVEPTDGSFMDAIEFAKKGAFD 130
Cdd:cd07766 3 RIVFGEGAIAKLGEIKRRGFDR-ALVVSDEGVVKGV-GEKVADSLKK-GLAVAIFDFVGENPTFEEVKNAVERARAAEAD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 131 AYVAVGGGSTMDTCKAANLyassphsefldyvnapigkgkpVTVPLKPLIAVPTTSGTGSETTGVAIFDYEHLKVKTGIA 210
Cdd:cd07766 80 AVIAVGGGSTLDTAKAVAA----------------------LLNRGIPFIIVPTTASTDSEVSPKSVITDKGGKNKQVGP 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 211 srAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALEsytaipysmrspcpsnpiqrpayqgsnpisdiwavhalqivak 290
Cdd:cd07766 138 --HYNPDVVFVDTDITKGLPPRQVASGGVDALAHAVE------------------------------------------- 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 291 ylkravrnpddleaRSKMHLASAFAGIGFGNA-GVHLCHGMSYPISGLVKTykakeynvdhplvPHGLSVVLTSPAVFTF 369
Cdd:cd07766 173 --------------LEKVVEAATLAGMGLFESpGLGLAHAIGHALTAFEGI-------------PHGEAVAVGLPYVLKV 225
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30424876 370 TAQMFPERHLETAgilganirtariqdaglvladALRKFLFDLNVDDGLAALGYSKDDIPSLVK 433
Cdd:cd07766 226 ANDMNPEPEAAIE---------------------AVFKFLEDLGLPTHLADLGVSKEDIPKLAE 268
|
|
| Fe-ADH_2 |
pfam13685 |
Iron-containing alcohol dehydrogenase; |
53-331 |
3.24e-08 |
|
Iron-containing alcohol dehydrogenase;
Pssm-ID: 404557 [Multi-domain] Cd Length: 251 Bit Score: 54.23 E-value: 3.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 53 RYGAGVTKEVGMDLQNMGAKNVCLMTDKNLSQLPpVQIVMDSLSKNGISFQVYDDVRVEPTDGSFMDAIEFAKKGAFDAY 132
Cdd:pfam13685 1 VIGPGALGRLGEYLAELGFRRVALVADANTYAAA-GRKVAESLKRAGIEVETRLEVAGNADMETAEKLVGALRERDADAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 133 VAVGGGSTMDTCKAA----NL-YASSPHSEFLDYVNAP----IGKGKPVTVPLKPLIAVpttsgtgsettgvaIFDyehl 203
Cdd:pfam13685 80 VGVGGGTVIDLAKYAafklGKpFISVPTAASNDGFASPgaslTVDGKKRSIPAAAPFGV--------------IAD---- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 204 kvkTGIASRAikptlglvdPLHTLHmpcqvvanSGF-DvlchALESYTAIPYSMRSpcpsnpiqrpayqGSNPISDIWAV 282
Cdd:pfam13685 142 ---TDVIAAA---------PRRLLA--------SGVgD----LLAKITAVADWELA-------------HAEEVAAPLAL 184
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 30424876 283 HALQIVAKYLKRAVRNPDDLEARSKMHLASAFAGIGFGNAGVHLCHGMS 331
Cdd:pfam13685 185 LSAAMVMNFADRPLRDPGDIEALAELLSALAMGGAGSSRPASGSEHLIS 233
|
|
| PRK15138 |
PRK15138 |
alcohol dehydrogenase; |
94-444 |
1.56e-07 |
|
alcohol dehydrogenase;
Pssm-ID: 185092 [Multi-domain] Cd Length: 387 Bit Score: 53.26 E-value: 1.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 94 SLSKNGISFQVYD-----DVR----VEP--TDGSFMDAIEFAKKGAFDAYVAVGGGSTMDTCK----AANLYASSPHSEF 158
Cdd:PRK15138 40 SVKKTGVLDQVLDalkgmDVLefggIEPnpTYETLMKAVKLVREEKITFLLAVGGGSVLDGTKfiaaAANYPENIDPWHI 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 159 LDYVNAPIGKGkpvtVPLKPLIAVPttsGTGSETTGVAIFDYEHLKVKTGIASRAIKPTLGLVDPLHTLHMPCQVVANSG 238
Cdd:PRK15138 120 LETGGKEIKSA----IPMGSVLTLP---ATGSESNAGAVISRKTTGDKQAFHSPHVQPVFAVLDPVYTYTLPPRQVANGV 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 239 FDVLCHALESYTAIPYSMRspcpsnpiqrpayqgsnpISDIWAVHALQIVAKYLKRAVRNPDDLEARSKMHLASAFAGIG 318
Cdd:PRK15138 193 VDAFVHTVEQYVTYPVDAK------------------IQDRFAEGILLTLIEEGPKALKEPENYDVRANVMWAATQALNG 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 319 FGNAGVH---LCHGMSYPISGLvktykakeYNVDHplvPHGLSVVLtsPAVFTFTAQMFPERHLETAGILGaNIRT---- 391
Cdd:PRK15138 255 LIGAGVPqdwATHMLGHELTAM--------HGLDH---AQTLAIVL--PALWNEKRDTKRAKLLQYAERVW-NITEgsdd 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 30424876 392 ARIqDAGLvlaDALRKFLFDLNVDDGLAALGYSKDDIPSLVKgTLPQERVTKL 444
Cdd:PRK15138 321 ERI-DAAI---AATRNFFEQMGVPTRLSDYGLDGSSIPALLK-KLEEHGMTQL 368
|
|
| Fe-ADH_KdnB-like |
cd08184 |
Iron-containing alcohol dehydrogenase similar to Shewanella oneidensis KdnB required for Kdo8N ... |
49-335 |
4.30e-06 |
|
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: 48.80 E-value: 4.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 49 VSNIRYGAGVTKEVGMDLQNMGAKN---VCLMTDKN------LSQLPPVQIvmDSLskngisfqVYDDVRVEPTDG---S 116
Cdd:cd08184 1 VPKYLFGRGSFDQLGELLAERRKSNndyVVFFIDDVfkgkplLDRLPLQNG--DLL--------IFVDTTDEPKTDqidA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 117 FMDAIEFAKKGAFDAYVAVGGGSTMDTCKA-ANLYA---SSPHSEFLDYVnapigKGKPVtvplkPLIAVPTTSGTGSET 192
Cdd:cd08184 71 LRAQIRAENDKLPAAVVGIGGGSTMDIAKAvSNMLTnpgSAADYQGWDLV-----KNPGI-----YKIGVPTLSGTGAEA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 193 TGVAIFDYEHLKVktGIASRAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTAipySMRspcpsnpiqrpayqg 272
Cdd:cd08184 141 SRTAVLTGPEKKL--GINSDYTVFDQVILDPELIATVPRDQYFYTGMDCYIHCVESLNG---TYR--------------- 200
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30424876 273 sNPISDIWAVHALQIVAK-YLKRAVRNPDDLEarsKMHLASAFAGIGFGNAGVHLCHGMSYPIS 335
Cdd:cd08184 201 -NAFGDAYAEKALELCRDvFLSDDMMSPENRE---KLMVASYLGGSSIANSQVGVCHALSYGLS 260
|
|
| G1PDH-like |
cd08174 |
Glycerol-1-phosphate dehydrogenase-like; These glycerol-1-phosphate dehydrogenase-like ... |
50-152 |
5.39e-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: 48.29 E-value: 5.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 50 SNIRYGAGVTKEVG--MDLQNMGAKNVCLMTDKNLSQLPpVQIVMDSLSKNGISFQVYDdvrvePTDGSFMDAIEFA-KK 126
Cdd:cd08174 2 LILKIEEGALEHLGkyLADRNQGFGKVAIVTGEGIDELL-GEDILESLEEAGEIVTVEE-----NTDNSAEELAEKAfSL 75
|
90 100
....*....|....*....|....*.
gi 30424876 127 GAFDAYVAVGGGSTMDTCKaanlYAS 152
Cdd:cd08174 76 PKVDAIVGIGGGKVLDVAK----YAA 97
|
|
| GldA |
COG0371 |
Glycerol dehydrogenase or related enzyme, iron-containing ADH family [Energy production and ... |
50-147 |
6.48e-06 |
|
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: 48.24 E-value: 6.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 50 SNIRYGAGVTKEVGMDLQNMGaKNVCLMTDKNLSQLppVQ-IVMDSLSKNGISFQVYDdVRVEPTDGSFMDAIEFAKKGA 128
Cdd:COG0371 7 RRYVQGEGALDELGEYLADLG-KRALIITGPTALKA--AGdRLEESLEDAGIEVEVEV-FGGECSEEEIERLAEEAKEQG 82
|
90
....*....|....*....
gi 30424876 129 FDAYVAVGGGSTMDTCKAA 147
Cdd:COG0371 83 ADVIIGVGGGKALDTAKAV 101
|
|
| Gro1PDH |
cd08173 |
Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) catalyzes the reversible conversion between ... |
50-182 |
5.09e-05 |
|
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: 45.24 E-value: 5.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 50 SNIRYGAGVTKEVGMDLQNMG-AKNVCLMTDKNLSQLPpVQIVMDSLSKNGISFQVYDDVRVEpTDGSFMDAIEFAKKGA 128
Cdd:cd08173 3 RNVVVGHGAINKIGEVLKKLLlGKRALIITGPNTYKIA-GKRVEDLLESSGVEVVIVDIATIE-EAAEVEKVKKLIKESK 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30424876 129 FDAYVAVGGGSTMDTCK--AANL---YASSPHSEFLDYVNAP----IGKGKPVTVPLKPLIAV 182
Cdd:cd08173 81 ADFIIGVGGGKVIDVAKyaAYKLnlpFISIPTSASHDGIASPfasiKGGDKPYSIKAKAPIAI 143
|
|
| GlyDH |
cd08170 |
Glycerol dehydrogenases (GlyDH) catalyzes oxidation of glycerol to dihydroxyacetone in ... |
53-154 |
6.96e-05 |
|
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: 44.71 E-value: 6.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 53 RY--GAGVTKEVGMDLQNMGaKNVCLMTDKNLsqLPPV-QIVMDSLSKNGISFQVYDdVRVEPTDGSFMDAIEFAKKGAF 129
Cdd:cd08170 3 RYvqGPGALDRLGEYLAPLG-KKALVIADPFV--LDLVgERLEESLEKAGLEVVFEV-FGGECSREEIERLAAIARANGA 78
|
90 100
....*....|....*....|....*
gi 30424876 130 DAYVAVGGGSTMDTCKAANLYASSP 154
Cdd:cd08170 79 DVVIGIGGGKTIDTAKAVADYLGLP 103
|
|
| GlyDH-like |
cd08550 |
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins. ... |
53-147 |
1.43e-03 |
|
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: 40.60 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424876 53 RY--GAGVTKEVGMDLQNMGaKNVCLMTDKN-LSQLppVQIVMDSLSKNGISFQV--YDDvrvEPTDGSFMDAIEFAKKG 127
Cdd:cd08550 3 RYiqEPGILAKAGEYIAPLG-KKALIIGGKTaLEAV--GEKLEKSLEEAGIDYEVevFGG---ECTEENIERLAEKAKEE 76
|
90 100
....*....|....*....|
gi 30424876 128 AFDAYVAVGGGSTMDTCKAA 147
Cdd:cd08550 77 GADVIIGIGGGKVLDTAKAV 96
|
|
| |
