|
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: 732.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 3 VSNIRYGAGVTKEVGMDLQNMGAKNVCLMTDKNLSQLPPVQIVMDSLSKNGISFQVYDNVRVEPTDGSFMDAIEFAKKGA 82
Cdd:cd08190 1 ASNIRFGPGATRELGMDLKRLGAKKVLVVTDPGLAKLGLVERVLESLEKAGIEVVVYDGVRVEPTDESFEEAIEFAKEGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 83 FDAYVAVGGGSTMDTCKAANLYACSPhSEFLDYVNAPIGKGKPVTVPLKPLIAVPTTSGTGSETTGVAIFDYEHLKVKTG 162
Cdd:cd08190 81 FDAFVAVGGGSVIDTAKAANLYATHP-GDFLDYVNAPIGKGKPVPGPLKPLIAIPTTAGTGSETTGVAIFDLEELKVKTG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 163 IASRAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTAIPYSMRsPCPSNPIQRPAYQGSNPISDIWAVHALRIV 242
Cdd:cd08190 160 ISSRYLRPTLAIVDPLLTLTLPPRVTASSGFDVLCHALESYTARPYNAR-PRPANPDERPAYQGSNPISDVWAEKAIELI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 243 AKYLKRAVRNPDDLEARSSMHLASAFAGIGFGNAGVHLCHGMSYPISGLVKTYKAKEYNVDHPLVPHGLSVVLTSPAVFT 322
Cdd:cd08190 239 GKYLRRAVNDGDDLEARSNMLLASTLAGIGFGNAGVHLPHAMAYPIAGLVKDYRPPGYPVDHPHVPHGLSVALTAPAVFR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 323 FTAQMFPERHLETAEILGANIRTAKIQDAGPVLADALRKFLFDLNVDDGLAALGYSKDDIPSLVKGTLPQERVTKLAPRA 402
Cdd:cd08190 319 FTAPACPERHLEAAELLGADTSGASDRDAGEVLADALIKLMRDIGIPNGLSALGYSEDDIPALVEGTLPQQRLLKLNPRP 398
|
410
....*....|....
gi 1958777067 403 QSEEDLSALFEASM 416
Cdd:cd08190 399 VTEEDLEEIFEDAL 412
|
|
| EutG |
COG1454 |
Alcohol dehydrogenase, class IV [Energy production and conversion]; |
6-416 |
3.87e-109 |
|
Alcohol dehydrogenase, class IV [Energy production and conversion];
Pssm-ID: 441063 [Multi-domain] Cd Length: 381 Bit Score: 326.31 E-value: 3.87e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 6 IRYGAGVTKEVGMDLQNMGAKNVCLMTDKNLSQLPPVQIVMDSLSKNGISFQVYDNVRVEPTDGSFMDAIEFAKKGAFDA 85
Cdd:COG1454 11 IVFGAGALAELGEELKRLGAKRALIVTDPGLAKLGLLDRVLDALEAAGIEVVVFDDVEPNPTVETVEAGAAAAREFGADV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 86 YVAVGGGSTMDTCKAANLYACSPHSeFLDYVNApigkgKPVTVPLKPLIAVP----------TtsgtgsettgVAIFDYE 155
Cdd:COG1454 91 VIALGGGSAIDAAKAIALLATNPGD-LEDYLGI-----KKVPGPPLPLIAIPttagtgsevtP----------FAVITDP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 156 HLKVKTGIASRAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTAIpysmrspcpsnpiqrpayqGSNPISDIWA 235
Cdd:COG1454 155 ETGVKKGIADPELLPDVAILDPELTLTLPPSLTAATGMDALTHAIEAYVSK-------------------GANPLTDALA 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 236 VHALRIVAKYLKRAVRNPDDLEARSSMHLASAFAGIGFGNAGVHLCHGMSYPISGLvktykakeYNvdhplVPHGLSVVL 315
Cdd:COG1454 216 LEAIRLIARNLPRAVADGDDLEAREKMALASLLAGMAFANAGLGAVHALAHPLGGL--------FH-----VPHGLANAI 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 316 TSPAVFTFTAQMFPERHLETAEILGANIrTAKIQDAGPVLADALRKFLFDLNVDDGLAALGYSKDDIPSLVKGTLpQERV 395
Cdd:COG1454 283 LLPHVLRFNAPAAPERYAEIARALGLDV-GLSDEEAAEALIEAIRELLRDLGIPTRLSELGVTEEDLPELAELAL-ADRC 360
|
410 420
....*....|....*....|.
gi 1958777067 396 TKLAPRAQSEEDLSALFEASM 416
Cdd:COG1454 361 LANNPRPLTEEDIEAILRAAY 381
|
|
| Fe-ADH |
cd08551 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains large ... |
4-412 |
2.12e-104 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains large metal-containing alcohol dehydrogenases (ADH), known as iron-containing alcohol dehydrogenases. They contain a dehydroquinate synthase-like protein structural fold and mostly contain iron. They are distinct from other alcohol dehydrogenases which contains different protein domains. There are several distinct families of alcohol dehydrogenases: Zinc-containing long-chain alcohol dehydrogenases, insect-type, or short-chain alcohol dehydrogenases, iron-containing alcohol dehydrogenases, among others. The iron-containing family has a Rossmann fold-like topology that resembles the fold of the zinc-dependent alcohol dehydrogenases, but lacks sequence homology, and differs in strand arrangement. ADH catalyzes the reversible oxidation of alcohol to acetaldehyde with the simultaneous reduction of NAD(P)+ to NAD(P)H.
Pssm-ID: 341481 [Multi-domain] Cd Length: 372 Bit Score: 313.62 E-value: 2.12e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 4 SNIRYGAGVTKEVGMDLQNMGAKNVCLMTDKNLSQLPPVQIVMDSLSKNGISFQVYDNVRVEPTDGSFMDAIEFAKKGAF 83
Cdd:cd08551 2 TRIVFGAGALARLGEELKALGGKKVLLVTDPGLVKAGLLDKVLESLKAAGIEVEVFDDVEPNPTVETVEAAAELAREEGA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 84 DAYVAVGGGSTMDTCKAANLYACSPHSeFLDYVNapigkGKPVTVPLKPLIAVPttsgtgsettGVAIFDYEHLKVKTGI 163
Cdd:cd08551 82 DLVIAVGGGSVLDTAKAIAVLATNGGS-IRDYEG-----IGKVPKPGLPLIAIPttagtgsevtPNAVITDPETGRKMGI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 164 ASRAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTAIPysmrspcpsnpiqrpayqgSNPISDIWAVHALRIVA 243
Cdd:cd08551 156 VSPYLLPDVAILDPELTLSLPPSVTAATGMDALTHAIEAYTSKK-------------------ANPISDALALEAIRLIG 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 244 KYLKRAVRNPDDLEARSSMHLASAFAGIGFGNAGVHLCHGMSYPISGlvktykakEYNvdhplVPHGLSVVLTSPAVFTF 323
Cdd:cd08551 217 KNLRRAVADGSDLEAREAMLLASLLAGIAFGNAGLGAVHALAYPLGG--------RYH-----IPHGVANAILLPYVMEF 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 324 TAQMFPERHLETAEILGANIRTAKIQDAGPVLADALRKFLFDLNVDDGLAALGYSKDDIPSLVKGTLPQERVTKLAPRAQ 403
Cdd:cd08551 284 NLPACPEKYAEIAEALGEDVEGLSDEEAAEAAVEAVRELLRDLGIPTSLSELGVTEEDIPELAEDAMKSGRLLSNNPRPL 363
|
....*....
gi 1958777067 404 SEEDLSALF 412
Cdd:cd08551 364 TEEDIREIY 372
|
|
| Fe-ADH |
pfam00465 |
Iron-containing alcohol dehydrogenase; |
4-408 |
2.96e-94 |
|
Iron-containing alcohol dehydrogenase;
Pssm-ID: 425696 [Multi-domain] Cd Length: 362 Bit Score: 287.58 E-value: 2.96e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 4 SNIRYGAGVTKEVGMDLQNMGAKnVCLMTDKNLSQLPPVQIVMDSLSKNGISFQVYDNVRVEPTDGSFMDAIEFAKKGAF 83
Cdd:pfam00465 2 TRIVFGAGALAELGEELKRLGAR-ALIVTDPGSLKSGLLDKVLASLEEAGIEVVVFDGVEPEPTLEEVDEAAALAREAGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 84 DAYVAVGGGSTMDTCKAANLYACSPHSEFLDYvnapigKGKPVTVPLKPLIAVPTTSGTGSETTGVAIFDYEHLKVKTGI 163
Cdd:pfam00465 81 DVIIAVGGGSVIDTAKAIALLLTNPGDVWDYL------GGKPLTKPALPLIAIPTTAGTGSEVTPLAVITDTETGEKLGI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 164 ASRAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTAipysmrspcpsnpiqrpayQGSNPISDIWAVHALRIVA 243
Cdd:pfam00465 155 FSPKLLPDLAILDPELTLTLPPRLTAATGMDALAHAVEAYVS-------------------KGANPLTDALALEAIRLIA 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 244 KYLKRAVRNPDDLEARSSMHLASAFAGIGFGNAGVHLCHGMSYPISGLVKtykakeynvdhplVPHGLSVVLTSPAVFTF 323
Cdd:pfam00465 216 ENLPRAVADGEDLEARENMLLASTLAGLAFSNAGLGAAHALAHALGGRYG-------------IPHGLANAILLPYVLRF 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 324 TAQMFPERHLETAEILGANIRTAKIQDAgpvlADALRKFLFDLNVDDGLAALGYSKDDIPSLVKGTLpQERVTKLAPRAQ 403
Cdd:pfam00465 283 NAPAAPEKLAQLARALGEDSDEEAAEEA----IEALRELLRELGLPTTLSELGVTEEDLDALAEAAL-RDRSLANNPRPL 357
|
....*
gi 1958777067 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 |
2.05e-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: 260.16 E-value: 2.05e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 6 IRYGAGVTKEVGMDLQNMGAKNVCLMTDKNLSQLPPVQIVMDSLSKNGISFQVYDNVRVEPTDGSFMDAIEFAKKGAFDA 85
Cdd:cd14863 8 VIFGAGAVEQIGELLKELGCKKVLLVTDKGLKKAGIVDKIIDLLEEAGIEVVVFDDVEPDPPDEIVDEAAEIAREEGADG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 86 YVAVGGGSTMDTCKAANLYACSPHsEFLDYvnapIGKGKPVTVPLKPLIAVPTTSGTGSETTGVAIFDYEHLKVKTGIAS 165
Cdd:cd14863 88 VIGIGGGSVLDTAKAIAVLLTNPG-PIIDY----ALAGPPVPKPGIPLIAIPTTAGTGSEVTPIAVITDEENGVKKSLLG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 166 RAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTAipysmrspcpsnpiqrpayQGSNPISDIWAVHALRIVAKY 245
Cdd:cd14863 163 PFLVPDLAILDPELTVGLPPSLTAATGMDALSHAIEAYTS-------------------KLANPMTDALALQAIRLIVKN 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 246 LKRAVRNPDDLEARSSMHLASAFAGIGFGNAGVHLCHGMSYPISGLvktykakeYNvdhplVPHGLSVVLTSPAVFTFTA 325
Cdd:cd14863 224 LPRAVKDGDNLEARENMLLASNLAGIAFNNAGTHIGHAIAHALGAL--------YH-----IPHGLACALALPVVLEFNA 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 326 QMFPERHLETAEILGANIRTAKIQDAGPVLADALRKFLFDLNVDDGLAALGYSKDDIPSLVKGTLpQERVTKLAPRAQSE 405
Cdd:cd14863 291 EAYPEKVKKIAKALGVSFPGESDEELGEAVADAIREFMKELGIPSLFEDYGIDKEDLDKIAEAVL-KDPFAMFNPRPITE 369
|
....*....
gi 1958777067 406 EDLSALFEA 414
Cdd:cd14863 370 EEVAEILEA 378
|
|
| Fe-ADH-like |
cd08191 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
4-416 |
6.41e-76 |
|
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: 241.36 E-value: 6.41e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 4 SNIRYGAGVTKEVGMDLQNMGAKnVCLMTDKNLSQLPPVQIVMDSLSKNGISFQVYDNVRVEPTDGSFMDAIEFAKKGAF 83
Cdd:cd08191 5 SRLLFGPGARRALGRVAARLGSR-VLIVTDPRLASTPLVAELLAALTAAGVAVEVFDGGQPELPVSTVADAAAAARAFDP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 84 DAYVAVGGGSTMDTCKAANLyACSPHSEFLDYvnapIGKGKpVTVPLKPLIAVPTTSGTGSETTGVAIFDYEHLKVKTGI 163
Cdd:cd08191 84 DVVIGLGGGSNMDLAKVVAL-LLAHGGDPRDY----YGEDR-VPGPVLPLIAVPTTAGTGSEVTPVAVLTDPARGMKVGV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 164 ASRAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTAIPysmRSPCPSNPiQRPAYQGSNPISDIWAVHALRIVA 243
Cdd:cd08191 158 SSPYLRPAVAIVDPELTLTCPPGVTADSGIDALTHAIESYTARD---FPPFPRLD-PDPVYVGKNPLTDLLALEAIRLIG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 244 KYLKRAVRNPDDLEARSSMHLASAFAGIGFGNAGVHLCHGMSYPISGLVKTykakeynvdhplvPHGLSVVLTSPAVFTF 323
Cdd:cd08191 234 RHLPRAVRDGDDLEARSGMALAALLAGLAFGTAGTAAAHALQYPIGALTHT-------------SHGVGNGLLLPYVMRF 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 324 taqMFPERHLETAEI---LGANIRTAKIQDAGPVLaDALRKFLFDLNVDDGLAALGYSKDDIPSLVKGTLPQERVTKLAP 400
Cdd:cd08191 301 ---NRPARAAELAEIaraLGVTTAGTSEEAADRAI-ERVEELLARIGIPTTLADLGVTEADLPGLAEKALSVTRLIANNP 376
|
410
....*....|....*.
gi 1958777067 401 RAQSEEDLSALFEASM 416
Cdd:cd08191 377 RPPTEEDLLRILRAAF 392
|
|
| Fe-ADH-like |
cd08185 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
5-413 |
7.36e-76 |
|
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: 240.86 E-value: 7.36e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 5 NIRYGAGVTKEVGmDLQNMGAKNVCLMTDKNLSQLPPV-QIVMDSLSKNGISFQVYDNVRVEPTDGSFMDAIEFAKKGAF 83
Cdd:cd08185 6 RILFGAGKLNELG-EEALRPGKKALIVTGKGSSKKTGLlDRVKKLLEKAGVEVVVFDKVEPNPLTTTVMEGAALAKEEGC 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 84 DAYVAVGGGSTMDTCKAANLYACSPHSEFlDYVNAPIGKGKPVTVPLkPLIAVPTTSGTGSETTGVAIFDYEHLKVKTGI 163
Cdd:cd08185 85 DFVIGLGGGSSMDAAKAIAFMATNPGDIW-DYIFGGTGKGPPPEKAL-PIIAIPTTAGTGSEVDPWAVITNPETKEKKGI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 164 ASRAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTAIpysmrspcpsnpiqrpayqGSNPISDIWAVHALRIVA 243
Cdd:cd08185 163 GHPALFPKVSIVDPELMLTVPPRVTAYTGFDALFHAFESYISK-------------------NANPFSDMLALEAIRLVA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 244 KYLKRAVRNPDDLEARSSMHLASAFAGIGFGNAGVHLCHGMSYPISGLvktykakeynvdHPLVPHGLSVVLTSPAVFTF 323
Cdd:cd08185 224 KYLPRAVKDGSDLEAREKMAWASTLAGIVIANSGTTLPHGLEHPLSGY------------HPNIPHGAGLAALYPAYFEF 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 324 TAQMFPERhleTAEILGANIRTAKIQDAGPVLADALRKFLFDLNVDDGLAALGYSKDDIPSLVkgtlpqERVTKLA---- 399
Cdd:cd08185 292 TIEKAPEK---FAFVARAEASGLSDAKAAEDFIEALRKLLKDIGLDDLLSDLGVTEEDIPWLA------ENAMETMgglf 362
|
410
....*....|....*..
gi 1958777067 400 ---PRAQSEEDLSALFE 413
Cdd:cd08185 363 annPVELTEEDIVEIYE 379
|
|
| Fe-ADH-like |
cd08194 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
4-414 |
4.04e-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: 230.88 E-value: 4.04e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 4 SNIRYGAGVTKEVGMDLQNMGAKNVCLMTDKNLSQLPPVQIVMDSLSKNGISFQVYDNVRVEPTDGSFMDAIEFAKKGAF 83
Cdd:cd08194 2 RTIIIGGGALEELGEEAASLGGKRALIVTDKVMVKLGLVDKVTQLLAEAGIAYAVFDDVVSEPTDEMVEEGLALYKEGGC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 84 DAYVAVGGGSTMDTCKAANLYACSPhSEFLDYVNAPIGKGKPVtvplkPLIAVPTTSGTGSETTGVAIFDYEHLKVKTGI 163
Cdd:cd08194 82 DFIVALGGGSPIDTAKAIAVLATNG-GPIRDYMGPRKVDKPGL-----PLIAIPTTAGTGSEVTRFTVITDTETDVKMLL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 164 ASRAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTaipySMRspcpsnpiqrpayqgSNPISDIWAVHALRIVA 243
Cdd:cd08194 156 KGPALLPAVAIVDPELTLSMPPRVTAATGIDALTHAIEAYV----SRK---------------AQPLTDTLALSAIKLIG 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 244 KYLKRAVRNPDDLEARSSMHLASAFAGIGFGNAGVHLCHGMSYPISGLVktykakeynvdHplVPHGLSVVLTSPAVFTF 323
Cdd:cd08194 217 RNLRRAYADGDDLEAREAMMLAALEAGIAFSNSSVALVHGMSRPIGALF-----------H--VPHGLSNAMLLPAVTEF 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 324 TAQMFPERHLETAEILGANIRTAKIQDAGPVLADALRKFLFDLNVdDGLAALGYSKDD----IPSLVKGTL----PQerv 395
Cdd:cd08194 284 SLPGAPERYAEIARAMGIATEGDSDEEAAEKLVEALERLCADLEI-PTLREYGIDEEEfeaaLDKMAEDALasgsPA--- 359
|
410
....*....|....*....
gi 1958777067 396 tkLAPRAQSEEDLSALFEA 414
Cdd:cd08194 360 --NNPRVPTKEEIIELYRE 376
|
|
| Fe-ADH-like |
cd08196 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
5-412 |
3.36e-71 |
|
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: 228.23 E-value: 3.36e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 5 NIRYGAGVTKEVGMDLQNMGAKNVCLMTDKNLSQLPPVQIVMDSLSKNGISfqVYDNVRVEPTDGSFMDAIEFAKKGAFD 84
Cdd:cd08196 8 KIIFGEGILKELPDIIKELGGKRGLLVTDPSFIKSGLAKRIVESLKGRIVA--VFSDVEPNPTVENVDKCARLARENGAD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 85 AYVAVGGGSTMDTCKAANLYACSPHSeFLDYvnapIGKGKPVTVPLKPLIAVPTTSGTGSETTGVAIFDYEHLKVKTGIA 164
Cdd:cd08196 86 FVIAIGGGSVLDTAKAAACLAKTDGS-IEDY----LEGKKKIPKKGLPLIAIPTTAGTGSEVTPVAVLTDKEKGKKAPLV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 165 SRAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTAIpysmrspcpsnpiqrpayqGSNPISDIWAVHALRIVAK 244
Cdd:cd08196 161 SPGFYPDIAIVDPELTYSMPPKVTASTGIDALCHAIEAYWSI-------------------NHQPISDALALEAAKLVLE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 245 YLKRAVRNPDDLEARSSMHLASAFAGIGFGNAGVHLCHGMSYPISglvktykaKEYNvdhplVPHGLSVVLTSPAVFTFT 324
Cdd:cd08196 222 NLEKAYNNPNDKEAREKMALASLLAGLAFSQTRTTASHACSYPLT--------SHFG-----IPHGEACALTLPSFIRLN 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 325 AQMFPERHLETAEILGANirtakiqDAGPvLADALRKFLFDLNVDDGLAALGYSKDDIPSLVKGTLPQERVtKLAPRAQS 404
Cdd:cd08196 289 AEALPGRLDELAKQLGFK-------DAEE-LADKIEELKKRIGLRTRLSELGITEEDLEEIVEESFHPNRA-NNNPVEVT 359
|
....*...
gi 1958777067 405 EEDLSALF 412
Cdd:cd08196 360 KEDLEKLL 367
|
|
| Fe-ADH-like |
cd17814 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
8-390 |
3.99e-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: 220.49 E-value: 3.99e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 8 YGAGVTKEVGMDLQNMGAKNVCLMTDKNLSQLPPVQIVMDSLSKNGISFQVYDNVRVEPTDGSFMDAIE-FAKKGAfDAY 86
Cdd:cd17814 9 FGVGARKLAGRYAKNLGARKVLVVTDPGVIKAGWVDEVLDSLEAEGLEYVVFSDVTPNPRDFEVMEGAElYREEGC-DGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 87 VAVGGGSTMDTCKAANLYAcSPHSEFLDYvnapIGKGKpVTVPLKPLIAVPTTSGTGSETTGVAIFDYEHLKVKTGIASR 166
Cdd:cd17814 88 VAVGGGSPIDCAKGIGIVV-SNGGHILDY----EGVDK-VRRPLPPLICIPTTAGSSADVSQFAIITDTERRVKMAIISK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 167 AIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTaipysmrspcpSNpiqrpayqGSNPISDIWAVHALRIVAKYL 246
Cdd:cd17814 162 TLVPDVSLIDPETLTTMDPELTACTGMDALTHAIEAYV-----------SN--------ASSPLTDLHALEAIRLISENL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 247 KRAVRNPDDLEARSSMHLASAFAGIGFGNAGVHLCHGMSYPISGLvktykakeynVDhplVPHGLSVVLTSPAVFTFTAQ 326
Cdd:cd17814 223 PKAVADPDDLEAREKMMLASLQAGLAFSNASLGAVHAMAHSLGGL----------LD---LPHGECNALLLPHVIRFNFP 289
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958777067 327 MFPERHLETAEILGANIRTAKIQDAGPVLADALRKFLFDLNVDDGLAALGYSKDDIPSLVKGTL 390
Cdd:cd17814 290 AAPERYRKIAEAMGLDVDGLDDEEVAERLIEAIRDLREDLGIPETLSELGVDEEDIPELAKRAM 353
|
|
| LPO |
cd08176 |
Lactadehyde:propanediol oxidoreductase (LPO) catalyzes the interconversion between ... |
8-413 |
5.72e-64 |
|
Lactadehyde:propanediol oxidoreductase (LPO) catalyzes the interconversion between L-lactaldehyde and L-1,2-propanediol in Escherichia coli and other enterobacteria; Lactadehyde:propanediol oxidoreductase (LPO) is a member of the group III iron-activated dehydrogenases which catalyze the interconversion between L-lactaldehyde and L-1,2-propanediol in Escherichia coli and other enterobacteria. L-fucose and L-rhamnose are used by Escherichia coli through an inducible pathway mediated by the fucose regulon comprising four linked operons fucO, fucA, fucPIK, and fucR. The fucA-encoded aldolase catalyzes the formation of dihydroxyacetone phosphate and L-lactaldehyde. Under anaerobic conditions, with NADH as a cofactor, lactaldehyde is converted by a fucO-encoded lactadehyde:propanediol oxidoreductase (LPO) to L-1,2-propanediol, which is excreted as a fermentation product. In mutant strains, E. coli adapted to grow on L-1,2-propanediol, FucO catalyzes the oxidation of the polyol to L-lactaldehyde. FucO is induced regardless of the respiratory conditions of the culture, remains fully active in the absence of oxygen. In the presence of oxygen, this enzyme becomes oxidatively inactivated by a metal-catalyzed oxidation mechanism. FucO is an iron-dependent metalloenzyme that is inactivated by other metals, such as zinc, copper, or cadmium. This enzyme can also reduce glycol aldehyde with similar efficiency. Beside L-1,2-propanediol, the enzyme is also able to oxidize methanol as an alternative substrate.
Pssm-ID: 341455 [Multi-domain] Cd Length: 378 Bit Score: 209.71 E-value: 5.72e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 8 YGAGVTKEVGMDLQNMGAKNVCLMTDKNLSQLPPVQIVMDSLSKNGISFQVYDNVRVEPTDGSFMDAIEFAKKGAFDAYV 87
Cdd:cd08176 11 FGWGAIEEIGEEAKKRGFKKALIVTDKGLVKFGIVDKVTDVLKEAGIAYTVFDEVKPNPTIENVMAGVAAYKESGADGII 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 88 AVGGGSTMDTCKAANLYACSPhseFLDyVNAPIGKgKPVTVPLKPLIAVPTTSGTGSETTGVA-IFDYEHlKVKTGIASR 166
Cdd:cd08176 91 AVGGGSSIDTAKAIGIIVANP---GAD-VRSLEGV-APTKNPAVPIIAVPTTAGTGSEVTINYvITDTEK-KRKFVCVDP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 167 AIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTAipysmrspcpsnpiqrpayQGSNPISDIWAVHALRIVAKYL 246
Cdd:cd08176 165 HDIPTVAIVDPDLMSSMPKGLTAATGMDALTHAIEGYIT-------------------KGAWELSDMLALKAIELIAKNL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 247 KRAVRNPDDLEARSSMHLASAFAGIGFGNAGVHLCHGMSYPISGLvktykakeYNvdhplVPHGLSVVLTSPAVFTFTAQ 326
Cdd:cd08176 226 RKAVANPNNVEARENMALAQYIAGMAFSNVGLGIVHSMAHPLSAF--------YD-----TPHGVANAILLPYVMEFNAP 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 327 MFPERHLETAEILGANIRTAKIQDAGPVLADALRKFLFDLNVDDGLAALGYSKDDIPSLVKGTLpQERVTKLAPRAQSEE 406
Cdd:cd08176 293 ATGEKYRDIARAMGVDTTGMSDEEAAEAAVDAVKKLSKDVGIPQKLSELGVKEEDIEALAEDAL-NDVCTPGNPREATKE 371
|
....*..
gi 1958777067 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 |
5.13e-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: 204.77 E-value: 5.13e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 20 LQNMGAKNVCLMTDKNLSQLPPVQIVMDSLSKNGISFQVYDNVRVEPTDGSFMDAIEFAKKGAFDAYVAVGGGSTMDTCK 99
Cdd:cd14862 19 LEQLSGKRALIVTDKVLVKLGLLKKVLKRLLQAGFEVEVFDEVEPEPPLETVLKGAEAMREFEPDLIIALGGGSVMDAAK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 100 AANLYACSPHSEFLDYV-NAPIGKGKpvtvplKP-LIAVPTTSGTGSETTGVAIFDYEHLKVKTGIASRAIKPTLGLVDP 177
Cdd:cd14862 99 AAWVLYERPDLDPEDISpLDLLGLRK------KAkLIAIPTTSGTGSEATWAIVLTDTEEPRKIAVANPELVPDVAILDP 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 178 LHTLHMPCQVVANSGFDVLCHALESYTAipysmrspcpsnpiqrpayQGSNPISDIWAVHALRIVAKYLKRAVRNPDDLE 257
Cdd:cd14862 173 EFVLGMPPKLTAGTGLDALAHAVEAYLS-------------------TWSNDFSDALALKAIELIFKYLPRAYKDGDDLE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 258 ARSSMHLASAFAGIGFGNAGVHLCHGMSYPISGLVKtykakeynvdhplVPHGLSVVLTSPAVFTFTAQmFPERHLETAE 337
Cdd:cd14862 234 AREKMHNAATIAGLAFGNSQAGLAHALGHSLGAVFH-------------VPHGIAVGLFLPYVIEFYAK-VTDERYDLLK 299
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958777067 338 ILGANIRTAKiqDAGPVLADALRKFLFDLNVDDGLAALGYSKDD----IPSLVKGTLpQERVTKLAPRAQSEEDLSALF 412
Cdd:cd14862 300 LLGIEARDEE--EALKKLVEAIRELYKEVGQPLSIKDLGISEEEfeekLDELVEYAM-EDSCTITSPRPPSEEDLKKLF 375
|
|
| PDDH |
cd08188 |
1,3-Propanediol (1,3-PD) dehydrogenase; This family includes 1,3-propanediol (1,3-PD) ... |
9-413 |
5.00e-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: 202.36 E-value: 5.00e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 9 GAGVTKEVGMDLQNMGAKNVCLMTDKNLSQLPPVQIVMDSLSKNGISFQVYDNVRVEPTDGSFMDAIEFAKKGAFDAYVA 88
Cdd:cd08188 12 GPGCLKEIGDELKKLGGKKALIVTDKGLVKLGLVKKVTDVLEEAGIEYVIFDGVQPNPTVTNVNEGLELFKENGCDFIIS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 89 VGGGSTMDTCKAANLYACSPhSEFLDYVNapIGKgkpVTVPLKPLIAVPTTSGTGSETTGVAIFDYEHLKVKTGIASRAI 168
Cdd:cd08188 92 VGGGSAHDCAKAIGILATNG-GEIEDYEG--VDK---SKKPGLPLIAINTTAGTASEVTRFAVITDEERHVKMVIVDWNV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 169 KPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTAIpysmrspcpsnpiqrpayqGSNPISDIWAVHALRIVAKYLKR 248
Cdd:cd08188 166 TPTIAVNDPELMLGMPPSLTAATGMDALTHAIEAYVST-------------------GATPLTDALALEAIRLIAENLPK 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 249 AVRNPDDLEARSSMHLASAFAGIGFGNAGVHLCHGMSYPISGLvktykakeYNvdhplVPHGL--SVVLtsPAVFTFTAQ 326
Cdd:cd08188 227 AVANGKDLEARENMAYAQFLAGMAFNNAGLGYVHAMAHQLGGF--------YN-----LPHGVcnAILL--PHVMEFNLP 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 327 MFPERHLETAEILGANIRTAKIQDAGPVLADALRKFLFDLNVDDGLAALGYSKDDIPSLVKGTLpQERVTKLAPRAQSEE 406
Cdd:cd08188 292 ACPERFADIARALGENTEGLSDEEAAEAAIEAIRKLSRRVGIPSGLKELGVKEEDFPLLAENAL-KDACGPTNPRQATKE 370
|
....*..
gi 1958777067 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 |
4.09e-59 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341487 [Multi-domain] Cd Length: 383 Bit Score: 197.38 E-value: 4.09e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 6 IRYGAGVTKEVGMDLQNMGAKNVCLMTDKNLSQLPPVQIVMDSLSKNGISFQVYDNVrvePTDGSF---MDAIEFAKKGA 82
Cdd:cd14865 9 IVSGAGALENLPAELARLGARRPLIVTDKGLAAAGLLKKVEDALGDAIEIVGVFDDV---PPDSSVavvNEAAARAREAG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 83 FDAYVAVGGGSTMDTCKAANLYAcSPHSEFLDYVNapiGKGKpVTVPLKPLIAVPTTSGTGSETTGVAIFDYEHLKVKTG 162
Cdd:cd14865 86 ADGIIAVGGGSVIDTAKGVNILL-SEGGDDLDDYG---GANR-LTRPLKPLIAIPTTAGTGSEVTLVAVIKDEEKKVKLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 163 IASRAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTAIpysmrspcpsnpiqrpayqGSNPISDIWAVHALRIV 242
Cdd:cd14865 161 FVSPFLLPDVAILDPRLTLSLPPKLTAATGMDALTHAIEAYTSL-------------------QKNPISDALALQAIRLI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 243 AKYLKRAVRNPDDLEARSSMHLASAFAGIGFGNAGVHLCHGMSYPISGLVKtykakeynvdhplVPHGL--SVVLtsPAV 320
Cdd:cd14865 222 SENLPKAVKNGKDLEARLALAIAATMAGIAFSNSMVGLVHAIAHAVGAVAG-------------VPHGLanSILL--PHV 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 321 FTFTAQMFPERHLETAEIL--GANIRTAKIQDAGPVLADALRKFLFDLNVDDGLAALGYSKDDIPSLVKGTLpQERVTKL 398
Cdd:cd14865 287 MRYNLDAAAERYAELALALayGVTPAGRRAEEAIEAAIDLVRRLHELCGLPTRLRDVGVPEEQLEAIAELAL-NDGAILF 365
|
410
....*....|....*...
gi 1958777067 399 APRAQSEEDLSALFEASM 416
Cdd:cd14865 366 NPREVDPEDILAILEAAY 383
|
|
| Fe-ADH-like |
cd14861 |
Iron-containing alcohol dehydrogenases-like; This family contains proteins similar to ... |
6-416 |
2.56e-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: 2.56e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 6 IRYGAGVTKEVGMDLQNMGAKNVCLMTDKNLSQLPPVQIVMDSLSKNGISFQVYDNVRVEPTDGSFMDAIEFAKKGAFDA 85
Cdd:cd14861 6 IRFGAGAIAELPEELKALGIRRPLLVTDPGLAALGIVDRVLEALGAAGLSPAVFSDVPPNPTEADVEAGVAAYREGGCDG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 86 YVAVGGGSTMDTCKAANLYACSPHSEFlDYVNAPIGkGKPVTVPLKPLIAVPTTSGTGSETTGVAIFDYEHLKVKTGIAS 165
Cdd:cd14861 86 IIALGGGSAIDAAKAIALMATHPGPLW-DYEDGEGG-PAAITPAVPPLIAIPTTAGTGSEVGRAAVITDDDTGRKKIIFS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 166 RAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTAIPYsmrspcpsnpiqrpayqgsNPISDIWAVHALRIVAKY 245
Cdd:cd14861 164 PKLLPKVAICDPELTLGLPPRLTAATGMDALTHCIEAYLSPGF-------------------HPMADGIALEGLRLISEW 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 246 LKRAVRNPDDLEARSSMHLASAFAGIGFGNaGVHLCHGMSYPISGLVKTykakeynvdhplvPHGLSVVLTSPAVFTFTA 325
Cdd:cd14861 225 LPRAVADGSDLEARGEMMMAALMGAVAFQK-GLGAVHALAHALGALYGL-------------HHGLLNAILLPYVLRFNR 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 326 QMFPERHLETAEILGANIRTAkiqDAgpvLADALRKFLFDLNVDDGLAALGYSKDDIPSLVKGTLpQERVTKLAPRAQSE 405
Cdd:cd14861 291 PAVEDKLARLARALGLGLGGF---DD---FIAWVEDLNERLGLPATLSELGVTEDDLDELAELAL-ADPCHATNPRPVTA 363
|
410
....*....|.
gi 1958777067 406 EDLSALFEASM 416
Cdd:cd14861 364 EDYRALLREAL 374
|
|
| HVD |
cd08193 |
5-hydroxyvalerate dehydrogenase (HVD) catalyzes the oxidation of 5-hydroxyvalerate to ... |
3-414 |
7.14e-56 |
|
5-hydroxyvalerate dehydrogenase (HVD) catalyzes the oxidation of 5-hydroxyvalerate to 5-oxovalerate with NAD+ as cofactor; 5-hydroxyvalerate dehydrogenase (HVD) is an iron-containing (type III) NAD-dependent alcohol dehydrogenase. It plays a role in the cyclopentanol metabolism biochemical pathway. It catalyzes the oxidation of 5-hydroxyvalerate to 5-oxovalerate with NAD+ as cofactor. This cyclopentanol (cpn) degradation pathway is present in some bacteria which can use cyclopentanol as sole carbon source. In Comamonas sp. strain NCIMB 9872, this enzyme is encoded by the CpnD gene.
Pssm-ID: 341472 [Multi-domain] Cd Length: 379 Bit Score: 188.88 E-value: 7.14e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 3 VSNIRYGAGVTKEVGMDLQNMGAKNVCLMTDKNLSQLPPVQIVMDSLSKNGISFQVYDNVRVEPTDGSFMDAIEFAKKGA 82
Cdd:cd08193 4 VPRIICGAGAAARLGELLRELGARRVLLVTDPGLVKAGLADPALAALEAAGIAVTVFDDVVADPPEAVVEAAVEQAREAG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 83 FDAYVAVGGGSTMDTCKAANLYACSPHSefldyVNAPIGKGKpVTVPLKPLIAVPTTSGTGSETTGVAIF-DYEHlkVKT 161
Cdd:cd08193 84 ADGVIGFGGGSSMDVAKLVALLAGSDQP-----LDDIYGVGK-ATGPRLPLILVPTTAGTGSEVTPISIVtTGET--EKK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 162 GIASRAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTAipysmRSpcpsnpiqrpayqGSNPISDIWAVHALRI 241
Cdd:cd08193 156 GVVSPQLLPDVALLDAELTLGLPPHVTAATGIDAMVHAIEAYTS-----RH-------------KKNPISDALAREALRL 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 242 VAKYLKRAVRNPDDLEARSSMHLASAFAGIGFGNAGVHLCHGMSYPISGLVKtykakeynvdhplVPHGLSVVLTSPAVF 321
Cdd:cd08193 218 LGANLRRAVEDGSDLEAREAMLLGSMLAGQAFANAPVAAVHALAYPLGGHFH-------------VPHGLSNALVLPHVL 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 322 TFTAQMFPERHLETAEILGANIRTAKIQDAGPVLADALRKFLFDLNVDDGLAALGYSKDDIPSLVKGTLPQERVTKLAPR 401
Cdd:cd08193 285 RFNLPAAEALYAELARALLPGLAFGSDAAAAEAFIDALEELVEASGLPTRLRDVGVTEEDLPMLAEDAMKQTRLLVNNPR 364
|
410
....*....|...
gi 1958777067 402 AQSEEDLSALFEA 414
Cdd:cd08193 365 EVTEEDALAIYQA 377
|
|
| Fe-ADH-like |
cd08183 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
6-413 |
2.65e-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: 187.32 E-value: 2.65e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 6 IRYGAGVTKEVGMDLQNMGaKNVCLMTDKNLSQLPPVQIVMDSLSKNGISFQVYDNVRvEPTDGSFMDAIEFAKKGAFDA 85
Cdd:cd08183 4 IVFGRGSLQELGELAAELG-KRALLVTGRSSLRSGRLARLLEALEAAGIEVALFSVSG-EPTVETVDAAVALAREAGCDV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 86 YVAVGGGSTMDTCKAANLYACSPHS--EFLDYVnapiGKGKPVTVPLKPLIAVPTtsgtgsettgVA-----------IF 152
Cdd:cd08183 82 VIAIGGGSVIDAAKAIAALLTNEGSvlDYLEVV----GKGRPLTEPPLPFIAIPT----------TAgtgsevtknavLS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 153 DYEHlKVKTGIASRAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTAIpysmrspcpsnpiqrpayqGSNPISD 232
Cdd:cd08183 148 SPEH-GVKVSLRSPSMLPDVALVDPELTLSLPPEVTAASGLDALTQLIEPYVSR-------------------KANPLTD 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 233 IWAVHALRIVAKYLKRAVRNPDDLEARSSMHLASAFAGIGFGNAGVHLCHGMSYPISGLVKtykakeynvdhplVPHGL- 311
Cdd:cd08183 208 ALAREGLRLAARSLRRAYEDGEDLEAREDMALASLLGGLALANAGLGAVHGLAGPLGGMFG-------------APHGAi 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 312 -SVVLtsPAVFTFTAQM----FPERHLETAEILGANIRTAKIQDAGPVLADALRKFLFDLNVdDGLAALGYSKDDIPSLV 386
Cdd:cd08183 275 cAALL--PPVLEANLRAlrerEPDSPALARYRELAGILTGDPDAAAEDGVEWLEELCEELGI-PRLSEYGLTEEDFPEIV 351
|
410 420
....*....|....*....|....*..
gi 1958777067 387 KGTLpQERVTKLAPRAQSEEDLSALFE 413
Cdd:cd08183 352 EKAR-GSSSMKGNPIELSDEELLEILE 377
|
|
| HEPD |
cd08182 |
Hydroxyethylphosphoate dehydrogenase (HEPD) catalyzes the reduction of phosphonoacetaldehyde ... |
4-413 |
6.06e-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: 175.49 E-value: 6.06e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 4 SNIRYGAGVTKEVGMDLQNMGAKNVCLMTDKNLSQLPPVQIVMDSLsKNGISFQVYDNVRVEPTDGSFMDAIEFAKKGAF 83
Cdd:cd08182 2 VKIIFGPGALAELKDLLGGLGARRVLLVTGPSAVRESGAADILDAL-GGRIPVVVFSDFSPNPDLEDLERGIELFRESGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 84 DAYVAVGGGSTMDTCKAANLYACSPHSEFLdyvnAPIGKGKPVTVPLKPLIAVPTtsgtgsettgVA-----------IF 152
Cdd:cd08182 81 DVIIAVGGGSVIDTAKAIAALLGSPGENLL----LLRTGEKAPEENALPLIAIPT----------TAgtgsevtpfatIW 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 153 DyEHLKVKTGIASRAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTAIpysmrspcpsnpiqrpayqGSNPISD 232
Cdd:cd08182 147 D-EAEGKKYSLAHPSLYPDAAILDPELTLSLPLYLTASTGLDALSHAIESIWSV-------------------NANPESR 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 233 IWAVHALRIVAKYLKRAVRNPDDLEARSSMHLASAFAGIGFGNAGVHLCHGMSYPISglvktykaKEYNvdhplVPHGLS 312
Cdd:cd08182 207 AYALRAIRLILENLPLLLENLPNLEAREAMAEASLLAGLAISITKTTAAHAISYPLT--------SRYG-----VPHGHA 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 313 VVLTSPAVFTFTAQMFPERhleTAEILGANIRTAKIQDAGPVLADALRKFLFDLNVDDGLAALGYSKDDIPSLVKGTLPQ 392
Cdd:cd08182 274 CALTLPAVLRYNAGADDEC---DDDPRGREILLALGASDPAEAAERLRALLESLGLPTRLSEYGVTAEDLEALAASVNTP 350
|
410 420
....*....|....*....|.
gi 1958777067 393 ERVtKLAPRAQSEEDLSALFE 413
Cdd:cd08182 351 ERL-KNNPVRLSEEDLLRLLE 370
|
|
| NADPH_BDH |
cd08179 |
NADPH-dependent butanol dehydrogenase involved in the butanol and ethanol formation pathway in ... |
20-414 |
8.89e-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: 172.76 E-value: 8.89e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 20 LQNMGAKNVCLMTDKN-LSQLPPVQIVMDSLSKNGISFQVYDNVRVEPTDGSFMDAIEFAKKGAFDAYVAVGGGSTMDTC 98
Cdd:cd08179 18 LKTLKGKRAFIVTGGGsMKRNGFLDKVEDYLKEAGMEVKVFEGVEPDPSVETVEKGAEAMREFEPDWIIAIGGGSVIDAA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 99 KAANLYACSPHSEFLDYVnapigkgKPVTVPLKP----LIAVPTTSGTGSETTGVAIF-DYEHlKVKTGIASRAIKPTLG 173
Cdd:cd08179 98 KAMWVFYEYPELTFEDAL-------VPFPLPELRkkarFIAIPSTSGTGSEVTRASVItDTEK-GIKYPLASFEITPDVA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 174 LVDPLHTLHMPCQVVANSGFDVLCHALESYTAIPysmrspcpsnpiqrpayqgSNPISDIWAVHALRIVAKYLKRAVRNP 253
Cdd:cd08179 170 ILDPELTMTMPPHVTANTGMDALTHAIEAYVSTL-------------------ANDFTDALALGAILDIFENLPKSYNGG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 254 DDLEARSSMHLASAFAGIGFGNAGVHLCHGMSYPISGlvktykakEYNvdhplVPHGL--SVVLtsPAVFTFTAQMFPER 331
Cdd:cd08179 231 KDLEAREKMHNASCLAGMAFSNSGLGIVHSMAHKGGA--------FFG-----IPHGLanAILL--PYVIEFNSKDPEAR 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 332 HLETAEILGANiRTAKIQDagpvLADALRKFLFDLNVDDGLAALGYSKDD----IPSLVKGTLpQERVTKLAPRAQSEED 407
Cdd:cd08179 296 ARYAALLIGLT-DEELVED----LIEAIEELNKKLGIPLSFKEAGIDEDEffakLDEMAENAM-NDACTGTNPRKPTVEE 369
|
....*..
gi 1958777067 408 LSALFEA 414
Cdd:cd08179 370 MKELLKA 376
|
|
| PDD |
cd08180 |
1,3-propanediol dehydrogenase (PPD) catalyzes the reduction of 3-hydroxypropionaldehyde (3-HPA) ... |
20-413 |
1.90e-45 |
|
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: 159.97 E-value: 1.90e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 20 LQNMGAKNVCLMTDKNLSQLPPVQIVMDSLSKNgISFQVYDNVRVEPTDGSFMDAIEFAKKGAFDAYVAVGGGSTMDTCK 99
Cdd:cd08180 17 LKELKGKRVFIVTDPFMVKSGMVDKVTDELDKS-NEVEIFSDVVPDPSIEVVAKGLAKILEFKPDTIIALGGGSAIDAAK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 100 AANLYacsphsefldYVNAPIGKGKPvtvplkPLIAVPTTSGTGSETTGVA-IFDYEHlKVKTGIASRAIKPTLGLVDPL 178
Cdd:cd08180 96 AIIYF----------ALKQKGNIKKP------LFIAIPTTSGTGSEVTSFAvITDPEK-GIKYPLVDDSMLPDIAILDPE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 179 HTLHMPCQVVANSGFDVLCHALESYTAIpysmrspcpsnpiqrpayqGSNPISDIWAVHALRIVAKYLKRAVRNPDDLEA 258
Cdd:cd08180 159 LVKSVPPKVTADTGMDVLTHALEAYVST-------------------NANDFTDALAEKAIKLVFENLPRAYRDGDDLEA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 259 RSSMHLASAFAGIGFGNAGVHLCHGMSYPISGLVKtykakeynvdhplVPHGLSVVLTSPAVFTFtaqmfperhletaei 338
Cdd:cd08180 220 REKMHNASCMAGIAFNNAGLGINHSLAHALGGRFH-------------IPHGRANAILLPYVIEF--------------- 271
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958777067 339 lganirtakiqdagpvLADALRKFLFDLNVDDGLAALGYSKDD----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 |
1.93e-43 |
|
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: 155.44 E-value: 1.93e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 5 NIRYGAGVTKEVGMDLQNMGaKNVCLMT-----DKNLSQlppvQIVMDSLSKNGISFQVYDNVRVEPTDGSFMDAIEFAK 79
Cdd:cd08181 6 KVYFGKNCVEKHADELAALG-KKALIVTgkhsaKKNGSL----DDVTEALEENGIEYFIFDEVEENPSIETVEKGAELAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 80 KGAFDAYVAVGGGSTMDTCKAANLYACSP-HSEFLDYVNAPigkGKPVtvplkPLIAVPTTSGTGSETTGVAIFDYEHLK 158
Cdd:cd08181 81 KEGADFVIGIGGGSPLDAAKAIALLAANKdGDEDLFQNGKY---NPPL-----PIVAIPTTAGTGSEVTPYSILTDHEKG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 159 VKTGIASRAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYtaipYSMRspcpsnpiqrpayqgSNPISDIWAVHA 238
Cdd:cd08181 153 TKKSFGNPLIFPKLALLDPKYTLSLPEELTIDTAVDALSHAIEGY----LSVK---------------ATPLSDALALEA 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 239 LRIVAKYLKRAVRNPDDLEARSSMHLASAFAGIGFGNAGVHLCHGMSYPIsglvkTYkakEYNvdhplVPHGLSVVLTSP 318
Cdd:cd08181 214 LRLIGECLPNLLGDELDEEDREKLMYASTLAGMVIAQTGTTLPHGLGYPL-----TY---FKG-----IPHGRANGILLP 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 319 AVFTFTAQMFPERHLETAEILGANIrtakiqdagpvlADALRKFLFDLNVDDGLaalgYSKDDIPSLVKGTLPQERVtKL 398
Cdd:cd08181 281 AYLKLCEKQEPEKVDKILKLLGFGS------------IEEFQKFLNRLLGKKEE----LSEEELEKYADEAMKAKNK-KN 343
|
410
....*....|....*
gi 1958777067 399 APRAQSEEDLSALFE 413
Cdd:cd08181 344 TPGNVTKEDILRIYR 358
|
|
| Fe-ADH-like |
cd08186 |
Iron-containing alcohol dehydrogenase; This family contains iron-containing alcohol ... |
8-416 |
2.46e-42 |
|
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: 152.80 E-value: 2.46e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 8 YGAGVTKEVGMDLQNMGAKNVCLMTDKNLSQLPPV-QIVMDSLSKNGISFQVYDNVRVEPTDGSFMDAIEFAKKGAFDAY 86
Cdd:cd08186 6 FGVGAIAKIKDILKDLGIDKVIIVTGRSSYKKSGAwDDVEKALEENGIEYVVYDKVTPNPTVDQADEAAKLARDFGADAV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 87 VAVGGGSTMDTCKAANLYACSPHS---EFLDYVNAPIGKgkpvtvplKPLIAVPTTSGTGSETTGVAIFDYEHLKVKTGI 163
Cdd:cd08186 86 IAIGGGSPIDTAKSVAVLLAYGGKtarDLYGFRFAPERA--------LPLVAINLTHGTGSEVDRFAVATIPEKGYKPGI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 164 ASRAIKPTLGLVDPLHTLHMPC-QVVANSgFDVLCHALESYTAipysmrspcpsnpiqrpayQGSNPISDIWAVHALRIV 242
Cdd:cd08186 158 AYDCIYPLYAIDDPRLTLTLPKeQTLYTS-IDAFNHVYEAATT-------------------KVSSPYVITLAKEAIRLI 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 243 AKYLKRAVRNPDDLEARSSMHLASAFAGIGFGNAGVHLCHGMSYPISGLVktykakeynvdhPLVPHGLSVVLTSPAVFT 322
Cdd:cd08186 218 AEYLPRALANPKDLEARYWLLYASMIAGIAIDNGLLHLTHALEHPLSGLK------------PELPHGLGLALLGPAVVK 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 323 FTAQMFPErhlETAEIL-----GANIRTAKIQDAgpvlADALRKFLFDLNVDDGLAALGYSKDDIPSLVK---GTLPQER 394
Cdd:cd08186 286 YIYKAVPE---TLADILrpivpGLKGTPDEAEKA----ARGVEEFLFSVGFTEKLSDYGFTEDDVDRLVElafTTPSLDL 358
|
410 420
....*....|....*....|..
gi 1958777067 395 VTKLAPRAQSEEDLSALFEASM 416
Cdd:cd08186 359 LLSLAPVEVTEEVVREIYEESL 380
|
|
| Fe-ADH-like |
cd08189 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
9-387 |
4.27e-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: 149.54 E-value: 4.27e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 9 GAGVTKEVGMDLQNMGAKNVCLMTDKNLSQLPPVQIVMDSLSKNGISFQVYDNVRVEPTDGSFMDAIEFAKKGAFDAYVA 88
Cdd:cd08189 11 GAGSLLQLPEALKKLGIKRVLIVTDKGLVKLGLLDPLLDALKKAGIEYVVFDGVVPDPTIDNVEEGLALYKENGCDAIIA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 89 VGGGSTMDTCKAANLYACSPHSEFLDYVnapiGKGKpVTVPLKPLIAVPTTSGTGSETTGVA-IFDYEHlKVKTGIASRA 167
Cdd:cd08189 91 IGGGSVIDCAKVIAARAANPKKSVRKLK----GLLK-VRKKLPPLIAVPTTAGTGSEATIAAvITDPET-HEKYAINDPK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 168 IKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTAIPYsmrspcpsnpiqrpayqgsNPISDIWAVHALRIVAKYLK 247
Cdd:cd08189 165 LIPDAAVLDPELTLGLPPAITAATGMDALTHAVEAYISRSA-------------------TKETDEYALEAVKLIFENLP 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 248 RAVRNPDDLEARSSMHLASAFAGIGFGNAGVHLCHGMSYPISGLvktykakeYNvdhplVPHGL--SVVLtsPAVFTFTA 325
Cdd:cd08189 226 KAYEDGSDLEARENMLLASYYAGLAFTRAYVGYVHAIAHQLGGL--------YG-----VPHGLanAVVL--PHVLEFYG 290
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958777067 326 QMFPERHLETAEILGanIRTAKIQDAgpVLADALRKFLFDLNVD----DGLAALgySKDDIPSLVK 387
Cdd:cd08189 291 PAAEKRLAELADAAG--LGDSGESDS--EKAEAFIAAIRELNRRmgipTTLEEL--KEEDIPEIAK 350
|
|
| PRK10624 |
PRK10624 |
L-1,2-propanediol oxidoreductase; Provisional |
8-416 |
9.98e-41 |
|
L-1,2-propanediol oxidoreductase; Provisional
Pssm-ID: 182595 [Multi-domain] Cd Length: 382 Bit Score: 148.61 E-value: 9.98e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 8 YGAGVTKEVGMDLQNMGAKNVCLMTDKNLSQLPPVQIVMDSLSKNGISFQVYDNVRVEPTDGSFMDAIE-FAKKGAfDAY 86
Cdd:PRK10624 13 FGRGAIGALTDEVKRRGFKKALIVTDKTLVKCGVVAKVTDVLDAAGLAYEIYDGVKPNPTIEVVKEGVEvFKASGA-DYL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 87 VAVGGGSTMDTCKAANLYACSPhsEFLDYVN----APIGKgkpvtvPLKPLIAVPTTS-GTGSETTGVAIFDYEHLKVKT 161
Cdd:PRK10624 92 IAIGGGSPQDTCKAIGIISNNP--EFADVRSlegvAPTKK------PSVPIIAIPTTAgTAAEVTINYVITDEEKRRKFV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 162 GIASRAIkPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTAipysmrspcpsnpiqrpayQGSNPISDIWAVHALRI 241
Cdd:PRK10624 164 CVDPHDI-PQVAFVDADMMDSMPPGLKAATGVDALTHAIEGYIT-------------------RGAWALTDMLHLKAIEI 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 242 VAKYLKRAVRNpdDLEARSSMHLASAFAGIGFGNAGVHLCHGMSYPISGLvktykakeYNvdhplVPHGLSVVLTSPAVF 321
Cdd:PRK10624 224 IAGALRGAVAG--DKEAGEGMALGQYIAGMGFSNVGLGLVHGMAHPLGAF--------YN-----TPHGVANAILLPHVM 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 322 TFTAQMFPERHLETAEILGANIRTAKIQDAGPVLADALRKFLFDLNVDDGLAALGYSKDDIPSLVKGTLpQERVTKLAPR 401
Cdd:PRK10624 289 EYNADFTGEKYRDIARAMGVKVEGMSLEEARNAAVEAVKALNRDVGIPPHLRDVGVKEEDIPALAQAAF-DDVCTGGNPR 367
|
410
....*....|....*
gi 1958777067 402 AQSEEDLSALFEASM 416
Cdd:PRK10624 368 EATLEDIVELYKKAW 382
|
|
| AAD_C |
cd08178 |
C-terminal alcohol dehydrogenase domain of the acetaldehyde dehydrogenase-alcohol ... |
23-381 |
1.77e-40 |
|
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: 148.49 E-value: 1.77e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 23 MGAKNVCLMTDKNLSQLPPVQIVMDSLSKNGISFQVYDNVRVEPTDGSFMDAIEFAKkgAF--DAYVAVGGGSTMDTCKA 100
Cdd:cd08178 21 PGVKRAFIVTDRVLYKLGYVDKVLDVLEARGVETEVFSDVEPDPTLSTVRKGLEAMN--AFkpDVIIALGGGSAMDAAKI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 101 ANLYACSPHSEFLD------------YVNAPIGKGKPvtvplkpLIAVPTTSGTGSETTGVA-IFDyEHLKVKTGIASRA 167
Cdd:cd08178 99 MWLFYEHPETKFEDlaqrfmdirkrvYKFPKLGKKAK-------LVAIPTTSGTGSEVTPFAvITD-DKTGKKYPLADYA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 168 IKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTAIPysmrspcpsnpiqrpayqgSNPISDIWAVHALRIVAKYLK 247
Cdd:cd08178 171 LTPDMAIVDPELVMTMPKRLTADTGIDALTHAIEAYVSVM-------------------ASDYTDGLALQAIKLIFEYLP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 248 RAVRNPDDLEARSSMHLASAFAGIGFGNAGVHLCHGMSYPISGlvktykakEYNvdhplVPHGLSVVLTSPAVFTFTAQ- 326
Cdd:cd08178 232 RSYNNGNDIEAREKMHNAATIAGMAFANAFLGICHSLAHKLGA--------AFH-----IPHGRANAILLPHVIRYNATd 298
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958777067 327 ------MFP--------ERHLETAEILG--ANIRTAKIQdagpVLADALRKFLFDLNVDDGLAALGYSKDD 381
Cdd:cd08178 299 pptkqaAFPqykyyvakERYAEIADLLGlgGKTPEEKVE----SLIKAIEDLKKDLGIPTSIREAGIDEAD 365
|
|
| Fe-ADH-like |
cd14864 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
4-414 |
4.55e-37 |
|
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: 138.59 E-value: 4.55e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 4 SNIRYGAGVTKEVGMDLQNMGAKNVcLMTDKNLSQLPPVQIVMDSLSKNGISFQVYDNVRVEPTDGSFMDAIEFAKKGAF 83
Cdd:cd14864 5 PNIVFGADSLERIGEEVKEYGSRFL-LITDPVLKESGLADKIVSSLEKAGISVIVFDEIPASATSDTIDEAAELARKAGA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 84 DAYVAVGGGSTMDTCKAANLYACSPHsEFLDYVNAPIGKGKPVtvplkPLIAVPTTSGTGSETTGVAIF-DYEHLKVKTg 162
Cdd:cd14864 84 DGIIAVGGGKVLDTAKAVAILANNDG-GAYDFLEGAKPKKKPL-----PLIAVPTTPRSGFEFSDRFPVvDSRSREVKL- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 163 IASRAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTAipysmrspcpsnpiqrpayQGSNPISDIWAVHALRIV 242
Cdd:cd14864 157 LKAQPGLPKAVIVDPNLMASLTGNQTAAMALAALALAVEAYLS-------------------KKSNFFSDALALKAIELV 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 243 AKYLKRAVRNPDDLEARSSMHLASAFAGIGFGNAGVHLCHGMSYPISGLvktykakeYNVDHPLVphgLSVVLtsPAVFT 322
Cdd:cd14864 218 SENLDGALADPKNTPAEELLAQAGCLAGLAASSSSPGLATALALAVNSR--------YKVSKSLV---ASILL--PHVIE 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 323 FTAQMFPERHLETAEILGANIRTAKIQDAGPVLADALRKFLFDLNVDDGLAALG--YSKDDIPSLVKgtlpQERVTKLAP 400
Cdd:cd14864 285 YAATSAPDKYAKIARALGEDVEGASPEEAAIAAVEGVRRLIAQLNLPTRLKDLDlaSSLEQLAAIAE----DAPKLNGLP 360
|
410
....*....|....
gi 1958777067 401 RAQSEEDLSALFEA 414
Cdd:cd14864 361 RSMSSDDIFDILKA 374
|
|
| PRK13805 |
PRK13805 |
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional |
23-381 |
1.94e-35 |
|
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional
Pssm-ID: 237515 [Multi-domain] Cd Length: 862 Bit Score: 138.78 E-value: 1.94e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 23 MGAKNVCLMTDKNLSQLPPVQIVMDSLSK--NGISFQVYDNVRVEPTdgsfmdaIEFAKKGA-----F--DAYVAVGGGS 93
Cdd:PRK13805 478 DGKKRAFIVTDRFMVELGYVDKVTDVLKKreNGVEYEVFSEVEPDPT-------LSTVRKGAelmrsFkpDTIIALGGGS 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 94 TMDTCKAANLYACSPHSEFLD------------YVNAPIG-KGKPVTVP--------LKPlIAVpttsgtgsettgvaIF 152
Cdd:PRK13805 551 PMDAAKIMWLFYEHPETDFEDlaqkfmdirkriYKFPKLGkKAKLVAIPttsgtgseVTP-FAV--------------IT 615
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 153 DyEHLKVKTGIASRAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTAIpysMrspcpsnpiqrpayqgSNPISD 232
Cdd:PRK13805 616 D-DKTGVKYPLADYELTPDVAIVDPNLVMTMPKSLTADTGIDALTHALEAYVSV---M----------------ASDYTD 675
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 233 IWAVHALRIVAKYLKRAVRN-PDDLEARSSMHLASAFAGIGFGNAGVHLCHGMSYPISGlvktykakEYNvdhplVPHGL 311
Cdd:PRK13805 676 GLALQAIKLVFEYLPRSYKNgAKDPEAREKMHNASTIAGMAFANAFLGICHSMAHKLGA--------EFH-----IPHGR 742
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 312 SVVLTSPAVFTFTAQ------MFP--------ERHLETAEILG--ANIRTAKIQdagpVLADALRKFLFDLNVDDGLAAL 375
Cdd:PRK13805 743 ANAILLPHVIRYNATdppkqaAFPqyeypradERYAEIARHLGlpGSTTEEKVE----SLIKAIEELKAELGIPMSIKEA 818
|
....*.
gi 1958777067 376 GYSKDD 381
Cdd:PRK13805 819 GVDEAD 824
|
|
| BDH |
cd08187 |
Butanol dehydrogenase catalyzes the conversion of butyraldehyde to butanol with the cofactor ... |
6-387 |
7.51e-35 |
|
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: 132.56 E-value: 7.51e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 6 IRYGAGVTKEVGMDLQNMGaKNVCLMTDKN-------LSQlppvqiVMDSLSKNGISFQVYDNVRVEPTDGSFMDAIEFA 78
Cdd:cd08187 10 IIFGKGAIEELGEEIKKYG-KKVLLVYGGGsikknglYDR------VVASLKEAGIEVVEFGGVEPNPRLETVREGIELA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 79 KKGAFDAYVAVGGGSTMDTCKAANLYACSPHsEFLDYVNapigKGKPVTVPLkPLIAVPTTSGTGSETTGVAIFDYEHLK 158
Cdd:cd08187 83 REENVDFILAVGGGSVIDAAKAIAAGAKYDG-DVWDFFT----GKAPPEKAL-PVGTVLTLAATGSEMNGGAVITNEETK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 159 VKTGIASRAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESY-TaipysmrspcpsnpiqrpaYQGSNPISDIWAVH 237
Cdd:cd08187 157 EKLGFGSPLLRPKFSILDPELTYTLPKYQTAAGIVDIFSHVLEQYfT-------------------GTEDAPLQDRLAEG 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 238 ALRIVAKYLKRAVRNPDDLEARSSMHLASAFA--GI-GFGNAGVHLCHGMSYPISGLvktykakeYNVDHplvPHGLSVV 314
Cdd:cd08187 218 LLRTVIENGPKALKDPDDYEARANLMWAATLAlnGLlGAGRGGDWATHAIEHELSAL--------YDITH---GAGLAIV 286
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958777067 315 LtsPAVFTFTAQMFPERHLETAE-ILGanIRTAKIQDAGPVLA-DALRKFLFDLNVDDGLAALGYSKDDIPSLVK 387
Cdd:cd08187 287 F--PAWMRYVLKKKPERFAQFARrVFG--IDPGGDDEETALEGiEALEEFFKSIGLPTTLSELGIDEEDIEEMAE 357
|
|
| PRK09860 |
PRK09860 |
putative alcohol dehydrogenase; Provisional |
9-416 |
4.47e-32 |
|
putative alcohol dehydrogenase; Provisional
Pssm-ID: 182118 [Multi-domain] Cd Length: 383 Bit Score: 125.07 E-value: 4.47e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 9 GAGVTKEVGMDLQNMGAKNVCLMTDKNLSQLPPVQIVMDSLSKNGISFQVYDNVRVEPTDGSFMDAIEFAKKGAFDAYVA 88
Cdd:PRK09860 15 GADSLTDAMNMMADYGFTRTLIVTDNMLTKLGMAGDVQKALEERNIFSVIYDGTQPNPTTENVAAGLKLLKENNCDSVIS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 89 VGGGSTMDTCKAANLYACSpHSEFLDYVNAPIGKGkpvtvPLKPLIAVPTTSGTGSETTGVAIFDYEHLKVKTGIASRAI 168
Cdd:PRK09860 95 LGGGSPHDCAKGIALVAAN-GGDIRDYEGVDRSAK-----PQLPMIAINTTAGTASEMTRFCIITDEARHIKMAIVDKHV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 169 KPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTAIpysmrspcpsnpiqrpayqGSNPISDIWAVHALRIVAKYLKR 248
Cdd:PRK09860 169 TPLLSVNDSSLMIGMPKSLTAATGMDALTHAIEAYVSI-------------------AATPITDACALKAVTMIAENLPL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 249 AVRNPDDLEARSSMHLASAFAGIGFGNAGVHLCHGMSYPISGLvktykakeYNvdhplVPHGLSVVLTSPAVFTFTAQMF 328
Cdd:PRK09860 230 AVEDGSNAKAREAMAYAQFLAGMAFNNASLGYVHAMAHQLGGF--------YN-----LPHGVCNAVLLPHVQVFNSKVA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 329 PERHLETAEILGANIRTAKIQDAGPVLADALRKFLFDLNVDDGLAALGYSKDDIPSLVKGTLpQERVTKLAPRAQSEEDL 408
Cdd:PRK09860 297 AARLRDCAAAMGVNVTGKNDAEGAEACINAIRELAKKVDIPAGLRDLNVKEEDFAVLATNAL-KDACGFTNPIQATHEEI 375
|
....*...
gi 1958777067 409 SALFEASM 416
Cdd:PRK09860 376 VAIYRAAM 383
|
|
| PRK15454 |
PRK15454 |
ethanolamine utilization ethanol dehydrogenase EutG; |
9-415 |
3.35e-31 |
|
ethanolamine utilization ethanol dehydrogenase EutG;
Pssm-ID: 185351 [Multi-domain] Cd Length: 395 Bit Score: 123.21 E-value: 3.35e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 9 GAGVTKEVGMDLQNMGAKNVCLMTDKNLSQLPPVQIVMDSLSKNGISFQVYDNVRVEPTDGSFMDAIEFAKKGAFDAYVA 88
Cdd:PRK15454 33 GPGAVSSCGQQAQTRGLKHLFVMADSFLHQAGMTAGLTRSLAVKGIAMTLWPCPVGEPCITDVCAAVAQLRESGCDGVIA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 89 VGGGSTMDTCKAANLYACSPHSEFLDYVNapigkgKPVTVPLKPLIAVPTTSGTGSETTGVAIFDYEHLKVKTGIASRAI 168
Cdd:PRK15454 113 FGGGSVLDAAKAVALLVTNPDSTLAEMSE------TSVLQPRLPLIAIPTTAGTGSETTNVTVIIDAVSGRKQVLAHASL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 169 KPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTAIpysmrspcpsnpiqrpayqGSNPISDIWAVHALRIVAKYLKR 248
Cdd:PRK15454 187 MPDVAILDAALTEGVPSHVTAMTGIDALTHAIEAYSAL-------------------NATPFTDSLAIGAIAMIGKSLPK 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 249 AVRNPDDLEARSSMHLASAFAGIGFGNAGVHLCHGMSY-PISGLvktykakeynvdHplVPHGLSVVLTSPAVFTFTAQM 327
Cdd:PRK15454 248 AVGYGHDLAARESMLLASCMAGMAFSSAGLGLCHAMAHqPGAAL------------H--IPHGLANAMLLPTVMEFNRMV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 328 FPERHLEtaeiLGANIRTAKIQDAGPVlaDALRKFLFDLNVDDGLAALGYSKDDIPSLVKGTLpQERVTKLAPRAQSEED 407
Cdd:PRK15454 314 CRERFSQ----IGRALRTKKSDDRDAI--NAVSELIAEVGIGKRLGDVGATSAHYGAWAQAAL-EDICLRSNPRTASLEQ 386
|
....*...
gi 1958777067 408 LSALFEAS 415
Cdd:PRK15454 387 IVGLYAAA 394
|
|
| 4HBD_NAD |
cd14860 |
4-hydroxybutyrate dehydrogenase, also called gamma-hydroxybutyrate dehydrogenase, catalyzes ... |
65-419 |
9.78e-26 |
|
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: 107.30 E-value: 9.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 65 EPTDGSFMDAIEFAKKGAFDAYVAVGGGSTMDTCKaanLYACSPHSEFLDYV--NAPIGKGKPvtvplkpLIAVPTTSGT 142
Cdd:cd14860 61 EPSDEMVEAIYKDIKKYGYKRVIAIGGGTVIDIAK---LLALKGISPVLDLFdgKIPLIKEKE-------LIIVPTTCGT 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 143 GSETTGVAIFDYEHLKVKTGIASRAIKPTLGLVDP--LHTLhmPCQVVANSGFDVLCHALESYTaipysmrSPcpsnpiq 220
Cdd:cd14860 131 GSEVTNISIVELTSLGTKKGLAVDELYADKAVLIPelLKGL--PYKVFATSSIDALIHAIESYL-------SP------- 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 221 rpayqGSNPISDIWAVHALR-IVAKYLKRAVRNPDDL-EARSSMHLASAFAGIGFGNAGVHLCHGMSYPISGlvkTYKak 298
Cdd:cd14860 195 -----KATPYTEMFSYKAIEmILEGYQEIAEKGEEARfPLLGDFLIASNYAGIAFGNAGCAAVHALSYPLGG---KYH-- 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 299 eynvdhplVPHGLSVVltspAVFTFTAQMFpERHLETAEILGANIRTAKIQDAGPVLA-DALRKFLFDLNVDDGLAALGY 377
Cdd:cd14860 265 --------VPHGEANY----AVFTGVLKNY-QEKNPDGEIKKLNEFLAKILGCDEEDVyDELEELLNKILPKKPLHEYGM 331
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1958777067 378 SKDDIPSLVKGTLP-QERVTKLAPRAQSEEDLSALFeasMKLY 419
Cdd:cd14860 332 KEEEIDEFADSVMEnQQRLLANNYVPLDREDVAEIY---KELY 371
|
|
| MAR-like |
cd08192 |
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic ... |
6-414 |
1.28e-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: 1.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 6 IRYGAGVTKEVGMDLQNMGAKNVCLMTDKNLSQLPPVqiVMDSLSKNGISF-QVYDNVRVEPTDGSFMDAIEFAKKGAFD 84
Cdd:cd08192 4 VSYGPGAVEALLHELATLGASRVFIVTSKSLATKTDV--IKRLEEALGDRHvGVFSGVRQHTPREDVLEAARAVREAGAD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 85 AYVAVGGGSTMDTCKAANLyaCSPH----SEFLDYVNAPIGKGKPVTVPLKPLIAVPTTSGTGSETTGVAIFDyEHLKVK 160
Cdd:cd08192 82 LLVSLGGGSPIDAAKAVAL--ALAEdvtdVDQLDALEDGKRIDPNVTGPTLPHIAIPTTLSGAEFTAGAGATD-DDTGHK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 161 TGIASRAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYtaipYSMRSpcpsnpiqrpayqgsNPISDIWAVHALR 240
Cdd:cd08192 159 QGFAHPELGPDAVILDPELTLHTPERLWLSTGIRAVDHAVETL----CSPQA---------------TPFVDALALKALR 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 241 IVAKYLKRAVRNPDDLEARSSMHLASAFAGIGFGN-AGVHLCHGMSYPISGLvktykakeYNvdhplVPHGLSVVLTSPA 319
Cdd:cd08192 220 LLFEGLPRSKADPEDLEARLKCQLAAWLSLFGLGSgVPMGASHAIGHQLGPL--------YG-----VPHGITSCIMLPA 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 320 VFTFTAQMFPERHLETAEILGANIRTAKIQDAGpvLADALRKFLFDLNVDDGLAALGYSKDDIPSLVKGTLPQERVTKLA 399
Cdd:cd08192 287 VLRFNAPVNAERQRLIARALGLVTGGLGREAAD--AADAIDALIRELGLPRTLRDVGVGRDQLEKIAENALTDVWCRTNP 364
|
410
....*....|....*
gi 1958777067 400 PRAQSEEDLSALFEA 414
Cdd:cd08192 365 RPITDKDDVLEILES 379
|
|
| Fe-ADH-like |
cd14866 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
6-414 |
2.74e-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: 100.38 E-value: 2.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 6 IRYGAGVTKEVGMDLQNMGAKNVCLMTDKNLSQLPPVqivMDSLsKNGIS---FQVYDNVRVEPTDGSFMDAIEFAKKGA 82
Cdd:cd14866 8 LFSGRGALARLGRELDRLGARRALVVCGSSVGANPDL---MDPV-RAALGdrlAGVFDGVRPHSPLETVEAAAEALREAD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 83 FDAYVAVGGGSTMDTCKAANLYACSPHSeFLDYVNAPIGKGKPVT----VPLKPLIAVPTTSGTGSETTGVAIFDYEHLK 158
Cdd:cd14866 84 ADAVVAVGGGSAIVTARAASILLAEDRD-VRELCTRRAEDGLMVSprldAPKLPIFVVPTTPTTADVKAGSAVTDPPAGQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 159 vKTGIASRAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESytaiPYSMRspcpsnpiqrpayqgSNPISDIWAVHA 238
Cdd:cd14866 163 -RLALFDPKTRPAAVFYDPELLATAPASLVAGAAMNGFDMAVEG----LYSRH---------------ADPLADATLMHA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 239 LRIVAKYLKRAVrNPDDLEARSSMHLASAFAGIGFGNAGVHLCHGMSYPISGlvktykakEYNVDHPLVpHglSVVLtsP 318
Cdd:cd14866 223 LRLLADGLPRLA-DDDDPAARADLVLAAVLAGYGTDHTGGGVIHALGHAIGA--------RYGVQNGVV-H--AILL--P 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 319 AVFTFTAQMFPERHLETAEILGAniRTAKIQDAGPVLADALRKFLFDLNVDDGLAALGYSKDDIPSLVKGTLPQERVTKL 398
Cdd:cd14866 289 HVLRFNAPATDGRLDRLAEALGV--ADAGDEASAAAVVDAVEALLDALGVPTRLRDLGVSREDLPAIAEAAMDDWFMDNN 366
|
410
....*....|....*.
gi 1958777067 399 APRAQSEEDLSALFEA 414
Cdd:cd14866 367 PRPVPTAEELEALLEA 382
|
|
| YqdH |
COG1979 |
Alcohol dehydrogenase YqhD, Fe-dependent ADH family [Energy production and conversion]; |
45-416 |
5.14e-20 |
|
Alcohol dehydrogenase YqhD, Fe-dependent ADH family [Energy production and conversion];
Pssm-ID: 441582 [Multi-domain] Cd Length: 387 Bit Score: 90.90 E-value: 5.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 45 VMDSLSKNGISFQVYDNVRVEPTDGSFMDAIEFAKKGAFDAYVAVGGGSTMDTCKAANLYACSPHsEFLDYVNapigKGK 124
Cdd:COG1979 51 VKAALKEAGIEVVEFGGVEPNPRLETVRKGVELCKEEGIDFILAVGGGSVIDGAKAIAAGAKYDG-DPWDILT----GKA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 125 PVTVPLkPLIAVPTTSGTGSETTGVAIFDYEHLKVKTGIASRAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYT 204
Cdd:COG1979 126 PVEKAL-PLGTVLTLPATGSEMNSGSVITNEETKEKLGFGSPLVFPKFSILDPELTYTLPKRQTANGIVDIFSHVMEQYF 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 205 aipysmrspcpSNPIQrpayqgsNPISDIWAVHALRIVAKYLKRAVRNPDDLEARSSMHLASAFAGIGFGNAGVH---LC 281
Cdd:COG1979 205 -----------TYPVD-------APLQDRFAEGLLRTLIEEGPKALKDPEDYDARANLMWAATLALNGLIGAGVPqdwAT 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 282 HGMSYPISGLvktykakeYNVDHplvPHGLSVVLtsPAVFTFTAQMFPERHLETAE-ILGANIRTAK-IQDAGpvlADAL 359
Cdd:COG1979 267 HMIEHELSAL--------YDIDH---GAGLAIVL--PAWMRYVLEEKPEKFAQYAErVWGITEGDDEeRALEG---IEAT 330
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958777067 360 RKFLFDLNVDDGLAALGYSKDDIPSLVKGTLPQERVTKLAPRAQSEEDLSALFEASM 416
Cdd:COG1979 331 EEFFESLGLPTRLSEYGIDEEDIEEMAEKATAHGMTALGEFKDLTPEDVREILELAL 387
|
|
| MAR |
cd08177 |
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic ... |
6-414 |
1.58e-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: 86.02 E-value: 1.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 6 IRYGAGVTKEVGMDLQNMGAKNVCLMTDKnlSQLPPVQIVMDSLSKNGISfqVYDNVR----VEPTDgsfmDAIEFAKKG 81
Cdd:cd08177 4 VVFGAGTLAELAEELERLGARRALVLSTP--RQRALAERVAALLGDRVAG--VFDGAVmhvpVEVAE----RALAAAREA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 82 AFDAYVAVGGGSTmdtckaanlyacsphsefldyvnapIGKGKPVTVPLK-PLIAVPTTSgtgsettgvA------IFDY 154
Cdd:cd08177 76 GADGLVAIGGGSA-------------------------IGLAKAIALRTGlPIVAVPTTY---------AgsemtpIWGE 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 155 EHLKVKTGIASRAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTAipysmrspcpsnpiqrpayQGSNPISDIW 234
Cdd:cd08177 122 TEDGVKTTGRDPRVLPRTVIYDPDLTLGLPAALSVASGLNALAHAVEALYA-------------------PDANPITSLL 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 235 AVHALRIVAKYLKRAVRNPDDLEARSSMHLASAFAGIGFGNAG--VH--LCH--GMSYpisGLvktykakeynvdhplvP 308
Cdd:cd08177 183 AEEGIRALARALPRLVADPSDLEARSDALYGAWLAGVVLGSVGmgLHhkLCHvlGGTF---DL----------------P 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 309 HGL--SVVLtsPAVFTFTAQMFPERHLETAEILGANirtakiqDAgpvlADALRKFLFDLNVDDGLAALGYSKDDIPSLV 386
Cdd:cd08177 244 HAEthAVVL--PHVLAYNAPAAPDAMARLARALGGG-------DA----AGGLYDLARRLGAPTSLRDLGMPEDDIDRAA 310
|
410 420 430
....*....|....*....|....*....|.
gi 1958777067 387 kgtlpqERVTKLA---PRAQSEEDLSALFEA 414
Cdd:cd08177 311 ------DLALANPypnPRPVERDALRALLER 335
|
|
| DHQ_Fe-ADH |
cd07766 |
Dehydroquinate synthase-like (DHQ-like) and iron-containing alcohol dehydrogenases (Fe-ADH); ... |
5-387 |
7.37e-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: 56.22 E-value: 7.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 5 NIRYGAGVTKEVGMDLQNMGAKnVCLMTDKNLSQLPpVQIVMDSLSKnGISFQVYDNVRVEPTDGSFMDAIEFAKKGAFD 84
Cdd:cd07766 3 RIVFGEGAIAKLGEIKRRGFDR-ALVVSDEGVVKGV-GEKVADSLKK-GLAVAIFDFVGENPTFEEVKNAVERARAAEAD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 85 AYVAVGGGSTMDTCKAANLyacsphsefldyvnapigkgkpVTVPLKPLIAVPTTSGTGSETTGVAIFDYEHLKVKTGIA 164
Cdd:cd07766 80 AVIAVGGGSTLDTAKAVAA----------------------LLNRGIPFIIVPTTASTDSEVSPKSVITDKGGKNKQVGP 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 165 srAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTAIpysmrspcpsnpiqrpayqgsnpisdiwavhalrivak 244
Cdd:cd07766 138 --HYNPDVVFVDTDITKGLPPRQVASGGVDALAHAVELEKVV-------------------------------------- 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 245 ylkravrnpddlearssmhLASAFAGIGFGNA-GVHLCHGMSYPISGLVKTykakeynvdhplvPHGLSVVLTSPAVFTF 323
Cdd:cd07766 178 -------------------EAATLAGMGLFESpGLGLAHAIGHALTAFEGI-------------PHGEAVAVGLPYVLKV 225
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958777067 324 TAQMFPERHLETAeilganirtakiqdagpvladALRKFLFDLNVDDGLAALGYSKDDIPSLVK 387
Cdd:cd07766 226 ANDMNPEPEAAIE---------------------AVFKFLEDLGLPTHLADLGVSKEDIPKLAE 268
|
|
| PRK15138 |
PRK15138 |
alcohol dehydrogenase; |
48-398 |
2.27e-07 |
|
alcohol dehydrogenase;
Pssm-ID: 185092 [Multi-domain] Cd Length: 387 Bit Score: 52.49 E-value: 2.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 48 SLSKNGISFQVYD-----NVR----VEP--TDGSFMDAIEFAKKGAFDAYVAVGGGSTMDTCK----AANLYACSPHSEF 112
Cdd:PRK15138 40 SVKKTGVLDQVLDalkgmDVLefggIEPnpTYETLMKAVKLVREEKITFLLAVGGGSVLDGTKfiaaAANYPENIDPWHI 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 113 LDYVNAPIGKGkpvtVPLKPLIAVPttsGTGSETTGVAIFDYEHLKVKTGIASRAIKPTLGLVDPLHTLHMPCQVVANSG 192
Cdd:PRK15138 120 LETGGKEIKSA----IPMGSVLTLP---ATGSESNAGAVISRKTTGDKQAFHSPHVQPVFAVLDPVYTYTLPPRQVANGV 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 193 FDVLCHALESYTAIPYSMRspcpsnpiqrpayqgsnpISDIWAVHALRIVAKYLKRAVRNPDDLEARSSMHLASAFAGIG 272
Cdd:PRK15138 193 VDAFVHTVEQYVTYPVDAK------------------IQDRFAEGILLTLIEEGPKALKEPENYDVRANVMWAATQALNG 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 273 FGNAGVH---LCHGMSYPISGLvktykakeYNVDHplvPHGLSVVLtsPAVFTFTAQMFPERHLETAEILGaNIRTAKIQ 349
Cdd:PRK15138 255 LIGAGVPqdwATHMLGHELTAM--------HGLDH---AQTLAIVL--PALWNEKRDTKRAKLLQYAERVW-NITEGSDD 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1958777067 350 DAGPVLADALRKFLFDLNVDDGLAALGYSKDDIPSLVKgTLPQERVTKL 398
Cdd:PRK15138 321 ERIDAAIAATRNFFEQMGVPTRLSDYGLDGSSIPALLK-KLEEHGMTQL 368
|
|
| Fe-ADH_2 |
pfam13685 |
Iron-containing alcohol dehydrogenase; |
7-285 |
5.39e-07 |
|
Iron-containing alcohol dehydrogenase;
Pssm-ID: 404557 [Multi-domain] Cd Length: 251 Bit Score: 50.38 E-value: 5.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 7 RYGAGVTKEVGMDLQNMGAKNVCLMTDKNLSQLPpVQIVMDSLSKNGISFQVYDNVRVEPTDGSFMDAIEFAKKGAFDAY 86
Cdd:pfam13685 1 VIGPGALGRLGEYLAELGFRRVALVADANTYAAA-GRKVAESLKRAGIEVETRLEVAGNADMETAEKLVGALRERDADAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 87 VAVGGGSTMDTCKAA----NLYACS-PHSEFLDYVNAP----IGKGKPVTVPLKPLIAVpttsgtgsettgvaIFDyehl 157
Cdd:pfam13685 80 VGVGGGTVIDLAKYAafklGKPFISvPTAASNDGFASPgaslTVDGKKRSIPAAAPFGV--------------IAD---- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 158 kvkTGIASRAikptlglvdPLHTLHmpcqvvanSGF-DvlchALESYTAIPYSMRSpcpsnpiqrpayqGSNPISDIWAV 236
Cdd:pfam13685 142 ---TDVIAAA---------PRRLLA--------SGVgD----LLAKITAVADWELA-------------HAEEVAAPLAL 184
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1958777067 237 HALRIVAKYLKRAVRNPDDLEARSSMHLASAFAGIGFGNAGVHLCHGMS 285
Cdd:pfam13685 185 LSAAMVMNFADRPLRDPGDIEALAELLSALAMGGAGSSRPASGSEHLIS 233
|
|
| G1PDH-like |
cd08174 |
Glycerol-1-phosphate dehydrogenase-like; These glycerol-1-phosphate dehydrogenase-like ... |
4-101 |
1.50e-06 |
|
Glycerol-1-phosphate dehydrogenase-like; These glycerol-1-phosphate dehydrogenase-like proteins have not been characterized. The protein sequences have high similarity with that of glycerol-1-phosphate dehydrogenase (G1PDH) which plays a role in the synthesis of phosphoglycerolipids in Gram-positive bacterial species. It catalyzes the reversibly reduction of dihydroxyacetone phosphate (DHAP) to glycerol-1-phosphate (G1P) in a NADH-dependent manner. Its activity requires Ni++ ion.
Pssm-ID: 341453 [Multi-domain] Cd Length: 332 Bit Score: 49.83 E-value: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 4 SNIRYGAGVTKEVG--MDLQNMGAKNVCLMTDKNLSQLPpVQIVMDSLSKNGISFQVYDNvrvepTDGSFMDAIEFA-KK 80
Cdd:cd08174 2 LILKIEEGALEHLGkyLADRNQGFGKVAIVTGEGIDELL-GEDILESLEEAGEIVTVEEN-----TDNSAEELAEKAfSL 75
|
90 100
....*....|....*....|.
gi 1958777067 81 GAFDAYVAVGGGSTMDTCKAA 101
Cdd:cd08174 76 PKVDAIVGIGGGKVLDVAKYA 96
|
|
| GldA |
COG0371 |
Glycerol dehydrogenase or related enzyme, iron-containing ADH family [Energy production and ... |
4-101 |
3.67e-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: 48.62 E-value: 3.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 4 SNIRYGAGVTKEVGMDLQNMGaKNVCLMTDKNLSQLppVQ-IVMDSLSKNGISFQVYdNVRVEPTDGSFMDAIEFAKKGA 82
Cdd:COG0371 7 RRYVQGEGALDELGEYLADLG-KRALIITGPTALKA--AGdRLEESLEDAGIEVEVE-VFGGECSEEEIERLAEEAKEQG 82
|
90
....*....|....*....
gi 1958777067 83 FDAYVAVGGGSTMDTCKAA 101
Cdd:COG0371 83 ADVIIGVGGGKALDTAKAV 101
|
|
| GlyDH |
cd08170 |
Glycerol dehydrogenases (GlyDH) catalyzes oxidation of glycerol to dihydroxyacetone in ... |
7-108 |
3.42e-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: 45.48 E-value: 3.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 7 RY--GAGVTKEVGMDLQNMGaKNVCLMTDKNLsqLPPV-QIVMDSLSKNGISFQVYDnVRVEPTDGSFMDAIEFAKKGAF 83
Cdd:cd08170 3 RYvqGPGALDRLGEYLAPLG-KKALVIADPFV--LDLVgERLEESLEKAGLEVVFEV-FGGECSREEIERLAAIARANGA 78
|
90 100
....*....|....*....|....*
gi 1958777067 84 DAYVAVGGGSTMDTCKAANLYACSP 108
Cdd:cd08170 79 DVVIGIGGGKTIDTAKAVADYLGLP 103
|
|
| Gro1PDH |
cd08173 |
Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) catalyzes the reversible conversion between ... |
4-101 |
1.71e-04 |
|
Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) catalyzes the reversible conversion between dihydroxyacetone phosphate and glycerol-1-phosphate using either NADH or NADPH as a coenzyme; Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH, EC 1.1.1.261) plays an important role in the formation of the enantiomeric configuration of the glycerophosphate backbone (sn-glycerol-1-phosphate) of archaeal ether lipids. It catalyzes the reversible conversion between dihydroxyacetone phosphate and glycerol-1-phosphate using either NADH or NADPH as a coenzyme. The activity is zinc-dependent. One characteristic feature of archaea is that their cellular membrane has an ether linkage between the glycerol backbone and the hydrocarbon residues. The polar lipids of the members of Archaea consist of di- and tetra-ethers of glycerol with isoprenoid alcohols bound at the sn-2 and sn-3 positions of the glycerol moiety. The archaeal polar lipids have the enantiomeric configuration of a glycerophosphate backbone [sn-glycerol-1-phosphate (G-1-P)] that is the mirror image structure of the bacterial or eukaryal counterpart [sn-glycerol- 3-phosphate (G-3-P)]. The absolute stereochemistry of the glycerol moiety in all archaeal polar lipids is opposite to that of glycerol ester lipids in bacteria and eukarya.
Pssm-ID: 341452 Cd Length: 343 Bit Score: 43.31 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 4 SNIRYGAGVTKEVGMDLQNMG-AKNVCLMTDKNLSQLPpVQIVMDSLSKNGISFQVYDNVRVEpTDGSFMDAIEFAKKGA 82
Cdd:cd08173 3 RNVVVGHGAINKIGEVLKKLLlGKRALIITGPNTYKIA-GKRVEDLLESSGVEVVIVDIATIE-EAAEVEKVKKLIKESK 80
|
90
....*....|....*....
gi 1958777067 83 FDAYVAVGGGSTMDTCKAA 101
Cdd:cd08173 81 ADFIIGVGGGKVIDVAKYA 99
|
|
| Fe-ADH_KdnB-like |
cd08184 |
Iron-containing alcohol dehydrogenase similar to Shewanella oneidensis KdnB required for Kdo8N ... |
3-339 |
2.26e-04 |
|
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: 43.03 E-value: 2.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 3 VSNIRYGAGVTKEVGMDLQNMGAKN---VCLMTDKN------LSQLPPVQIvmDSLskngisfqVYDNVRVEPTDG---S 70
Cdd:cd08184 1 VPKYLFGRGSFDQLGELLAERRKSNndyVVFFIDDVfkgkplLDRLPLQNG--DLL--------IFVDTTDEPKTDqidA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 71 FMDAIEFAKKGAFDAYVAVGGGSTMDTCKA-ANLYACSPHSEflDYVNAPIGKGKPVtvplkPLIAVPTTSGTGSETTGV 149
Cdd:cd08184 71 LRAQIRAENDKLPAAVVGIGGGSTMDIAKAvSNMLTNPGSAA--DYQGWDLVKNPGI-----YKIGVPTLSGTGAEASRT 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 150 AIFDYEHLKVktGIASRAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTAipySMRspcpsnpiqrpayqgsNP 229
Cdd:cd08184 144 AVLTGPEKKL--GINSDYTVFDQVILDPELIATVPRDQYFYTGMDCYIHCVESLNG---TYR----------------NA 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 230 ISDIWAVHALRIVAK-YLKRAVRNPDDLEarsSMHLASAFAGIGFGNAGVHLCHGMSYPISGLVKTykakeynvdhplvP 308
Cdd:cd08184 203 FGDAYAEKALELCRDvFLSDDMMSPENRE---KLMVASYLGGSSIANSQVGVCHALSYGLSVVLGT-------------H 266
|
330 340 350
....*....|....*....|....*....|.
gi 1958777067 309 HGLSVVLtspaVFTFTAQMFPERHLETAEIL 339
Cdd:cd08184 267 HGVANCI----VFNVLEEFYPEGVKEFREML 293
|
|
| GlyDH-like |
cd08550 |
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins. ... |
7-101 |
7.06e-04 |
|
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: 41.37 E-value: 7.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777067 7 RY--GAGVTKEVGMDLQNMGaKNVCLMTDKN-LSQLppVQIVMDSLSKNGISFQVYDNvRVEPTDGSFMDAIEFAKKGAF 83
Cdd:cd08550 3 RYiqEPGILAKAGEYIAPLG-KKALIIGGKTaLEAV--GEKLEKSLEEAGIDYEVEVF-GGECTEENIERLAEKAKEEGA 78
|
90
....*....|....*...
gi 1958777067 84 DAYVAVGGGSTMDTCKAA 101
Cdd:cd08550 79 DVIIGIGGGKVLDTAKAV 96
|
|
| |
