|
Name |
Accession |
Description |
Interval |
E-value |
| HOT |
cd08190 |
Hydroxyacid-oxoacid transhydrogenase (HOT) involved in gamma-hydroxybutyrate metabolism; This ... |
23-368 |
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: 618.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 23 FMDAIEFAKKGAFDAYVAVGGGSTMDTCKAANLYACSPhSEFLDYVNAPIGKGKPVTVPLKPLIAVPTTSGTGSETTGVA 102
Cdd:cd08190 69 FEEAIEFAKEGDFDAFVAVGGGSVIDTAKAANLYATHP-GDFLDYVNAPIGKGKPVPGPLKPLIAIPTTAGTGSETTGVA 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 103 IFDYEHLKVKTGIASRAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTAIPYSMRsPCPSNPIQRPAYQGSNPI 182
Cdd:cd08190 148 IFDLEELKVKTGISSRYLRPTLAIVDPLLTLTLPPRVTASSGFDVLCHALESYTARPYNAR-PRPANPDERPAYQGSNPI 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 183 SDIWAVHALRIVAKYLKRAVRNPDDLEARSSMHLASAFAGIGFGNAGVHLCHGMSYPISGLVKTYKAKEYNVDHPLVPHG 262
Cdd:cd08190 227 SDVWAEKAIELIGKYLRRAVNDGDDLEARSNMLLASTLAGIGFGNAGVHLPHAMAYPIAGLVKDYRPPGYPVDHPHVPHG 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 263 LSVVLTSPAVFTFTAQMFPERHLETAEILGANIRTAKIQDAGPVLADALRKFLFDLNVDDGLAALGYSKDDIPSLVKGTL 342
Cdd:cd08190 307 LSVALTAPAVFRFTAPACPERHLEAAELLGADTSGASDRDAGEVLADALIKLMRDIGIPNGLSALGYSEDDIPALVEGTL 386
|
330 340
....*....|....*....|....*.
gi 1958777079 343 PQERVTKLAPRAQSEEDLSALFEASM 368
Cdd:cd08190 387 PQQRLLKLNPRPVTEEDLEEIFEDAL 412
|
|
| EutG |
COG1454 |
Alcohol dehydrogenase, class IV [Energy production and conversion]; |
24-368 |
3.91e-87 |
|
Alcohol dehydrogenase, class IV [Energy production and conversion];
Pssm-ID: 441063 [Multi-domain] Cd Length: 381 Bit Score: 268.14 E-value: 3.91e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 24 MDAIEFAKKGAFDAYVAVGGGSTMDTCKAANLYACSPHSeFLDYVNApigkgKPVTVPLKPLIAVP----------Ttsg 93
Cdd:COG1454 77 EAGAAAAREFGADVVIALGGGSAIDAAKAIALLATNPGD-LEDYLGI-----KKVPGPPLPLIAIPttagtgsevtP--- 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 94 tgsettgVAIFDYEHLKVKTGIASRAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTAIpysmrspcpsnpiqr 173
Cdd:COG1454 148 -------FAVITDPETGVKKGIADPELLPDVAILDPELTLTLPPSLTAATGMDALTHAIEAYVSK--------------- 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 174 payqGSNPISDIWAVHALRIVAKYLKRAVRNPDDLEARSSMHLASAFAGIGFGNAGVHLCHGMSYPISGLvktykakeYN 253
Cdd:COG1454 206 ----GANPLTDALALEAIRLIARNLPRAVADGDDLEAREKMALASLLAGMAFANAGLGAVHALAHPLGGL--------FH 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 254 vdhplVPHGLSVVLTSPAVFTFTAQMFPERHLETAEILGANIrTAKIQDAGPVLADALRKFLFDLNVDDGLAALGYSKDD 333
Cdd:COG1454 274 -----VPHGLANAILLPHVLRFNAPAAPERYAEIARALGLDV-GLSDEEAAEALIEAIRELLRDLGIPTRLSELGVTEED 347
|
330 340 350
....*....|....*....|....*....|....*
gi 1958777079 334 IPSLVKGTLpQERVTKLAPRAQSEEDLSALFEASM 368
Cdd:COG1454 348 LPELAELAL-ADRCLANNPRPLTEEDIEAILRAAY 381
|
|
| Fe-ADH |
cd08551 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains large ... |
21-364 |
1.60e-80 |
|
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: 250.83 E-value: 1.60e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 21 ACFMDAIEFAKKGAFDAYVAVGGGSTMDTCKAANLYACSPHSeFLDYVNapigkGKPVTVPLKPLIAVPTTSGTGSETTG 100
Cdd:cd08551 67 ETVEAAAELAREEGADLVIAVGGGSVLDTAKAIAVLATNGGS-IRDYEG-----IGKVPKPGLPLIAIPTTAGTGSEVTP 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 101 VAIFDYEHLKVKTGIASRAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTAIPysmrspcpsnpiqrpayqgSN 180
Cdd:cd08551 141 NAVITDPETGRKMGIVSPYLLPDVAILDPELTLSLPPSVTAATGMDALTHAIEAYTSKK-------------------AN 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 181 PISDIWAVHALRIVAKYLKRAVRNPDDLEARSSMHLASAFAGIGFGNAGVHLCHGMSYPISGlvktykakEYNvdhplVP 260
Cdd:cd08551 202 PISDALALEAIRLIGKNLRRAVADGSDLEAREAMLLASLLAGIAFGNAGLGAVHALAYPLGG--------RYH-----IP 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 261 HGLSVVLTSPAVFTFTAQMFPERHLETAEILGANIRTAKIQDAGPVLADALRKFLFDLNVDDGLAALGYSKDDIPSLVKG 340
Cdd:cd08551 269 HGVANAILLPYVMEFNLPACPEKYAEIAEALGEDVEGLSDEEAAEAAVEAVRELLRDLGIPTSLSELGVTEEDIPELAED 348
|
330 340
....*....|....*....|....
gi 1958777079 341 TLPQERVTKLAPRAQSEEDLSALF 364
Cdd:cd08551 349 AMKSGRLLSNNPRPLTEEDIREIY 372
|
|
| Fe-ADH |
pfam00465 |
Iron-containing alcohol dehydrogenase; |
24-360 |
1.32e-75 |
|
Iron-containing alcohol dehydrogenase;
Pssm-ID: 425696 [Multi-domain] Cd Length: 362 Bit Score: 237.89 E-value: 1.32e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 24 MDAIEFAKKGAFDAYVAVGGGSTMDTCKAANLYACSPHSEFLDYvnapigKGKPVTVPLKPLIAVPTTSGTGSETTGVAI 103
Cdd:pfam00465 69 DEAAALAREAGADVIIAVGGGSVIDTAKAIALLLTNPGDVWDYL------GGKPLTKPALPLIAIPTTAGTGSEVTPLAV 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 104 FDYEHLKVKTGIASRAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTAipysmrspcpsnpiqrpayQGSNPIS 183
Cdd:pfam00465 143 ITDTETGEKLGIFSPKLLPDLAILDPELTLTLPPRLTAATGMDALAHAVEAYVS-------------------KGANPLT 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 184 DIWAVHALRIVAKYLKRAVRNPDDLEARSSMHLASAFAGIGFGNAGVHLCHGMSYPISGLVKtykakeynvdhplVPHGL 263
Cdd:pfam00465 204 DALALEAIRLIAENLPRAVADGEDLEARENMLLASTLAGLAFSNAGLGAAHALAHALGGRYG-------------IPHGL 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 264 SVVLTSPAVFTFTAQMFPERHLETAEILGANIRTAKIQDAgpvlADALRKFLFDLNVDDGLAALGYSKDDIPSLVKGTLp 343
Cdd:pfam00465 271 ANAILLPYVLRFNAPAAPEKLAQLARALGEDSDEEAAEEA----IEALRELLRELGLPTTLSELGVTEEDLDALAEAAL- 345
|
330
....*....|....*..
gi 1958777079 344 QERVTKLAPRAQSEEDL 360
Cdd:pfam00465 346 RDRSLANNPRPLTAEDI 362
|
|
| Fe-ADH-like |
cd08185 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
24-365 |
2.53e-68 |
|
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: 219.68 E-value: 2.53e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 24 MDAIEFAKKGAFDAYVAVGGGSTMDTCKAANLYACSPHSEFlDYVNAPIGKGKPVTVPLkPLIAVPTTSGTGSETTGVAI 103
Cdd:cd08185 73 MEGAALAKEEGCDFVIGLGGGSSMDAAKAIAFMATNPGDIW-DYIFGGTGKGPPPEKAL-PIIAIPTTAGTGSEVDPWAV 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 104 FDYEHLKVKTGIASRAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTAIpysmrspcpsnpiqrpayqGSNPIS 183
Cdd:cd08185 151 ITNPETKEKKGIGHPALFPKVSIVDPELMLTVPPRVTAYTGFDALFHAFESYISK-------------------NANPFS 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 184 DIWAVHALRIVAKYLKRAVRNPDDLEARSSMHLASAFAGIGFGNAGVHLCHGMSYPISGLvktykakeynvdHPLVPHGL 263
Cdd:cd08185 212 DMLALEAIRLVAKYLPRAVKDGSDLEAREKMAWASTLAGIVIANSGTTLPHGLEHPLSGY------------HPNIPHGA 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 264 SVVLTSPAVFTFTAQMFPERhleTAEILGANIRTAKIQDAGPVLADALRKFLFDLNVDDGLAALGYSKDDIPSLVkgtlp 343
Cdd:cd08185 280 GLAALYPAYFEFTIEKAPEK---FAFVARAEASGLSDAKAAEDFIEALRKLLKDIGLDDLLSDLGVTEEDIPWLA----- 351
|
330 340
....*....|....*....|....*....
gi 1958777079 344 qERVTKLA-------PRAQSEEDLSALFE 365
Cdd:cd08185 352 -ENAMETMgglfannPVELTEEDIVEIYE 379
|
|
| Fe-ADH-like |
cd14863 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
25-366 |
3.11e-66 |
|
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: 214.32 E-value: 3.11e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 25 DAIEFAKKGAFDAYVAVGGGSTMDTCKAANLYACSPHsEFLDYvnapIGKGKPVTVPLKPLIAVPTTSGTGSETTGVAIF 104
Cdd:cd14863 75 EAAEIAREEGADGVIGIGGGSVLDTAKAIAVLLTNPG-PIIDY----ALAGPPVPKPGIPLIAIPTTAGTGSEVTPIAVI 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 105 DYEHLKVKTGIASRAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTAipysmrspcpsnpiqrpayQGSNPISD 184
Cdd:cd14863 150 TDEENGVKKSLLGPFLVPDLAILDPELTVGLPPSLTAATGMDALSHAIEAYTS-------------------KLANPMTD 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 185 IWAVHALRIVAKYLKRAVRNPDDLEARSSMHLASAFAGIGFGNAGVHLCHGMSYPISGLvktykakeYNvdhplVPHGLS 264
Cdd:cd14863 211 ALALQAIRLIVKNLPRAVKDGDNLEARENMLLASNLAGIAFNNAGTHIGHAIAHALGAL--------YH-----IPHGLA 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 265 VVLTSPAVFTFTAQMFPERHLETAEILGANIRTAKIQDAGPVLADALRKFLFDLNVDDGLAALGYSKDDIPSLVKGTLpQ 344
Cdd:cd14863 278 CALALPVVLEFNAEAYPEKVKKIAKALGVSFPGESDEELGEAVADAIREFMKELGIPSLFEDYGIDKEDLDKIAEAVL-K 356
|
330 340
....*....|....*....|..
gi 1958777079 345 ERVTKLAPRAQSEEDLSALFEA 366
Cdd:cd14863 357 DPFAMFNPRPITEEEVAEILEA 378
|
|
| Fe-ADH-like |
cd08191 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
25-368 |
2.99e-64 |
|
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: 209.39 E-value: 2.99e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 25 DAIEFAKKGAFDAYVAVGGGSTMDTCKAANLyACSPHSEFLDYvnapIGKGKpVTVPLKPLIAVPTTSGTGSETTGVAIF 104
Cdd:cd08191 73 DAAAAARAFDPDVVIGLGGGSNMDLAKVVAL-LLAHGGDPRDY----YGEDR-VPGPVLPLIAVPTTAGTGSEVTPVAVL 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 105 DYEHLKVKTGIASRAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTAIPysmRSPCPSNPiQRPAYQGSNPISD 184
Cdd:cd08191 147 TDPARGMKVGVSSPYLRPAVAIVDPELTLTCPPGVTADSGIDALTHAIESYTARD---FPPFPRLD-PDPVYVGKNPLTD 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 185 IWAVHALRIVAKYLKRAVRNPDDLEARSSMHLASAFAGIGFGNAGVHLCHGMSYPISGLVKTykakeynvdhplvPHGLS 264
Cdd:cd08191 223 LLALEAIRLIGRHLPRAVRDGDDLEARSGMALAALLAGLAFGTAGTAAAHALQYPIGALTHT-------------SHGVG 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 265 VVLTSPAVFTFtaqMFPERHLETAEI---LGANIRTAKIQDAGPVLaDALRKFLFDLNVDDGLAALGYSKDDIPSLVKGT 341
Cdd:cd08191 290 NGLLLPYVMRF---NRPARAAELAEIaraLGVTTAGTSEEAADRAI-ERVEELLARIGIPTTLADLGVTEADLPGLAEKA 365
|
330 340
....*....|....*....|....*..
gi 1958777079 342 LPQERVTKLAPRAQSEEDLSALFEASM 368
Cdd:cd08191 366 LSVTRLIANNPRPPTEEDLLRILRAAF 392
|
|
| Fe-ADH-like |
cd08196 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
25-364 |
2.29e-62 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341475 [Multi-domain] Cd Length: 367 Bit Score: 203.96 E-value: 2.29e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 25 DAIEFAKKGAFDAYVAVGGGSTMDTCKAANLYACSPHSeFLDYvnapIGKGKPVTVPLKPLIAVPTTSGTGSETTGVAIF 104
Cdd:cd08196 74 KCARLARENGADFVIAIGGGSVLDTAKAAACLAKTDGS-IEDY----LEGKKKIPKKGLPLIAIPTTAGTGSEVTPVAVL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 105 DYEHLKVKTGIASRAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTAIpysmrspcpsnpiqrpayqGSNPISD 184
Cdd:cd08196 149 TDKEKGKKAPLVSPGFYPDIAIVDPELTYSMPPKVTASTGIDALCHAIEAYWSI-------------------NHQPISD 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 185 IWAVHALRIVAKYLKRAVRNPDDLEARSSMHLASAFAGIGFGNAGVHLCHGMSYPISglvktykaKEYNvdhplVPHGLS 264
Cdd:cd08196 210 ALALEAAKLVLENLEKAYNNPNDKEAREKMALASLLAGLAFSQTRTTASHACSYPLT--------SHFG-----IPHGEA 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 265 VVLTSPAVFTFTAQMFPERHLETAEILGANirtakiqDAGPvLADALRKFLFDLNVDDGLAALGYSKDDIPSLVKGTLPQ 344
Cdd:cd08196 277 CALTLPSFIRLNAEALPGRLDELAKQLGFK-------DAEE-LADKIEELKKRIGLRTRLSELGITEEDLEEIVEESFHP 348
|
330 340
....*....|....*....|
gi 1958777079 345 ERVtKLAPRAQSEEDLSALF 364
Cdd:cd08196 349 NRA-NNNPVEVTKEDLEKLL 367
|
|
| Fe-ADH-like |
cd17814 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
36-342 |
4.44e-55 |
|
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: 185.05 E-value: 4.44e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 36 DAYVAVGGGSTMDTCKAANLYAcSPHSEFLDYvnapIGKGKpVTVPLKPLIAVPTTSGTGSETTGVAIFDYEHLKVKTGI 115
Cdd:cd17814 85 DGIVAVGGGSPIDCAKGIGIVV-SNGGHILDY----EGVDK-VRRPLPPLICIPTTAGSSADVSQFAIITDTERRVKMAI 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 116 ASRAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTaipysmrspcpSNpiqrpayqGSNPISDIWAVHALRIVA 195
Cdd:cd17814 159 ISKTLVPDVSLIDPETLTTMDPELTACTGMDALTHAIEAYV-----------SN--------ASSPLTDLHALEAIRLIS 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 196 KYLKRAVRNPDDLEARSSMHLASAFAGIGFGNAGVHLCHGMSYPISGLvktykakeynVDhplVPHGLSVVLTSPAVFTF 275
Cdd:cd17814 220 ENLPKAVADPDDLEAREKMMLASLQAGLAFSNASLGAVHAMAHSLGGL----------LD---LPHGECNALLLPHVIRF 286
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958777079 276 TAQMFPERHLETAEILGANIRTAKIQDAGPVLADALRKFLFDLNVDDGLAALGYSKDDIPSLVKGTL 342
Cdd:cd17814 287 NFPAAPERYRKIAEAMGLDVDGLDDEEVAERLIEAIRDLREDLGIPETLSELGVDEEDIPELAKRAM 353
|
|
| Fe-ADH-like |
cd08194 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
24-366 |
1.45e-51 |
|
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: 175.80 E-value: 1.45e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 24 MDAIEFAKKGAFDAYVAVGGGSTMDTCKAANLYACSPhSEFLDYVNAPIGKGKPVtvplkPLIAVPTTSGTGSETTGVAI 103
Cdd:cd08194 70 EEGLALYKEGGCDFIVALGGGSPIDTAKAIAVLATNG-GPIRDYMGPRKVDKPGL-----PLIAIPTTAGTGSEVTRFTV 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 104 FDYEHLKVKTGIASRAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTaipySMRSpcpsnpiqrpayqgsNPIS 183
Cdd:cd08194 144 ITDTETDVKMLLKGPALLPAVAIVDPELTLSMPPRVTAATGIDALTHAIEAYV----SRKA---------------QPLT 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 184 DIWAVHALRIVAKYLKRAVRNPDDLEARSSMHLASAFAGIGFGNAGVHLCHGMSYPISGLVktykakeynvdHplVPHGL 263
Cdd:cd08194 205 DTLALSAIKLIGRNLRRAYADGDDLEAREAMMLAALEAGIAFSNSSVALVHGMSRPIGALF-----------H--VPHGL 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 264 SVVLTSPAVFTFTAQMFPERHLETAEILGANIRTAKIQDAGPVLADALRKFLFDLNVdDGLAALGYSKDD----IPSLVK 339
Cdd:cd08194 272 SNAMLLPAVTEFSLPGAPERYAEIARAMGIATEGDSDEEAAEKLVEALERLCADLEI-PTLREYGIDEEEfeaaLDKMAE 350
|
330 340 350
....*....|....*....|....*....|.
gi 1958777079 340 GTL----PQervtkLAPRAQSEEDLSALFEA 366
Cdd:cd08194 351 DALasgsPA-----NNPRVPTKEEIIELYRE 376
|
|
| LPO |
cd08176 |
Lactadehyde:propanediol oxidoreductase (LPO) catalyzes the interconversion between ... |
24-365 |
1.09e-49 |
|
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: 171.19 E-value: 1.09e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 24 MDAIEFAKKGAFDAYVAVGGGSTMDTCKAANLYACSPhseFLDyVNAPIGKgKPVTVPLKPLIAVPTTSGTGSETTGVA- 102
Cdd:cd08176 75 MAGVAAYKESGADGIIAVGGGSSIDTAKAIGIIVANP---GAD-VRSLEGV-APTKNPAVPIIAVPTTAGTGSEVTINYv 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 103 IFDYEHlKVKTGIASRAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTAipysmrspcpsnpiqrpayQGSNPI 182
Cdd:cd08176 150 ITDTEK-KRKFVCVDPHDIPTVAIVDPDLMSSMPKGLTAATGMDALTHAIEGYIT-------------------KGAWEL 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 183 SDIWAVHALRIVAKYLKRAVRNPDDLEARSSMHLASAFAGIGFGNAGVHLCHGMSYPISGLvktykakeYNvdhplVPHG 262
Cdd:cd08176 210 SDMLALKAIELIAKNLRKAVANPNNVEARENMALAQYIAGMAFSNVGLGIVHSMAHPLSAF--------YD-----TPHG 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 263 LSVVLTSPAVFTFTAQMFPERHLETAEILGANIRTAKIQDAGPVLADALRKFLFDLNVDDGLAALGYSKDDIPSLVKGTL 342
Cdd:cd08176 277 VANAILLPYVMEFNAPATGEKYRDIARAMGVDTTGMSDEEAAEAAVDAVKKLSKDVGIPQKLSELGVKEEDIEALAEDAL 356
|
330 340
....*....|....*....|...
gi 1958777079 343 pQERVTKLAPRAQSEEDLSALFE 365
Cdd:cd08176 357 -NDVCTPGNPREATKEDIIALYK 378
|
|
| Fe-ADH-like |
cd14862 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
24-364 |
1.38e-48 |
|
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: 168.17 E-value: 1.38e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 24 MDAIEFAKKGAFDAYVAVGGGSTMDTCKAANLYACSPHSEFLDYV-NAPIGKGKpvtvplKP-LIAVPTTSGTGSETTGV 101
Cdd:cd14862 71 LKGAEAMREFEPDLIIALGGGSVMDAAKAAWVLYERPDLDPEDISpLDLLGLRK------KAkLIAIPTTSGTGSEATWA 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 102 AIFDYEHLKVKTGIASRAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTAipysmrspcpsnpiqrpayQGSNP 181
Cdd:cd14862 145 IVLTDTEEPRKIAVANPELVPDVAILDPEFVLGMPPKLTAGTGLDALAHAVEAYLS-------------------TWSND 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 182 ISDIWAVHALRIVAKYLKRAVRNPDDLEARSSMHLASAFAGIGFGNAGVHLCHGMSYPISGLVKtykakeynvdhplVPH 261
Cdd:cd14862 206 FSDALALKAIELIFKYLPRAYKDGDDLEAREKMHNAATIAGLAFGNSQAGLAHALGHSLGAVFH-------------VPH 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 262 GLSVVLTSPAVFTFTAQmFPERHLETAEILGANIRTAKiqDAGPVLADALRKFLFDLNVDDGLAALGYSKDD----IPSL 337
Cdd:cd14862 273 GIAVGLFLPYVIEFYAK-VTDERYDLLKLLGIEARDEE--EALKKLVEAIRELYKEVGQPLSIKDLGISEEEfeekLDEL 349
|
330 340
....*....|....*....|....*..
gi 1958777079 338 VKGTLpQERVTKLAPRAQSEEDLSALF 364
Cdd:cd14862 350 VEYAM-EDSCTITSPRPPSEEDLKKLF 375
|
|
| Fe-ADH-like |
cd14865 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
26-368 |
2.29e-47 |
|
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: 165.02 E-value: 2.29e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 26 AIEFAKKGAfDAYVAVGGGSTMDTCKAANLYAcSPHSEFLDYVNapiGKGKpVTVPLKPLIAVPTTSGTGSETTGVAIFD 105
Cdd:cd14865 78 AARAREAGA-DGIIAVGGGSVIDTAKGVNILL-SEGGDDLDDYG---GANR-LTRPLKPLIAIPTTAGTGSEVTLVAVIK 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 106 YEHLKVKTGIASRAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTAIpysmrspcpsnpiqrpayqGSNPISDI 185
Cdd:cd14865 152 DEEKKVKLLFVSPFLLPDVAILDPRLTLSLPPKLTAATGMDALTHAIEAYTSL-------------------QKNPISDA 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 186 WAVHALRIVAKYLKRAVRNPDDLEARSSMHLASAFAGIGFGNAGVHLCHGMSYPISGLVKtykakeynvdhplVPHGL-- 263
Cdd:cd14865 213 LALQAIRLISENLPKAVKNGKDLEARLALAIAATMAGIAFSNSMVGLVHAIAHAVGAVAG-------------VPHGLan 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 264 SVVLtsPAVFTFTAQMFPERHLETAEIL--GANIRTAKIQDAGPVLADALRKFLFDLNVDDGLAALGYSKDDIPSLVKGT 341
Cdd:cd14865 280 SILL--PHVMRYNLDAAAERYAELALALayGVTPAGRRAEEAIEAAIDLVRRLHELCGLPTRLRDVGVPEEQLEAIAELA 357
|
330 340
....*....|....*....|....*..
gi 1958777079 342 LpQERVTKLAPRAQSEEDLSALFEASM 368
Cdd:cd14865 358 L-NDGAILFNPREVDPEDILAILEAAY 383
|
|
| Fe-ADH-like |
cd08183 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
24-365 |
1.14e-44 |
|
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: 157.66 E-value: 1.14e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 24 MDAIEFAKKGAFDAYVAVGGGSTMDTCKAANLYACSPHS--EFLDYVnapiGKGKPVTVPLKPLIAVPTtsgtgsettgV 101
Cdd:cd08183 68 DAAVALAREAGCDVVIAIGGGSVIDAAKAIAALLTNEGSvlDYLEVV----GKGRPLTEPPLPFIAIPT----------T 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 102 A-----------IFDYEHlKVKTGIASRAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTAIpysmrspcpsnp 170
Cdd:cd08183 134 AgtgsevtknavLSSPEH-GVKVSLRSPSMLPDVALVDPELTLSLPPEVTAASGLDALTQLIEPYVSR------------ 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 171 iqrpayqGSNPISDIWAVHALRIVAKYLKRAVRNPDDLEARSSMHLASAFAGIGFGNAGVHLCHGMSYPISGLVKtykak 250
Cdd:cd08183 201 -------KANPLTDALAREGLRLAARSLRRAYEDGEDLEAREDMALASLLGGLALANAGLGAVHGLAGPLGGMFG----- 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 251 eynvdhplVPHGL--SVVLtsPAVFTFTAQM----FPERHLETAEILGANIRTAKIQDAGPVLADALRKFLFDLNVdDGL 324
Cdd:cd08183 269 --------APHGAicAALL--PPVLEANLRAlrerEPDSPALARYRELAGILTGDPDAAAEDGVEWLEELCEELGI-PRL 337
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1958777079 325 AALGYSKDDIPSLVKGTLpQERVTKLAPRAQSEEDLSALFE 365
Cdd:cd08183 338 SEYGLTEEDFPEIVEKAR-GSSSMKGNPIELSDEELLEILE 377
|
|
| PDDH |
cd08188 |
1,3-Propanediol (1,3-PD) dehydrogenase; This family includes 1,3-propanediol (1,3-PD) ... |
24-365 |
2.60e-44 |
|
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: 156.91 E-value: 2.60e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 24 MDAIEFAKKGAFDAYVAVGGGSTMDTCKAANLYACSPhSEFLDYVNapIGKgkpVTVPLKPLIAVPTTSGTGSETTGVAI 103
Cdd:cd08188 75 NEGLELFKENGCDFIISVGGGSAHDCAKAIGILATNG-GEIEDYEG--VDK---SKKPGLPLIAINTTAGTASEVTRFAV 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 104 FDYEHLKVKTGIASRAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTAIpysmrspcpsnpiqrpayqGSNPIS 183
Cdd:cd08188 149 ITDEERHVKMVIVDWNVTPTIAVNDPELMLGMPPSLTAATGMDALTHAIEAYVST-------------------GATPLT 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 184 DIWAVHALRIVAKYLKRAVRNPDDLEARSSMHLASAFAGIGFGNAGVHLCHGMSYPISGLvktykakeYNvdhplVPHGL 263
Cdd:cd08188 210 DALALEAIRLIAENLPKAVANGKDLEARENMAYAQFLAGMAFNNAGLGYVHAMAHQLGGF--------YN-----LPHGV 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 264 --SVVLtsPAVFTFTAQMFPERHLETAEILGANIRTAKIQDAGPVLADALRKFLFDLNVDDGLAALGYSKDDIPSLVKGT 341
Cdd:cd08188 277 cnAILL--PHVMEFNLPACPERFADIARALGENTEGLSDEEAAEAAIEAIRKLSRRVGIPSGLKELGVKEEDFPLLAENA 354
|
330 340
....*....|....*....|....
gi 1958777079 342 LpQERVTKLAPRAQSEEDLSALFE 365
Cdd:cd08188 355 L-KDACGPTNPRQATKEDVIAIYR 377
|
|
| HEPD |
cd08182 |
Hydroxyethylphosphoate dehydrogenase (HEPD) catalyzes the reduction of phosphonoacetaldehyde ... |
25-365 |
2.71e-44 |
|
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: 156.62 E-value: 2.71e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 25 DAIEFAKKGAFDAYVAVGGGSTMDTCKAANLYACSPHSEFLdyvnAPIGKGKPVTVPLKPLIAVPTtsgtgsettgVA-- 102
Cdd:cd08182 70 RGIELFRESGPDVIIAVGGGSVIDTAKAIAALLGSPGENLL----LLRTGEKAPEENALPLIAIPT----------TAgt 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 103 ---------IFDyEHLKVKTGIASRAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTAIpysmrspcpsnpiqr 173
Cdd:cd08182 136 gsevtpfatIWD-EAEGKKYSLAHPSLYPDAAILDPELTLSLPLYLTASTGLDALSHAIESIWSV--------------- 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 174 payqGSNPISDIWAVHALRIVAKYLKRAVRNPDDLEARSSMHLASAFAGIGFGNAGVHLCHGMSYPISglvktykaKEYN 253
Cdd:cd08182 200 ----NANPESRAYALRAIRLILENLPLLLENLPNLEAREAMAEASLLAGLAISITKTTAAHAISYPLT--------SRYG 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 254 vdhplVPHGLSVVLTSPAVFTFTAQMFPERhleTAEILGANIRTAKIQDAGPVLADALRKFLFDLNVDDGLAALGYSKDD 333
Cdd:cd08182 268 -----VPHGHACALTLPAVLRYNAGADDEC---DDDPRGREILLALGASDPAEAAERLRALLESLGLPTRLSEYGVTAED 339
|
330 340 350
....*....|....*....|....*....|..
gi 1958777079 334 IPSLVKGTLPQERVtKLAPRAQSEEDLSALFE 365
Cdd:cd08182 340 LEALAASVNTPERL-KNNPVRLSEEDLLRLLE 370
|
|
| NADPH_BDH |
cd08179 |
NADPH-dependent butanol dehydrogenase involved in the butanol and ethanol formation pathway in ... |
24-366 |
2.49e-43 |
|
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: 154.27 E-value: 2.49e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 24 MDAIEFAKKGAFDAYVAVGGGSTMDTCKAANLYACSPHSEFLDYVnapigkgKPVTVPLKP----LIAVPTTSGTGSETT 99
Cdd:cd08179 71 EKGAEAMREFEPDWIIAIGGGSVIDAAKAMWVFYEYPELTFEDAL-------VPFPLPELRkkarFIAIPSTSGTGSEVT 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 100 GVAIF-DYEHlKVKTGIASRAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTAIPysmrspcpsnpiqrpayqg 178
Cdd:cd08179 144 RASVItDTEK-GIKYPLASFEITPDVAILDPELTMTMPPHVTANTGMDALTHAIEAYVSTL------------------- 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 179 SNPISDIWAVHALRIVAKYLKRAVRNPDDLEARSSMHLASAFAGIGFGNAGVHLCHGMSYPISGlvktykakEYNvdhpl 258
Cdd:cd08179 204 ANDFTDALALGAILDIFENLPKSYNGGKDLEAREKMHNASCLAGMAFSNSGLGIVHSMAHKGGA--------FFG----- 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 259 VPHGL--SVVLtsPAVFTFTAQMFPERHLETAEILGANiRTAKIQDagpvLADALRKFLFDLNVDDGLAALGYSKDD--- 333
Cdd:cd08179 271 IPHGLanAILL--PYVIEFNSKDPEARARYAALLIGLT-DEELVED----LIEAIEELNKKLGIPLSFKEAGIDEDEffa 343
|
330 340 350
....*....|....*....|....*....|....
gi 1958777079 334 -IPSLVKGTLpQERVTKLAPRAQSEEDLSALFEA 366
Cdd:cd08179 344 kLDEMAENAM-NDACTGTNPRKPTVEEMKELLKA 376
|
|
| HVD |
cd08193 |
5-hydroxyvalerate dehydrogenase (HVD) catalyzes the oxidation of 5-hydroxyvalerate to ... |
25-366 |
4.86e-41 |
|
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: 148.04 E-value: 4.86e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 25 DAIEFAKKGAFDAYVAVGGGSTMDTCKAANLYACSPHSefldyVNAPIGKGKpVTVPLKPLIAVPTTSGTGSETTGVAIF 104
Cdd:cd08193 74 AAVEQAREAGADGVIGFGGGSSMDVAKLVALLAGSDQP-----LDDIYGVGK-ATGPRLPLILVPTTAGTGSEVTPISIV 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 105 -DYEHLKvkTGIASRAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTAipysmRSpcpsnpiqrpayqGSNPIS 183
Cdd:cd08193 148 tTGETEK--KGVVSPQLLPDVALLDAELTLGLPPHVTAATGIDAMVHAIEAYTS-----RH-------------KKNPIS 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 184 DIWAVHALRIVAKYLKRAVRNPDDLEARSSMHLASAFAGIGFGNAGVHLCHGMSYPISGLVKtykakeynvdhplVPHGL 263
Cdd:cd08193 208 DALAREALRLLGANLRRAVEDGSDLEAREAMLLGSMLAGQAFANAPVAAVHALAYPLGGHFH-------------VPHGL 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 264 SVVLTSPAVFTFTAQMFPERHLETAEILGANIRTAKIQDAGPVLADALRKFLFDLNVDDGLAALGYSKDDIPSLVKGTLP 343
Cdd:cd08193 275 SNALVLPHVLRFNLPAAEALYAELARALLPGLAFGSDAAAAEAFIDALEELVEASGLPTRLRDVGVTEEDLPMLAEDAMK 354
|
330 340
....*....|....*....|...
gi 1958777079 344 QERVTKLAPRAQSEEDLSALFEA 366
Cdd:cd08193 355 QTRLLVNNPREVTEEDALAIYQA 377
|
|
| Fe-ADH-like |
cd14861 |
Iron-containing alcohol dehydrogenases-like; This family contains proteins similar to ... |
24-368 |
2.48e-38 |
|
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: 140.72 E-value: 2.48e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 24 MDAIEFAKKGAFDAYVAVGGGSTMDTCKAANLYACSPHSEFlDYVNAPIGkGKPVTVPLKPLIAVPTTSGTGSETTGVAI 103
Cdd:cd14861 72 EAGVAAYREGGCDGIIALGGGSAIDAAKAIALMATHPGPLW-DYEDGEGG-PAAITPAVPPLIAIPTTAGTGSEVGRAAV 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 104 FDYEHLKVKTGIASRAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTAIPYsmrspcpsnpiqrpayqgsNPIS 183
Cdd:cd14861 150 ITDDDTGRKKIIFSPKLLPKVAICDPELTLGLPPRLTAATGMDALTHCIEAYLSPGF-------------------HPMA 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 184 DIWAVHALRIVAKYLKRAVRNPDDLEARSSMHLASAFAGIGFGNaGVHLCHGMSYPISGLVKTykakeynvdhplvPHGL 263
Cdd:cd14861 211 DGIALEGLRLISEWLPRAVADGSDLEARGEMMMAALMGAVAFQK-GLGAVHALAHALGALYGL-------------HHGL 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 264 SVVLTSPAVFTFTAQMFPERHLETAEILGANIRTAkiqDAgpvLADALRKFLFDLNVDDGLAALGYSKDDIPSLVKGTLp 343
Cdd:cd14861 277 LNAILLPYVLRFNRPAVEDKLARLARALGLGLGGF---DD---FIAWVEDLNERLGLPATLSELGVTEDDLDELAELAL- 349
|
330 340
....*....|....*....|....*
gi 1958777079 344 QERVTKLAPRAQSEEDLSALFEASM 368
Cdd:cd14861 350 ADPCHATNPRPVTAEDYRALLREAL 374
|
|
| PPD-like |
cd08181 |
1,3-propanediol dehydrogenase-like (PPD); This family contains proteins similar to 1, ... |
24-365 |
1.18e-37 |
|
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: 138.49 E-value: 1.18e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 24 MDAIEFAKKGAFDAYVAVGGGSTMDTCKAANLYACSP-HSEFLDYVNAPigkGKPVtvplkPLIAVPTTSGTGSETTGVA 102
Cdd:cd08181 73 EKGAELARKEGADFVIGIGGGSPLDAAKAIALLAANKdGDEDLFQNGKY---NPPL-----PIVAIPTTAGTGSEVTPYS 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 103 IFDYEHLKVKTGIASRAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYtaipYSMRspcpsnpiqrpayqgSNPI 182
Cdd:cd08181 145 ILTDHEKGTKKSFGNPLIFPKLALLDPKYTLSLPEELTIDTAVDALSHAIEGY----LSVK---------------ATPL 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 183 SDIWAVHALRIVAKYLKRAVRNPDDLEARSSMHLASAFAGIGFGNAGVHLCHGMSYPIsglvkTYkakEYNvdhplVPHG 262
Cdd:cd08181 206 SDALALEALRLIGECLPNLLGDELDEEDREKLMYASTLAGMVIAQTGTTLPHGLGYPL-----TY---FKG-----IPHG 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 263 LSVVLTSPAVFTFTAQMFPERHLETAEILGANIrtakiqdagpvlADALRKFLFDLNVDDGLaalgYSKDDIPSLVKGTL 342
Cdd:cd08181 273 RANGILLPAYLKLCEKQEPEKVDKILKLLGFGS------------IEEFQKFLNRLLGKKEE----LSEEELEKYADEAM 336
|
330 340
....*....|....*....|...
gi 1958777079 343 PQERVtKLAPRAQSEEDLSALFE 365
Cdd:cd08181 337 KAKNK-KNTPGNVTKEDILRIYR 358
|
|
| PDD |
cd08180 |
1,3-propanediol dehydrogenase (PPD) catalyzes the reduction of 3-hydroxypropionaldehyde (3-HPA) ... |
24-365 |
7.95e-36 |
|
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: 133.00 E-value: 7.95e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 24 MDAIEFAKKGAFDAYVAVGGGSTMDTCKAANLYacsphsefldYVNAPIGKGKPvtvplkPLIAVPTTSGTGSETTGVA- 102
Cdd:cd08180 68 AKGLAKILEFKPDTIIALGGGSAIDAAKAIIYF----------ALKQKGNIKKP------LFIAIPTTSGTGSEVTSFAv 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 103 IFDYEHlKVKTGIASRAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTAIpysmrspcpsnpiqrpayqGSNPI 182
Cdd:cd08180 132 ITDPEK-GIKYPLVDDSMLPDIAILDPELVKSVPPKVTADTGMDVLTHALEAYVST-------------------NANDF 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 183 SDIWAVHALRIVAKYLKRAVRNPDDLEARSSMHLASAFAGIGFGNAGVHLCHGMSYPISGLVKtykakeynvdhplVPHG 262
Cdd:cd08180 192 TDALAEKAIKLVFENLPRAYRDGDDLEAREKMHNASCMAGIAFNNAGLGINHSLAHALGGRFH-------------IPHG 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 263 LSVVLTSPAVFTFtaqmfperhletaeilganirtakiqdagpvLADALRKFLFDLNVDDGLAALGYSKDD----IPSLV 338
Cdd:cd08180 259 RANAILLPYVIEF-------------------------------LIAAIRRLNKKLGIPSTLKELGIDEEEfekaIDEMA 307
|
330 340
....*....|....*....|....*..
gi 1958777079 339 KGTLpQERVTKLAPRAQSEEDLSALFE 365
Cdd:cd08180 308 EAAL-ADRCTATNPRKPTAEDLIELLR 333
|
|
| Fe-ADH-like |
cd08186 |
Iron-containing alcohol dehydrogenase; This family contains iron-containing alcohol ... |
25-368 |
1.21e-34 |
|
Iron-containing alcohol dehydrogenase; This family contains iron-containing alcohol dehydrogenase (ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. The ADH of hyperthermophilic archaeon Thermococcus hydrothermalis oxidizes a series of primary aliphatic and aromatic alcohols, preferentially from C2 to C8, but is also active towards methanol and glycerol, and is stereospecific for monoterpenes. It has been suggested that the type III ADHs in microorganisms are involved in acetaldehyde detoxication rather than in alcohol turnover.
Pssm-ID: 341465 [Multi-domain] Cd Length: 380 Bit Score: 131.23 E-value: 1.21e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 25 DAIEFAKKGAFDAYVAVGGGSTMDTCKAANLYACSPHS---EFLDYVNAPIGKgkpvtvplKPLIAVPTTSGTGSETTGV 101
Cdd:cd08186 72 EAAKLARDFGADAVIAIGGGSPIDTAKSVAVLLAYGGKtarDLYGFRFAPERA--------LPLVAINLTHGTGSEVDRF 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 102 AIFDYEHLKVKTGIASRAIKPTLGLVDPLHTLHMPC-QVVANSgFDVLCHALESYTAipysmrspcpsnpiqrpayQGSN 180
Cdd:cd08186 144 AVATIPEKGYKPGIAYDCIYPLYAIDDPRLTLTLPKeQTLYTS-IDAFNHVYEAATT-------------------KVSS 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 181 PISDIWAVHALRIVAKYLKRAVRNPDDLEARSSMHLASAFAGIGFGNAGVHLCHGMSYPISGLVktykakeynvdhPLVP 260
Cdd:cd08186 204 PYVITLAKEAIRLIAEYLPRALANPKDLEARYWLLYASMIAGIAIDNGLLHLTHALEHPLSGLK------------PELP 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 261 HGLSVVLTSPAVFTFTAQMFPErhlETAEIL-----GANIRTAKIQDAgpvlADALRKFLFDLNVDDGLAALGYSKDDIP 335
Cdd:cd08186 272 HGLGLALLGPAVVKYIYKAVPE---TLADILrpivpGLKGTPDEAEKA----ARGVEEFLFSVGFTEKLSDYGFTEDDVD 344
|
330 340 350
....*....|....*....|....*....|....*.
gi 1958777079 336 SLVK---GTLPQERVTKLAPRAQSEEDLSALFEASM 368
Cdd:cd08186 345 RLVElafTTPSLDLLLSLAPVEVTEEVVREIYEESL 380
|
|
| AAD_C |
cd08178 |
C-terminal alcohol dehydrogenase domain of the acetaldehyde dehydrogenase-alcohol ... |
36-333 |
2.40e-31 |
|
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: 122.30 E-value: 2.40e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 36 DAYVAVGGGSTMDTCKAANL-YAC------SPHSEFLD-----YVNAPIGKGKPvtvplkpLIAVPTTSGTGSETTGVA- 102
Cdd:cd08178 82 DVIIALGGGSAMDAAKIMWLfYEHpetkfeDLAQRFMDirkrvYKFPKLGKKAK-------LVAIPTTSGTGSEVTPFAv 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 103 IFDyEHLKVKTGIASRAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTAIPysmrspcpsnpiqrpayqgSNPI 182
Cdd:cd08178 155 ITD-DKTGKKYPLADYALTPDMAIVDPELVMTMPKRLTADTGIDALTHAIEAYVSVM-------------------ASDY 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 183 SDIWAVHALRIVAKYLKRAVRNPDDLEARSSMHLASAFAGIGFGNAGVHLCHGMSYPISGlvktykakEYNvdhplVPHG 262
Cdd:cd08178 215 TDGLALQAIKLIFEYLPRSYNNGNDIEAREKMHNAATIAGMAFANAFLGICHSLAHKLGA--------AFH-----IPHG 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 263 LSVVLTSPAVFTFTAQ-------MFP--------ERHLETAEILG--ANIRTAKIQdagpVLADALRKFLFDLNVDDGLA 325
Cdd:cd08178 282 RANAILLPHVIRYNATdpptkqaAFPqykyyvakERYAEIADLLGlgGKTPEEKVE----SLIKAIEDLKKDLGIPTSIR 357
|
....*...
gi 1958777079 326 ALGYSKDD 333
Cdd:cd08178 358 EAGIDEAD 365
|
|
| PRK10624 |
PRK10624 |
L-1,2-propanediol oxidoreductase; Provisional |
29-368 |
3.07e-30 |
|
L-1,2-propanediol oxidoreductase; Provisional
Pssm-ID: 182595 [Multi-domain] Cd Length: 382 Bit Score: 118.95 E-value: 3.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 29 FAKKGAfDAYVAVGGGSTMDTCKAANLYACSPhsEFLDYVN----APIGKgkpvtvPLKPLIAVPTTS-GTGSETTGVAI 103
Cdd:PRK10624 83 FKASGA-DYLIAIGGGSPQDTCKAIGIISNNP--EFADVRSlegvAPTKK------PSVPIIAIPTTAgTAAEVTINYVI 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 104 FDYEHLKVKTGIASRAIkPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTAipysmrspcpsnpiqrpayQGSNPIS 183
Cdd:PRK10624 154 TDEEKRRKFVCVDPHDI-PQVAFVDADMMDSMPPGLKAATGVDALTHAIEGYIT-------------------RGAWALT 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 184 DIWAVHALRIVAKYLKRAVRNpdDLEARSSMHLASAFAGIGFGNAGVHLCHGMSYPISGLvktykakeYNvdhplVPHGL 263
Cdd:PRK10624 214 DMLHLKAIEIIAGALRGAVAG--DKEAGEGMALGQYIAGMGFSNVGLGLVHGMAHPLGAF--------YN-----TPHGV 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 264 SVVLTSPAVFTFTAQMFPERHLETAEILGANIRTAKIQDAGPVLADALRKFLFDLNVDDGLAALGYSKDDIPSLVKGTLp 343
Cdd:PRK10624 279 ANAILLPHVMEYNADFTGEKYRDIARAMGVKVEGMSLEEARNAAVEAVKALNRDVGIPPHLRDVGVKEEDIPALAQAAF- 357
|
330 340
....*....|....*....|....*
gi 1958777079 344 QERVTKLAPRAQSEEDLSALFEASM 368
Cdd:PRK10624 358 DDVCTGGNPREATLEDIVELYKKAW 382
|
|
| BDH |
cd08187 |
Butanol dehydrogenase catalyzes the conversion of butyraldehyde to butanol with the cofactor ... |
24-339 |
8.53e-30 |
|
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: 117.92 E-value: 8.53e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 24 MDAIEFAKKGAFDAYVAVGGGSTMDTCKAANLYACSPHsEFLDYVNapigKGKPVTVPLkPLIAVPTTSGTGSETTGVAI 103
Cdd:cd08187 76 REGIELAREENVDFILAVGGGSVIDAAKAIAAGAKYDG-DVWDFFT----GKAPPEKAL-PVGTVLTLAATGSEMNGGAV 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 104 FDYEHLKVKTGIASRAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESY-TaipysmrspcpsnpiqrpaYQGSNPI 182
Cdd:cd08187 150 ITNEETKEKLGFGSPLLRPKFSILDPELTYTLPKYQTAAGIVDIFSHVLEQYfT-------------------GTEDAPL 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 183 SDIWAVHALRIVAKYLKRAVRNPDDLEARSSMHLASAFA--GI-GFGNAGVHLCHGMSYPISGLvktykakeYNVDHplv 259
Cdd:cd08187 211 QDRLAEGLLRTVIENGPKALKDPDDYEARANLMWAATLAlnGLlGAGRGGDWATHAIEHELSAL--------YDITH--- 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 260 PHGLSVVLtsPAVFTFTAQMFPERHLETAE-ILGanIRTAKIQDAGPVLA-DALRKFLFDLNVDDGLAALGYSKDDIPSL 337
Cdd:cd08187 280 GAGLAIVF--PAWMRYVLKKKPERFAQFARrVFG--IDPGGDDEETALEGiEALEEFFKSIGLPTTLSELGIDEEDIEEM 355
|
..
gi 1958777079 338 VK 339
Cdd:cd08187 356 AE 357
|
|
| PRK13805 |
PRK13805 |
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional |
27-333 |
1.05e-28 |
|
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional
Pssm-ID: 237515 [Multi-domain] Cd Length: 862 Bit Score: 117.59 E-value: 1.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 27 IEFAKKGA-----F--DAYVAVGGGSTMDTCKAANLYACSPHSEFLD------------YVNAPIG-KGKPVTVP----- 81
Cdd:PRK13805 525 LSTVRKGAelmrsFkpDTIIALGGGSPMDAAKIMWLFYEHPETDFEDlaqkfmdirkriYKFPKLGkKAKLVAIPttsgt 604
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 82 ---LKPlIAVpttsgtgsettgvaIFDyEHLKVKTGIASRAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTAI 158
Cdd:PRK13805 605 gseVTP-FAV--------------ITD-DKTGVKYPLADYELTPDVAIVDPNLVMTMPKSLTADTGIDALTHALEAYVSV 668
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 159 pysMrspcpsnpiqrpayqgSNPISDIWAVHALRIVAKYLKRAVRN-PDDLEARSSMHLASAFAGIGFGNAGVHLCHGMS 237
Cdd:PRK13805 669 ---M----------------ASDYTDGLALQAIKLVFEYLPRSYKNgAKDPEAREKMHNASTIAGMAFANAFLGICHSMA 729
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 238 YPISGlvktykakEYNvdhplVPHGLSVVLTSPAVFTFTAQ------MFP--------ERHLETAEILG--ANIRTAKIQ 301
Cdd:PRK13805 730 HKLGA--------EFH-----IPHGRANAILLPHVIRYNATdppkqaAFPqyeypradERYAEIARHLGlpGSTTEEKVE 796
|
330 340 350
....*....|....*....|....*....|..
gi 1958777079 302 dagpVLADALRKFLFDLNVDDGLAALGYSKDD 333
Cdd:PRK13805 797 ----SLIKAIEELKAELGIPMSIKEAGVDEAD 824
|
|
| Fe-ADH-like |
cd08189 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
25-339 |
5.36e-28 |
|
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: 112.95 E-value: 5.36e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 25 DAIEFAKKGAFDAYVAVGGGSTMDTCKAANLYACSPHSEFLDYVnapiGKGKpVTVPLKPLIAVPTtsgtgsettgVA-- 102
Cdd:cd08189 75 EGLALYKENGCDAIIAIGGGSVIDCAKVIAARAANPKKSVRKLK----GLLK-VRKKLPPLIAVPT----------TAgt 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 103 ---------IFDYEHlKVKTGIASRAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTAIPYsmrspcpsnpiqr 173
Cdd:cd08189 140 gseatiaavITDPET-HEKYAINDPKLIPDAAVLDPELTLGLPPAITAATGMDALTHAVEAYISRSA------------- 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 174 payqgsNPISDIWAVHALRIVAKYLKRAVRNPDDLEARSSMHLASAFAGIGFGNAGVHLCHGMSYPISGLvktykakeYN 253
Cdd:cd08189 206 ------TKETDEYALEAVKLIFENLPKAYEDGSDLEARENMLLASYYAGLAFTRAYVGYVHAIAHQLGGL--------YG 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 254 vdhplVPHGL--SVVLtsPAVFTFTAQMFPERHLETAEILGanIRTAKIQDAgpVLADALRKFLFDLNVD----DGLAAL 327
Cdd:cd08189 272 -----VPHGLanAVVL--PHVLEFYGPAAEKRLAELADAAG--LGDSGESDS--EKAEAFIAAIRELNRRmgipTTLEEL 340
|
330
....*....|..
gi 1958777079 328 gySKDDIPSLVK 339
Cdd:cd08189 341 --KEEDIPEIAK 350
|
|
| Fe-ADH-like |
cd14864 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
26-366 |
1.05e-27 |
|
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: 112.01 E-value: 1.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 26 AIEFAKKGAFDAYVAVGGGSTMDTCKAANLYACSPHsEFLDYVNAPIGKGKPVtvplkPLIAVPTTSGTGSETTGVAIF- 104
Cdd:cd14864 74 AAELARKAGADGIIAVGGGKVLDTAKAVAILANNDG-GAYDFLEGAKPKKKPL-----PLIAVPTTPRSGFEFSDRFPVv 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 105 DYEHLKVKTgIASRAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTAipysmrspcpsnpiqrpayQGSNPISD 184
Cdd:cd14864 148 DSRSREVKL-LKAQPGLPKAVIVDPNLMASLTGNQTAAMALAALALAVEAYLS-------------------KKSNFFSD 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 185 IWAVHALRIVAKYLKRAVRNPDDLEARSSMHLASAFAGIGFGNAGVHLCHGMSYPISGLvktykakeYNVDHPLVphgLS 264
Cdd:cd14864 208 ALALKAIELVSENLDGALADPKNTPAEELLAQAGCLAGLAASSSSPGLATALALAVNSR--------YKVSKSLV---AS 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 265 VVLtsPAVFTFTAQMFPERHLETAEILGANIRTAKIQDAGPVLADALRKFLFDLNVDDGLAALG--YSKDDIPSLVKgtl 342
Cdd:cd14864 277 ILL--PHVIEYAATSAPDKYAKIARALGEDVEGASPEEAAIAAVEGVRRLIAQLNLPTRLKDLDlaSSLEQLAAIAE--- 351
|
330 340
....*....|....*....|....
gi 1958777079 343 pQERVTKLAPRAQSEEDLSALFEA 366
Cdd:cd14864 352 -DAPKLNGLPRSMSSDDIFDILKA 374
|
|
| PRK15454 |
PRK15454 |
ethanolamine utilization ethanol dehydrogenase EutG; |
22-367 |
2.38e-26 |
|
ethanolamine utilization ethanol dehydrogenase EutG;
Pssm-ID: 185351 [Multi-domain] Cd Length: 395 Bit Score: 108.58 E-value: 2.38e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 22 CFMD---AIEFAKKGAFDAYVAVGGGSTMDTCKAANLYACSPHSEFLDYVNapigkgKPVTVPLKPLIAVPTTSGTGSET 98
Cdd:PRK15454 91 CITDvcaAVAQLRESGCDGVIAFGGGSVLDAAKAVALLVTNPDSTLAEMSE------TSVLQPRLPLIAIPTTAGTGSET 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 99 TGVAIFDYEHLKVKTGIASRAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTAIpysmrspcpsnpiqrpayqG 178
Cdd:PRK15454 165 TNVTVIIDAVSGRKQVLAHASLMPDVAILDAALTEGVPSHVTAMTGIDALTHAIEAYSAL-------------------N 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 179 SNPISDIWAVHALRIVAKYLKRAVRNPDDLEARSSMHLASAFAGIGFGNAGVHLCHGMSY-PISGLvktykakeynvdHp 257
Cdd:PRK15454 226 ATPFTDSLAIGAIAMIGKSLPKAVGYGHDLAARESMLLASCMAGMAFSSAGLGLCHAMAHqPGAAL------------H- 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 258 lVPHGLSVVLTSPAVFTFTAQMFPERHLEtaeiLGANIRTAKIQDAGPVlaDALRKFLFDLNVDDGLAALGYSKDDIPSL 337
Cdd:PRK15454 293 -IPHGLANAMLLPTVMEFNRMVCRERFSQ----IGRALRTKKSDDRDAI--NAVSELIAEVGIGKRLGDVGATSAHYGAW 365
|
330 340 350
....*....|....*....|....*....|
gi 1958777079 338 VKGTLpQERVTKLAPRAQSEEDLSALFEAS 367
Cdd:PRK15454 366 AQAAL-EDICLRSNPRTASLEQIVGLYAAA 394
|
|
| PRK09860 |
PRK09860 |
putative alcohol dehydrogenase; Provisional |
36-368 |
2.89e-25 |
|
putative alcohol dehydrogenase; Provisional
Pssm-ID: 182118 [Multi-domain] Cd Length: 383 Bit Score: 105.42 E-value: 2.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 36 DAYVAVGGGSTMDTCKAANLYACSpHSEFLDYVNAPIGKGkpvtvPLKPLIAVPTTSGTGSETTGVAIFDYEHLKVKTGI 115
Cdd:PRK09860 90 DSVISLGGGSPHDCAKGIALVAAN-GGDIRDYEGVDRSAK-----PQLPMIAINTTAGTASEMTRFCIITDEARHIKMAI 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 116 ASRAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTAIpysmrspcpsnpiqrpayqGSNPISDIWAVHALRIVA 195
Cdd:PRK09860 164 VDKHVTPLLSVNDSSLMIGMPKSLTAATGMDALTHAIEAYVSI-------------------AATPITDACALKAVTMIA 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 196 KYLKRAVRNPDDLEARSSMHLASAFAGIGFGNAGVHLCHGMSYPISGLvktykakeYNvdhplVPHGLSVVLTSPAVFTF 275
Cdd:PRK09860 225 ENLPLAVEDGSNAKAREAMAYAQFLAGMAFNNASLGYVHAMAHQLGGF--------YN-----LPHGVCNAVLLPHVQVF 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 276 TAQMFPERHLETAEILGANIRTAKIQDAGPVLADALRKFLFDLNVDDGLAALGYSKDDIPSLVKGTLpQERVTKLAPRAQ 355
Cdd:PRK09860 292 NSKVAAARLRDCAAAMGVNVTGKNDAEGAEACINAIRELAKKVDIPAGLRDLNVKEEDFAVLATNAL-KDACGFTNPIQA 370
|
330
....*....|...
gi 1958777079 356 SEEDLSALFEASM 368
Cdd:PRK09860 371 THEEIVAIYRAAM 383
|
|
| 4HBD_NAD |
cd14860 |
4-hydroxybutyrate dehydrogenase, also called gamma-hydroxybutyrate dehydrogenase, catalyzes ... |
24-371 |
1.77e-24 |
|
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: 103.06 E-value: 1.77e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 24 MDAI-EFAKKGAFDAYVAVGGGSTMDTCKaanLYACSPHSEFLDYV--NAPIGKGKPvtvplkpLIAVPTTSGTGSETTG 100
Cdd:cd14860 67 VEAIyKDIKKYGYKRVIAIGGGTVIDIAK---LLALKGISPVLDLFdgKIPLIKEKE-------LIIVPTTCGTGSEVTN 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 101 VAIFDYEHLKVKTGIASRAIKPTLGLVDP--LHTLhmPCQVVANSGFDVLCHALESYTaipysmrSPcpsnpiqrpayqG 178
Cdd:cd14860 137 ISIVELTSLGTKKGLAVDELYADKAVLIPelLKGL--PYKVFATSSIDALIHAIESYL-------SP------------K 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 179 SNPISDIWAVHALR-IVAKYLKRAVRNPDDL-EARSSMHLASAFAGIGFGNAGVHLCHGMSYPISGlvkTYKakeynvdh 256
Cdd:cd14860 196 ATPYTEMFSYKAIEmILEGYQEIAEKGEEARfPLLGDFLIASNYAGIAFGNAGCAAVHALSYPLGG---KYH-------- 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 257 plVPHGLSVVltspAVFTFTAQMFpERHLETAEILGANIRTAKIQDAGPVLA-DALRKFLFDLNVDDGLAALGYSKDDIP 335
Cdd:cd14860 265 --VPHGEANY----AVFTGVLKNY-QEKNPDGEIKKLNEFLAKILGCDEEDVyDELEELLNKILPKKPLHEYGMKEEEID 337
|
330 340 350
....*....|....*....|....*....|....*..
gi 1958777079 336 SLVKGTLP-QERVTKLAPRAQSEEDLSALFeasMKLY 371
Cdd:cd14860 338 EFADSVMEnQQRLLANNYVPLDREDVAEIY---KELY 371
|
|
| MAR-like |
cd08192 |
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic ... |
20-366 |
5.37e-24 |
|
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: 101.56 E-value: 5.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 20 WACFMDAIEFAKKGAFDAYVAVGGGSTMDTCKAANLyaCSPH----SEFLDYVNAPIGKGKPVTVPLKPLIAVPTTSGTG 95
Cdd:cd08192 65 REDVLEAARAVREAGADLLVSLGGGSPIDAAKAVAL--ALAEdvtdVDQLDALEDGKRIDPNVTGPTLPHIAIPTTLSGA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 96 SETTGVAIFDyEHLKVKTGIASRAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYtaipYSMRSpcpsnpiqrpa 175
Cdd:cd08192 143 EFTAGAGATD-DDTGHKQGFAHPELGPDAVILDPELTLHTPERLWLSTGIRAVDHAVETL----CSPQA----------- 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 176 yqgsNPISDIWAVHALRIVAKYLKRAVRNPDDLEARSSMHLASAFAGIGFGN-AGVHLCHGMSYPISGLvktykakeYNv 254
Cdd:cd08192 207 ----TPFVDALALKALRLLFEGLPRSKADPEDLEARLKCQLAAWLSLFGLGSgVPMGASHAIGHQLGPL--------YG- 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 255 dhplVPHGLSVVLTSPAVFTFTAQMFPERHLETAEILGANIRTAKIQDAGpvLADALRKFLFDLNVDDGLAALGYSKDDI 334
Cdd:cd08192 274 ----VPHGITSCIMLPAVLRFNAPVNAERQRLIARALGLVTGGLGREAAD--AADAIDALIRELGLPRTLRDVGVGRDQL 347
|
330 340 350
....*....|....*....|....*....|..
gi 1958777079 335 PSLVKGTLPQERVTKLAPRAQSEEDLSALFEA 366
Cdd:cd08192 348 EKIAENALTDVWCRTNPRPITDKDDVLEILES 379
|
|
| Fe-ADH-like |
cd14866 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
24-366 |
1.25e-19 |
|
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: 89.21 E-value: 1.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 24 MDAIEFAKKGAFDAYVAVGGGSTMDTCKAANLYACSPHSeFLDYVNAPIGKGKPVT----VPLKPLIAVPTTSGTGSETT 99
Cdd:cd14866 73 EAAAEALREADADAVVAVGGGSAIVTARAASILLAEDRD-VRELCTRRAEDGLMVSprldAPKLPIFVVPTTPTTADVKA 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 100 GVAIFDYEHLKvKTGIASRAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESytaiPYSMRspcpsnpiqrpayqgS 179
Cdd:cd14866 152 GSAVTDPPAGQ-RLALFDPKTRPAAVFYDPELLATAPASLVAGAAMNGFDMAVEG----LYSRH---------------A 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 180 NPISDIWAVHALRIVAKYLKRAVrNPDDLEARSSMHLASAFAGIGFGNAGVHLCHGMSYPISGlvktykakEYNVDHPLV 259
Cdd:cd14866 212 DPLADATLMHALRLLADGLPRLA-DDDDPAARADLVLAAVLAGYGTDHTGGGVIHALGHAIGA--------RYGVQNGVV 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 260 pHglSVVLtsPAVFTFTAQMFPERHLETAEILGAniRTAKIQDAGPVLADALRKFLFDLNVDDGLAALGYSKDDIPSLVK 339
Cdd:cd14866 283 -H--AILL--PHVLRFNAPATDGRLDRLAEALGV--ADAGDEASAAAVVDAVEALLDALGVPTRLRDLGVSREDLPAIAE 355
|
330 340
....*....|....*....|....*..
gi 1958777079 340 GTLPQERVTKLAPRAQSEEDLSALFEA 366
Cdd:cd14866 356 AAMDDWFMDNNPRPVPTAEELEALLEA 382
|
|
| YqdH |
COG1979 |
Alcohol dehydrogenase YqhD, Fe-dependent ADH family [Energy production and conversion]; |
24-368 |
9.88e-17 |
|
Alcohol dehydrogenase YqhD, Fe-dependent ADH family [Energy production and conversion];
Pssm-ID: 441582 [Multi-domain] Cd Length: 387 Bit Score: 80.50 E-value: 9.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 24 MDAIEFAKKGAFDAYVAVGGGSTMDTCKAANLYACSPHsEFLDYVNapigKGKPVTVPLkPLIAVPTTSGTGSETTGVAI 103
Cdd:COG1979 78 RKGVELCKEEGIDFILAVGGGSVIDGAKAIAAGAKYDG-DPWDILT----GKAPVEKAL-PLGTVLTLPATGSEMNSGSV 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 104 FDYEHLKVKTGIASRAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTaipysmrspcpSNPIQrpayqgsNPIS 183
Cdd:COG1979 152 ITNEETKEKLGFGSPLVFPKFSILDPELTYTLPKRQTANGIVDIFSHVMEQYF-----------TYPVD-------APLQ 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 184 DIWAVHALRIVAKYLKRAVRNPDDLEARSSMHLASAFAGIGFGNAGVH---LCHGMSYPISGLvktykakeYNVDHplvP 260
Cdd:COG1979 214 DRFAEGLLRTLIEEGPKALKDPEDYDARANLMWAATLALNGLIGAGVPqdwATHMIEHELSAL--------YDIDH---G 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 261 HGLSVVLtsPAVFTFTAQMFPERHLETAE-ILGANIRTAK-IQDAGpvlADALRKFLFDLNVDDGLAALGYSKDDIPSLV 338
Cdd:COG1979 283 AGLAIVL--PAWMRYVLEEKPEKFAQYAErVWGITEGDDEeRALEG---IEATEEFFESLGLPTRLSEYGIDEEDIEEMA 357
|
330 340 350
....*....|....*....|....*....|
gi 1958777079 339 KGTLPQERVTKLAPRAQSEEDLSALFEASM 368
Cdd:COG1979 358 EKATAHGMTALGEFKDLTPEDVREILELAL 387
|
|
| MAR |
cd08177 |
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic ... |
25-366 |
2.29e-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: 79.09 E-value: 2.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 25 DAIEFAKKGAFDAYVAVGGGSTmdtckaanlyacsphsefldyvnapIGKGKPVTVPLK-PLIAVPTTSgtgsettgvA- 102
Cdd:cd08177 67 RALAAAREAGADGLVAIGGGSA-------------------------IGLAKAIALRTGlPIVAVPTTY---------Ag 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 103 -----IFDYEHLKVKTGIASRAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTAipysmrspcpsnpiqrpayQ 177
Cdd:cd08177 113 semtpIWGETEDGVKTTGRDPRVLPRTVIYDPDLTLGLPAALSVASGLNALAHAVEALYA-------------------P 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 178 GSNPISDIWAVHALRIVAKYLKRAVRNPDDLEARSSMHLASAFAGIGFGNAG--VH--LCH--GMSYpisGLvktykake 251
Cdd:cd08177 174 DANPITSLLAEEGIRALARALPRLVADPSDLEARSDALYGAWLAGVVLGSVGmgLHhkLCHvlGGTF---DL-------- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 252 ynvdhplvPHGL--SVVLtsPAVFTFTAQMFPERHLETAEILGANirtakiqDAgpvlADALRKFLFDLNVDDGLAALGY 329
Cdd:cd08177 243 --------PHAEthAVVL--PHVLAYNAPAAPDAMARLARALGGG-------DA----AGGLYDLARRLGAPTSLRDLGM 301
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1958777079 330 SKDDIPSLVkgtlpqERVTKLA---PRAQSEEDLSALFEA 366
Cdd:cd08177 302 PEDDIDRAA------DLALANPypnPRPVERDALRALLER 335
|
|
| PRK15138 |
PRK15138 |
alcohol dehydrogenase; |
24-350 |
1.44e-05 |
|
alcohol dehydrogenase;
Pssm-ID: 185092 [Multi-domain] Cd Length: 387 Bit Score: 46.71 E-value: 1.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 24 MDAIEFAKKGAFDAYVAVGGGSTMDTCK----AANLYACSPHSEFLDYVNAPIGKGkpvtVPLKPLIAVPttsGTGSETT 99
Cdd:PRK15138 75 MKAVKLVREEKITFLLAVGGGSVLDGTKfiaaAANYPENIDPWHILETGGKEIKSA----IPMGSVLTLP---ATGSESN 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 100 GVAIFDYEHLKVKTGIASRAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTAIPYSMRspcpsnpiqrpayqgs 179
Cdd:PRK15138 148 AGAVISRKTTGDKQAFHSPHVQPVFAVLDPVYTYTLPPRQVANGVVDAFVHTVEQYVTYPVDAK---------------- 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 180 npISDIWAVHALRIVAKYLKRAVRNPDDLEARSSMHLASAFAGIGFGNAGVH---LCHGMSYPISGLvktykakeYNVDH 256
Cdd:PRK15138 212 --IQDRFAEGILLTLIEEGPKALKEPENYDVRANVMWAATQALNGLIGAGVPqdwATHMLGHELTAM--------HGLDH 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 257 plvPHGLSVVLtsPAVFTFTAQMFPERHLETAEILGaNIRTAKIQDAGPVLADALRKFLFDLNVDDGLAALGYSKDDIPS 336
Cdd:PRK15138 282 ---AQTLAIVL--PALWNEKRDTKRAKLLQYAERVW-NITEGSDDERIDAAIAATRNFFEQMGVPTRLSDYGLDGSSIPA 355
|
330
....*....|....
gi 1958777079 337 LVKgTLPQERVTKL 350
Cdd:PRK15138 356 LLK-KLEEHGMTQL 368
|
|
| DHQ_Fe-ADH |
cd07766 |
Dehydroquinate synthase-like (DHQ-like) and iron-containing alcohol dehydrogenases (Fe-ADH); ... |
24-339 |
3.20e-05 |
|
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: 45.05 E-value: 3.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 24 MDAIEFAKKGAFDAYVAVGGGSTMDTCKAANLyacsphsefldyvnapigkgkpVTVPLKPLIAVPTTSGTGSETTGVAI 103
Cdd:cd07766 67 KNAVERARAAEADAVIAVGGGSTLDTAKAVAA----------------------LLNRGIPFIIVPTTASTDSEVSPKSV 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 104 FDYEHLKVKTGIAsrAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTAIpysmrspcpsnpiqrpayqgsnpis 183
Cdd:cd07766 125 ITDKGGKNKQVGP--HYNPDVVFVDTDITKGLPPRQVASGGVDALAHAVELEKVV------------------------- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777079 184 diwavhalrivakylkravrnpddlearssmhLASAFAGIGFGNA-GVHLCHGMSYPISGLVKTykakeynvdhplvPHG 262
Cdd:cd07766 178 --------------------------------EAATLAGMGLFESpGLGLAHAIGHALTAFEGI-------------PHG 212
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958777079 263 LSVVLTSPAVFTFTAQMFPERHLETAeilganirtakiqdagpvladALRKFLFDLNVDDGLAALGYSKDDIPSLVK 339
Cdd:cd07766 213 EAVAVGLPYVLKVANDMNPEPEAAIE---------------------AVFKFLEDLGLPTHLADLGVSKEDIPKLAE 268
|
|
| |
