|
Name |
Accession |
Description |
Interval |
E-value |
| HOT |
cd08190 |
Hydroxyacid-oxoacid transhydrogenase (HOT) involved in gamma-hydroxybutyrate metabolism; This ... |
1-394 |
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: 691.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 1 MGAKNVCLMTDKNLSQLPPVQIVMDSLSKNGISFQVYDDVRVEPTDGSFMDAIEFAKKGAFDAYVAVGGGSTMDTCKAAN 80
Cdd:cd08190 21 LGAKKVLVVTDPGLAKLGLVERVLESLEKAGIEVVVYDGVRVEPTDESFEEAIEFAKEGDFDAFVAVGGGSVIDTAKAAN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 81 LYASSPhSEFLDYVNAPIGKGKPVTVPLKPLIAVPTTSGTGSETTGVAIFDYEHLKVKTGIASRAIKPTLGLVDPLHTLH 160
Cdd:cd08190 101 LYATHP-GDFLDYVNAPIGKGKPVPGPLKPLIAIPTTAGTGSETTGVAIFDLEELKVKTGISSRYLRPTLAIVDPLLTLT 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 161 MPCQVVANSGFDVLCHALESYTAIPYSMRsPCPSNPIQRPAYQGSNPISDIWAVHALQIVAKYLKRAVRNPDDLEARSKM 240
Cdd:cd08190 180 LPPRVTASSGFDVLCHALESYTARPYNAR-PRPANPDERPAYQGSNPISDVWAEKAIELIGKYLRRAVNDGDDLEARSNM 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 241 HLASAFAGIGFGNAGVHLCHGMSYPISGLVKTYKAKEYNVDHPLVPHGLSVVLTSPAVFTFTAQMFPERHLETAGILGAN 320
Cdd:cd08190 259 LLASTLAGIGFGNAGVHLPHAMAYPIAGLVKDYRPPGYPVDHPHVPHGLSVALTAPAVFRFTAPACPERHLEAAELLGAD 338
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1270111384 321 IRTARIQDAGLVLADALRKFLFDLNVDDGLAALGYSKDDIPSLVKGTLPQERVTKLAPRAQSEEDLSALFEASM 394
Cdd:cd08190 339 TSGASDRDAGEVLADALIKLMRDIGIPNGLSALGYSEDDIPALVEGTLPQQRLLKLNPRPVTEEDLEEIFEDAL 412
|
|
| EutG |
COG1454 |
Alcohol dehydrogenase, class IV [Energy production and conversion]; |
1-394 |
1.43e-104 |
|
Alcohol dehydrogenase, class IV [Energy production and conversion];
Pssm-ID: 441063 [Multi-domain] Cd Length: 381 Bit Score: 313.59 E-value: 1.43e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 1 MGAKNVCLMTDKNLSQLPPVQIVMDSLSKNGISFQVYDDVRVEPTDGSFMDAIEFAKKGAFDAYVAVGGGSTMDTCKAAN 80
Cdd:COG1454 28 LGAKRALIVTDPGLAKLGLLDRVLDALEAAGIEVVVFDDVEPNPTVETVEAGAAAAREFGADVVIALGGGSAIDAAKAIA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 81 LYASSPHSeFLDYVNApigkgKPVTVPLKPLIAVP----------TtsgtgsettgVAIFDYEHLKVKTGIASRAIKPTL 150
Cdd:COG1454 108 LLATNPGD-LEDYLGI-----KKVPGPPLPLIAIPttagtgsevtP----------FAVITDPETGVKKGIADPELLPDV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 151 GLVDPLHTLHMPCQVVANSGFDVLCHALESYTAIpysmrspcpsnpiqrpayqGSNPISDIWAVHALQIVAKYLKRAVRN 230
Cdd:COG1454 172 AILDPELTLTLPPSLTAATGMDALTHAIEAYVSK-------------------GANPLTDALALEAIRLIARNLPRAVAD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 231 PDDLEARSKMHLASAFAGIGFGNAGVHLCHGMSYPISGLvktykakeYNvdhplVPHGLSVVLTSPAVFTFTAQMFPERH 310
Cdd:COG1454 233 GDDLEAREKMALASLLAGMAFANAGLGAVHALAHPLGGL--------FH-----VPHGLANAILLPHVLRFNAPAAPERY 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 311 LETAGILGANIrTARIQDAGLVLADALRKFLFDLNVDDGLAALGYSKDDIPSLVKGTLpQERVTKLAPRAQSEEDLSALF 390
Cdd:COG1454 300 AEIARALGLDV-GLSDEEAAEALIEAIRELLRDLGIPTRLSELGVTEEDLPELAELAL-ADRCLANNPRPLTEEDIEAIL 377
|
....
gi 1270111384 391 EASM 394
Cdd:COG1454 378 RAAY 381
|
|
| Fe-ADH |
cd08551 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains large ... |
1-390 |
8.79e-99 |
|
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: 298.59 E-value: 8.79e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 1 MGAKNVCLMTDKNLSQLPPVQIVMDSLSKNGISFQVYDDVRVEPTDGSFMDAIEFAKKGAFDAYVAVGGGSTMDTCKAAN 80
Cdd:cd08551 21 LGGKKVLLVTDPGLVKAGLLDKVLESLKAAGIEVEVFDDVEPNPTVETVEAAAELAREEGADLVIAVGGGSVLDTAKAIA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 81 LYASSPHSeFLDYVNapigkGKPVTVPLKPLIAVPTTSGTGSETTGVAIFDYEHLKVKTGIASRAIKPTLGLVDPLHTLH 160
Cdd:cd08551 101 VLATNGGS-IRDYEG-----IGKVPKPGLPLIAIPTTAGTGSEVTPNAVITDPETGRKMGIVSPYLLPDVAILDPELTLS 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 161 MPCQVVANSGFDVLCHALESYTAIPysmrspcpsnpiqrpayqgSNPISDIWAVHALQIVAKYLKRAVRNPDDLEARSKM 240
Cdd:cd08551 175 LPPSVTAATGMDALTHAIEAYTSKK-------------------ANPISDALALEAIRLIGKNLRRAVADGSDLEAREAM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 241 HLASAFAGIGFGNAGVHLCHGMSYPISGlvktykakEYNvdhplVPHGLSVVLTSPAVFTFTAQMFPERHLETAGILGAN 320
Cdd:cd08551 236 LLASLLAGIAFGNAGLGAVHALAYPLGG--------RYH-----IPHGVANAILLPYVMEFNLPACPEKYAEIAEALGED 302
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 321 IRTARIQDAGLVLADALRKFLFDLNVDDGLAALGYSKDDIPSLVKGTLPQERVTKLAPRAQSEEDLSALF 390
Cdd:cd08551 303 VEGLSDEEAAEAAVEAVRELLRDLGIPTSLSELGVTEEDIPELAEDAMKSGRLLSNNPRPLTEEDIREIY 372
|
|
| Fe-ADH |
pfam00465 |
Iron-containing alcohol dehydrogenase; |
4-386 |
4.26e-89 |
|
Iron-containing alcohol dehydrogenase;
Pssm-ID: 425696 [Multi-domain] Cd Length: 362 Bit Score: 273.32 E-value: 4.26e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 4 KNVCLMTDKNLSQLPPVQIVMDSLSKNGISFQVYDDVRVEPTDGSFMDAIEFAKKGAFDAYVAVGGGSTMDTCKAANLYA 83
Cdd:pfam00465 23 ARALIVTDPGSLKSGLLDKVLASLEEAGIEVVVFDGVEPEPTLEEVDEAAALAREAGADVIIAVGGGSVIDTAKAIALLL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 84 SSPHSEFLDYvnapigKGKPVTVPLKPLIAVPTTSGTGSETTGVAIFDYEHLKVKTGIASRAIKPTLGLVDPLHTLHMPC 163
Cdd:pfam00465 103 TNPGDVWDYL------GGKPLTKPALPLIAIPTTAGTGSEVTPLAVITDTETGEKLGIFSPKLLPDLAILDPELTLTLPP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 164 QVVANSGFDVLCHALESYTAipysmrspcpsnpiqrpayQGSNPISDIWAVHALQIVAKYLKRAVRNPDDLEARSKMHLA 243
Cdd:pfam00465 177 RLTAATGMDALAHAVEAYVS-------------------KGANPLTDALALEAIRLIAENLPRAVADGEDLEARENMLLA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 244 SAFAGIGFGNAGVHLCHGMSYPISGLVKtykakeynvdhplVPHGLSVVLTSPAVFTFTAQMFPERHLETAGILGANIRT 323
Cdd:pfam00465 238 STLAGLAFSNAGLGAAHALAHALGGRYG-------------IPHGLANAILLPYVLRFNAPAAPEKLAQLARALGEDSDE 304
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1270111384 324 ARIQDAglvlADALRKFLFDLNVDDGLAALGYSKDDIPSLVKGTLpQERVTKLAPRAQSEEDL 386
Cdd:pfam00465 305 EAAEEA----IEALRELLRELGLPTTLSELGVTEEDLDALAEAAL-RDRSLANNPRPLTAEDI 362
|
|
| Fe-ADH-like |
cd14863 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
1-392 |
4.23e-79 |
|
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: 248.22 E-value: 4.23e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 1 MGAKNVCLMTDKNLSQLPPVQIVMDSLSKNGISFQVYDDVRVEPTDGSFMDAIEFAKKGAFDAYVAVGGGSTMDTCKAAN 80
Cdd:cd14863 25 LGCKKVLLVTDKGLKKAGIVDKIIDLLEEAGIEVVVFDDVEPDPPDEIVDEAAEIAREEGADGVIGIGGGSVLDTAKAIA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 81 LYASSPHsEFLDYvnapIGKGKPVTVPLKPLIAVPTTSGTGSETTGVAIFDYEHLKVKTGIASRAIKPTLGLVDPLHTLH 160
Cdd:cd14863 105 VLLTNPG-PIIDY----ALAGPPVPKPGIPLIAIPTTAGTGSEVTPIAVITDEENGVKKSLLGPFLVPDLAILDPELTVG 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 161 MPCQVVANSGFDVLCHALESYTAipysmrspcpsnpiqrpayQGSNPISDIWAVHALQIVAKYLKRAVRNPDDLEARSKM 240
Cdd:cd14863 180 LPPSLTAATGMDALSHAIEAYTS-------------------KLANPMTDALALQAIRLIVKNLPRAVKDGDNLEARENM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 241 HLASAFAGIGFGNAGVHLCHGMSYPISGLvktykakeYNvdhplVPHGLSVVLTSPAVFTFTAQMFPERHLETAGILGAN 320
Cdd:cd14863 241 LLASNLAGIAFNNAGTHIGHAIAHALGAL--------YH-----IPHGLACALALPVVLEFNAEAYPEKVKKIAKALGVS 307
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1270111384 321 IRTARIQDAGLVLADALRKFLFDLNVDDGLAALGYSKDDIPSLVKGTLpQERVTKLAPRAQSEEDLSALFEA 392
Cdd:cd14863 308 FPGESDEELGEAVADAIREFMKELGIPSLFEDYGIDKEDLDKIAEAVL-KDPFAMFNPRPITEEEVAEILEA 378
|
|
| Fe-ADH-like |
cd08185 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
23-391 |
4.47e-75 |
|
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol dehydrogenase-like (ADH) proteins. Alcohol dehydrogenase catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase fold and is a member of the iron-containing alcohol dehydrogenase-like family. They are distinct from other alcohol dehydrogenases which contain different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341464 [Multi-domain] Cd Length: 379 Bit Score: 237.78 E-value: 4.47e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 23 VMDSLSKNGISFQVYDDVRVEPTDGSFMDAIEFAKKGAFDAYVAVGGGSTMDTCKAANLYASSPHSEFlDYVNAPIGKGK 102
Cdd:cd08185 46 VKKLLEKAGVEVVVFDKVEPNPLTTTVMEGAALAKEEGCDFVIGLGGGSSMDAAKAIAFMATNPGDIW-DYIFGGTGKGP 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 103 PVTVPLkPLIAVPTTSGTGSETTGVAIFDYEHLKVKTGIASRAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYT 182
Cdd:cd08185 125 PPEKAL-PIIAIPTTAGTGSEVDPWAVITNPETKEKKGIGHPALFPKVSIVDPELMLTVPPRVTAYTGFDALFHAFESYI 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 183 AIpysmrspcpsnpiqrpayqGSNPISDIWAVHALQIVAKYLKRAVRNPDDLEARSKMHLASAFAGIGFGNAGVHLCHGM 262
Cdd:cd08185 204 SK-------------------NANPFSDMLALEAIRLVAKYLPRAVKDGSDLEAREKMAWASTLAGIVIANSGTTLPHGL 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 263 SYPISGLvktykakeynvdHPLVPHGLSVVLTSPAVFTFTAQMFPERhleTAGILGANIRTARIQDAGLVLADALRKFLF 342
Cdd:cd08185 265 EHPLSGY------------HPNIPHGAGLAALYPAYFEFTIEKAPEK---FAFVARAEASGLSDAKAAEDFIEALRKLLK 329
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1270111384 343 DLNVDDGLAALGYSKDDIPSLVkgtlpqERVTKLA-------PRAQSEEDLSALFE 391
Cdd:cd08185 330 DIGLDDLLSDLGVTEEDIPWLA------ENAMETMgglfannPVELTEEDIVEIYE 379
|
|
| Fe-ADH-like |
cd08191 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
6-394 |
1.10e-72 |
|
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: 232.12 E-value: 1.10e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 6 VCLMTDKNLSQLPPVQIVMDSLSKNGISFQVYDDVRVEPTDGSFMDAIEFAKKGAFDAYVAVGGGSTMDTCKAANLYASS 85
Cdd:cd08191 28 VLIVTDPRLASTPLVAELLAALTAAGVAVEVFDGGQPELPVSTVADAAAAARAFDPDVVIGLGGGSNMDLAKVVALLLAH 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 86 PhSEFLDYvnapIGKGKpVTVPLKPLIAVPTTSGTGSETTGVAIFDYEHLKVKTGIASRAIKPTLGLVDPLHTLHMPCQV 165
Cdd:cd08191 108 G-GDPRDY----YGEDR-VPGPVLPLIAVPTTAGTGSEVTPVAVLTDPARGMKVGVSSPYLRPAVAIVDPELTLTCPPGV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 166 VANSGFDVLCHALESYTAIPysmRSPCPSNPiQRPAYQGSNPISDIWAVHALQIVAKYLKRAVRNPDDLEARSKMHLASA 245
Cdd:cd08191 182 TADSGIDALTHAIESYTARD---FPPFPRLD-PDPVYVGKNPLTDLLALEAIRLIGRHLPRAVRDGDDLEARSGMALAAL 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 246 FAGIGFGNAGVHLCHGMSYPISGLVKTykakeynvdhplvPHGLSVVLTSPAVFTFTAQMFPERHLETAGILGANiRTAR 325
Cdd:cd08191 258 LAGLAFGTAGTAAAHALQYPIGALTHT-------------SHGVGNGLLLPYVMRFNRPARAAELAEIARALGVT-TAGT 323
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1270111384 326 IQDAGLVLADALRKFLFDLNVDDGLAALGYSKDDIPSLVKGTLPQERVTKLAPRAQSEEDLSALFEASM 394
Cdd:cd08191 324 SEEAADRAIERVEELLARIGIPTTLADLGVTEADLPGLAEKALSVTRLIANNPRPPTEEDLLRILRAAF 392
|
|
| Fe-ADH-like |
cd08196 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
1-390 |
2.26e-69 |
|
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: 222.84 E-value: 2.26e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 1 MGAKNVCLMTDKNLSQLPPVQIVMDSLSKNGISfqVYDDVRVEPTDGSFMDAIEFAKKGAFDAYVAVGGGSTMDTCKAAN 80
Cdd:cd08196 26 LGGKRGLLVTDPSFIKSGLAKRIVESLKGRIVA--VFSDVEPNPTVENVDKCARLARENGADFVIAIGGGSVLDTAKAAA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 81 LYASSPHSeFLDYvnapIGKGKPVTVPLKPLIAVPTTSGTGSETTGVAIFDYEHLKVKTGIASRAIKPTLGLVDPLHTLH 160
Cdd:cd08196 104 CLAKTDGS-IEDY----LEGKKKIPKKGLPLIAIPTTAGTGSEVTPVAVLTDKEKGKKAPLVSPGFYPDIAIVDPELTYS 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 161 MPCQVVANSGFDVLCHALESYTAIpysmrspcpsnpiqrpayqGSNPISDIWAVHALQIVAKYLKRAVRNPDDLEARSKM 240
Cdd:cd08196 179 MPPKVTASTGIDALCHAIEAYWSI-------------------NHQPISDALALEAAKLVLENLEKAYNNPNDKEAREKM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 241 HLASAFAGIGFGNAGVHLCHGMSYPISglvktykaKEYNvdhplVPHGLSVVLTSPAVFTFTAQMFPERHLETAGILGAN 320
Cdd:cd08196 240 ALASLLAGLAFSQTRTTASHACSYPLT--------SHFG-----IPHGEACALTLPSFIRLNAEALPGRLDELAKQLGFK 306
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 321 irtariqDAGLvLADALRKFLFDLNVDDGLAALGYSKDDIPSLVKGTLPQERVtKLAPRAQSEEDLSALF 390
Cdd:cd08196 307 -------DAEE-LADKIEELKKRIGLRTRLSELGITEEDLEEIVEESFHPNRA-NNNPVEVTKEDLEKLL 367
|
|
| Fe-ADH-like |
cd08194 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
1-392 |
3.56e-67 |
|
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: 217.40 E-value: 3.56e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 1 MGAKNVCLMTDKNLSQLPPVQIVMDSLSKNGISFQVYDDVRVEPTDGSFMDAIEFAKKGAFDAYVAVGGGSTMDTCKAAN 80
Cdd:cd08194 21 LGGKRALIVTDKVMVKLGLVDKVTQLLAEAGIAYAVFDDVVSEPTDEMVEEGLALYKEGGCDFIVALGGGSPIDTAKAIA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 81 LYASSPhSEFLDYVNAPIGKGKPVtvplkPLIAVPTTSGTGSETTGVAIFDYEHLKVKTGIASRAIKPTLGLVDPLHTLH 160
Cdd:cd08194 101 VLATNG-GPIRDYMGPRKVDKPGL-----PLIAIPTTAGTGSEVTRFTVITDTETDVKMLLKGPALLPAVAIVDPELTLS 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 161 MPCQVVANSGFDVLCHALESYTaipySMRspcpsnpiqrpayqgSNPISDIWAVHALQIVAKYLKRAVRNPDDLEARSKM 240
Cdd:cd08194 175 MPPRVTAATGIDALTHAIEAYV----SRK---------------AQPLTDTLALSAIKLIGRNLRRAYADGDDLEAREAM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 241 HLASAFAGIGFGNAGVHLCHGMSYPISGLVktykakeynvdHplVPHGLSVVLTSPAVFTFTAQMFPERHLETAGILGAN 320
Cdd:cd08194 236 MLAALEAGIAFSNSSVALVHGMSRPIGALF-----------H--VPHGLSNAMLLPAVTEFSLPGAPERYAEIARAMGIA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 321 IRTARIQDAGLVLADALRKFLFDLNVdDGLAALGYSKDD----IPSLVKGTL----PQervtkLAPRAQSEEDLSALFEA 392
Cdd:cd08194 303 TEGDSDEEAAEKLVEALERLCADLEI-PTLREYGIDEEEfeaaLDKMAEDALasgsPA-----NNPRVPTKEEIIELYRE 376
|
|
| Fe-ADH-like |
cd17814 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
1-368 |
1.38e-65 |
|
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: 213.17 E-value: 1.38e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 1 MGAKNVCLMTDKNLSQLPPVQIVMDSLSKNGISFQVYDDVRVEPTDGSFMDAIE-FAKKGAfDAYVAVGGGSTMDTCKAA 79
Cdd:cd17814 24 LGARKVLVVTDPGVIKAGWVDEVLDSLEAEGLEYVVFSDVTPNPRDFEVMEGAElYREEGC-DGIVAVGGGSPIDCAKGI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 80 NLYASSpHSEFLDYvnapIGKGKpVTVPLKPLIAVPTTSGTGSETTGVAIFDYEHLKVKTGIASRAIKPTLGLVDPLHTL 159
Cdd:cd17814 103 GIVVSN-GGHILDY----EGVDK-VRRPLPPLICIPTTAGSSADVSQFAIITDTERRVKMAIISKTLVPDVSLIDPETLT 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 160 HMPCQVVANSGFDVLCHALESYTaipysmrspcpSNpiqrpayqGSNPISDIWAVHALQIVAKYLKRAVRNPDDLEARSK 239
Cdd:cd17814 177 TMDPELTACTGMDALTHAIEAYV-----------SN--------ASSPLTDLHALEAIRLISENLPKAVADPDDLEAREK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 240 MHLASAFAGIGFGNAGVHLCHGMSYPISGLvktykakeynVDhplVPHGLSVVLTSPAVFTFTAQMFPERHLETAGILGA 319
Cdd:cd17814 238 MMLASLQAGLAFSNASLGAVHAMAHSLGGL----------LD---LPHGECNALLLPHVIRFNFPAAPERYRKIAEAMGL 304
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1270111384 320 NIRTARIQDAGLVLADALRKFLFDLNVDDGLAALGYSKDDIPSLVKGTL 368
Cdd:cd17814 305 DVDGLDDEEVAERLIEAIRDLREDLGIPETLSELGVDEEDIPELAKRAM 353
|
|
| LPO |
cd08176 |
Lactadehyde:propanediol oxidoreductase (LPO) catalyzes the interconversion between ... |
1-391 |
2.68e-62 |
|
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: 204.70 E-value: 2.68e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 1 MGAKNVCLMTDKNLSQLPPVQIVMDSLSKNGISFQVYDDVRVEPTDGSFMDAIEFAKKGAFDAYVAVGGGSTMDTCKAAN 80
Cdd:cd08176 26 RGFKKALIVTDKGLVKFGIVDKVTDVLKEAGIAYTVFDEVKPNPTIENVMAGVAAYKESGADGIIAVGGGSSIDTAKAIG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 81 LYASSPhseFLDyVNAPIGKgKPVTVPLKPLIAVPTTSGTGSETTGVA-IFDYEHlKVKTGIASRAIKPTLGLVDPLHTL 159
Cdd:cd08176 106 IIVANP---GAD-VRSLEGV-APTKNPAVPIIAVPTTAGTGSEVTINYvITDTEK-KRKFVCVDPHDIPTVAIVDPDLMS 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 160 HMPCQVVANSGFDVLCHALESYTAipysmrspcpsnpiqrpayQGSNPISDIWAVHALQIVAKYLKRAVRNPDDLEARSK 239
Cdd:cd08176 180 SMPKGLTAATGMDALTHAIEGYIT-------------------KGAWELSDMLALKAIELIAKNLRKAVANPNNVEAREN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 240 MHLASAFAGIGFGNAGVHLCHGMSYPISGLvktykakeYNvdhplVPHGLSVVLTSPAVFTFTAQMFPERHLETAGILGA 319
Cdd:cd08176 241 MALAQYIAGMAFSNVGLGIVHSMAHPLSAF--------YD-----TPHGVANAILLPYVMEFNAPATGEKYRDIARAMGV 307
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1270111384 320 NIRTARIQDAGLVLADALRKFLFDLNVDDGLAALGYSKDDIPSLVKGTLpQERVTKLAPRAQSEEDLSALFE 391
Cdd:cd08176 308 DTTGMSDEEAAEAAVDAVKKLSKDVGIPQKLSELGVKEEDIEALAEDAL-NDVCTPGNPREATKEDIIALYK 378
|
|
| Fe-ADH-like |
cd14862 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
1-390 |
2.58e-61 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341484 [Multi-domain] Cd Length: 375 Bit Score: 202.07 E-value: 2.58e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 1 MGAKNVCLMTDKNLSQLPPVQIVMDSLSKNGISFQVYDDVRVEPTDGSFMDAIEFAKKGAFDAYVAVGGGSTMDTCKAAN 80
Cdd:cd14862 22 LSGKRALIVTDKVLVKLGLLKKVLKRLLQAGFEVEVFDEVEPEPPLETVLKGAEAMREFEPDLIIALGGGSVMDAAKAAW 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 81 LYASSPHSEFLDYV-NAPIGKGKpvtvplKP-LIAVPTTSGTGSETTGVAIFDYEHLKVKTGIASRAIKPTLGLVDPLHT 158
Cdd:cd14862 102 VLYERPDLDPEDISpLDLLGLRK------KAkLIAIPTTSGTGSEATWAIVLTDTEEPRKIAVANPELVPDVAILDPEFV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 159 LHMPCQVVANSGFDVLCHALESYTAipysmrspcpsnpiqrpayQGSNPISDIWAVHALQIVAKYLKRAVRNPDDLEARS 238
Cdd:cd14862 176 LGMPPKLTAGTGLDALAHAVEAYLS-------------------TWSNDFSDALALKAIELIFKYLPRAYKDGDDLEARE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 239 KMHLASAFAGIGFGNAGVHLCHGMSYPISGLVKtykakeynvdhplVPHGLSVVLTSPAVFTFTAQmFPERHLETAGILG 318
Cdd:cd14862 237 KMHNAATIAGLAFGNSQAGLAHALGHSLGAVFH-------------VPHGIAVGLFLPYVIEFYAK-VTDERYDLLKLLG 302
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1270111384 319 ANIRTAriQDAGLVLADALRKFLFDLNVDDGLAALGYSKDD----IPSLVKGTLpQERVTKLAPRAQSEEDLSALF 390
Cdd:cd14862 303 IEARDE--EEALKKLVEAIRELYKEVGQPLSIKDLGISEEEfeekLDELVEYAM-EDSCTITSPRPPSEEDLKKLF 375
|
|
| PDDH |
cd08188 |
1,3-Propanediol (1,3-PD) dehydrogenase; This family includes 1,3-propanediol (1,3-PD) ... |
1-391 |
1.95e-57 |
|
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: 191.96 E-value: 1.95e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 1 MGAKNVCLMTDKNLSQLPPVQIVMDSLSKNGISFQVYDDVRVEPTDGSFMDAIEFAKKGAFDAYVAVGGGSTMDTCKAAN 80
Cdd:cd08188 26 LGGKKALIVTDKGLVKLGLVKKVTDVLEEAGIEYVIFDGVQPNPTVTNVNEGLELFKENGCDFIISVGGGSAHDCAKAIG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 81 LYASSPhSEFLDYVNapIGKgkpVTVPLKPLIAVPTTSGTGSETTGVAIFDYEHLKVKTGIASRAIKPTLGLVDPLHTLH 160
Cdd:cd08188 106 ILATNG-GEIEDYEG--VDK---SKKPGLPLIAINTTAGTASEVTRFAVITDEERHVKMVIVDWNVTPTIAVNDPELMLG 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 161 MPCQVVANSGFDVLCHALESYTAIpysmrspcpsnpiqrpayqGSNPISDIWAVHALQIVAKYLKRAVRNPDDLEARSKM 240
Cdd:cd08188 180 MPPSLTAATGMDALTHAIEAYVST-------------------GATPLTDALALEAIRLIAENLPKAVANGKDLEARENM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 241 HLASAFAGIGFGNAGVHLCHGMSYPISGLvktykakeYNvdhplVPHGL--SVVLtsPAVFTFTAQMFPERHLETAGILG 318
Cdd:cd08188 241 AYAQFLAGMAFNNAGLGYVHAMAHQLGGF--------YN-----LPHGVcnAILL--PHVMEFNLPACPERFADIARALG 305
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1270111384 319 ANIRTARIQDAGLVLADALRKFLFDLNVDDGLAALGYSKDDIPSLVKGTLpQERVTKLAPRAQSEEDLSALFE 391
Cdd:cd08188 306 ENTEGLSDEEAAEAAIEAIRKLSRRVGIPSGLKELGVKEEDFPLLAENAL-KDACGPTNPRQATKEDVIAIYR 377
|
|
| Fe-ADH-like |
cd14865 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
1-394 |
3.48e-57 |
|
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: 191.60 E-value: 3.48e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 1 MGAKNVCLMTDKNLSQLPPVQIVMDSLSKNGISFQVYDDVrvePTDGSF---MDAIEFAKKGAFDAYVAVGGGSTMDTCK 77
Cdd:cd14865 26 LGARRPLIVTDKGLAAAGLLKKVEDALGDAIEIVGVFDDV---PPDSSVavvNEAAARAREAGADGIIAVGGGSVIDTAK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 78 AANLYASSPHSEFLDYVNAPIgkgkpVTVPLKPLIAVPTTSGTGSETTGVAIFDYEHLKVKTGIASRAIKPTLGLVDPLH 157
Cdd:cd14865 103 GVNILLSEGGDDLDDYGGANR-----LTRPLKPLIAIPTTAGTGSEVTLVAVIKDEEKKVKLLFVSPFLLPDVAILDPRL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 158 TLHMPCQVVANSGFDVLCHALESYTAIpysmrspcpsnpiqrpayqGSNPISDIWAVHALQIVAKYLKRAVRNPDDLEAR 237
Cdd:cd14865 178 TLSLPPKLTAATGMDALTHAIEAYTSL-------------------QKNPISDALALQAIRLISENLPKAVKNGKDLEAR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 238 SKMHLASAFAGIGFGNAGVHLCHGMSYPISGLVKtykakeynvdhplVPHGL--SVVLtsPAVFTFTAQMFPERHLETAG 315
Cdd:cd14865 239 LALAIAATMAGIAFSNSMVGLVHAIAHAVGAVAG-------------VPHGLanSILL--PHVMRYNLDAAAERYAELAL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 316 IL--GANIRTARIQDAGLVLADALRKFLFDLNVDDGLAALGYSKDDIPSLVKGTLpQERVTKLAPRAQSEEDLSALFEAS 393
Cdd:cd14865 304 ALayGVTPAGRRAEEAIEAAIDLVRRLHELCGLPTRLRDVGVPEEQLEAIAELAL-NDGAILFNPREVDPEDILAILEAA 382
|
.
gi 1270111384 394 M 394
Cdd:cd14865 383 Y 383
|
|
| HVD |
cd08193 |
5-hydroxyvalerate dehydrogenase (HVD) catalyzes the oxidation of 5-hydroxyvalerate to ... |
1-392 |
3.75e-53 |
|
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: 180.79 E-value: 3.75e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 1 MGAKNVCLMTDKNLSQLPPVQIVMDSLSKNGISFQVYDDVRVEPTDGSFMDAIEFAKKGAFDAYVAVGGGSTMDTCKAAN 80
Cdd:cd08193 24 LGARRVLLVTDPGLVKAGLADPALAALEAAGIAVTVFDDVVADPPEAVVEAAVEQAREAGADGVIGFGGGSSMDVAKLVA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 81 LYASSPHSefldyVNAPIGKGKpVTVPLKPLIAVPTTSGTGSETTGVAIF-DYEHlkVKTGIASRAIKPTLGLVDPLHTL 159
Cdd:cd08193 104 LLAGSDQP-----LDDIYGVGK-ATGPRLPLILVPTTAGTGSEVTPISIVtTGET--EKKGVVSPQLLPDVALLDAELTL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 160 HMPCQVVANSGFDVLCHALESYTAipysmRSpcpsnpiqrpayqGSNPISDIWAVHALQIVAKYLKRAVRNPDDLEARSK 239
Cdd:cd08193 176 GLPPHVTAATGIDAMVHAIEAYTS-----RH-------------KKNPISDALAREALRLLGANLRRAVEDGSDLEAREA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 240 MHLASAFAGIGFGNAGVHLCHGMSYPISGLVKtykakeynvdhplVPHGLSVVLTSPAVFTFTAQMFPERHLETAGILGA 319
Cdd:cd08193 238 MLLGSMLAGQAFANAPVAAVHALAYPLGGHFH-------------VPHGLSNALVLPHVLRFNLPAAEALYAELARALLP 304
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1270111384 320 NIRTARIQDAGLVLADALRKFLFDLNVDDGLAALGYSKDDIPSLVKGTLPQERVTKLAPRAQSEEDLSALFEA 392
Cdd:cd08193 305 GLAFGSDAAAAEAFIDALEELVEASGLPTRLRDVGVTEEDLPMLAEDAMKQTRLLVNNPREVTEEDALAIYQA 377
|
|
| Fe-ADH-like |
cd08183 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
3-391 |
7.59e-52 |
|
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: 177.31 E-value: 7.59e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 3 AKNVCLMTDKNLSQLPPVQIVMDSLSKNGISFQVYDDVRvEPTDGSFMDAIEFAKKGAFDAYVAVGGGSTMDTCKAANLY 82
Cdd:cd08183 22 GKRALLVTGRSSLRSGRLARLLEALEAAGIEVALFSVSG-EPTVETVDAAVALAREAGCDVVIAIGGGSVIDAAKAIAAL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 83 ASSPHS--EFLDYVnapiGKGKPVTVPLKPLIAVPTtsgtgsettgVA-----------IFDYEHlKVKTGIASRAIKPT 149
Cdd:cd08183 101 LTNEGSvlDYLEVV----GKGRPLTEPPLPFIAIPT----------TAgtgsevtknavLSSPEH-GVKVSLRSPSMLPD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 150 LGLVDPLHTLHMPCQVVANSGFDVLCHALESYTAIpysmrspcpsnpiqrpayqGSNPISDIWAVHALQIVAKYLKRAVR 229
Cdd:cd08183 166 VALVDPELTLSLPPEVTAASGLDALTQLIEPYVSR-------------------KANPLTDALAREGLRLAARSLRRAYE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 230 NPDDLEARSKMHLASAFAGIGFGNAGVHLCHGMSYPISGLVKtykakeynvdhplVPHGL--SVVLtsPAVFTFTAQM-- 305
Cdd:cd08183 227 DGEDLEAREDMALASLLGGLALANAGLGAVHGLAGPLGGMFG-------------APHGAicAALL--PPVLEANLRAlr 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 306 --FPERHLETAGILGANIRTARIQDAGLVLADALRKFLFDLNVdDGLAALGYSKDDIPSLVKGTLpQERVTKLAPRAQSE 383
Cdd:cd08183 292 erEPDSPALARYRELAGILTGDPDAAAEDGVEWLEELCEELGI-PRLSEYGLTEEDFPEIVEKAR-GSSSMKGNPIELSD 369
|
....*...
gi 1270111384 384 EDLSALFE 391
Cdd:cd08183 370 EELLEILE 377
|
|
| Fe-ADH-like |
cd14861 |
Iron-containing alcohol dehydrogenases-like; This family contains proteins similar to ... |
1-394 |
2.12e-51 |
|
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: 176.16 E-value: 2.12e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 1 MGAKNVCLMTDKNLSQLPPVQIVMDSLSKNGISFQVYDDVRVEPTDGSFMDAIEFAKKGAFDAYVAVGGGSTMDTCKAAN 80
Cdd:cd14861 23 LGIRRPLLVTDPGLAALGIVDRVLEALGAAGLSPAVFSDVPPNPTEADVEAGVAAYREGGCDGIIALGGGSAIDAAKAIA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 81 LYASSPHSEFlDYVNAPIGkGKPVTVPLKPLIAVPTTSGTGSETTGVAIFDYEHLKVKTGIASRAIKPTLGLVDPLHTLH 160
Cdd:cd14861 103 LMATHPGPLW-DYEDGEGG-PAAITPAVPPLIAIPTTAGTGSEVGRAAVITDDDTGRKKIIFSPKLLPKVAICDPELTLG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 161 MPCQVVANSGFDVLCHALESYTAIPYsmrspcpsnpiqrpayqgsNPISDIWAVHALQIVAKYLKRAVRNPDDLEARSKM 240
Cdd:cd14861 181 LPPRLTAATGMDALTHCIEAYLSPGF-------------------HPMADGIALEGLRLISEWLPRAVADGSDLEARGEM 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 241 HLASAFAGIGFGNaGVHLCHGMSYPISGLVKTykakeynvdhplvPHGLSVVLTSPAVFTFTAQMFPERHLETAGILGAN 320
Cdd:cd14861 242 MMAALMGAVAFQK-GLGAVHALAHALGALYGL-------------HHGLLNAILLPYVLRFNRPAVEDKLARLARALGLG 307
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1270111384 321 IRTAriqDAglvLADALRKFLFDLNVDDGLAALGYSKDDIPSLVKGTLpQERVTKLAPRAQSEEDLSALFEASM 394
Cdd:cd14861 308 LGGF---DD---FIAWVEDLNERLGLPATLSELGVTEDDLDELAELAL-ADPCHATNPRPVTAEDYRALLREAL 374
|
|
| NADPH_BDH |
cd08179 |
NADPH-dependent butanol dehydrogenase involved in the butanol and ethanol formation pathway in ... |
23-392 |
1.86e-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: 173.92 E-value: 1.86e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 23 VMDSLSKNGISFQVYDDVRVEPTDGSFMDAIEFAKKGAFDAYVAVGGGSTMDTCKAANLYASSPHSEFLDYVnapigkgK 102
Cdd:cd08179 44 VEDYLKEAGMEVKVFEGVEPDPSVETVEKGAEAMREFEPDWIIAIGGGSVIDAAKAMWVFYEYPELTFEDAL-------V 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 103 PVTVPLKP----LIAVPTTSGTGSETTGVAIF-DYEHlKVKTGIASRAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHA 177
Cdd:cd08179 117 PFPLPELRkkarFIAIPSTSGTGSEVTRASVItDTEK-GIKYPLASFEITPDVAILDPELTMTMPPHVTANTGMDALTHA 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 178 LESYTAIPysmrspcpsnpiqrpayqgSNPISDIWAVHALQIVAKYLKRAVRNPDDLEARSKMHLASAFAGIGFGNAGVH 257
Cdd:cd08179 196 IEAYVSTL-------------------ANDFTDALALGAILDIFENLPKSYNGGKDLEAREKMHNASCLAGMAFSNSGLG 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 258 LCHGMSYPISGlvktykakEYNvdhplVPHGL--SVVLtsPAVFTFTAQMFPERHLETAGILGANirtariqdaGLVLAD 335
Cdd:cd08179 257 IVHSMAHKGGA--------FFG-----IPHGLanAILL--PYVIEFNSKDPEARARYAALLIGLT---------DEELVE 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1270111384 336 ALRKFLFDLN----VDDGLAALGYSKDD----IPSLVKGTLpQERVTKLAPRAQSEEDLSALFEA 392
Cdd:cd08179 313 DLIEAIEELNkklgIPLSFKEAGIDEDEffakLDEMAENAM-NDACTGTNPRKPTVEEMKELLKA 376
|
|
| HEPD |
cd08182 |
Hydroxyethylphosphoate dehydrogenase (HEPD) catalyzes the reduction of phosphonoacetaldehyde ... |
1-391 |
6.00e-48 |
|
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: 167.02 E-value: 6.00e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 1 MGAKNVCLMTDKNLSQLPPVQIVMDSLsKNGISFQVYDDVRVEPTDGSFMDAIEFAKKGAFDAYVAVGGGSTMDTCKAAN 80
Cdd:cd08182 21 LGARRVLLVTGPSAVRESGAADILDAL-GGRIPVVVFSDFSPNPDLEDLERGIELFRESGPDVIIAVGGGSVIDTAKAIA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 81 LYASSPHSEFLdyvnAPIGKGKPVTVPLKPLIAVPTtsgtgsettgVA-----------IFDyEHLKVKTGIASRAIKPT 149
Cdd:cd08182 100 ALLGSPGENLL----LLRTGEKAPEENALPLIAIPT----------TAgtgsevtpfatIWD-EAEGKKYSLAHPSLYPD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 150 LGLVDPLHTLHMPCQVVANSGFDVLCHALESYTAIpysmrspcpsnpiqrpayqGSNPISDIWAVHALQIVAKYLKRAVR 229
Cdd:cd08182 165 AAILDPELTLSLPLYLTASTGLDALSHAIESIWSV-------------------NANPESRAYALRAIRLILENLPLLLE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 230 NPDDLEARSKMHLASAFAGIGFGNAGVHLCHGMSYPISglvktykaKEYNvdhplVPHGLSVVLTSPAVFTFTAQMFPER 309
Cdd:cd08182 226 NLPNLEAREAMAEASLLAGLAISITKTTAAHAISYPLT--------SRYG-----VPHGHACALTLPAVLRYNAGADDEC 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 310 HletagilgANIRTARIQDAGLV-----LADALRKFLFDLNVDDGLAALGYSKDDIPSLVKGTLPQERVtKLAPRAQSEE 384
Cdd:cd08182 293 D--------DDPRGREILLALGAsdpaeAAERLRALLESLGLPTRLSEYGVTAEDLEALAASVNTPERL-KNNPVRLSEE 363
|
....*..
gi 1270111384 385 DLSALFE 391
Cdd:cd08182 364 DLLRLLE 370
|
|
| PDD |
cd08180 |
1,3-propanediol dehydrogenase (PPD) catalyzes the reduction of 3-hydroxypropionaldehyde (3-HPA) ... |
1-391 |
7.98e-46 |
|
1,3-propanediol dehydrogenase (PPD) catalyzes the reduction of 3-hydroxypropionaldehyde (3-HPA) to 1,3-propanediol in glycerol metabolism; 1,3-propanediol dehydrogenase (PPD) plays a role in glycerol metabolism of some bacteria in anaerobic conditions. In this degradation pathway, glycerol is converted in a two-step process to 1,3-propanediol (1,3-PD) which is then excreted into the extracellular medium. The first reaction involves the transformation of glycerol into 3-hydroxypropionaldehyde (3-HPA) by a coenzyme B-12-dependent dehydratase. The second reaction involves the dismutation of the 3-hydroxypropionaldehyde (3-HPA) to 1,3-propanediol by the NADH-linked 1,3-propanediol dehydrogenase (PPD). The enzyme requires iron ion for its function. Because many genes in this pathway are present in the propanediol utilization (pdu) operon, they are also named pdu genes. PPD is a member of the iron-containing alcohol dehydrogenase superfamily. The PPD structure has a dehydroquinate synthase-like fold.
Pssm-ID: 341459 [Multi-domain] Cd Length: 333 Bit Score: 160.35 E-value: 7.98e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 1 MGAKNVCLMTDKNLSQLPPVQIVMDSLSKNgISFQVYDDVRVEPTDGSFMDAIEFAKKGAFDAYVAVGGGSTMDTCKAAN 80
Cdd:cd08180 20 LKGKRVFIVTDPFMVKSGMVDKVTDELDKS-NEVEIFSDVVPDPSIEVVAKGLAKILEFKPDTIIALGGGSAIDAAKAII 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 81 LYassphsefldYVNAPIGKGKPvtvplkPLIAVPTTSGTGSETTGVA-IFDYEHlKVKTGIASRAIKPTLGLVDPLHTL 159
Cdd:cd08180 99 YF----------ALKQKGNIKKP------LFIAIPTTSGTGSEVTSFAvITDPEK-GIKYPLVDDSMLPDIAILDPELVK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 160 HMPCQVVANSGFDVLCHALESYTAIpysmrspcpsnpiqrpayqGSNPISDIWAVHALQIVAKYLKRAVRNPDDLEARSK 239
Cdd:cd08180 162 SVPPKVTADTGMDVLTHALEAYVST-------------------NANDFTDALAEKAIKLVFENLPRAYRDGDDLEAREK 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 240 MHLASAFAGIGFGNAGVHLCHGMSYPISGLVKtykakeynvdhplVPHGLSVVLTSPAVFTFtaqmfperhletagilga 319
Cdd:cd08180 223 MHNASCMAGIAFNNAGLGINHSLAHALGGRFH-------------IPHGRANAILLPYVIEF------------------ 271
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1270111384 320 nirtariqdaglvLADALRKFLFDLNVDDGLAALGYSKDD----IPSLVKGTLpQERVTKLAPRAQSEEDLSALFE 391
Cdd:cd08180 272 -------------LIAAIRRLNKKLGIPSTLKELGIDEEEfekaIDEMAEAAL-ADRCTATNPRKPTAEDLIELLR 333
|
|
| PPD-like |
cd08181 |
1,3-propanediol dehydrogenase-like (PPD); This family contains proteins similar to 1, ... |
21-391 |
3.71e-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: 153.90 E-value: 3.71e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 21 QIVMDSLSKNGISFQVYDDVRVEPTDGSFMDAIEFAKKGAFDAYVAVGGGSTMDTCKAANLYASSP-HSEFLDYVNAPig 99
Cdd:cd08181 44 DDVTEALEENGIEYFIFDEVEENPSIETVEKGAELARKEGADFVIGIGGGSPLDAAKAIALLAANKdGDEDLFQNGKY-- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 100 kGKPVtvplkPLIAVPTTSGTGSETTGVAIFDYEHLKVKTGIASRAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALE 179
Cdd:cd08181 122 -NPPL-----PIVAIPTTAGTGSEVTPYSILTDHEKGTKKSFGNPLIFPKLALLDPKYTLSLPEELTIDTAVDALSHAIE 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 180 SYtaipYSMRspcpsnpiqrpayqgSNPISDIWAVHALQIVAKYLKRAVRNPDDLEARSKMHLASAFAGIGFGNAGVHLC 259
Cdd:cd08181 196 GY----LSVK---------------ATPLSDALALEALRLIGECLPNLLGDELDEEDREKLMYASTLAGMVIAQTGTTLP 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 260 HGMSYPIsglvkTYkakEYNvdhplVPHGLSVVLTSPAVFTFTAQMFPERHLETAGILganirtariqdaGLVLADALRK 339
Cdd:cd08181 257 HGLGYPL-----TY---FKG-----IPHGRANGILLPAYLKLCEKQEPEKVDKILKLL------------GFGSIEEFQK 311
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1270111384 340 FLFDLNVDDGLaalgYSKDDIPSLVKGTLPQERVtKLAPRAQSEEDLSALFE 391
Cdd:cd08181 312 FLNRLLGKKEE----LSEEELEKYADEAMKAKNK-KNTPGNVTKEDILRIYR 358
|
|
| AAD_C |
cd08178 |
C-terminal alcohol dehydrogenase domain of the acetaldehyde dehydrogenase-alcohol ... |
1-359 |
9.65e-42 |
|
C-terminal alcohol dehydrogenase domain of the acetaldehyde dehydrogenase-alcohol dehydrogenase bifunctional two-domain protein (AAD); This alcohol dehydrogenase domain is located on the C-terminal of a bifunctional two-domain protein. The N-terminal of the protein contains an acetaldehyde-CoA dehydrogenase domain. This protein is involved in pyruvate metabolism whereby pyruvate is converted to acetyl-CoA and formate by pyruvate formate-lysase (PFL). Under anaerobic condition, acetyl-CoA is reduced to acetaldehyde and ethanol by this two-domain protein. Acetyl-CoA is first converted into an enzyme-bound thiohemiacetal by the N-terminal acetaldehyde dehydrogenase domain. The enzyme-bound thiohemiacetal is subsequently reduced by the C-terminal NAD+-dependent alcohol dehydrogenase domain. In E. coli, this protein is called AdhE and has been shown to have pyruvate formate-lyase (PFL) deactivase activity, which leads to the inactivation of PFL, a key enzyme in anaerobic metabolism. In Escherichia coli and Entamoeba histolytica, this enzyme forms homopolymeric peptides composed of more than 20 protomers associated in a helical rod-like structure.
Pssm-ID: 341457 [Multi-domain] Cd Length: 400 Bit Score: 151.19 E-value: 9.65e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 1 MGAKNVCLMTDKNLSQLPPVQIVMDSLSKNGISFQVYDDVRVEPTDGSFMDAIEFAKkgAF--DAYVAVGGGSTMDTCKA 78
Cdd:cd08178 21 PGVKRAFIVTDRVLYKLGYVDKVLDVLEARGVETEVFSDVEPDPTLSTVRKGLEAMN--AFkpDVIIALGGGSAMDAAKI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 79 ANLYASSPHSEFLD------------YVNAPIGKGKPvtvplkpLIAVPTTSGTGSETTGVA-IFDyEHLKVKTGIASRA 145
Cdd:cd08178 99 MWLFYEHPETKFEDlaqrfmdirkrvYKFPKLGKKAK-------LVAIPTTSGTGSEVTPFAvITD-DKTGKKYPLADYA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 146 IKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTAIPysmrspcpsnpiqrpayqgSNPISDIWAVHALQIVAKYLK 225
Cdd:cd08178 171 LTPDMAIVDPELVMTMPKRLTADTGIDALTHAIEAYVSVM-------------------ASDYTDGLALQAIKLIFEYLP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 226 RAVRNPDDLEARSKMHLASAFAGIGFGNAGVHLCHGMSYPISGlvktykakEYNvdhplVPHGLSVVLTSPAVFTFTAQ- 304
Cdd:cd08178 232 RSYNNGNDIEAREKMHNAATIAGMAFANAFLGICHSLAHKLGA--------AFH-----IPHGRANAILLPHVIRYNATd 298
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1270111384 305 ------MFP--------ERHLETAGILGANIRTariqDAGLV--LADALRKFLFDLNVDDGLAALGYSKDD 359
Cdd:cd08178 299 pptkqaAFPqykyyvakERYAEIADLLGLGGKT----PEEKVesLIKAIEDLKKDLGIPTSIREAGIDEAD 365
|
|
| Fe-ADH-like |
cd08189 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
1-365 |
2.38e-40 |
|
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: 146.84 E-value: 2.38e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 1 MGAKNVCLMTDKNLSQLPPVQIVMDSLSKNGISFQVYDDVRVEPTDGSFMDAIEFAKKGAFDAYVAVGGGSTMDTCKAAN 80
Cdd:cd08189 25 LGIKRVLIVTDKGLVKLGLLDPLLDALKKAGIEYVVFDGVVPDPTIDNVEEGLALYKENGCDAIIAIGGGSVIDCAKVIA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 81 LYASSPHSEFLDYVnapiGKGKpVTVPLKPLIAVPttsgtgsettGVA-----------IFDYEHlKVKTGIASRAIKPT 149
Cdd:cd08189 105 ARAANPKKSVRKLK----GLLK-VRKKLPPLIAVP----------TTAgtgseatiaavITDPET-HEKYAINDPKLIPD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 150 LGLVDPLHTLHMPCQVVANSGFDVLCHALESYTAIPYsmrspcpsnpiqrpayqgsNPISDIWAVHALQIVAKYLKRAVR 229
Cdd:cd08189 169 AAVLDPELTLGLPPAITAATGMDALTHAVEAYISRSA-------------------TKETDEYALEAVKLIFENLPKAYE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 230 NPDDLEARSKMHLASAFAGIGFGNAGVHLCHGMSYPISGLvktykakeYNvdhplVPHGL--SVVLtsPAVFTFTAQMFP 307
Cdd:cd08189 230 DGSDLEARENMLLASYYAGLAFTRAYVGYVHAIAHQLGGL--------YG-----VPHGLanAVVL--PHVLEFYGPAAE 294
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1270111384 308 ERHLETAGILGANIRTARIQDAGLVLADALRKFLFDLNVDDGLAALgySKDDIPSLVK 365
Cdd:cd08189 295 KRLAELADAAGLGDSGESDSEKAEAFIAAIRELNRRMGIPTTLEEL--KEEDIPEIAK 350
|
|
| Fe-ADH-like |
cd08186 |
Iron-containing alcohol dehydrogenase; This family contains iron-containing alcohol ... |
2-394 |
3.74e-40 |
|
Iron-containing alcohol dehydrogenase; This family contains iron-containing alcohol dehydrogenase (ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. The ADH of hyperthermophilic archaeon Thermococcus hydrothermalis oxidizes a series of primary aliphatic and aromatic alcohols, preferentially from C2 to C8, but is also active towards methanol and glycerol, and is stereospecific for monoterpenes. It has been suggested that the type III ADHs in microorganisms are involved in acetaldehyde detoxication rather than in alcohol turnover.
Pssm-ID: 341465 [Multi-domain] Cd Length: 380 Bit Score: 146.64 E-value: 3.74e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 2 GAKNVCLMTDKNLSQLPPV-QIVMDSLSKNGISFQVYDDVRVEPTDGSFMDAIEFAKKGAFDAYVAVGGGSTMDTCKAAN 80
Cdd:cd08186 22 GIDKVIIVTGRSSYKKSGAwDDVEKALEENGIEYVVYDKVTPNPTVDQADEAAKLARDFGADAVIAIGGGSPIDTAKSVA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 81 LYASSPHS---EFLDYVNAPIGKgkpvtvplKPLIAVPTTSGTGSETTGVAIFDYEHLKVKTGIASRAIKPTLGLVDPLH 157
Cdd:cd08186 102 VLLAYGGKtarDLYGFRFAPERA--------LPLVAINLTHGTGSEVDRFAVATIPEKGYKPGIAYDCIYPLYAIDDPRL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 158 TLHMPC-QVVANSgFDVLCHALESYTAipysmrspcpsnpiqrpayQGSNPISDIWAVHALQIVAKYLKRAVRNPDDLEA 236
Cdd:cd08186 174 TLTLPKeQTLYTS-IDAFNHVYEAATT-------------------KVSSPYVITLAKEAIRLIAEYLPRALANPKDLEA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 237 RSKMHLASAFAGIGFGNAGVHLCHGMSYPISGLVktykakeynvdhPLVPHGLSVVLTSPAVFTFTAQMFPErhlETAGI 316
Cdd:cd08186 234 RYWLLYASMIAGIAIDNGLLHLTHALEHPLSGLK------------PELPHGLGLALLGPAVVKYIYKAVPE---TLADI 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 317 LganirtaRIQDAGLV--------LADALRKFLFDLNVDDGLAALGYSKDDIPSLVK---GTLPQERVTKLAPRAQSEED 385
Cdd:cd08186 299 L-------RPIVPGLKgtpdeaekAARGVEEFLFSVGFTEKLSDYGFTEDDVDRLVElafTTPSLDLLLSLAPVEVTEEV 371
|
....*....
gi 1270111384 386 LSALFEASM 394
Cdd:cd08186 372 VREIYEESL 380
|
|
| PRK10624 |
PRK10624 |
L-1,2-propanediol oxidoreductase; Provisional |
2-394 |
1.21e-38 |
|
L-1,2-propanediol oxidoreductase; Provisional
Pssm-ID: 182595 [Multi-domain] Cd Length: 382 Bit Score: 142.44 E-value: 1.21e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 2 GAKNVCLMTDKNLSQLPPVQIVMDSLSKNGISFQVYDDVRVEPTDGSFMDAIE-FAKKGAfDAYVAVGGGSTMDTCKAAN 80
Cdd:PRK10624 29 GFKKALIVTDKTLVKCGVVAKVTDVLDAAGLAYEIYDGVKPNPTIEVVKEGVEvFKASGA-DYLIAIGGGSPQDTCKAIG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 81 LYASSPhsEFLDYVN----APIGKgkpvtvPLKPLIAVPTTS-GTGSETTGVAIFDYEHLKVKTGIASRAIkPTLGLVDP 155
Cdd:PRK10624 108 IISNNP--EFADVRSlegvAPTKK------PSVPIIAIPTTAgTAAEVTINYVITDEEKRRKFVCVDPHDI-PQVAFVDA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 156 LHTLHMPCQVVANSGFDVLCHALESYTAipysmrspcpsnpiqrpayQGSNPISDIWAVHALQIVAKYLKRAVRNpdDLE 235
Cdd:PRK10624 179 DMMDSMPPGLKAATGVDALTHAIEGYIT-------------------RGAWALTDMLHLKAIEIIAGALRGAVAG--DKE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 236 ARSKMHLASAFAGIGFGNAGVHLCHGMSYPISGLvktykakeYNvdhplVPHGLSVVLTSPAVFTFTAQMFPERHLETAG 315
Cdd:PRK10624 238 AGEGMALGQYIAGMGFSNVGLGLVHGMAHPLGAF--------YN-----TPHGVANAILLPHVMEYNADFTGEKYRDIAR 304
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1270111384 316 ILGANIRTARIQDAGLVLADALRKFLFDLNVDDGLAALGYSKDDIPSLVKGTLpQERVTKLAPRAQSEEDLSALFEASM 394
Cdd:PRK10624 305 AMGVKVEGMSLEEARNAAVEAVKALNRDVGIPPHLRDVGVKEEDIPALAQAAF-DDVCTGGNPREATLEDIVELYKKAW 382
|
|
| Fe-ADH-like |
cd14864 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
8-392 |
2.99e-38 |
|
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: 141.28 E-value: 2.99e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 8 LMTDKNLSQLPPVQIVMDSLSKNGISFQVYDDVRVEPTDGSFMDAIEFAKKGAFDAYVAVGGGSTMDTCKAANLYASSPH 87
Cdd:cd14864 30 LITDPVLKESGLADKIVSSLEKAGISVIVFDEIPASATSDTIDEAAELARKAGADGIIAVGGGKVLDTAKAVAILANNDG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 88 sEFLDYVNAPIGKGKPVtvplkPLIAVPTTSGTGSETTGVAIF-DYEHLKVKTgIASRAIKPTLGLVDPLHTLHMPCQVV 166
Cdd:cd14864 110 -GAYDFLEGAKPKKKPL-----PLIAVPTTPRSGFEFSDRFPVvDSRSREVKL-LKAQPGLPKAVIVDPNLMASLTGNQT 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 167 ANSGFDVLCHALESYTAipysmrspcpsnpiqrpayQGSNPISDIWAVHALQIVAKYLKRAVRNPDDLEARSKMHLASAF 246
Cdd:cd14864 183 AAMALAALALAVEAYLS-------------------KKSNFFSDALALKAIELVSENLDGALADPKNTPAEELLAQAGCL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 247 AGIGFGNAGVHLCHGMSYPISGLvktykakeYNVDHPLVphgLSVVLtsPAVFTFTAQMFPERHLETAGILGANIRTARI 326
Cdd:cd14864 244 AGLAASSSSPGLATALALAVNSR--------YKVSKSLV---ASILL--PHVIEYAATSAPDKYAKIARALGEDVEGASP 310
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1270111384 327 QDAGLVLADALRKFLFDLNVDDGLAALG--YSKDDIPSLVKgtlpQERVTKLAPRAQSEEDLSALFEA 392
Cdd:cd14864 311 EEAAIAAVEGVRRLIAQLNLPTRLKDLDlaSSLEQLAAIAE----DAPKLNGLPRSMSSDDIFDILKA 374
|
|
| PRK13805 |
PRK13805 |
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional |
1-359 |
7.16e-37 |
|
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional
Pssm-ID: 237515 [Multi-domain] Cd Length: 862 Bit Score: 142.63 E-value: 7.16e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 1 MGAKNVCLMTDKNLSQLPPVQIVMDSLSK--NGISFQVYDDVRVEPTdgsfmdaIEFAKKGA-----F--DAYVAVGGGS 71
Cdd:PRK13805 478 DGKKRAFIVTDRFMVELGYVDKVTDVLKKreNGVEYEVFSEVEPDPT-------LSTVRKGAelmrsFkpDTIIALGGGS 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 72 TMDTCKAANLYASSPHSEFLD------------YVNAPIG-KGKPVTVP--------LKPlIAVpttsgtgsettgvaIF 130
Cdd:PRK13805 551 PMDAAKIMWLFYEHPETDFEDlaqkfmdirkriYKFPKLGkKAKLVAIPttsgtgseVTP-FAV--------------IT 615
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 131 DyEHLKVKTGIASRAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTAIpysMrspcpsnpiqrpayqgSNPISD 210
Cdd:PRK13805 616 D-DKTGVKYPLADYELTPDVAIVDPNLVMTMPKSLTADTGIDALTHALEAYVSV---M----------------ASDYTD 675
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 211 IWAVHALQIVAKYLKRAVRN-PDDLEARSKMHLASAFAGIGFGNAGVHLCHGMSYPISGlvktykakEYNvdhplVPHGL 289
Cdd:PRK13805 676 GLALQAIKLVFEYLPRSYKNgAKDPEAREKMHNASTIAGMAFANAFLGICHSMAHKLGA--------EFH-----IPHGR 742
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 290 SVVLTSPAVFTFTAQ------MFP--------ERHLETAGILGANIRTariqDAGLV--LADALRKFLFDLNVDDGLAAL 353
Cdd:PRK13805 743 ANAILLPHVIRYNATdppkqaAFPqyeypradERYAEIARHLGLPGST----TEEKVesLIKAIEELKAELGIPMSIKEA 818
|
....*.
gi 1270111384 354 GYSKDD 359
Cdd:PRK13805 819 GVDEAD 824
|
|
| BDH |
cd08187 |
Butanol dehydrogenase catalyzes the conversion of butyraldehyde to butanol with the cofactor ... |
23-365 |
1.27e-32 |
|
Butanol dehydrogenase catalyzes the conversion of butyraldehyde to butanol with the cofactor NAD(P)H being oxidized in the process; The butanol dehydrogenase (BDH) is involved in the final step of the butanol formation pathway in anaerobic micro-organism. Butanol dehydrogenase catalyzes the conversion of butyraldehyde to butanol with the cofactor NAD(P)H being oxidized in the process. Activity in the reverse direction is 50-fold lower than that in the forward direction. The NADH-BDH has higher activity with longer chained aldehydes and is inhibited by metabolites containing an adenine moiety. This protein family belongs to the so-called iron-containing alcohol dehydrogenase superfamily. Since members of this superfamily use different divalent ions, preferentially iron or zinc, it has been suggested to be renamed to family III metal-dependent polyol dehydrogenases. This family also includes E. coli YqhD enzyme, an NADP-dependent dehydrogenase whose activity measurements with several alcohols demonstrate preference for alcohols longer than C3. The active site of YqhD contains a Zn metal, and a modified NADPH cofactor bearing OH groups on the saturated C5 and C6 atoms, possibly due to oxygen stress on the enzyme, which would functionally work under anaerobic conditions.
Pssm-ID: 341466 [Multi-domain] Cd Length: 382 Bit Score: 126.01 E-value: 1.27e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 23 VMDSLSKNGISFQVYDDVRVEPTDGSFMDAIEFAKKGAFDAYVAVGGGSTMDTCKAANLYASSPHsEFLDYVNapigKGK 102
Cdd:cd08187 49 VVASLKEAGIEVVEFGGVEPNPRLETVREGIELAREENVDFILAVGGGSVIDAAKAIAAGAKYDG-DVWDFFT----GKA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 103 PVTVPLkPLIAVPTTSGTGSETTGVAIFDYEHLKVKTGIASRAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESY- 181
Cdd:cd08187 124 PPEKAL-PVGTVLTLAATGSEMNGGAVITNEETKEKLGFGSPLLRPKFSILDPELTYTLPKYQTAAGIVDIFSHVLEQYf 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 182 TaipysmrspcpsnpiqrpaYQGSNPISDIWAVHALQIVAKYLKRAVRNPDDLEARSKMHLASAFA--GI-GFGNAGVHL 258
Cdd:cd08187 203 T-------------------GTEDAPLQDRLAEGLLRTVIENGPKALKDPDDYEARANLMWAATLAlnGLlGAGRGGDWA 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 259 CHGMSYPISGLvktykakeYNVDHplvPHGLSVVLtsPAVFTFTAQMFPERHLETA----GILGANIRTARIQDAglvlA 334
Cdd:cd08187 264 THAIEHELSAL--------YDITH---GAGLAIVF--PAWMRYVLKKKPERFAQFArrvfGIDPGGDDEETALEG----I 326
|
330 340 350
....*....|....*....|....*....|.
gi 1270111384 335 DALRKFLFDLNVDDGLAALGYSKDDIPSLVK 365
Cdd:cd08187 327 EALEEFFKSIGLPTTLSELGIDEEDIEEMAE 357
|
|
| PRK09860 |
PRK09860 |
putative alcohol dehydrogenase; Provisional |
2-394 |
7.26e-31 |
|
putative alcohol dehydrogenase; Provisional
Pssm-ID: 182118 [Multi-domain] Cd Length: 383 Bit Score: 121.60 E-value: 7.26e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 2 GAKNVCLMTDKNLSQLPPVQIVMDSLSKNGISFQVYDDVRVEPTDGSFMDAIEFAKKGAFDAYVAVGGGSTMDTCKAANL 81
Cdd:PRK09860 30 GFTRTLIVTDNMLTKLGMAGDVQKALEERNIFSVIYDGTQPNPTTENVAAGLKLLKENNCDSVISLGGGSPHDCAKGIAL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 82 YASSpHSEFLDYVNAPIGKGkpvtvPLKPLIAVPTTSGTGSETTGVAIFDYEHLKVKTGIASRAIKPTLGLVDPLHTLHM 161
Cdd:PRK09860 110 VAAN-GGDIRDYEGVDRSAK-----PQLPMIAINTTAGTASEMTRFCIITDEARHIKMAIVDKHVTPLLSVNDSSLMIGM 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 162 PCQVVANSGFDVLCHALESYTAIpysmrspcpsnpiqrpayqGSNPISDIWAVHALQIVAKYLKRAVRNPDDLEARSKMH 241
Cdd:PRK09860 184 PKSLTAATGMDALTHAIEAYVSI-------------------AATPITDACALKAVTMIAENLPLAVEDGSNAKAREAMA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 242 LASAFAGIGFGNAGVHLCHGMSYPISGLvktykakeYNvdhplVPHGLSVVLTSPAVFTFTAQMFPERHLETAGILGANI 321
Cdd:PRK09860 245 YAQFLAGMAFNNASLGYVHAMAHQLGGF--------YN-----LPHGVCNAVLLPHVQVFNSKVAAARLRDCAAAMGVNV 311
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1270111384 322 RTARIQDAGLVLADALRKFLFDLNVDDGLAALGYSKDDIPSLVKGTLpQERVTKLAPRAQSEEDLSALFEASM 394
Cdd:PRK09860 312 TGKNDAEGAEACINAIRELAKKVDIPAGLRDLNVKEEDFAVLATNAL-KDACGFTNPIQATHEEIVAIYRAAM 383
|
|
| PRK15454 |
PRK15454 |
ethanolamine utilization ethanol dehydrogenase EutG; |
2-393 |
2.34e-28 |
|
ethanolamine utilization ethanol dehydrogenase EutG;
Pssm-ID: 185351 [Multi-domain] Cd Length: 395 Bit Score: 114.74 E-value: 2.34e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 2 GAKNVCLMTDKNLSQLPPVQIVMDSLSKNGISFQVYDDVRVEPTDGSFMDAIEFAKKGAFDAYVAVGGGSTMDTCKAANL 81
Cdd:PRK15454 48 GLKHLFVMADSFLHQAGMTAGLTRSLAVKGIAMTLWPCPVGEPCITDVCAAVAQLRESGCDGVIAFGGGSVLDAAKAVAL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 82 YASSPHSEFLDYVNapigkgKPVTVPLKPLIAVPTTSGTGSETTGVAIFDYEHLKVKTGIASRAIKPTLGLVDPLHTLHM 161
Cdd:PRK15454 128 LVTNPDSTLAEMSE------TSVLQPRLPLIAIPTTAGTGSETTNVTVIIDAVSGRKQVLAHASLMPDVAILDAALTEGV 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 162 PCQVVANSGFDVLCHALESYTAIpysmrspcpsnpiqrpayqGSNPISDIWAVHALQIVAKYLKRAVRNPDDLEARSKMH 241
Cdd:PRK15454 202 PSHVTAMTGIDALTHAIEAYSAL-------------------NATPFTDSLAIGAIAMIGKSLPKAVGYGHDLAARESML 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 242 LASAFAGIGFGNAGVHLCHGMSY-PISGLvktykakeynvdHplVPHGLSVVLTSPAVFTFTAQMFPERHLEtagiLGAN 320
Cdd:PRK15454 263 LASCMAGMAFSSAGLGLCHAMAHqPGAAL------------H--IPHGLANAMLLPTVMEFNRMVCRERFSQ----IGRA 324
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1270111384 321 IRTARIQDAGLVlaDALRKFLFDLNVDDGLAALGYSKDDIPSLVKGTLpQERVTKLAPRAQSEEDLSALFEAS 393
Cdd:PRK15454 325 LRTKKSDDRDAI--NAVSELIAEVGIGKRLGDVGATSAHYGAWAQAAL-EDICLRSNPRTASLEQIVGLYAAA 394
|
|
| 4HBD_NAD |
cd14860 |
4-hydroxybutyrate dehydrogenase, also called gamma-hydroxybutyrate dehydrogenase, catalyzes ... |
43-397 |
4.33e-25 |
|
4-hydroxybutyrate dehydrogenase, also called gamma-hydroxybutyrate dehydrogenase, catalyzes the reduction of succinic simialdehyde to 4-hydroxybutyrate in the succinic degradation pathway; 4-hydroxybutyrate dehydrogenase (4HBD) is an iron-containing (type III) NAD-dependent alcohol dehydrogenase. It plays a role in the succinate metabolism biochemical pathway. It catalyzes the reduction of succinic simialdehide to 4-hydroxybutyrate in the succinate degradation pathway This succinate degradation pathway is present in some bacteria which can use succinate as sole carbon source.
Pssm-ID: 341482 Cd Length: 371 Bit Score: 104.99 E-value: 4.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 43 EPTDGSFMDAIEFAKKGAFDAYVAVGGGSTMDTCKAANLYASSPHSEFLDYvNAPIGKGKPvtvplkpLIAVPTTSGTGS 122
Cdd:cd14860 61 EPSDEMVEAIYKDIKKYGYKRVIAIGGGTVIDIAKLLALKGISPVLDLFDG-KIPLIKEKE-------LIIVPTTCGTGS 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 123 ETTGVAIFDYEHLKVKTGIASRAIKPTLGLVDP--LHTLhmPCQVVANSGFDVLCHALESYTaipysmrSPcpsnpiqrp 200
Cdd:cd14860 133 EVTNISIVELTSLGTKKGLAVDELYADKAVLIPelLKGL--PYKVFATSSIDALIHAIESYL-------SP--------- 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 201 ayqGSNPISDIWAVHALQ-IVAKYLKRAVRNPDDL-EARSKMHLASAFAGIGFGNAGVHLCHGMSYPISGlvkTYKakey 278
Cdd:cd14860 195 ---KATPYTEMFSYKAIEmILEGYQEIAEKGEEARfPLLGDFLIASNYAGIAFGNAGCAAVHALSYPLGG---KYH---- 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 279 nvdhplVPHGLS--VVLTspAVFTFTAQMFPERHLET-----AGILGAnirtariqDAGLVLaDALRKFLFDLNVDDGLA 351
Cdd:cd14860 265 ------VPHGEAnyAVFT--GVLKNYQEKNPDGEIKKlneflAKILGC--------DEEDVY-DELEELLNKILPKKPLH 327
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1270111384 352 ALGYSKDDIPSLVKGTLP-QERVTKLAPRAQSEEDLSALFeasMKLY 397
Cdd:cd14860 328 EYGMKEEEIDEFADSVMEnQQRLLANNYVPLDREDVAEIY---KELY 371
|
|
| MAR-like |
cd08192 |
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic ... |
2-392 |
1.36e-23 |
|
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: 100.79 E-value: 1.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 2 GAKNVCLMTDKNLSQLPPVqiVMDSLSKNGISF-QVYDDVRVEPTDGSFMDAIEFAKKGAFDAYVAVGGGSTMDTCKAAN 80
Cdd:cd08192 22 GASRVFIVTSKSLATKTDV--IKRLEEALGDRHvGVFSGVRQHTPREDVLEAARAVREAGADLLVSLGGGSPIDAAKAVA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 81 L-YASSPH-SEFLDYVNAPIGKGKPVTVPLKPLIAVPTTSGTGSETTGVAIFDyEHLKVKTGIASRAIKPTLGLVDPLHT 158
Cdd:cd08192 100 LaLAEDVTdVDQLDALEDGKRIDPNVTGPTLPHIAIPTTLSGAEFTAGAGATD-DDTGHKQGFAHPELGPDAVILDPELT 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 159 LHMPCQVVANSGFDVLCHALESYtaipYSMRSpcpsnpiqrpayqgsNPISDIWAVHALQIVAKYLKRAVRNPDDLEARS 238
Cdd:cd08192 179 LHTPERLWLSTGIRAVDHAVETL----CSPQA---------------TPFVDALALKALRLLFEGLPRSKADPEDLEARL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 239 KMHLASAFAGIGFGN-AGVHLCHGMSYPISGLvktykakeYNvdhplVPHGLSVVLTSPAVFTFTAQMFPERHLETAGIL 317
Cdd:cd08192 240 KCQLAAWLSLFGLGSgVPMGASHAIGHQLGPL--------YG-----VPHGITSCIMLPAVLRFNAPVNAERQRLIARAL 306
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1270111384 318 GANIRTARIQDAGlvLADALRKFLFDLNVDDGLAALGYSKDDIPSLVKGTLPQERVTKLAPRAQSEEDLSALFEA 392
Cdd:cd08192 307 GLVTGGLGREAAD--AADAIDALIRELGLPRTLRDVGVGRDQLEKIAENALTDVWCRTNPRPITDKDDVLEILES 379
|
|
| Fe-ADH-like |
cd14866 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
36-392 |
3.94e-21 |
|
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: 93.83 E-value: 3.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 36 VYDDVRVEPTDGSFMDAIEFAKKGAFDAYVAVGGGSTMDTCKAANLYASSPHSeFLDYVNAPIGKGKPVT----VPLKPL 111
Cdd:cd14866 59 VFDGVRPHSPLETVEAAAEALREADADAVVAVGGGSAIVTARAASILLAEDRD-VRELCTRRAEDGLMVSprldAPKLPI 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 112 IAVPTTSGTGSETTGVAIFDYEHLKvKTGIASRAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESytaiPYSMRsp 191
Cdd:cd14866 138 FVVPTTPTTADVKAGSAVTDPPAGQ-RLALFDPKTRPAAVFYDPELLATAPASLVAGAAMNGFDMAVEG----LYSRH-- 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 192 cpsnpiqrpayqgSNPISDIWAVHALQIVAKYLKRAVrNPDDLEARSKMHLASAFAGIGFGNAGVHLCHGMSYPISGlvk 271
Cdd:cd14866 211 -------------ADPLADATLMHALRLLADGLPRLA-DDDDPAARADLVLAAVLAGYGTDHTGGGVIHALGHAIGA--- 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 272 tykakEYNVDHPLVpHglSVVLtsPAVFTFTAQMFPERHLETAGILGAniRTARIQDAGLVLADALRKFLFDLNVDDGLA 351
Cdd:cd14866 274 -----RYGVQNGVV-H--AILL--PHVLRFNAPATDGRLDRLAEALGV--ADAGDEASAAAVVDAVEALLDALGVPTRLR 341
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1270111384 352 ALGYSKDDIPSLVKGTLPQERVTKLAPRAQSEEDLSALFEA 392
Cdd:cd14866 342 DLGVSREDLPAIAEAAMDDWFMDNNPRPVPTAEELEALLEA 382
|
|
| YqdH |
COG1979 |
Alcohol dehydrogenase YqhD, Fe-dependent ADH family [Energy production and conversion]; |
23-394 |
3.88e-19 |
|
Alcohol dehydrogenase YqhD, Fe-dependent ADH family [Energy production and conversion];
Pssm-ID: 441582 [Multi-domain] Cd Length: 387 Bit Score: 88.21 E-value: 3.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 23 VMDSLSKNGISFQVYDDVRVEPTDGSFMDAIEFAKKGAFDAYVAVGGGSTMDTCK---AANLYASSPHseflDYVNapig 99
Cdd:COG1979 51 VKAALKEAGIEVVEFGGVEPNPRLETVRKGVELCKEEGIDFILAVGGGSVIDGAKaiaAGAKYDGDPW----DILT---- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 100 KGKPVTVPLkPLIAVPTTSGTGSETTGVAIFDYEHLKVKTGIASRAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALE 179
Cdd:COG1979 123 GKAPVEKAL-PLGTVLTLPATGSEMNSGSVITNEETKEKLGFGSPLVFPKFSILDPELTYTLPKRQTANGIVDIFSHVME 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 180 SYTaipysmrspcpSNPIQrpayqgsNPISDIWAVHALQIVAKYLKRAVRNPDDLEARSKMHLASAFAGIGFGNAGVH-- 257
Cdd:COG1979 202 QYF-----------TYPVD-------APLQDRFAEGLLRTLIEEGPKALKDPEDYDARANLMWAATLALNGLIGAGVPqd 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 258 -LCHGMSYPISGLvktykakeYNVDHplvPHGLSVVLtsPAVFTFTAQMFPERHLETA----GILGANIRtARIQDAglv 332
Cdd:COG1979 264 wATHMIEHELSAL--------YDIDH---GAGLAIVL--PAWMRYVLEEKPEKFAQYAervwGITEGDDE-ERALEG--- 326
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1270111384 333 lADALRKFLFDLNVDDGLAALGYSKDDIPSLVKGTLPQERVTKLAPRAQSEEDLSALFEASM 394
Cdd:COG1979 327 -IEATEEFFESLGLPTRLSEYGIDEEDIEEMAEKATAHGMTALGEFKDLTPEDVREILELAL 387
|
|
| MAR |
cd08177 |
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic ... |
36-392 |
2.19e-16 |
|
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: 79.47 E-value: 2.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 36 VYDDVR----VEPTDgsfmDAIEFAKKGAFDAYVAVGGGSTmdtckaanlyassphsefldyvnapIGKGKPVTVPLK-P 110
Cdd:cd08177 52 VFDGAVmhvpVEVAE----RALAAAREAGADGLVAIGGGSA-------------------------IGLAKAIALRTGlP 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 111 LIAVPTTSgtgsettgvA------IFDYEHLKVKTGIASRAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTAi 184
Cdd:cd08177 103 IVAVPTTY---------AgsemtpIWGETEDGVKTTGRDPRVLPRTVIYDPDLTLGLPAALSVASGLNALAHAVEALYA- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 185 pysmrspcpsnpiqrpayQGSNPISDIWAVHALQIVAKYLKRAVRNPDDLEARSKMHLASAFAGIGFGNAG--VH--LCH 260
Cdd:cd08177 173 ------------------PDANPITSLLAEEGIRALARALPRLVADPSDLEARSDALYGAWLAGVVLGSVGmgLHhkLCH 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 261 --GMSYpisGLvktykakeynvdhplvPHGL--SVVLtsPAVFTFTAQMFPERHletagilganirtARIQDAGLV--LA 334
Cdd:cd08177 235 vlGGTF---DL----------------PHAEthAVVL--PHVLAYNAPAAPDAM-------------ARLARALGGgdAA 280
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1270111384 335 DALRKFLFDLNVDDGLAALGYSKDDIPSLVkgtlpqERVTKLA---PRAQSEEDLSALFEA 392
Cdd:cd08177 281 GGLYDLARRLGAPTSLRDLGMPEDDIDRAA------DLALANPypnPRPVERDALRALLER 335
|
|
| PRK15138 |
PRK15138 |
alcohol dehydrogenase; |
26-376 |
9.75e-08 |
|
alcohol dehydrogenase;
Pssm-ID: 185092 [Multi-domain] Cd Length: 387 Bit Score: 53.64 E-value: 9.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 26 SLSKNGISFQVYD-----DVR----VEP--TDGSFMDAIEFAKKGAFDAYVAVGGGSTMDTCK----AANLYASSPHSEF 90
Cdd:PRK15138 40 SVKKTGVLDQVLDalkgmDVLefggIEPnpTYETLMKAVKLVREEKITFLLAVGGGSVLDGTKfiaaAANYPENIDPWHI 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 91 LDYVNAPIGKGkpvtVPLKPLIAVPttsGTGSETTGVAIFDYEHLKVKTGIASRAIKPTLGLVDPLHTLHMPCQVVANSG 170
Cdd:PRK15138 120 LETGGKEIKSA----IPMGSVLTLP---ATGSESNAGAVISRKTTGDKQAFHSPHVQPVFAVLDPVYTYTLPPRQVANGV 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 171 FDVLCHALESYTAIPYSMRspcpsnpiqrpayqgsnpISDIWAVHALQIVAKYLKRAVRNPDDLEARSKMHLASAFAGIG 250
Cdd:PRK15138 193 VDAFVHTVEQYVTYPVDAK------------------IQDRFAEGILLTLIEEGPKALKEPENYDVRANVMWAATQALNG 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 251 FGNAGVH---LCHGMSYPISGLvktykakeYNVDHplvPHGLSVVLtsPAVFTFTAQMFPERHLETAGILGaNIRT---- 323
Cdd:PRK15138 255 LIGAGVPqdwATHMLGHELTAM--------HGLDH---AQTLAIVL--PALWNEKRDTKRAKLLQYAERVW-NITEgsdd 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1270111384 324 ARIqDAGLvlaDALRKFLFDLNVDDGLAALGYSKDDIPSLVKgTLPQERVTKL 376
Cdd:PRK15138 321 ERI-DAAI---AATRNFFEQMGVPTRLSDYGLDGSSIPALLK-KLEEHGMTQL 368
|
|
| DHQ_Fe-ADH |
cd07766 |
Dehydroquinate synthase-like (DHQ-like) and iron-containing alcohol dehydrogenases (Fe-ADH); ... |
4-365 |
2.92e-07 |
|
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: 51.60 E-value: 2.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 4 KNVCLMTDKNLSQLPpVQIVMDSLSKnGISFQVYDDVRVEPTDGSFMDAIEFAKKGAFDAYVAVGGGSTMDTCKAANLya 83
Cdd:cd07766 23 DRALVVSDEGVVKGV-GEKVADSLKK-GLAVAIFDFVGENPTFEEVKNAVERARAAEADAVIAVGGGSTLDTAKAVAA-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 84 ssphsefldyvnapigkgkpVTVPLKPLIAVPTTSGTGSETTGVAIFDYEHLKVKTGIAsrAIKPTLGLVDPLHTLHMPC 163
Cdd:cd07766 99 --------------------LLNRGIPFIIVPTTASTDSEVSPKSVITDKGGKNKQVGP--HYNPDVVFVDTDITKGLPP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 164 QVVANSGFDVLCHALEsytaipysmrspcpsnpiqrpayqgsnpisdiwavhalqivakylkravrnpddleaRSKMHLA 243
Cdd:cd07766 157 RQVASGGVDALAHAVE---------------------------------------------------------LEKVVEA 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 244 SAFAGIGFGNA-GVHLCHGMSYPISGLVKTykakeynvdhplvPHGLSVVLTSPAVFTFTAQMFPERHLETAgilganir 322
Cdd:cd07766 180 ATLAGMGLFESpGLGLAHAIGHALTAFEGI-------------PHGEAVAVGLPYVLKVANDMNPEPEAAIE-------- 238
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1270111384 323 tariqdaglvladALRKFLFDLNVDDGLAALGYSKDDIPSLVK 365
Cdd:cd07766 239 -------------AVFKFLEDLGLPTHLADLGVSKEDIPKLAE 268
|
|
| Fe-ADH_2 |
pfam13685 |
Iron-containing alcohol dehydrogenase; |
1-263 |
3.87e-07 |
|
Iron-containing alcohol dehydrogenase;
Pssm-ID: 404557 [Multi-domain] Cd Length: 251 Bit Score: 50.76 E-value: 3.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 1 MGAKNVCLMTDKNLSQLPpVQIVMDSLSKNGISFQVYDDVRVEPTDGSFMDAIEFAKKGAFDAYVAVGGGSTMDTCKAA- 79
Cdd:pfam13685 17 LGFRRVALVADANTYAAA-GRKVAESLKRAGIEVETRLEVAGNADMETAEKLVGALRERDADAVVGVGGGTVIDLAKYAa 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 80 ---NL-YASSPHSEFLDYVNAP----IGKGKPVTVPLKPLIAVpttsgtgsettgvaIFDyehlkvkTGIASRAikptlg 151
Cdd:pfam13685 96 fklGKpFISVPTAASNDGFASPgaslTVDGKKRSIPAAAPFGV--------------IAD-------TDVIAAA------ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 152 lvdPLHTLHmpcqvvanSGF-DvlchALESYTAIPYSMRSpcpsnpiqrpayqGSNPISDIWAVHALQIVAKYLKRAVRN 230
Cdd:pfam13685 149 ---PRRLLA--------SGVgD----LLAKITAVADWELA-------------HAEEVAAPLALLSAAMVMNFADRPLRD 200
|
250 260 270
....*....|....*....|....*....|...
gi 1270111384 231 PDDLEARSKMHLASAFAGIGFGNAGVHLCHGMS 263
Cdd:pfam13685 201 PGDIEALAELLSALAMGGAGSSRPASGSEHLIS 233
|
|
| G1PDH-like |
cd08174 |
Glycerol-1-phosphate dehydrogenase-like; These glycerol-1-phosphate dehydrogenase-like ... |
1-84 |
1.80e-05 |
|
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: 46.36 E-value: 1.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 1 MGAKNVCLMTDKNLSQLPpVQIVMDSLSKNGISFQVYDdvrvePTDGSFMDAIEFA-KKGAFDAYVAVGGGSTMDTCKaa 79
Cdd:cd08174 23 QGFGKVAIVTGEGIDELL-GEDILESLEEAGEIVTVEE-----NTDNSAEELAEKAfSLPKVDAIVGIGGGKVLDVAK-- 94
|
....*
gi 1270111384 80 nlYAS 84
Cdd:cd08174 95 --YAA 97
|
|
| Fe-ADH_KdnB-like |
cd08184 |
Iron-containing alcohol dehydrogenase similar to Shewanella oneidensis KdnB required for Kdo8N ... |
36-267 |
3.96e-05 |
|
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: 45.34 E-value: 3.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 36 VYDDVRVEPTDG---SFMDAIEFAKKGAFDAYVAVGGGSTMDTCKA-ANLYA---SSPHSEFLDYVnapigKGKPVtvpl 108
Cdd:cd08184 55 IFVDTTDEPKTDqidALRAQIRAENDKLPAAVVGIGGGSTMDIAKAvSNMLTnpgSAADYQGWDLV-----KNPGI---- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 109 kPLIAVPTTSGTGSETTGVAIFDYEHLKVktGIASRAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTAipySM 188
Cdd:cd08184 126 -YKIGVPTLSGTGAEASRTAVLTGPEKKL--GINSDYTVFDQVILDPELIATVPRDQYFYTGMDCYIHCVESLNG---TY 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 189 RspcpsnpiqrpayqgsNPISDIWAVHALQIVAK-YLKRAVRNPDDLEarsKMHLASAFAGIGFGNAGVHLCHGMSYPIS 267
Cdd:cd08184 200 R----------------NAFGDAYAEKALELCRDvFLSDDMMSPENRE---KLMVASYLGGSSIANSQVGVCHALSYGLS 260
|
|
| GldA |
COG0371 |
Glycerol dehydrogenase or related enzyme, iron-containing ADH family [Energy production and ... |
23-79 |
2.93e-04 |
|
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: 42.46 E-value: 2.93e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1270111384 23 VMDSLSKNGISFQVYDdVRVEPTDGSFMDAIEFAKKGAFDAYVAVGGGSTMDTCKAA 79
Cdd:COG0371 46 LEESLEDAGIEVEVEV-FGGECSEEEIERLAEEAKEQGADVIIGVGGGKALDTAKAV 101
|
|
| Gro1PDH |
cd08173 |
Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) catalyzes the reversible conversion between ... |
2-114 |
7.23e-03 |
|
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: 38.30 E-value: 7.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111384 2 GAKNVCLMTDKNLSQLPpVQIVMDSLSKNGISFQVYDDVRVEpTDGSFMDAIEFAKKGAFDAYVAVGGGSTMDTCK--AA 79
Cdd:cd08173 24 LGKRALIITGPNTYKIA-GKRVEDLLESSGVEVVIVDIATIE-EAAEVEKVKKLIKESKADFIIGVGGGKVIDVAKyaAY 101
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1270111384 80 NL---YASSPHSEFLDYVNAP----IGKGKPVTVPLKPLIAV 114
Cdd:cd08173 102 KLnlpFISIPTSASHDGIASPfasiKGGDKPYSIKAKAPIAI 143
|
|
| |
