|
Name |
Accession |
Description |
Interval |
E-value |
| HOT |
cd08190 |
Hydroxyacid-oxoacid transhydrogenase (HOT) involved in gamma-hydroxybutyrate metabolism; This ... |
3-416 |
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: 727.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 3 VSNIRYGAGVTKEVGMDLQNMGAKNVCLMTDKNLSQLPPVQIVMDSLSKNGISFQVYDDVRVEPTDGSFMDAIEFAKKGA 82
Cdd:cd08190 1 ASNIRFGPGATRELGMDLKRLGAKKVLVVTDPGLAKLGLVERVLESLEKAGIEVVVYDGVRVEPTDESFEEAIEFAKEGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 83 FDAYVAVGGGSTMDTCKAANLYASSPhSEFLDYVNAPIGKGKPVTVPLKPLIAVPTTSGTGSETTGVAIFDYEHLKVKTG 162
Cdd:cd08190 81 FDAFVAVGGGSVIDTAKAANLYATHP-GDFLDYVNAPIGKGKPVPGPLKPLIAIPTTAGTGSETTGVAIFDLEELKVKTG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 163 IASRAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTAIPYSMRsPCPSNPIQRPAYQGSNPISDIWAVHALQIV 242
Cdd:cd08190 160 ISSRYLRPTLAIVDPLLTLTLPPRVTASSGFDVLCHALESYTARPYNAR-PRPANPDERPAYQGSNPISDVWAEKAIELI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 243 AKYLKRAVRNPDDLEARSKMHLASAFAGIGFGNAGVHLCHGMSYPISGLVKTYKAKEYNVDHPLVPHGLSVVLTSPAVFT 322
Cdd:cd08190 239 GKYLRRAVNDGDDLEARSNMLLASTLAGIGFGNAGVHLPHAMAYPIAGLVKDYRPPGYPVDHPHVPHGLSVALTAPAVFR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 323 FTAQMFPERHLETAGILGANIRTARIQDAGLVLADALRKFLFDLNVDDGLAALGYSKDDIPSLVKGTLPQERVTKLAPRA 402
Cdd:cd08190 319 FTAPACPERHLEAAELLGADTSGASDRDAGEVLADALIKLMRDIGIPNGLSALGYSEDDIPALVEGTLPQQRLLKLNPRP 398
|
410
....*....|....
gi 568905513 403 QSEEDLSALFEASM 416
Cdd:cd08190 399 VTEEDLEEIFEDAL 412
|
|
| EutG |
COG1454 |
Alcohol dehydrogenase, class IV [Energy production and conversion]; |
6-416 |
7.43e-110 |
|
Alcohol dehydrogenase, class IV [Energy production and conversion];
Pssm-ID: 441063 [Multi-domain] Cd Length: 381 Bit Score: 327.85 E-value: 7.43e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 6 IRYGAGVTKEVGMDLQNMGAKNVCLMTDKNLSQLPPVQIVMDSLSKNGISFQVYDDVRVEPTDGSFMDAIEFAKKGAFDA 85
Cdd:COG1454 11 IVFGAGALAELGEELKRLGAKRALIVTDPGLAKLGLLDRVLDALEAAGIEVVVFDDVEPNPTVETVEAGAAAAREFGADV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 86 YVAVGGGSTMDTCKAANLYASSPHSeFLDYVNApigkgKPVTVPLKPLIAVPttsgtgsettGVAIFDYEHLKVKTGIAS 165
Cdd:COG1454 91 VIALGGGSAIDAAKAIALLATNPGD-LEDYLGI-----KKVPGPPLPLIAIPttagtgsevtPFAVITDPETGVKKGIAD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 166 RAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTAIpysmrspcpsnpiqrpayqGSNPISDIWAVHALQIVAKY 245
Cdd:COG1454 165 PELLPDVAILDPELTLTLPPSLTAATGMDALTHAIEAYVSK-------------------GANPLTDALALEAIRLIARN 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 246 LKRAVRNPDDLEARSKMHLASAFAGIGFGNAGVHLCHGMSYPISGLvktykakeYNvdhplVPHGLSVVLTSPAVFTFTA 325
Cdd:COG1454 226 LPRAVADGDDLEAREKMALASLLAGMAFANAGLGAVHALAHPLGGL--------FH-----VPHGLANAILLPHVLRFNA 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 326 QMFPERHLETAGILGANIrTARIQDAGLVLADALRKFLFDLNVDDGLAALGYSKDDIPSLVKGTLpQERVTKLAPRAQSE 405
Cdd:COG1454 293 PAAPERYAEIARALGLDV-GLSDEEAAEALIEAIRELLRDLGIPTRLSELGVTEEDLPELAELAL-ADRCLANNPRPLTE 370
|
410
....*....|.
gi 568905513 406 EDLSALFEASM 416
Cdd:COG1454 371 EDIEAILRAAY 381
|
|
| Fe-ADH |
cd08551 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains large ... |
4-412 |
3.62e-105 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains large metal-containing alcohol dehydrogenases (ADH), known as iron-containing alcohol dehydrogenases. They contain a dehydroquinate synthase-like protein structural fold and mostly contain iron. They are distinct from other alcohol dehydrogenases which contains different protein domains. There are several distinct families of alcohol dehydrogenases: Zinc-containing long-chain alcohol dehydrogenases, insect-type, or short-chain alcohol dehydrogenases, iron-containing alcohol dehydrogenases, among others. The iron-containing family has a Rossmann fold-like topology that resembles the fold of the zinc-dependent alcohol dehydrogenases, but lacks sequence homology, and differs in strand arrangement. ADH catalyzes the reversible oxidation of alcohol to acetaldehyde with the simultaneous reduction of NAD(P)+ to NAD(P)H.
Pssm-ID: 341481 [Multi-domain] Cd Length: 372 Bit Score: 315.54 E-value: 3.62e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 4 SNIRYGAGVTKEVGMDLQNMGAKNVCLMTDKNLSQLPPVQIVMDSLSKNGISFQVYDDVRVEPTDGSFMDAIEFAKKGAF 83
Cdd:cd08551 2 TRIVFGAGALARLGEELKALGGKKVLLVTDPGLVKAGLLDKVLESLKAAGIEVEVFDDVEPNPTVETVEAAAELAREEGA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 84 DAYVAVGGGSTMDTCKAANLYASSPHSeFLDYVNapigkGKPVTVPLKPLIAVPttsgtgsettGVAIFDYEHLKVKTGI 163
Cdd:cd08551 82 DLVIAVGGGSVLDTAKAIAVLATNGGS-IRDYEG-----IGKVPKPGLPLIAIPttagtgsevtPNAVITDPETGRKMGI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 164 ASRAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTAIPysmrspcpsnpiqrpayqgSNPISDIWAVHALQIVA 243
Cdd:cd08551 156 VSPYLLPDVAILDPELTLSLPPSVTAATGMDALTHAIEAYTSKK-------------------ANPISDALALEAIRLIG 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 244 KYLKRAVRNPDDLEARSKMHLASAFAGIGFGNAGVHLCHGMSYPISGlvktykakEYNvdhplVPHGLSVVLTSPAVFTF 323
Cdd:cd08551 217 KNLRRAVADGSDLEAREAMLLASLLAGIAFGNAGLGAVHALAYPLGG--------RYH-----IPHGVANAILLPYVMEF 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 324 TAQMFPERHLETAGILGANIRTARIQDAGLVLADALRKFLFDLNVDDGLAALGYSKDDIPSLVKGTLPQERVTKLAPRAQ 403
Cdd:cd08551 284 NLPACPEKYAEIAEALGEDVEGLSDEEAAEAAVEAVRELLRDLGIPTSLSELGVTEEDIPELAEDAMKSGRLLSNNPRPL 363
|
....*....
gi 568905513 404 SEEDLSALF 412
Cdd:cd08551 364 TEEDIREIY 372
|
|
| Fe-ADH |
pfam00465 |
Iron-containing alcohol dehydrogenase; |
4-408 |
4.82e-94 |
|
Iron-containing alcohol dehydrogenase;
Pssm-ID: 425696 [Multi-domain] Cd Length: 362 Bit Score: 286.81 E-value: 4.82e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 4 SNIRYGAGVTKEVGMDLQNMGAKnVCLMTDKNLSQLPPVQIVMDSLSKNGISFQVYDDVRVEPTDGSFMDAIEFAKKGAF 83
Cdd:pfam00465 2 TRIVFGAGALAELGEELKRLGAR-ALIVTDPGSLKSGLLDKVLASLEEAGIEVVVFDGVEPEPTLEEVDEAAALAREAGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 84 DAYVAVGGGSTMDTCKAANLYASSPHSEFLDYvnapigKGKPVTVPLKPLIAVPTTSGTGSETTGVAIFDYEHLKVKTGI 163
Cdd:pfam00465 81 DVIIAVGGGSVIDTAKAIALLLTNPGDVWDYL------GGKPLTKPALPLIAIPTTAGTGSEVTPLAVITDTETGEKLGI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 164 ASRAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTAipysmrspcpsnpiqrpayQGSNPISDIWAVHALQIVA 243
Cdd:pfam00465 155 FSPKLLPDLAILDPELTLTLPPRLTAATGMDALAHAVEAYVS-------------------KGANPLTDALALEAIRLIA 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 244 KYLKRAVRNPDDLEARSKMHLASAFAGIGFGNAGVHLCHGMSYPISGLVKtykakeynvdhplVPHGLSVVLTSPAVFTF 323
Cdd:pfam00465 216 ENLPRAVADGEDLEARENMLLASTLAGLAFSNAGLGAAHALAHALGGRYG-------------IPHGLANAILLPYVLRF 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 324 TAQMFPERHLETAGILGANIRTARIQDAglvlADALRKFLFDLNVDDGLAALGYSKDDIPSLVKGTLpQERVTKLAPRAQ 403
Cdd:pfam00465 283 NAPAAPEKLAQLARALGEDSDEEAAEEA----IEALRELLRELGLPTTLSELGVTEEDLDALAEAAL-RDRSLANNPRPL 357
|
....*
gi 568905513 404 SEEDL 408
Cdd:pfam00465 358 TAEDI 362
|
|
| Fe-ADH-like |
cd14863 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
6-414 |
1.44e-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: 260.55 E-value: 1.44e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 6 IRYGAGVTKEVGMDLQNMGAKNVCLMTDKNLSQLPPVQIVMDSLSKNGISFQVYDDVRVEPTDGSFMDAIEFAKKGAFDA 85
Cdd:cd14863 8 VIFGAGAVEQIGELLKELGCKKVLLVTDKGLKKAGIVDKIIDLLEEAGIEVVVFDDVEPDPPDEIVDEAAEIAREEGADG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 86 YVAVGGGSTMDTCKAANLYASSPHsEFLDYvnapIGKGKPVTVPLKPLIAVPTTSGTGSETTGVAIFDYEHLKVKTGIAS 165
Cdd:cd14863 88 VIGIGGGSVLDTAKAIAVLLTNPG-PIIDY----ALAGPPVPKPGIPLIAIPTTAGTGSEVTPIAVITDEENGVKKSLLG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 166 RAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTAipysmrspcpsnpiqrpayQGSNPISDIWAVHALQIVAKY 245
Cdd:cd14863 163 PFLVPDLAILDPELTVGLPPSLTAATGMDALSHAIEAYTS-------------------KLANPMTDALALQAIRLIVKN 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 246 LKRAVRNPDDLEARSKMHLASAFAGIGFGNAGVHLCHGMSYPISGLvktykakeYNvdhplVPHGLSVVLTSPAVFTFTA 325
Cdd:cd14863 224 LPRAVKDGDNLEARENMLLASNLAGIAFNNAGTHIGHAIAHALGAL--------YH-----IPHGLACALALPVVLEFNA 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 326 QMFPERHLETAGILGANIRTARIQDAGLVLADALRKFLFDLNVDDGLAALGYSKDDIPSLVKGTLpQERVTKLAPRAQSE 405
Cdd:cd14863 291 EAYPEKVKKIAKALGVSFPGESDEELGEAVADAIREFMKELGIPSLFEDYGIDKEDLDKIAEAVL-KDPFAMFNPRPITE 369
|
....*....
gi 568905513 406 EDLSALFEA 414
Cdd:cd14863 370 EEVAEILEA 378
|
|
| Fe-ADH-like |
cd08185 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
5-413 |
1.33e-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: 240.09 E-value: 1.33e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 5 NIRYGAGVTKEVGmDLQNMGAKNVCLMTDKNLSQLPPV-QIVMDSLSKNGISFQVYDDVRVEPTDGSFMDAIEFAKKGAF 83
Cdd:cd08185 6 RILFGAGKLNELG-EEALRPGKKALIVTGKGSSKKTGLlDRVKKLLEKAGVEVVVFDKVEPNPLTTTVMEGAALAKEEGC 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 84 DAYVAVGGGSTMDTCKAANLYASSPHSEFlDYVNAPIGKGKPVTVPLkPLIAVPTTSGTGSETTGVAIFDYEHLKVKTGI 163
Cdd:cd08185 85 DFVIGLGGGSSMDAAKAIAFMATNPGDIW-DYIFGGTGKGPPPEKAL-PIIAIPTTAGTGSEVDPWAVITNPETKEKKGI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 164 ASRAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTAIpysmrspcpsnpiqrpayqGSNPISDIWAVHALQIVA 243
Cdd:cd08185 163 GHPALFPKVSIVDPELMLTVPPRVTAYTGFDALFHAFESYISK-------------------NANPFSDMLALEAIRLVA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 244 KYLKRAVRNPDDLEARSKMHLASAFAGIGFGNAGVHLCHGMSYPISGLvktykakeynvdHPLVPHGLSVVLTSPAVFTF 323
Cdd:cd08185 224 KYLPRAVKDGSDLEAREKMAWASTLAGIVIANSGTTLPHGLEHPLSGY------------HPNIPHGAGLAALYPAYFEF 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 324 TAQMFPERhleTAGILGANIRTARIQDAGLVLADALRKFLFDLNVDDGLAALGYSKDDIPSLVkgtlpqERVTKLA---- 399
Cdd:cd08185 292 TIEKAPEK---FAFVARAEASGLSDAKAAEDFIEALRKLLKDIGLDDLLSDLGVTEEDIPWLA------ENAMETMgglf 362
|
410
....*....|....*..
gi 568905513 400 ---PRAQSEEDLSALFE 413
Cdd:cd08185 363 annPVELTEEDIVEIYE 379
|
|
| Fe-ADH-like |
cd08191 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
4-416 |
5.41e-75 |
|
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: 239.05 E-value: 5.41e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 4 SNIRYGAGVTKEVGMDLQNMGAKnVCLMTDKNLSQLPPVQIVMDSLSKNGISFQVYDDVRVEPTDGSFMDAIEFAKKGAF 83
Cdd:cd08191 5 SRLLFGPGARRALGRVAARLGSR-VLIVTDPRLASTPLVAELLAALTAAGVAVEVFDGGQPELPVSTVADAAAAARAFDP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 84 DAYVAVGGGSTMDTCKAANLYASSPhSEFLDYvnapIGKGKpVTVPLKPLIAVPTTSGTGSETTGVAIFDYEHLKVKTGI 163
Cdd:cd08191 84 DVVIGLGGGSNMDLAKVVALLLAHG-GDPRDY----YGEDR-VPGPVLPLIAVPTTAGTGSEVTPVAVLTDPARGMKVGV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 164 ASRAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTAIPysmRSPCPSNPiQRPAYQGSNPISDIWAVHALQIVA 243
Cdd:cd08191 158 SSPYLRPAVAIVDPELTLTCPPGVTADSGIDALTHAIESYTARD---FPPFPRLD-PDPVYVGKNPLTDLLALEAIRLIG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 244 KYLKRAVRNPDDLEARSKMHLASAFAGIGFGNAGVHLCHGMSYPISGLVKTykakeynvdhplvPHGLSVVLTSPAVFTF 323
Cdd:cd08191 234 RHLPRAVRDGDDLEARSGMALAALLAGLAFGTAGTAAAHALQYPIGALTHT-------------SHGVGNGLLLPYVMRF 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 324 TAQMFPERHLETAGILGANiRTARIQDAGLVLADALRKFLFDLNVDDGLAALGYSKDDIPSLVKGTLPQERVTKLAPRAQ 403
Cdd:cd08191 301 NRPARAAELAEIARALGVT-TAGTSEEAADRAIERVEELLARIGIPTTLADLGVTEADLPGLAEKALSVTRLIANNPRPP 379
|
410
....*....|...
gi 568905513 404 SEEDLSALFEASM 416
Cdd:cd08191 380 TEEDLLRILRAAF 392
|
|
| Fe-ADH-like |
cd08196 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
5-412 |
1.08e-72 |
|
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: 232.08 E-value: 1.08e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 5 NIRYGAGVTKEVGMDLQNMGAKNVCLMTDKNLSQLPPVQIVMDSLSKNGISfqVYDDVRVEPTDGSFMDAIEFAKKGAFD 84
Cdd:cd08196 8 KIIFGEGILKELPDIIKELGGKRGLLVTDPSFIKSGLAKRIVESLKGRIVA--VFSDVEPNPTVENVDKCARLARENGAD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 85 AYVAVGGGSTMDTCKAANLYASSPHSeFLDYvnapIGKGKPVTVPLKPLIAVPTTSGTGSETTGVAIFDYEHLKVKTGIA 164
Cdd:cd08196 86 FVIAIGGGSVLDTAKAAACLAKTDGS-IEDY----LEGKKKIPKKGLPLIAIPTTAGTGSEVTPVAVLTDKEKGKKAPLV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 165 SRAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTAIpysmrspcpsnpiqrpayqGSNPISDIWAVHALQIVAK 244
Cdd:cd08196 161 SPGFYPDIAIVDPELTYSMPPKVTASTGIDALCHAIEAYWSI-------------------NHQPISDALALEAAKLVLE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 245 YLKRAVRNPDDLEARSKMHLASAFAGIGFGNAGVHLCHGMSYPISglvktykaKEYNvdhplVPHGLSVVLTSPAVFTFT 324
Cdd:cd08196 222 NLEKAYNNPNDKEAREKMALASLLAGLAFSQTRTTASHACSYPLT--------SHFG-----IPHGEACALTLPSFIRLN 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 325 AQMFPERHLETAGILGANirtariqDAGLvLADALRKFLFDLNVDDGLAALGYSKDDIPSLVKGTLPQERVtKLAPRAQS 404
Cdd:cd08196 289 AEALPGRLDELAKQLGFK-------DAEE-LADKIEELKKRIGLRTRLSELGITEEDLEEIVEESFHPNRA-NNNPVEVT 359
|
....*...
gi 568905513 405 EEDLSALF 412
Cdd:cd08196 360 KEDLEKLL 367
|
|
| Fe-ADH-like |
cd08194 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
4-414 |
7.13e-72 |
|
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: 230.50 E-value: 7.13e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 4 SNIRYGAGVTKEVGMDLQNMGAKNVCLMTDKNLSQLPPVQIVMDSLSKNGISFQVYDDVRVEPTDGSFMDAIEFAKKGAF 83
Cdd:cd08194 2 RTIIIGGGALEELGEEAASLGGKRALIVTDKVMVKLGLVDKVTQLLAEAGIAYAVFDDVVSEPTDEMVEEGLALYKEGGC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 84 DAYVAVGGGSTMDTCKAANLYASSPhSEFLDYVNAPIGKGKPVtvplkPLIAVPTTSGTGSETTGVAIFDYEHLKVKTGI 163
Cdd:cd08194 82 DFIVALGGGSPIDTAKAIAVLATNG-GPIRDYMGPRKVDKPGL-----PLIAIPTTAGTGSEVTRFTVITDTETDVKMLL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 164 ASRAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTaipySMRspcpsnpiqrpayqgSNPISDIWAVHALQIVA 243
Cdd:cd08194 156 KGPALLPAVAIVDPELTLSMPPRVTAATGIDALTHAIEAYV----SRK---------------AQPLTDTLALSAIKLIG 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 244 KYLKRAVRNPDDLEARSKMHLASAFAGIGFGNAGVHLCHGMSYPISGLVktykakeynvdHplVPHGLSVVLTSPAVFTF 323
Cdd:cd08194 217 RNLRRAYADGDDLEAREAMMLAALEAGIAFSNSSVALVHGMSRPIGALF-----------H--VPHGLSNAMLLPAVTEF 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 324 TAQMFPERHLETAGILGANIRTARIQDAGLVLADALRKFLFDLNVdDGLAALGYSKDD----IPSLVKGTL----PQerv 395
Cdd:cd08194 284 SLPGAPERYAEIARAMGIATEGDSDEEAAEKLVEALERLCADLEI-PTLREYGIDEEEfeaaLDKMAEDALasgsPA--- 359
|
410
....*....|....*....
gi 568905513 396 tkLAPRAQSEEDLSALFEA 414
Cdd:cd08194 360 --NNPRVPTKEEIIELYRE 376
|
|
| Fe-ADH-like |
cd17814 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
8-390 |
2.93e-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: 220.88 E-value: 2.93e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 8 YGAGVTKEVGMDLQNMGAKNVCLMTDKNLSQLPPVQIVMDSLSKNGISFQVYDDVRVEPTDGSFMDAIE-FAKKGAfDAY 86
Cdd:cd17814 9 FGVGARKLAGRYAKNLGARKVLVVTDPGVIKAGWVDEVLDSLEAEGLEYVVFSDVTPNPRDFEVMEGAElYREEGC-DGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 87 VAVGGGSTMDTCKAANLYASSpHSEFLDYvnapIGKGKpVTVPLKPLIAVPTTSGTGSETTGVAIFDYEHLKVKTGIASR 166
Cdd:cd17814 88 VAVGGGSPIDCAKGIGIVVSN-GGHILDY----EGVDK-VRRPLPPLICIPTTAGSSADVSQFAIITDTERRVKMAIISK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 167 AIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTaipysmrspcpSNpiqrpayqGSNPISDIWAVHALQIVAKYL 246
Cdd:cd17814 162 TLVPDVSLIDPETLTTMDPELTACTGMDALTHAIEAYV-----------SN--------ASSPLTDLHALEAIRLISENL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 247 KRAVRNPDDLEARSKMHLASAFAGIGFGNAGVHLCHGMSYPISGLvktykakeynVDhplVPHGLSVVLTSPAVFTFTAQ 326
Cdd:cd17814 223 PKAVADPDDLEAREKMMLASLQAGLAFSNASLGAVHAMAHSLGGL----------LD---LPHGECNALLLPHVIRFNFP 289
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568905513 327 MFPERHLETAGILGANIRTARIQDAGLVLADALRKFLFDLNVDDGLAALGYSKDDIPSLVKGTL 390
Cdd:cd17814 290 AAPERYRKIAEAMGLDVDGLDDEEVAERLIEAIRDLREDLGIPETLSELGVDEEDIPELAKRAM 353
|
|
| LPO |
cd08176 |
Lactadehyde:propanediol oxidoreductase (LPO) catalyzes the interconversion between ... |
8-413 |
9.66e-65 |
|
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: 212.02 E-value: 9.66e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 8 YGAGVTKEVGMDLQNMGAKNVCLMTDKNLSQLPPVQIVMDSLSKNGISFQVYDDVRVEPTDGSFMDAIEFAKKGAFDAYV 87
Cdd:cd08176 11 FGWGAIEEIGEEAKKRGFKKALIVTDKGLVKFGIVDKVTDVLKEAGIAYTVFDEVKPNPTIENVMAGVAAYKESGADGII 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 88 AVGGGSTMDTCKAANLYASSPhseFLDyVNAPIGKgKPVTVPLKPLIAVPTTSGTGSETTGVA-IFDYEHlKVKTGIASR 166
Cdd:cd08176 91 AVGGGSSIDTAKAIGIIVANP---GAD-VRSLEGV-APTKNPAVPIIAVPTTAGTGSEVTINYvITDTEK-KRKFVCVDP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 167 AIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTAipysmrspcpsnpiqrpayQGSNPISDIWAVHALQIVAKYL 246
Cdd:cd08176 165 HDIPTVAIVDPDLMSSMPKGLTAATGMDALTHAIEGYIT-------------------KGAWELSDMLALKAIELIAKNL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 247 KRAVRNPDDLEARSKMHLASAFAGIGFGNAGVHLCHGMSYPISGLvktykakeYNvdhplVPHGLSVVLTSPAVFTFTAQ 326
Cdd:cd08176 226 RKAVANPNNVEARENMALAQYIAGMAFSNVGLGIVHSMAHPLSAF--------YD-----TPHGVANAILLPYVMEFNAP 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 327 MFPERHLETAGILGANIRTARIQDAGLVLADALRKFLFDLNVDDGLAALGYSKDDIPSLVKGTLpQERVTKLAPRAQSEE 406
Cdd:cd08176 293 ATGEKYRDIARAMGVDTTGMSDEEAAEAAVDAVKKLSKDVGIPQKLSELGVKEEDIEALAEDAL-NDVCTPGNPREATKE 371
|
....*..
gi 568905513 407 DLSALFE 413
Cdd:cd08176 372 DIIALYK 378
|
|
| Fe-ADH-like |
cd14862 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
20-412 |
2.41e-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: 205.54 E-value: 2.41e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 20 LQNMGAKNVCLMTDKNLSQLPPVQIVMDSLSKNGISFQVYDDVRVEPTDGSFMDAIEFAKKGAFDAYVAVGGGSTMDTCK 99
Cdd:cd14862 19 LEQLSGKRALIVTDKVLVKLGLLKKVLKRLLQAGFEVEVFDEVEPEPPLETVLKGAEAMREFEPDLIIALGGGSVMDAAK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 100 AANLYASSPHSEFLDYV-NAPIGKGKpvtvplKP-LIAVPTTSGTGSETTGVAIFDYEHLKVKTGIASRAIKPTLGLVDP 177
Cdd:cd14862 99 AAWVLYERPDLDPEDISpLDLLGLRK------KAkLIAIPTTSGTGSEATWAIVLTDTEEPRKIAVANPELVPDVAILDP 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 178 LHTLHMPCQVVANSGFDVLCHALESYTAipysmrspcpsnpiqrpayQGSNPISDIWAVHALQIVAKYLKRAVRNPDDLE 257
Cdd:cd14862 173 EFVLGMPPKLTAGTGLDALAHAVEAYLS-------------------TWSNDFSDALALKAIELIFKYLPRAYKDGDDLE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 258 ARSKMHLASAFAGIGFGNAGVHLCHGMSYPISGLVKtykakeynvdhplVPHGLSVVLTSPAVFTFTAQmFPERHLETAG 337
Cdd:cd14862 234 AREKMHNAATIAGLAFGNSQAGLAHALGHSLGAVFH-------------VPHGIAVGLFLPYVIEFYAK-VTDERYDLLK 299
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568905513 338 ILGANIRTAriQDAGLVLADALRKFLFDLNVDDGLAALGYSKDD----IPSLVKGTLpQERVTKLAPRAQSEEDLSALF 412
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) ... |
9-413 |
3.23e-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: 202.74 E-value: 3.23e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 9 GAGVTKEVGMDLQNMGAKNVCLMTDKNLSQLPPVQIVMDSLSKNGISFQVYDDVRVEPTDGSFMDAIEFAKKGAFDAYVA 88
Cdd:cd08188 12 GPGCLKEIGDELKKLGGKKALIVTDKGLVKLGLVKKVTDVLEEAGIEYVIFDGVQPNPTVTNVNEGLELFKENGCDFIIS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 89 VGGGSTMDTCKAANLYASSPhSEFLDYVNapIGKgkpVTVPLKPLIAVPTTSGTGSETTGVAIFDYEHLKVKTGIASRAI 168
Cdd:cd08188 92 VGGGSAHDCAKAIGILATNG-GEIEDYEG--VDK---SKKPGLPLIAINTTAGTASEVTRFAVITDEERHVKMVIVDWNV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 169 KPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTAIpysmrspcpsnpiqrpayqGSNPISDIWAVHALQIVAKYLKR 248
Cdd:cd08188 166 TPTIAVNDPELMLGMPPSLTAATGMDALTHAIEAYVST-------------------GATPLTDALALEAIRLIAENLPK 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 249 AVRNPDDLEARSKMHLASAFAGIGFGNAGVHLCHGMSYPISGLvktykakeYNvdhplVPHGL--SVVLtsPAVFTFTAQ 326
Cdd:cd08188 227 AVANGKDLEARENMAYAQFLAGMAFNNAGLGYVHAMAHQLGGF--------YN-----LPHGVcnAILL--PHVMEFNLP 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 327 MFPERHLETAGILGANIRTARIQDAGLVLADALRKFLFDLNVDDGLAALGYSKDDIPSLVKGTLpQERVTKLAPRAQSEE 406
Cdd:cd08188 292 ACPERFADIARALGENTEGLSDEEAAEAAIEAIRKLSRRVGIPSGLKELGVKEEDFPLLAENAL-KDACGPTNPRQATKE 370
|
....*..
gi 568905513 407 DLSALFE 413
Cdd:cd08188 371 DVIAIYR 377
|
|
| Fe-ADH-like |
cd14865 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
6-416 |
2.36e-60 |
|
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: 2.36e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 6 IRYGAGVTKEVGMDLQNMGAKNVCLMTDKNLSQLPPVQIVMDSLSKNGISFQVYDDVrvePTDGSF---MDAIEFAKKGA 82
Cdd:cd14865 9 IVSGAGALENLPAELARLGARRPLIVTDKGLAAAGLLKKVEDALGDAIEIVGVFDDV---PPDSSVavvNEAAARAREAG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 83 FDAYVAVGGGSTMDTCKAANLYASSPHSEFLDYVNAPIgkgkpVTVPLKPLIAVPTTSGTGSETTGVAIFDYEHLKVKTG 162
Cdd:cd14865 86 ADGIIAVGGGSVIDTAKGVNILLSEGGDDLDDYGGANR-----LTRPLKPLIAIPTTAGTGSEVTLVAVIKDEEKKVKLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 163 IASRAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTAIpysmrspcpsnpiqrpayqGSNPISDIWAVHALQIV 242
Cdd:cd14865 161 FVSPFLLPDVAILDPRLTLSLPPKLTAATGMDALTHAIEAYTSL-------------------QKNPISDALALQAIRLI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 243 AKYLKRAVRNPDDLEARSKMHLASAFAGIGFGNAGVHLCHGMSYPISGLVKtykakeynvdhplVPHGL--SVVLtsPAV 320
Cdd:cd14865 222 SENLPKAVKNGKDLEARLALAIAATMAGIAFSNSMVGLVHAIAHAVGAVAG-------------VPHGLanSILL--PHV 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 321 FTFTAQMFPERHLETAGIL--GANIRTARIQDAGLVLADALRKFLFDLNVDDGLAALGYSKDDIPSLVKGTLpQERVTKL 398
Cdd:cd14865 287 MRYNLDAAAERYAELALALayGVTPAGRRAEEAIEAAIDLVRRLHELCGLPTRLRDVGVPEEQLEAIAELAL-NDGAILF 365
|
410
....*....|....*...
gi 568905513 399 APRAQSEEDLSALFEASM 416
Cdd:cd14865 366 NPREVDPEDILAILEAAY 383
|
|
| HVD |
cd08193 |
5-hydroxyvalerate dehydrogenase (HVD) catalyzes the oxidation of 5-hydroxyvalerate to ... |
3-414 |
3.81e-57 |
|
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: 191.96 E-value: 3.81e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 3 VSNIRYGAGVTKEVGMDLQNMGAKNVCLMTDKNLSQLPPVQIVMDSLSKNGISFQVYDDVRVEPTDGSFMDAIEFAKKGA 82
Cdd:cd08193 4 VPRIICGAGAAARLGELLRELGARRVLLVTDPGLVKAGLADPALAALEAAGIAVTVFDDVVADPPEAVVEAAVEQAREAG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 83 FDAYVAVGGGSTMDTCKAANLYASSPHSefldyVNAPIGKGKpVTVPLKPLIAVPTTSGTGSETTGVAIF-DYEHlkVKT 161
Cdd:cd08193 84 ADGVIGFGGGSSMDVAKLVALLAGSDQP-----LDDIYGVGK-ATGPRLPLILVPTTAGTGSEVTPISIVtTGET--EKK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 162 GIASRAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTAipysmRSpcpsnpiqrpayqGSNPISDIWAVHALQI 241
Cdd:cd08193 156 GVVSPQLLPDVALLDAELTLGLPPHVTAATGIDAMVHAIEAYTS-----RH-------------KKNPISDALAREALRL 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 242 VAKYLKRAVRNPDDLEARSKMHLASAFAGIGFGNAGVHLCHGMSYPISGLVKtykakeynvdhplVPHGLSVVLTSPAVF 321
Cdd:cd08193 218 LGANLRRAVEDGSDLEAREAMLLGSMLAGQAFANAPVAAVHALAYPLGGHFH-------------VPHGLSNALVLPHVL 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 322 TFTAQMFPERHLETAGILGANIRTARIQDAGLVLADALRKFLFDLNVDDGLAALGYSKDDIPSLVKGTLPQERVTKLAPR 401
Cdd:cd08193 285 RFNLPAAEALYAELARALLPGLAFGSDAAAAEAFIDALEELVEASGLPTRLRDVGVTEEDLPMLAEDAMKQTRLLVNNPR 364
|
410
....*....|...
gi 568905513 402 AQSEEDLSALFEA 414
Cdd:cd08193 365 EVTEEDALAIYQA 377
|
|
| Fe-ADH-like |
cd14861 |
Iron-containing alcohol dehydrogenases-like; This family contains proteins similar to ... |
6-416 |
2.73e-56 |
|
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: 189.64 E-value: 2.73e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 6 IRYGAGVTKEVGMDLQNMGAKNVCLMTDKNLSQLPPVQIVMDSLSKNGISFQVYDDVRVEPTDGSFMDAIEFAKKGAFDA 85
Cdd:cd14861 6 IRFGAGAIAELPEELKALGIRRPLLVTDPGLAALGIVDRVLEALGAAGLSPAVFSDVPPNPTEADVEAGVAAYREGGCDG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 86 YVAVGGGSTMDTCKAANLYASSPHSEFlDYVNAPIGkGKPVTVPLKPLIAVPTTSGTGSETTGVAIFDYEHLKVKTGIAS 165
Cdd:cd14861 86 IIALGGGSAIDAAKAIALMATHPGPLW-DYEDGEGG-PAAITPAVPPLIAIPTTAGTGSEVGRAAVITDDDTGRKKIIFS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 166 RAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTAIPYsmrspcpsnpiqrpayqgsNPISDIWAVHALQIVAKY 245
Cdd:cd14861 164 PKLLPKVAICDPELTLGLPPRLTAATGMDALTHCIEAYLSPGF-------------------HPMADGIALEGLRLISEW 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 246 LKRAVRNPDDLEARSKMHLASAFAGIGFGNaGVHLCHGMSYPISGLVKTykakeynvdhplvPHGLSVVLTSPAVFTFTA 325
Cdd:cd14861 225 LPRAVADGSDLEARGEMMMAALMGAVAFQK-GLGAVHALAHALGALYGL-------------HHGLLNAILLPYVLRFNR 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 326 QMFPERHLETAGILGANIRTAriqDAglvLADALRKFLFDLNVDDGLAALGYSKDDIPSLVKGTLpQERVTKLAPRAQSE 405
Cdd:cd14861 291 PAVEDKLARLARALGLGLGGF---DD---FIAWVEDLNERLGLPATLSELGVTEDDLDELAELAL-ADPCHATNPRPVTA 363
|
410
....*....|.
gi 568905513 406 EDLSALFEASM 416
Cdd:cd14861 364 EDYRALLREAL 374
|
|
| Fe-ADH-like |
cd08183 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
6-413 |
3.34e-55 |
|
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: 186.94 E-value: 3.34e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 6 IRYGAGVTKEVGMDLQNMGaKNVCLMTDKNLSQLPPVQIVMDSLSKNGISFQVYDDVRvEPTDGSFMDAIEFAKKGAFDA 85
Cdd:cd08183 4 IVFGRGSLQELGELAAELG-KRALLVTGRSSLRSGRLARLLEALEAAGIEVALFSVSG-EPTVETVDAAVALAREAGCDV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 86 YVAVGGGSTMDTCKAANLYASSPHS--EFLDYVnapiGKGKPVTVPLKPLIAVPTtsgtgsettgVA-----------IF 152
Cdd:cd08183 82 VIAIGGGSVIDAAKAIAALLTNEGSvlDYLEVV----GKGRPLTEPPLPFIAIPT----------TAgtgsevtknavLS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 153 DYEHlKVKTGIASRAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTAIpysmrspcpsnpiqrpayqGSNPISD 232
Cdd:cd08183 148 SPEH-GVKVSLRSPSMLPDVALVDPELTLSLPPEVTAASGLDALTQLIEPYVSR-------------------KANPLTD 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 233 IWAVHALQIVAKYLKRAVRNPDDLEARSKMHLASAFAGIGFGNAGVHLCHGMSYPISGLVKtykakeynvdhplVPHGL- 311
Cdd:cd08183 208 ALAREGLRLAARSLRRAYEDGEDLEAREDMALASLLGGLALANAGLGAVHGLAGPLGGMFG-------------APHGAi 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 312 -SVVLtsPAVFTFTAQM----FPERHLETAGILGANIRTARIQDAGLVLADALRKFLFDLNVdDGLAALGYSKDDIPSLV 386
Cdd:cd08183 275 cAALL--PPVLEANLRAlrerEPDSPALARYRELAGILTGDPDAAAEDGVEWLEELCEELGI-PRLSEYGLTEEDFPEIV 351
|
410 420
....*....|....*....|....*..
gi 568905513 387 KGTLpQERVTKLAPRAQSEEDLSALFE 413
Cdd:cd08183 352 EKAR-GSSSMKGNPIELSDEELLEILE 377
|
|
| HEPD |
cd08182 |
Hydroxyethylphosphoate dehydrogenase (HEPD) catalyzes the reduction of phosphonoacetaldehyde ... |
4-413 |
5.34e-51 |
|
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: 175.88 E-value: 5.34e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 4 SNIRYGAGVTKEVGMDLQNMGAKNVCLMTDKNLSQLPPVQIVMDSLsKNGISFQVYDDVRVEPTDGSFMDAIEFAKKGAF 83
Cdd:cd08182 2 VKIIFGPGALAELKDLLGGLGARRVLLVTGPSAVRESGAADILDAL-GGRIPVVVFSDFSPNPDLEDLERGIELFRESGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 84 DAYVAVGGGSTMDTCKAANLYASSPHSEFLdyvnAPIGKGKPVTVPLKPLIAVPTtsgtgsettgVA-----------IF 152
Cdd:cd08182 81 DVIIAVGGGSVIDTAKAIAALLGSPGENLL----LLRTGEKAPEENALPLIAIPT----------TAgtgsevtpfatIW 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 153 DyEHLKVKTGIASRAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTAIpysmrspcpsnpiqrpayqGSNPISD 232
Cdd:cd08182 147 D-EAEGKKYSLAHPSLYPDAAILDPELTLSLPLYLTASTGLDALSHAIESIWSV-------------------NANPESR 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 233 IWAVHALQIVAKYLKRAVRNPDDLEARSKMHLASAFAGIGFGNAGVHLCHGMSYPISglvktykaKEYNvdhplVPHGLS 312
Cdd:cd08182 207 AYALRAIRLILENLPLLLENLPNLEAREAMAEASLLAGLAISITKTTAAHAISYPLT--------SRYG-----VPHGHA 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 313 VVLTSPAVFTFTAQMFPERHletagilgANIRTARIQDAGLV-----LADALRKFLFDLNVDDGLAALGYSKDDIPSLVK 387
Cdd:cd08182 274 CALTLPAVLRYNAGADDECD--------DDPRGREILLALGAsdpaeAAERLRALLESLGLPTRLSEYGVTAEDLEALAA 345
|
410 420
....*....|....*....|....*.
gi 568905513 388 GTLPQERVtKLAPRAQSEEDLSALFE 413
Cdd:cd08182 346 SVNTPERL-KNNPVRLSEEDLLRLLE 370
|
|
| NADPH_BDH |
cd08179 |
NADPH-dependent butanol dehydrogenase involved in the butanol and ethanol formation pathway in ... |
20-414 |
1.05e-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: 175.07 E-value: 1.05e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 20 LQNMGAKNVCLMTDKN-LSQLPPVQIVMDSLSKNGISFQVYDDVRVEPTDGSFMDAIEFAKKGAFDAYVAVGGGSTMDTC 98
Cdd:cd08179 18 LKTLKGKRAFIVTGGGsMKRNGFLDKVEDYLKEAGMEVKVFEGVEPDPSVETVEKGAEAMREFEPDWIIAIGGGSVIDAA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 99 KAANLYASSPHSEFLDYVnapigkgKPVTVPLKP----LIAVPTTSGTGSETTGVAIF-DYEHlKVKTGIASRAIKPTLG 173
Cdd:cd08179 98 KAMWVFYEYPELTFEDAL-------VPFPLPELRkkarFIAIPSTSGTGSEVTRASVItDTEK-GIKYPLASFEITPDVA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 174 LVDPLHTLHMPCQVVANSGFDVLCHALESYTAIPysmrspcpsnpiqrpayqgSNPISDIWAVHALQIVAKYLKRAVRNP 253
Cdd:cd08179 170 ILDPELTMTMPPHVTANTGMDALTHAIEAYVSTL-------------------ANDFTDALALGAILDIFENLPKSYNGG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 254 DDLEARSKMHLASAFAGIGFGNAGVHLCHGMSYPISGlvktykakEYNvdhplVPHGL--SVVLtsPAVFTFTAQMFPER 331
Cdd:cd08179 231 KDLEAREKMHNASCLAGMAFSNSGLGIVHSMAHKGGA--------FFG-----IPHGLanAILL--PYVIEFNSKDPEAR 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 332 HLETAGILGANirtariqdaGLVLADALRKFLFDLN----VDDGLAALGYSKDD----IPSLVKGTLpQERVTKLAPRAQ 403
Cdd:cd08179 296 ARYAALLIGLT---------DEELVEDLIEAIEELNkklgIPLSFKEAGIDEDEffakLDEMAENAM-NDACTGTNPRKP 365
|
410
....*....|.
gi 568905513 404 SEEDLSALFEA 414
Cdd:cd08179 366 TVEEMKELLKA 376
|
|
| PDD |
cd08180 |
1,3-propanediol dehydrogenase (PPD) catalyzes the reduction of 3-hydroxypropionaldehyde (3-HPA) ... |
20-413 |
6.22e-47 |
|
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: 163.82 E-value: 6.22e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 20 LQNMGAKNVCLMTDKNLSQLPPVQIVMDSLSKNgISFQVYDDVRVEPTDGSFMDAIEFAKKGAFDAYVAVGGGSTMDTCK 99
Cdd:cd08180 17 LKELKGKRVFIVTDPFMVKSGMVDKVTDELDKS-NEVEIFSDVVPDPSIEVVAKGLAKILEFKPDTIIALGGGSAIDAAK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 100 AANLYassphsefldYVNAPIGKGKPvtvplkPLIAVPTTSGTGSETTGVA-IFDYEHlKVKTGIASRAIKPTLGLVDPL 178
Cdd:cd08180 96 AIIYF----------ALKQKGNIKKP------LFIAIPTTSGTGSEVTSFAvITDPEK-GIKYPLVDDSMLPDIAILDPE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 179 HTLHMPCQVVANSGFDVLCHALESYTAIpysmrspcpsnpiqrpayqGSNPISDIWAVHALQIVAKYLKRAVRNPDDLEA 258
Cdd:cd08180 159 LVKSVPPKVTADTGMDVLTHALEAYVST-------------------NANDFTDALAEKAIKLVFENLPRAYRDGDDLEA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 259 RSKMHLASAFAGIGFGNAGVHLCHGMSYPISGLVKtykakeynvdhplVPHGLSVVLTSPAVFTFtaqmfperhletagi 338
Cdd:cd08180 220 REKMHNASCMAGIAFNNAGLGINHSLAHALGGRFH-------------IPHGRANAILLPYVIEF--------------- 271
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568905513 339 lganirtariqdaglvLADALRKFLFDLNVDDGLAALGYSKDD----IPSLVKGTLpQERVTKLAPRAQSEEDLSALFE 413
Cdd:cd08180 272 ----------------LIAAIRRLNKKLGIPSTLKELGIDEEEfekaIDEMAEAAL-ADRCTATNPRKPTAEDLIELLR 333
|
|
| PPD-like |
cd08181 |
1,3-propanediol dehydrogenase-like (PPD); This family contains proteins similar to 1, ... |
5-413 |
7.27e-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: 156.59 E-value: 7.27e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 5 NIRYGAGVTKEVGMDLQNMGaKNVCLMT-----DKNLSQlppvQIVMDSLSKNGISFQVYDDVRVEPTDGSFMDAIEFAK 79
Cdd:cd08181 6 KVYFGKNCVEKHADELAALG-KKALIVTgkhsaKKNGSL----DDVTEALEENGIEYFIFDEVEENPSIETVEKGAELAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 80 KGAFDAYVAVGGGSTMDTCKAANLYASSP-HSEFLDYVNAPigkGKPVtvplkPLIAVPTTSGTGSETTGVAIFDYEHLK 158
Cdd:cd08181 81 KEGADFVIGIGGGSPLDAAKAIALLAANKdGDEDLFQNGKY---NPPL-----PIVAIPTTAGTGSEVTPYSILTDHEKG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 159 VKTGIASRAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYtaipYSMRspcpsnpiqrpayqgSNPISDIWAVHA 238
Cdd:cd08181 153 TKKSFGNPLIFPKLALLDPKYTLSLPEELTIDTAVDALSHAIEGY----LSVK---------------ATPLSDALALEA 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 239 LQIVAKYLKRAVRNPDDLEARSKMHLASAFAGIGFGNAGVHLCHGMSYPIsglvkTYkakEYNvdhplVPHGLSVVLTSP 318
Cdd:cd08181 214 LRLIGECLPNLLGDELDEEDREKLMYASTLAGMVIAQTGTTLPHGLGYPL-----TY---FKG-----IPHGRANGILLP 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 319 AVFTFTAQMFPERHLETAGILganirtariqdaGLVLADALRKFLFDLNVDDGLaalgYSKDDIPSLVKGTLPQERVtKL 398
Cdd:cd08181 281 AYLKLCEKQEPEKVDKILKLL------------GFGSIEEFQKFLNRLLGKKEE----LSEEELEKYADEAMKAKNK-KN 343
|
410
....*....|....*
gi 568905513 399 APRAQSEEDLSALFE 413
Cdd:cd08181 344 TPGNVTKEDILRIYR 358
|
|
| AAD_C |
cd08178 |
C-terminal alcohol dehydrogenase domain of the acetaldehyde dehydrogenase-alcohol ... |
23-381 |
1.26e-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: 151.57 E-value: 1.26e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 23 MGAKNVCLMTDKNLSQLPPVQIVMDSLSKNGISFQVYDDVRVEPTDGSFMDAIEFAKkgAF--DAYVAVGGGSTMDTCKA 100
Cdd:cd08178 21 PGVKRAFIVTDRVLYKLGYVDKVLDVLEARGVETEVFSDVEPDPTLSTVRKGLEAMN--AFkpDVIIALGGGSAMDAAKI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 101 ANLYASSPHSEFLD------------YVNAPIGKGKPvtvplkpLIAVPTTSGTGSETTGVA-IFDyEHLKVKTGIASRA 167
Cdd:cd08178 99 MWLFYEHPETKFEDlaqrfmdirkrvYKFPKLGKKAK-------LVAIPTTSGTGSEVTPFAvITD-DKTGKKYPLADYA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 168 IKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTAIPysmrspcpsnpiqrpayqgSNPISDIWAVHALQIVAKYLK 247
Cdd:cd08178 171 LTPDMAIVDPELVMTMPKRLTADTGIDALTHAIEAYVSVM-------------------ASDYTDGLALQAIKLIFEYLP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 248 RAVRNPDDLEARSKMHLASAFAGIGFGNAGVHLCHGMSYPISGlvktykakEYNvdhplVPHGLSVVLTSPAVFTFTAQ- 326
Cdd:cd08178 232 RSYNNGNDIEAREKMHNAATIAGMAFANAFLGICHSLAHKLGA--------AFH-----IPHGRANAILLPHVIRYNATd 298
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568905513 327 ------MFP--------ERHLETAGILGANIRTariqDAGLV--LADALRKFLFDLNVDDGLAALGYSKDD 381
Cdd:cd08178 299 pptkqaAFPqykyyvakERYAEIADLLGLGGKT----PEEKVesLIKAIEDLKKDLGIPTSIREAGIDEAD 365
|
|
| Fe-ADH-like |
cd08189 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
9-387 |
2.77e-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: 2.77e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 9 GAGVTKEVGMDLQNMGAKNVCLMTDKNLSQLPPVQIVMDSLSKNGISFQVYDDVRVEPTDGSFMDAIEFAKKGAFDAYVA 88
Cdd:cd08189 11 GAGSLLQLPEALKKLGIKRVLIVTDKGLVKLGLLDPLLDALKKAGIEYVVFDGVVPDPTIDNVEEGLALYKENGCDAIIA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 89 VGGGSTMDTCKAANLYASSPHSEFLDYVnapiGKGKpVTVPLKPLIAVPTTSGTGSETTGVA-IFDYEHlKVKTGIASRA 167
Cdd:cd08189 91 IGGGSVIDCAKVIAARAANPKKSVRKLK----GLLK-VRKKLPPLIAVPTTAGTGSEATIAAvITDPET-HEKYAINDPK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 168 IKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTAIPYsmrspcpsnpiqrpayqgsNPISDIWAVHALQIVAKYLK 247
Cdd:cd08189 165 LIPDAAVLDPELTLGLPPAITAATGMDALTHAVEAYISRSA-------------------TKETDEYALEAVKLIFENLP 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 248 RAVRNPDDLEARSKMHLASAFAGIGFGNAGVHLCHGMSYPISGLvktykakeYNvdhplVPHGL--SVVLtsPAVFTFTA 325
Cdd:cd08189 226 KAYEDGSDLEARENMLLASYYAGLAFTRAYVGYVHAIAHQLGGL--------YG-----VPHGLanAVVL--PHVLEFYG 290
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568905513 326 QMFPERHLETAGILGANIRTARIQDAGLVLADALRKFLFDLNVDDGLAALgySKDDIPSLVK 387
Cdd:cd08189 291 PAAEKRLAELADAAGLGDSGESDSEKAEAFIAAIRELNRRMGIPTTLEEL--KEEDIPEIAK 350
|
|
| PRK10624 |
PRK10624 |
L-1,2-propanediol oxidoreductase; Provisional |
8-416 |
6.34e-41 |
|
L-1,2-propanediol oxidoreductase; Provisional
Pssm-ID: 182595 [Multi-domain] Cd Length: 382 Bit Score: 149.38 E-value: 6.34e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 8 YGAGVTKEVGMDLQNMGAKNVCLMTDKNLSQLPPVQIVMDSLSKNGISFQVYDDVRVEPTDGSFMDAIE-FAKKGAfDAY 86
Cdd:PRK10624 13 FGRGAIGALTDEVKRRGFKKALIVTDKTLVKCGVVAKVTDVLDAAGLAYEIYDGVKPNPTIEVVKEGVEvFKASGA-DYL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 87 VAVGGGSTMDTCKAANLYASSPhsEFLDYVN----APIGKgkpvtvPLKPLIAVPTTS-GTGSETTGVAIFDYEHLKVKT 161
Cdd:PRK10624 92 IAIGGGSPQDTCKAIGIISNNP--EFADVRSlegvAPTKK------PSVPIIAIPTTAgTAAEVTINYVITDEEKRRKFV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 162 GIASRAIkPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTAipysmrspcpsnpiqrpayQGSNPISDIWAVHALQI 241
Cdd:PRK10624 164 CVDPHDI-PQVAFVDADMMDSMPPGLKAATGVDALTHAIEGYIT-------------------RGAWALTDMLHLKAIEI 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 242 VAKYLKRAVRNpdDLEARSKMHLASAFAGIGFGNAGVHLCHGMSYPISGLvktykakeYNvdhplVPHGLSVVLTSPAVF 321
Cdd:PRK10624 224 IAGALRGAVAG--DKEAGEGMALGQYIAGMGFSNVGLGLVHGMAHPLGAF--------YN-----TPHGVANAILLPHVM 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 322 TFTAQMFPERHLETAGILGANIRTARIQDAGLVLADALRKFLFDLNVDDGLAALGYSKDDIPSLVKGTLpQERVTKLAPR 401
Cdd:PRK10624 289 EYNADFTGEKYRDIARAMGVKVEGMSLEEARNAAVEAVKALNRDVGIPPHLRDVGVKEEDIPALAQAAF-DDVCTGGNPR 367
|
410
....*....|....*
gi 568905513 402 AQSEEDLSALFEASM 416
Cdd:PRK10624 368 EATLEDIVELYKKAW 382
|
|
| Fe-ADH-like |
cd08186 |
Iron-containing alcohol dehydrogenase; This family contains iron-containing alcohol ... |
8-416 |
8.17e-41 |
|
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: 148.95 E-value: 8.17e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 8 YGAGVTKEVGMDLQNMGAKNVCLMTDKNLSQLPPV-QIVMDSLSKNGISFQVYDDVRVEPTDGSFMDAIEFAKKGAFDAY 86
Cdd:cd08186 6 FGVGAIAKIKDILKDLGIDKVIIVTGRSSYKKSGAwDDVEKALEENGIEYVVYDKVTPNPTVDQADEAAKLARDFGADAV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 87 VAVGGGSTMDTCKAANLYASSPHS---EFLDYVNAPIGKgkpvtvplKPLIAVPTTSGTGSETTGVAIFDYEHLKVKTGI 163
Cdd:cd08186 86 IAIGGGSPIDTAKSVAVLLAYGGKtarDLYGFRFAPERA--------LPLVAINLTHGTGSEVDRFAVATIPEKGYKPGI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 164 ASRAIKPTLGLVDPLHTLHMPC-QVVANSgFDVLCHALESYTAipysmrspcpsnpiqrpayQGSNPISDIWAVHALQIV 242
Cdd:cd08186 158 AYDCIYPLYAIDDPRLTLTLPKeQTLYTS-IDAFNHVYEAATT-------------------KVSSPYVITLAKEAIRLI 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 243 AKYLKRAVRNPDDLEARSKMHLASAFAGIGFGNAGVHLCHGMSYPISGLVktykakeynvdhPLVPHGLSVVLTSPAVFT 322
Cdd:cd08186 218 AEYLPRALANPKDLEARYWLLYASMIAGIAIDNGLLHLTHALEHPLSGLK------------PELPHGLGLALLGPAVVK 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 323 FTAQMFPErhlETAGILganirtaRIQDAGLV--------LADALRKFLFDLNVDDGLAALGYSKDDIPSLVK---GTLP 391
Cdd:cd08186 286 YIYKAVPE---TLADIL-------RPIVPGLKgtpdeaekAARGVEEFLFSVGFTEKLSDYGFTEDDVDRLVElafTTPS 355
|
410 420
....*....|....*....|....*
gi 568905513 392 QERVTKLAPRAQSEEDLSALFEASM 416
Cdd:cd08186 356 LDLLLSLAPVEVTEEVVREIYEESL 380
|
|
| Fe-ADH-like |
cd14864 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
4-414 |
2.38e-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: 147.45 E-value: 2.38e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 4 SNIRYGAGVTKEVGMDLQNMGAKNVcLMTDKNLSQLPPVQIVMDSLSKNGISFQVYDDVRVEPTDGSFMDAIEFAKKGAF 83
Cdd:cd14864 5 PNIVFGADSLERIGEEVKEYGSRFL-LITDPVLKESGLADKIVSSLEKAGISVIVFDEIPASATSDTIDEAAELARKAGA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 84 DAYVAVGGGSTMDTCKAANLYASSPHsEFLDYVNAPIGKGKPVtvplkPLIAVPTTSGTGSETTGVAIF-DYEHLKVKTg 162
Cdd:cd14864 84 DGIIAVGGGKVLDTAKAVAILANNDG-GAYDFLEGAKPKKKPL-----PLIAVPTTPRSGFEFSDRFPVvDSRSREVKL- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 163 IASRAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTAipysmrspcpsnpiqrpayQGSNPISDIWAVHALQIV 242
Cdd:cd14864 157 LKAQPGLPKAVIVDPNLMASLTGNQTAAMALAALALAVEAYLS-------------------KKSNFFSDALALKAIELV 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 243 AKYLKRAVRNPDDLEARSKMHLASAFAGIGFGNAGVHLCHGMSYPISGLvktykakeYNVDHPLVphgLSVVLtsPAVFT 322
Cdd:cd14864 218 SENLDGALADPKNTPAEELLAQAGCLAGLAASSSSPGLATALALAVNSR--------YKVSKSLV---ASILL--PHVIE 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 323 FTAQMFPERHLETAGILGANIRTARIQDAGLVLADALRKFLFDLNVDDGLAALG--YSKDDIPSLVKgtlpQERVTKLAP 400
Cdd:cd14864 285 YAATSAPDKYAKIARALGEDVEGASPEEAAIAAVEGVRRLIAQLNLPTRLKDLDlaSSLEQLAAIAE----DAPKLNGLP 360
|
410
....*....|....
gi 568905513 401 RAQSEEDLSALFEA 414
Cdd:cd14864 361 RSMSSDDIFDILKA 374
|
|
| PRK13805 |
PRK13805 |
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional |
23-381 |
1.31e-36 |
|
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional
Pssm-ID: 237515 [Multi-domain] Cd Length: 862 Bit Score: 142.25 E-value: 1.31e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 23 MGAKNVCLMTDKNLSQLPPVQIVMDSLSK--NGISFQVYDDVRVEPTdgsfmdaIEFAKKGA-----F--DAYVAVGGGS 93
Cdd:PRK13805 478 DGKKRAFIVTDRFMVELGYVDKVTDVLKKreNGVEYEVFSEVEPDPT-------LSTVRKGAelmrsFkpDTIIALGGGS 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 94 TMDTCKAANLYASSPHSEFLD------------YVNAPIG-KGKPVTVP--------LKPlIAVpttsgtgsettgvaIF 152
Cdd:PRK13805 551 PMDAAKIMWLFYEHPETDFEDlaqkfmdirkriYKFPKLGkKAKLVAIPttsgtgseVTP-FAV--------------IT 615
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 153 DyEHLKVKTGIASRAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTAIpysMrspcpsnpiqrpayqgSNPISD 232
Cdd:PRK13805 616 D-DKTGVKYPLADYELTPDVAIVDPNLVMTMPKSLTADTGIDALTHALEAYVSV---M----------------ASDYTD 675
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 233 IWAVHALQIVAKYLKRAVRN-PDDLEARSKMHLASAFAGIGFGNAGVHLCHGMSYPISGlvktykakEYNvdhplVPHGL 311
Cdd:PRK13805 676 GLALQAIKLVFEYLPRSYKNgAKDPEAREKMHNASTIAGMAFANAFLGICHSMAHKLGA--------EFH-----IPHGR 742
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 312 SVVLTSPAVFTFTAQ------MFP--------ERHLETAGILGANIRTariqDAGLV--LADALRKFLFDLNVDDGLAAL 375
Cdd:PRK13805 743 ANAILLPHVIRYNATdppkqaAFPqyeypradERYAEIARHLGLPGST----TEEKVesLIKAIEELKAELGIPMSIKEA 818
|
....*.
gi 568905513 376 GYSKDD 381
Cdd:PRK13805 819 GVDEAD 824
|
|
| BDH |
cd08187 |
Butanol dehydrogenase catalyzes the conversion of butyraldehyde to butanol with the cofactor ... |
6-387 |
1.23e-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: 126.78 E-value: 1.23e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 6 IRYGAGVTKEVGMDLQNMGaKNVCLMTDKN-------LSQlppvqiVMDSLSKNGISFQVYDDVRVEPTDGSFMDAIEFA 78
Cdd:cd08187 10 IIFGKGAIEELGEEIKKYG-KKVLLVYGGGsikknglYDR------VVASLKEAGIEVVEFGGVEPNPRLETVREGIELA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 79 KKGAFDAYVAVGGGSTMDTCKAANLYASSPHsEFLDYVNapigKGKPVTVPLkPLIAVPTTSGTGSETTGVAIFDYEHLK 158
Cdd:cd08187 83 REENVDFILAVGGGSVIDAAKAIAAGAKYDG-DVWDFFT----GKAPPEKAL-PVGTVLTLAATGSEMNGGAVITNEETK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 159 VKTGIASRAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESY-TaipysmrspcpsnpiqrpaYQGSNPISDIWAVH 237
Cdd:cd08187 157 EKLGFGSPLLRPKFSILDPELTYTLPKYQTAAGIVDIFSHVLEQYfT-------------------GTEDAPLQDRLAEG 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 238 ALQIVAKYLKRAVRNPDDLEARSKMHLASAFA--GI-GFGNAGVHLCHGMSYPISGLvktykakeYNVDHplvPHGLSVV 314
Cdd:cd08187 218 LLRTVIENGPKALKDPDDYEARANLMWAATLAlnGLlGAGRGGDWATHAIEHELSAL--------YDITH---GAGLAIV 286
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568905513 315 LtsPAVFTFTAQMFPERHLETA----GILGANIRTARIQDAglvlADALRKFLFDLNVDDGLAALGYSKDDIPSLVK 387
Cdd:cd08187 287 F--PAWMRYVLKKKPERFAQFArrvfGIDPGGDDEETALEG----IEALEEFFKSIGLPTTLSELGIDEEDIEEMAE 357
|
|
| PRK09860 |
PRK09860 |
putative alcohol dehydrogenase; Provisional |
9-416 |
1.48e-31 |
|
putative alcohol dehydrogenase; Provisional
Pssm-ID: 182118 [Multi-domain] Cd Length: 383 Bit Score: 123.91 E-value: 1.48e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 9 GAGVTKEVGMDLQNMGAKNVCLMTDKNLSQLPPVQIVMDSLSKNGISFQVYDDVRVEPTDGSFMDAIEFAKKGAFDAYVA 88
Cdd:PRK09860 15 GADSLTDAMNMMADYGFTRTLIVTDNMLTKLGMAGDVQKALEERNIFSVIYDGTQPNPTTENVAAGLKLLKENNCDSVIS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 89 VGGGSTMDTCKAANLYASSpHSEFLDYVNAPIGKGkpvtvPLKPLIAVPTTSGTGSETTGVAIFDYEHLKVKTGIASRAI 168
Cdd:PRK09860 95 LGGGSPHDCAKGIALVAAN-GGDIRDYEGVDRSAK-----PQLPMIAINTTAGTASEMTRFCIITDEARHIKMAIVDKHV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 169 KPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTAIpysmrspcpsnpiqrpayqGSNPISDIWAVHALQIVAKYLKR 248
Cdd:PRK09860 169 TPLLSVNDSSLMIGMPKSLTAATGMDALTHAIEAYVSI-------------------AATPITDACALKAVTMIAENLPL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 249 AVRNPDDLEARSKMHLASAFAGIGFGNAGVHLCHGMSYPISGLvktykakeYNvdhplVPHGLSVVLTSPAVFTFTAQMF 328
Cdd:PRK09860 230 AVEDGSNAKAREAMAYAQFLAGMAFNNASLGYVHAMAHQLGGF--------YN-----LPHGVCNAVLLPHVQVFNSKVA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 329 PERHLETAGILGANIRTARIQDAGLVLADALRKFLFDLNVDDGLAALGYSKDDIPSLVKGTLpQERVTKLAPRAQSEEDL 408
Cdd:PRK09860 297 AARLRDCAAAMGVNVTGKNDAEGAEACINAIRELAKKVDIPAGLRDLNVKEEDFAVLATNAL-KDACGFTNPIQATHEEI 375
|
....*...
gi 568905513 409 SALFEASM 416
Cdd:PRK09860 376 VAIYRAAM 383
|
|
| PRK15454 |
PRK15454 |
ethanolamine utilization ethanol dehydrogenase EutG; |
9-415 |
1.84e-30 |
|
ethanolamine utilization ethanol dehydrogenase EutG;
Pssm-ID: 185351 [Multi-domain] Cd Length: 395 Bit Score: 120.90 E-value: 1.84e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 9 GAGVTKEVGMDLQNMGAKNVCLMTDKNLSQLPPVQIVMDSLSKNGISFQVYDDVRVEPTDGSFMDAIEFAKKGAFDAYVA 88
Cdd:PRK15454 33 GPGAVSSCGQQAQTRGLKHLFVMADSFLHQAGMTAGLTRSLAVKGIAMTLWPCPVGEPCITDVCAAVAQLRESGCDGVIA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 89 VGGGSTMDTCKAANLYASSPHSEFLDYVNapigkgKPVTVPLKPLIAVPTTSGTGSETTGVAIFDYEHLKVKTGIASRAI 168
Cdd:PRK15454 113 FGGGSVLDAAKAVALLVTNPDSTLAEMSE------TSVLQPRLPLIAIPTTAGTGSETTNVTVIIDAVSGRKQVLAHASL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 169 KPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTAIpysmrspcpsnpiqrpayqGSNPISDIWAVHALQIVAKYLKR 248
Cdd:PRK15454 187 MPDVAILDAALTEGVPSHVTAMTGIDALTHAIEAYSAL-------------------NATPFTDSLAIGAIAMIGKSLPK 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 249 AVRNPDDLEARSKMHLASAFAGIGFGNAGVHLCHGMSY-PISGLvktykakeynvdHplVPHGLSVVLTSPAVFTFTAQM 327
Cdd:PRK15454 248 AVGYGHDLAARESMLLASCMAGMAFSSAGLGLCHAMAHqPGAAL------------H--IPHGLANAMLLPTVMEFNRMV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 328 FPERHLEtagiLGANIRTARIQDAGLVlaDALRKFLFDLNVDDGLAALGYSKDDIPSLVKGTLpQERVTKLAPRAQSEED 407
Cdd:PRK15454 314 CRERFSQ----IGRALRTKKSDDRDAI--NAVSELIAEVGIGKRLGDVGATSAHYGAWAQAAL-EDICLRSNPRTASLEQ 386
|
....*...
gi 568905513 408 LSALFEAS 415
Cdd:PRK15454 387 IVGLYAAA 394
|
|
| MAR-like |
cd08192 |
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic ... |
6-414 |
1.60e-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: 106.95 E-value: 1.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 6 IRYGAGVTKEVGMDLQNMGAKNVCLMTDKNLSQLPPVqiVMDSLSKNGISF-QVYDDVRVEPTDGSFMDAIEFAKKGAFD 84
Cdd:cd08192 4 VSYGPGAVEALLHELATLGASRVFIVTSKSLATKTDV--IKRLEEALGDRHvGVFSGVRQHTPREDVLEAARAVREAGAD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 85 AYVAVGGGSTMDTCKAANL-YASSPH-SEFLDYVNAPIGKGKPVTVPLKPLIAVPTTSGTGSETTGVAIFDyEHLKVKTG 162
Cdd:cd08192 82 LLVSLGGGSPIDAAKAVALaLAEDVTdVDQLDALEDGKRIDPNVTGPTLPHIAIPTTLSGAEFTAGAGATD-DDTGHKQG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 163 IASRAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYtaipYSMRSpcpsnpiqrpayqgsNPISDIWAVHALQIV 242
Cdd:cd08192 161 FAHPELGPDAVILDPELTLHTPERLWLSTGIRAVDHAVETL----CSPQA---------------TPFVDALALKALRLL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 243 AKYLKRAVRNPDDLEARSKMHLASAFAGIGFGN-AGVHLCHGMSYPISGLvktykakeYNvdhplVPHGLSVVLTSPAVF 321
Cdd:cd08192 222 FEGLPRSKADPEDLEARLKCQLAAWLSLFGLGSgVPMGASHAIGHQLGPL--------YG-----VPHGITSCIMLPAVL 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 322 TFTAQMFPERHLETAGILGANIRTARIQDAGlvLADALRKFLFDLNVDDGLAALGYSKDDIPSLVKGTLPQERVTKLAPR 401
Cdd:cd08192 289 RFNAPVNAERQRLIARALGLVTGGLGREAAD--AADAIDALIRELGLPRTLRDVGVGRDQLEKIAENALTDVWCRTNPRP 366
|
410
....*....|...
gi 568905513 402 AQSEEDLSALFEA 414
Cdd:cd08192 367 ITDKDDVLEILES 379
|
|
| 4HBD_NAD |
cd14860 |
4-hydroxybutyrate dehydrogenase, also called gamma-hydroxybutyrate dehydrogenase, catalyzes ... |
65-419 |
5.69e-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: 104.99 E-value: 5.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 65 EPTDGSFMDAIEFAKKGAFDAYVAVGGGSTMDTCKAANLYASSPHSEFLDYvNAPIGKGKPvtvplkpLIAVPTTSGTGS 144
Cdd:cd14860 61 EPSDEMVEAIYKDIKKYGYKRVIAIGGGTVIDIAKLLALKGISPVLDLFDG-KIPLIKEKE-------LIIVPTTCGTGS 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 145 ETTGVAIFDYEHLKVKTGIASRAIKPTLGLVDP--LHTLhmPCQVVANSGFDVLCHALESYTaipysmrSPcpsnpiqrp 222
Cdd:cd14860 133 EVTNISIVELTSLGTKKGLAVDELYADKAVLIPelLKGL--PYKVFATSSIDALIHAIESYL-------SP--------- 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 223 ayqGSNPISDIWAVHALQ-IVAKYLKRAVRNPDDL-EARSKMHLASAFAGIGFGNAGVHLCHGMSYPISGlvkTYKakey 300
Cdd:cd14860 195 ---KATPYTEMFSYKAIEmILEGYQEIAEKGEEARfPLLGDFLIASNYAGIAFGNAGCAAVHALSYPLGG---KYH---- 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 301 nvdhplVPHGLS--VVLTspAVFTFTAQMFPERHLET-----AGILGAnirtariqDAGLVLaDALRKFLFDLNVDDGLA 373
Cdd:cd14860 265 ------VPHGEAnyAVFT--GVLKNYQEKNPDGEIKKlneflAKILGC--------DEEDVY-DELEELLNKILPKKPLH 327
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 568905513 374 ALGYSKDDIPSLVKGTLP-QERVTKLAPRAQSEEDLSALFeasMKLY 419
Cdd:cd14860 328 EYGMKEEEIDEFADSVMEnQQRLLANNYVPLDREDVAEIY---KELY 371
|
|
| Fe-ADH-like |
cd14866 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
6-414 |
2.41e-23 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341488 [Multi-domain] Cd Length: 384 Bit Score: 100.77 E-value: 2.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 6 IRYGAGVTKEVGMDLQNMGAKNVCLMTDKNLSQLPPVqivMDSLsKNGIS---FQVYDDVRVEPTDGSFMDAIEFAKKGA 82
Cdd:cd14866 8 LFSGRGALARLGRELDRLGARRALVVCGSSVGANPDL---MDPV-RAALGdrlAGVFDGVRPHSPLETVEAAAEALREAD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 83 FDAYVAVGGGSTMDTCKAANLYASSPHSeFLDYVNAPIGKGKPVT----VPLKPLIAVPTTSGTGSETTGVAIFDYEHLK 158
Cdd:cd14866 84 ADAVVAVGGGSAIVTARAASILLAEDRD-VRELCTRRAEDGLMVSprldAPKLPIFVVPTTPTTADVKAGSAVTDPPAGQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 159 vKTGIASRAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESytaiPYSMRspcpsnpiqrpayqgSNPISDIWAVHA 238
Cdd:cd14866 163 -RLALFDPKTRPAAVFYDPELLATAPASLVAGAAMNGFDMAVEG----LYSRH---------------ADPLADATLMHA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 239 LQIVAKYLKRAVrNPDDLEARSKMHLASAFAGIGFGNAGVHLCHGMSYPISGlvktykakEYNVDHPLVpHglSVVLtsP 318
Cdd:cd14866 223 LRLLADGLPRLA-DDDDPAARADLVLAAVLAGYGTDHTGGGVIHALGHAIGA--------RYGVQNGVV-H--AILL--P 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 319 AVFTFTAQMFPERHLETAGILGAniRTARIQDAGLVLADALRKFLFDLNVDDGLAALGYSKDDIPSLVKGTLPQERVTKL 398
Cdd:cd14866 289 HVLRFNAPATDGRLDRLAEALGV--ADAGDEASAAAVVDAVEALLDALGVPTRLRDLGVSREDLPAIAEAAMDDWFMDNN 366
|
410
....*....|....*.
gi 568905513 399 APRAQSEEDLSALFEA 414
Cdd:cd14866 367 PRPVPTAEELEALLEA 382
|
|
| YqdH |
COG1979 |
Alcohol dehydrogenase YqhD, Fe-dependent ADH family [Energy production and conversion]; |
45-416 |
5.50e-19 |
|
Alcohol dehydrogenase YqhD, Fe-dependent ADH family [Energy production and conversion];
Pssm-ID: 441582 [Multi-domain] Cd Length: 387 Bit Score: 87.82 E-value: 5.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 45 VMDSLSKNGISFQVYDDVRVEPTDGSFMDAIEFAKKGAFDAYVAVGGGSTMDTCK---AANLYASSPHseflDYVNapig 121
Cdd:COG1979 51 VKAALKEAGIEVVEFGGVEPNPRLETVRKGVELCKEEGIDFILAVGGGSVIDGAKaiaAGAKYDGDPW----DILT---- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 122 KGKPVTVPLkPLIAVPTTSGTGSETTGVAIFDYEHLKVKTGIASRAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALE 201
Cdd:COG1979 123 GKAPVEKAL-PLGTVLTLPATGSEMNSGSVITNEETKEKLGFGSPLVFPKFSILDPELTYTLPKRQTANGIVDIFSHVME 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 202 SYTaipysmrspcpSNPIQrpayqgsNPISDIWAVHALQIVAKYLKRAVRNPDDLEARSKMHLASAFAGIGFGNAGVH-- 279
Cdd:COG1979 202 QYF-----------TYPVD-------APLQDRFAEGLLRTLIEEGPKALKDPEDYDARANLMWAATLALNGLIGAGVPqd 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 280 -LCHGMSYPISGLvktykakeYNVDHplvPHGLSVVLtsPAVFTFTAQMFPERHLETA----GILGANIRtARIQDAglv 354
Cdd:COG1979 264 wATHMIEHELSAL--------YDIDH---GAGLAIVL--PAWMRYVLEEKPEKFAQYAervwGITEGDDE-ERALEG--- 326
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568905513 355 lADALRKFLFDLNVDDGLAALGYSKDDIPSLVKGTLPQERVTKLAPRAQSEEDLSALFEASM 416
Cdd:COG1979 327 -IEATEEFFESLGLPTRLSEYGIDEEDIEEMAEKATAHGMTALGEFKDLTPEDVREILELAL 387
|
|
| MAR |
cd08177 |
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic ... |
6-414 |
4.65e-18 |
|
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: 84.48 E-value: 4.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 6 IRYGAGVTKEVGMDLQNMGAKNVCLMTDKnlSQLPPVQIVMDSLSKNGISfqVYDDVR----VEPTDgsfmDAIEFAKKG 81
Cdd:cd08177 4 VVFGAGTLAELAEELERLGARRALVLSTP--RQRALAERVAALLGDRVAG--VFDGAVmhvpVEVAE----RALAAAREA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 82 AFDAYVAVGGGSTmdtckaanlyassphsefldyvnapIGKGKPVTVPLK-PLIAVPTTSgtgsettgvA------IFDY 154
Cdd:cd08177 76 GADGLVAIGGGSA-------------------------IGLAKAIALRTGlPIVAVPTTY---------AgsemtpIWGE 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 155 EHLKVKTGIASRAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTAipysmrspcpsnpiqrpayQGSNPISDIW 234
Cdd:cd08177 122 TEDGVKTTGRDPRVLPRTVIYDPDLTLGLPAALSVASGLNALAHAVEALYA-------------------PDANPITSLL 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 235 AVHALQIVAKYLKRAVRNPDDLEARSKMHLASAFAGIGFGNAG--VH--LCH--GMSYpisGLvktykakeynvdhplvP 308
Cdd:cd08177 183 AEEGIRALARALPRLVADPSDLEARSDALYGAWLAGVVLGSVGmgLHhkLCHvlGGTF---DL----------------P 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 309 HGL--SVVLtsPAVFTFTAQMFPERHletagilganirtARIQDAGLV--LADALRKFLFDLNVDDGLAALGYSKDDIPS 384
Cdd:cd08177 244 HAEthAVVL--PHVLAYNAPAAPDAM-------------ARLARALGGgdAAGGLYDLARRLGAPTSLRDLGMPEDDIDR 308
|
410 420 430
....*....|....*....|....*....|...
gi 568905513 385 LVkgtlpqERVTKLA---PRAQSEEDLSALFEA 414
Cdd:cd08177 309 AA------DLALANPypnPRPVERDALRALLER 335
|
|
| DHQ_Fe-ADH |
cd07766 |
Dehydroquinate synthase-like (DHQ-like) and iron-containing alcohol dehydrogenases (Fe-ADH); ... |
5-387 |
7.04e-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: 56.60 E-value: 7.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 5 NIRYGAGVTKEVGMDLQNMGAKnVCLMTDKNLSQLPpVQIVMDSLSKnGISFQVYDDVRVEPTDGSFMDAIEFAKKGAFD 84
Cdd:cd07766 3 RIVFGEGAIAKLGEIKRRGFDR-ALVVSDEGVVKGV-GEKVADSLKK-GLAVAIFDFVGENPTFEEVKNAVERARAAEAD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 85 AYVAVGGGSTMDTCKAANLyassphsefldyvnapigkgkpVTVPLKPLIAVPTTSGTGSETTGVAIFDYEHLKVKTGIA 164
Cdd:cd07766 80 AVIAVGGGSTLDTAKAVAA----------------------LLNRGIPFIIVPTTASTDSEVSPKSVITDKGGKNKQVGP 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 165 srAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALEsytaipysmrspcpsnpiqrpayqgsnpisdiwavhalqivak 244
Cdd:cd07766 138 --HYNPDVVFVDTDITKGLPPRQVASGGVDALAHAVE------------------------------------------- 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 245 ylkravrnpddleaRSKMHLASAFAGIGFGNA-GVHLCHGMSYPISGLVKTykakeynvdhplvPHGLSVVLTSPAVFTF 323
Cdd:cd07766 173 --------------LEKVVEAATLAGMGLFESpGLGLAHAIGHALTAFEGI-------------PHGEAVAVGLPYVLKV 225
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568905513 324 TAQMFPERHLETAgilganirtariqdaglvladALRKFLFDLNVDDGLAALGYSKDDIPSLVK 387
Cdd:cd07766 226 ANDMNPEPEAAIE---------------------AVFKFLEDLGLPTHLADLGVSKEDIPKLAE 268
|
|
| Fe-ADH_2 |
pfam13685 |
Iron-containing alcohol dehydrogenase; |
7-285 |
1.79e-08 |
|
Iron-containing alcohol dehydrogenase;
Pssm-ID: 404557 [Multi-domain] Cd Length: 251 Bit Score: 55.00 E-value: 1.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 7 RYGAGVTKEVGMDLQNMGAKNVCLMTDKNLSQLPpVQIVMDSLSKNGISFQVYDDVRVEPTDGSFMDAIEFAKKGAFDAY 86
Cdd:pfam13685 1 VIGPGALGRLGEYLAELGFRRVALVADANTYAAA-GRKVAESLKRAGIEVETRLEVAGNADMETAEKLVGALRERDADAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 87 VAVGGGSTMDTCKAA----NL-YASSPHSEFLDYVNAP----IGKGKPVTVPLKPLIAVpttsgtgsettgvaIFDyehl 157
Cdd:pfam13685 80 VGVGGGTVIDLAKYAafklGKpFISVPTAASNDGFASPgaslTVDGKKRSIPAAAPFGV--------------IAD---- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 158 kvkTGIASRAikptlglvdPLHTLHmpcqvvanSGF-DvlchALESYTAIPYSMRSpcpsnpiqrpayqGSNPISDIWAV 236
Cdd:pfam13685 142 ---TDVIAAA---------PRRLLA--------SGVgD----LLAKITAVADWELA-------------HAEEVAAPLAL 184
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 568905513 237 HALQIVAKYLKRAVRNPDDLEARSKMHLASAFAGIGFGNAGVHLCHGMS 285
Cdd:pfam13685 185 LSAAMVMNFADRPLRDPGDIEALAELLSALAMGGAGSSRPASGSEHLIS 233
|
|
| PRK15138 |
PRK15138 |
alcohol dehydrogenase; |
48-398 |
1.02e-07 |
|
alcohol dehydrogenase;
Pssm-ID: 185092 [Multi-domain] Cd Length: 387 Bit Score: 53.64 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 48 SLSKNGISFQVYD-----DVR----VEP--TDGSFMDAIEFAKKGAFDAYVAVGGGSTMDTCK----AANLYASSPHSEF 112
Cdd:PRK15138 40 SVKKTGVLDQVLDalkgmDVLefggIEPnpTYETLMKAVKLVREEKITFLLAVGGGSVLDGTKfiaaAANYPENIDPWHI 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 113 LDYVNAPIGKGkpvtVPLKPLIAVPttsGTGSETTGVAIFDYEHLKVKTGIASRAIKPTLGLVDPLHTLHMPCQVVANSG 192
Cdd:PRK15138 120 LETGGKEIKSA----IPMGSVLTLP---ATGSESNAGAVISRKTTGDKQAFHSPHVQPVFAVLDPVYTYTLPPRQVANGV 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 193 FDVLCHALESYTAIPYSMRspcpsnpiqrpayqgsnpISDIWAVHALQIVAKYLKRAVRNPDDLEARSKMHLASAFAGIG 272
Cdd:PRK15138 193 VDAFVHTVEQYVTYPVDAK------------------IQDRFAEGILLTLIEEGPKALKEPENYDVRANVMWAATQALNG 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 273 FGNAGVH---LCHGMSYPISGLvktykakeYNVDHplvPHGLSVVLtsPAVFTFTAQMFPERHLETAGILGaNIRT---- 345
Cdd:PRK15138 255 LIGAGVPqdwATHMLGHELTAM--------HGLDH---AQTLAIVL--PALWNEKRDTKRAKLLQYAERVW-NITEgsdd 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 568905513 346 ARIqDAGLvlaDALRKFLFDLNVDDGLAALGYSKDDIPSLVKgTLPQERVTKL 398
Cdd:PRK15138 321 ERI-DAAI---AATRNFFEQMGVPTRLSDYGLDGSSIPALLK-KLEEHGMTQL 368
|
|
| GldA |
COG0371 |
Glycerol dehydrogenase or related enzyme, iron-containing ADH family [Energy production and ... |
4-101 |
5.10e-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: 5.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 4 SNIRYGAGVTKEVGMDLQNMGaKNVCLMTDKNLSQLppVQ-IVMDSLSKNGISFQVYDdVRVEPTDGSFMDAIEFAKKGA 82
Cdd:COG0371 7 RRYVQGEGALDELGEYLADLG-KRALIITGPTALKA--AGdRLEESLEDAGIEVEVEV-FGGECSEEEIERLAEEAKEQG 82
|
90
....*....|....*....
gi 568905513 83 FDAYVAVGGGSTMDTCKAA 101
Cdd:COG0371 83 ADVIIGVGGGKALDTAKAV 101
|
|
| G1PDH-like |
cd08174 |
Glycerol-1-phosphate dehydrogenase-like; These glycerol-1-phosphate dehydrogenase-like ... |
4-106 |
5.55e-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: 47.90 E-value: 5.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 4 SNIRYGAGVTKEVG--MDLQNMGAKNVCLMTDKNLSQLPpVQIVMDSLSKNGISFQVYDdvrvePTDGSFMDAIEFA-KK 80
Cdd:cd08174 2 LILKIEEGALEHLGkyLADRNQGFGKVAIVTGEGIDELL-GEDILESLEEAGEIVTVEE-----NTDNSAEELAEKAfSL 75
|
90 100
....*....|....*....|....*.
gi 568905513 81 GAFDAYVAVGGGSTMDTCKaanlYAS 106
Cdd:cd08174 76 PKVDAIVGIGGGKVLDVAK----YAA 97
|
|
| Fe-ADH_KdnB-like |
cd08184 |
Iron-containing alcohol dehydrogenase similar to Shewanella oneidensis KdnB required for Kdo8N ... |
3-289 |
6.19e-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: 48.03 E-value: 6.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 3 VSNIRYGAGVTKEVGMDLQNMGAKN---VCLMTDKN------LSQLPPVQIvmDSLskngisfqVYDDVRVEPTDG---S 70
Cdd:cd08184 1 VPKYLFGRGSFDQLGELLAERRKSNndyVVFFIDDVfkgkplLDRLPLQNG--DLL--------IFVDTTDEPKTDqidA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 71 FMDAIEFAKKGAFDAYVAVGGGSTMDTCKA-ANLYA---SSPHSEFLDYVnapigKGKPVtvplkPLIAVPTTSGTGSET 146
Cdd:cd08184 71 LRAQIRAENDKLPAAVVGIGGGSTMDIAKAvSNMLTnpgSAADYQGWDLV-----KNPGI-----YKIGVPTLSGTGAEA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 147 TGVAIFDYEHLKVktGIASRAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTAipySMRspcpsnpiqrpayqg 226
Cdd:cd08184 141 SRTAVLTGPEKKL--GINSDYTVFDQVILDPELIATVPRDQYFYTGMDCYIHCVESLNG---TYR--------------- 200
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568905513 227 sNPISDIWAVHALQIVAK-YLKRAVRNPDDLEarsKMHLASAFAGIGFGNAGVHLCHGMSYPIS 289
Cdd:cd08184 201 -NAFGDAYAEKALELCRDvFLSDDMMSPENRE---KLMVASYLGGSSIANSQVGVCHALSYGLS 260
|
|
| GlyDH |
cd08170 |
Glycerol dehydrogenases (GlyDH) catalyzes oxidation of glycerol to dihydroxyacetone in ... |
7-108 |
5.05e-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: 45.09 E-value: 5.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 7 RY--GAGVTKEVGMDLQNMGaKNVCLMTDKNLsqLPPV-QIVMDSLSKNGISFQVYDdVRVEPTDGSFMDAIEFAKKGAF 83
Cdd:cd08170 3 RYvqGPGALDRLGEYLAPLG-KKALVIADPFV--LDLVgERLEESLEKAGLEVVFEV-FGGECSREEIERLAAIARANGA 78
|
90 100
....*....|....*....|....*
gi 568905513 84 DAYVAVGGGSTMDTCKAANLYASSP 108
Cdd:cd08170 79 DVVIGIGGGKTIDTAKAVADYLGLP 103
|
|
| Gro1PDH |
cd08173 |
Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) catalyzes the reversible conversion between ... |
4-136 |
5.41e-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: 44.85 E-value: 5.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 4 SNIRYGAGVTKEVGMDLQNMG-AKNVCLMTDKNLSQLPpVQIVMDSLSKNGISFQVYDDVRVEpTDGSFMDAIEFAKKGA 82
Cdd:cd08173 3 RNVVVGHGAINKIGEVLKKLLlGKRALIITGPNTYKIA-GKRVEDLLESSGVEVVIVDIATIE-EAAEVEKVKKLIKESK 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568905513 83 FDAYVAVGGGSTMDTCK--AANL---YASSPHSEFLDYVNAP----IGKGKPVTVPLKPLIAV 136
Cdd:cd08173 81 ADFIIGVGGGKVIDVAKyaAYKLnlpFISIPTSASHDGIASPfasiKGGDKPYSIKAKAPIAI 143
|
|
| GlyDH-like |
cd08550 |
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins. ... |
7-101 |
1.11e-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: 40.98 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905513 7 RY--GAGVTKEVGMDLQNMGaKNVCLMTDKN-LSQLppVQIVMDSLSKNGISFQV--YDDvrvEPTDGSFMDAIEFAKKG 81
Cdd:cd08550 3 RYiqEPGILAKAGEYIAPLG-KKALIIGGKTaLEAV--GEKLEKSLEEAGIDYEVevFGG---ECTEENIERLAEKAKEE 76
|
90 100
....*....|....*....|
gi 568905513 82 AFDAYVAVGGGSTMDTCKAA 101
Cdd:cd08550 77 GADVIIGIGGGKVLDTAKAV 96
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