|
Name |
Accession |
Description |
Interval |
E-value |
| HOT |
cd08190 |
Hydroxyacid-oxoacid transhydrogenase (HOT) involved in gamma-hydroxybutyrate metabolism; This ... |
3-421 |
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: 709.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 3 VSNIRYGAAVTKEVGMasirdDLKNMGAKNVCLMTDKNLSKLPPVQVAMDSLVKNGIPFTVYDNVRVEPTDSSFMEAIEF 82
Cdd:cd08190 1 ASNIRFGPGATRELGM-----DLKRLGAKKVLVVTDPGLAKLGLVERVLESLEKAGIEVVVYDGVRVEPTDESFEEAIEF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 83 AQKGAFDAYVAVGGGSTMDTCKAANLYASSPhSDFLDYVSAPIGKGKPVSVPLKPLIAVPTTSGTGSETTGVAIFDYEHL 162
Cdd:cd08190 76 AKEGDFDAFVAVGGGSVIDTAKAANLYATHP-GDFLDYVNAPIGKGKPVPGPLKPLIAIPTTAGTGSETTGVAIFDLEEL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 163 KVKIGITSRAIKPTLGLIDPLHTLHMPARVVANSGFDVLCHALESYTTLPYHLRsPCPSNPITRPAYQGSNPISDIWAIH 242
Cdd:cd08190 155 KVKTGISSRYLRPTLAIVDPLLTLTLPPRVTASSGFDVLCHALESYTARPYNAR-PRPANPDERPAYQGSNPISDVWAEK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 243 ALRIVAKYLKRAVRNPDDLEARSHMHLASAFAGIGFGNAGVHLCHGMSYPISGLVKMYKAKDYNVDHPLVPHGLSVVLTS 322
Cdd:cd08190 234 AIELIGKYLRRAVNDGDDLEARSNMLLASTLAGIGFGNAGVHLPHAMAYPIAGLVKDYRPPGYPVDHPHVPHGLSVALTA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 323 PAVFTFTAQMFPERHLEMAEILGADTRTARIQDAGLVLADTLRKFLFDLDVDDGLAAVGYSKADIPALVKGTLPQERVTK 402
Cdd:cd08190 314 PAVFRFTAPACPERHLEAAELLGADTSGASDRDAGEVLADALIKLMRDIGIPNGLSALGYSEDDIPALVEGTLPQQRLLK 393
|
410
....*....|....*....
gi 119607307 403 LAPCPQSEEDLAALFEASM 421
Cdd:cd08190 394 LNPRPVTEEDLEEIFEDAL 412
|
|
| EutG |
COG1454 |
Alcohol dehydrogenase, class IV [Energy production and conversion]; |
6-421 |
3.99e-107 |
|
Alcohol dehydrogenase, class IV [Energy production and conversion];
Pssm-ID: 441063 [Multi-domain] Cd Length: 381 Bit Score: 321.30 E-value: 3.99e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 6 IRYGAAVTKEVGmasirDDLKNMGAKNVCLMTDKNLSKLPPVQVAMDSLVKNGIPFTVYDNVRVEPTDSSFMEAIEFAQK 85
Cdd:COG1454 11 IVFGAGALAELG-----EELKRLGAKRALIVTDPGLAKLGLLDRVLDALEAAGIEVVVFDDVEPNPTVETVEAGAAAARE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 86 GAFDAYVAVGGGSTMDTCKAANLYASSPHsDFLDYVSApigkgKPVSVPLKPLIAVP----------TtsgtgsettgVA 155
Cdd:COG1454 86 FGADVVIALGGGSAIDAAKAIALLATNPG-DLEDYLGI-----KKVPGPPLPLIAIPttagtgsevtP----------FA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 156 IFDYEHLKVKIGITSRAIKPTLGLIDPLHTLHMPARVVANSGFDVLCHALESYTTLpyhlrspcpsnpitrpayqGSNPI 235
Cdd:COG1454 150 VITDPETGVKKGIADPELLPDVAILDPELTLTLPPSLTAATGMDALTHAIEAYVSK-------------------GANPL 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 236 SDIWAIHALRIVAKYLKRAVRNPDDLEARSHMHLASAFAGIGFGNAGVHLCHGMSYPISGLvkmykakdYNvdhplVPHG 315
Cdd:COG1454 211 TDALALEAIRLIARNLPRAVADGDDLEAREKMALASLLAGMAFANAGLGAVHALAHPLGGL--------FH-----VPHG 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 316 LSVVLTSPAVFTFTAQMFPERHLEMAEILGADTrTARIQDAGLVLADTLRKFLFDLDVDDGLAAVGYSKADIPALVKGTL 395
Cdd:COG1454 278 LANAILLPHVLRFNAPAAPERYAEIARALGLDV-GLSDEEAAEALIEAIRELLRDLGIPTRLSELGVTEEDLPELAELAL 356
|
410 420
....*....|....*....|....*.
gi 119607307 396 pQERVTKLAPCPQSEEDLAALFEASM 421
Cdd:COG1454 357 -ADRCLANNPRPLTEEDIEAILRAAY 381
|
|
| Fe-ADH |
cd08551 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains large ... |
4-417 |
7.33e-102 |
|
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: 307.45 E-value: 7.33e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 4 SNIRYGAAVTKEVGmasirDDLKNMGAKNVCLMTDKNLSKLPPVQVAMDSLVKNGIPFTVYDNVRVEPTDSSFMEAIEFA 83
Cdd:cd08551 2 TRIVFGAGALARLG-----EELKALGGKKVLLVTDPGLVKAGLLDKVLESLKAAGIEVEVFDDVEPNPTVETVEAAAELA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 84 QKGAFDAYVAVGGGSTMDTCKAANLYASSPHSDfLDYVSapigkGKPVSVPLKPLIAVPTTSGTGSETTGVAIFDYEHLK 163
Cdd:cd08551 77 REEGADLVIAVGGGSVLDTAKAIAVLATNGGSI-RDYEG-----IGKVPKPGLPLIAIPTTAGTGSEVTPNAVITDPETG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 164 VKIGITSRAIKPTLGLIDPLHTLHMPARVVANSGFDVLCHALESYTTLPyhlrspcpsnpitrpayqgSNPISDIWAIHA 243
Cdd:cd08551 151 RKMGIVSPYLLPDVAILDPELTLSLPPSVTAATGMDALTHAIEAYTSKK-------------------ANPISDALALEA 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 244 LRIVAKYLKRAVRNPDDLEARSHMHLASAFAGIGFGNAGVHLCHGMSYPISGlvkMYKakdynvdhplVPHGLSVVLTSP 323
Cdd:cd08551 212 IRLIGKNLRRAVADGSDLEAREAMLLASLLAGIAFGNAGLGAVHALAYPLGG---RYH----------IPHGVANAILLP 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 324 AVFTFTAQMFPERHLEMAEILGADTRTARIQDAGLVLADTLRKFLFDLDVDDGLAAVGYSKADIPALVKGTLPQERVTKL 403
Cdd:cd08551 279 YVMEFNLPACPEKYAEIAEALGEDVEGLSDEEAAEAAVEAVRELLRDLGIPTSLSELGVTEEDIPELAEDAMKSGRLLSN 358
|
410
....*....|....
gi 119607307 404 APCPQSEEDLAALF 417
Cdd:cd08551 359 NPRPLTEEDIREIY 372
|
|
| Fe-ADH |
pfam00465 |
Iron-containing alcohol dehydrogenase; |
4-413 |
2.99e-92 |
|
Iron-containing alcohol dehydrogenase;
Pssm-ID: 425696 [Multi-domain] Cd Length: 362 Bit Score: 282.57 E-value: 2.99e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 4 SNIRYGAAVTKEVGmasirDDLKNMGAKnVCLMTDKNLSKLPPVQVAMDSLVKNGIPFTVYDNVRVEPTDSSFMEAIEFA 83
Cdd:pfam00465 2 TRIVFGAGALAELG-----EELKRLGAR-ALIVTDPGSLKSGLLDKVLASLEEAGIEVVVFDGVEPEPTLEEVDEAAALA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 84 QKGAFDAYVAVGGGSTMDTCKAANLYASSPHSDFLDYvsapigKGKPVSVPLKPLIAVPTTSGTGSETTGVAIFDYEHLK 163
Cdd:pfam00465 76 REAGADVIIAVGGGSVIDTAKAIALLLTNPGDVWDYL------GGKPLTKPALPLIAIPTTAGTGSEVTPLAVITDTETG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 164 VKIGITSRAIKPTLGLIDPLHTLHMPARVVANSGFDVLCHALESYTTlpyhlrspcpsnpitrpayQGSNPISDIWAIHA 243
Cdd:pfam00465 150 EKLGIFSPKLLPDLAILDPELTLTLPPRLTAATGMDALAHAVEAYVS-------------------KGANPLTDALALEA 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 244 LRIVAKYLKRAVRNPDDLEARSHMHLASAFAGIGFGNAGVHLCHGMSYPISGLVKmykakdynvdhplVPHGLSVVLTSP 323
Cdd:pfam00465 211 IRLIAENLPRAVADGEDLEARENMLLASTLAGLAFSNAGLGAAHALAHALGGRYG-------------IPHGLANAILLP 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 324 AVFTFTAQMFPERHLEMAEILGADTRTARIQDAglvlADTLRKFLFDLDVDDGLAAVGYSKADIPALVKGTLpQERVTKL 403
Cdd:pfam00465 278 YVLRFNAPAAPEKLAQLARALGEDSDEEAAEEA----IEALRELLRELGLPTTLSELGVTEEDLDALAEAAL-RDRSLAN 352
|
410
....*....|
gi 119607307 404 APCPQSEEDL 413
Cdd:pfam00465 353 NPRPLTAEDI 362
|
|
| Fe-ADH-like |
cd14863 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
6-419 |
8.81e-80 |
|
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: 250.92 E-value: 8.81e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 6 IRYGAAVTKEVGMAsirddLKNMGAKNVCLMTDKNLSKLPPVQVAMDSLVKNGIPFTVYDNVRVEPTDSSFMEAIEFAQK 85
Cdd:cd14863 8 VIFGAGAVEQIGEL-----LKELGCKKVLLVTDKGLKKAGIVDKIIDLLEEAGIEVVVFDDVEPDPPDEIVDEAAEIARE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 86 GAFDAYVAVGGGSTMDTCKAANLYASSPHSDfLDYvsapIGKGKPVSVPLKPLIAVPTTSGTGSETTGVAIFDYEHLKVK 165
Cdd:cd14863 83 EGADGVIGIGGGSVLDTAKAIAVLLTNPGPI-IDY----ALAGPPVPKPGIPLIAIPTTAGTGSEVTPIAVITDEENGVK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 166 IGITSRAIKPTLGLIDPLHTLHMPARVVANSGFDVLCHALESYTTlpyhlrspcpsnpitrpayQGSNPISDIWAIHALR 245
Cdd:cd14863 158 KSLLGPFLVPDLAILDPELTVGLPPSLTAATGMDALSHAIEAYTS-------------------KLANPMTDALALQAIR 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 246 IVAKYLKRAVRNPDDLEARSHMHLASAFAGIGFGNAGVHLCHGMSYPISGLvkmykakdYNvdhplVPHGLSVVLTSPAV 325
Cdd:cd14863 219 LIVKNLPRAVKDGDNLEARENMLLASNLAGIAFNNAGTHIGHAIAHALGAL--------YH-----IPHGLACALALPVV 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 326 FTFTAQMFPERHLEMAEILGADTRTARIQDAGLVLADTLRKFLFDLDVDDGLAAVGYSKADIPALVKGTLpQERVTKLAP 405
Cdd:cd14863 286 LEFNAEAYPEKVKKIAKALGVSFPGESDEELGEAVADAIREFMKELGIPSLFEDYGIDKEDLDKIAEAVL-KDPFAMFNP 364
|
410
....*....|....
gi 119607307 406 CPQSEEDLAALFEA 419
Cdd:cd14863 365 RPITEEEVAEILEA 378
|
|
| Fe-ADH-like |
cd08185 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
5-418 |
1.61e-75 |
|
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol dehydrogenase-like (ADH) proteins. Alcohol dehydrogenase catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase fold and is a member of the iron-containing alcohol dehydrogenase-like family. They are distinct from other alcohol dehydrogenases which contain different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341464 [Multi-domain] Cd Length: 379 Bit Score: 240.09 E-value: 1.61e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 5 NIRYGAAVTKEVGmasirdDLKNMGAKNVCLMTDKNLSKLPPV-QVAMDSLVKNGIPFTVYDNVRVEPTDSSFMEAIEFA 83
Cdd:cd08185 6 RILFGAGKLNELG------EEALRPGKKALIVTGKGSSKKTGLlDRVKKLLEKAGVEVVVFDKVEPNPLTTTVMEGAALA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 84 QKGAFDAYVAVGGGSTMDTCKAANLYASSPHsDFLDYVSAPIGKGKPVSVPLkPLIAVPTTSGTGSETTGVAIFDYEHLK 163
Cdd:cd08185 80 KEEGCDFVIGLGGGSSMDAAKAIAFMATNPG-DIWDYIFGGTGKGPPPEKAL-PIIAIPTTAGTGSEVDPWAVITNPETK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 164 VKIGITSRAIKPTLGLIDPLHTLHMPARVVANSGFDVLCHALESYTtlpyhlrspcpSNpitrpayqGSNPISDIWAIHA 243
Cdd:cd08185 158 EKKGIGHPALFPKVSIVDPELMLTVPPRVTAYTGFDALFHAFESYI-----------SK--------NANPFSDMLALEA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 244 LRIVAKYLKRAVRNPDDLEARSHMHLASAFAGIGFGNAGVHLCHGMSYPISGLvkmykakdynvdHPLVPHGLSVVLTSP 323
Cdd:cd08185 219 IRLVAKYLPRAVKDGSDLEAREKMAWASTLAGIVIANSGTTLPHGLEHPLSGY------------HPNIPHGAGLAALYP 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 324 AVFTFTAQMFPER--HLEMAEILGADTrtariQDAGLVLADTLRKFLFDLDVDDGLAAVGYSKADIPALVkgtlpqERVT 401
Cdd:cd08185 287 AYFEFTIEKAPEKfaFVARAEASGLSD-----AKAAEDFIEALRKLLKDIGLDDLLSDLGVTEEDIPWLA------ENAM 355
|
410 420
....*....|....*....|....
gi 119607307 402 KLA-------PCPQSEEDLAALFE 418
Cdd:cd08185 356 ETMgglfannPVELTEEDIVEIYE 379
|
|
| Fe-ADH-like |
cd08191 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
33-421 |
1.06e-73 |
|
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contain different protein domain. Proteins of this family have not been characterized.
Pssm-ID: 341470 [Multi-domain] Cd Length: 392 Bit Score: 235.59 E-value: 1.06e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 33 VCLMTDKNLSKLPPVQVAMDSLVKNGIPFTVYDNVRVEPTDSSFMEAIEFAQKGAFDAYVAVGGGSTMDTCKAANLYASS 112
Cdd:cd08191 28 VLIVTDPRLASTPLVAELLAALTAAGVAVEVFDGGQPELPVSTVADAAAAARAFDPDVVIGLGGGSNMDLAKVVALLLAH 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 113 PhSDFLDYvsapIGKGKpVSVPLKPLIAVPTTSGTGSETTGVAIFDYEHLKVKIGITSRAIKPTLGLIDPLHTLHMPARV 192
Cdd:cd08191 108 G-GDPRDY----YGEDR-VPGPVLPLIAVPTTAGTGSEVTPVAVLTDPARGMKVGVSSPYLRPAVAIVDPELTLTCPPGV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 193 VANSGFDVLCHALESYTTLPyhlRSPCPSNPiTRPAYQGSNPISDIWAIHALRIVAKYLKRAVRNPDDLEARSHMHLASA 272
Cdd:cd08191 182 TADSGIDALTHAIESYTARD---FPPFPRLD-PDPVYVGKNPLTDLLALEAIRLIGRHLPRAVRDGDDLEARSGMALAAL 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 273 FAGIGFGNAGVHLCHGMSYPISGLVkmykakdynvdHplVPHGLSVVLTSPAVFTFTAQMFPERHLEMAEILGADTrTAR 352
Cdd:cd08191 258 LAGLAFGTAGTAAAHALQYPIGALT-----------H--TSHGVGNGLLLPYVMRFNRPARAAELAEIARALGVTT-AGT 323
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119607307 353 IQDAGLVLADTLRKFLFDLDVDDGLAAVGYSKADIPALVKGTLPQERVTKLAPCPQSEEDLAALFEASM 421
Cdd:cd08191 324 SEEAADRAIERVEELLARIGIPTTLADLGVTEADLPGLAEKALSVTRLIANNPRPPTEEDLLRILRAAF 392
|
|
| Fe-ADH-like |
cd17814 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
25-417 |
9.07e-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: 341489 [Multi-domain] Cd Length: 374 Bit Score: 222.42 E-value: 9.07e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 25 LKNMGAKNVCLMTDKNLSKLPPVQVAMDSLVKNGIPFTVYDNVRVEPTDSSFMEAIE-FAQKGAfDAYVAVGGGSTMDTC 103
Cdd:cd17814 21 AKNLGARKVLVVTDPGVIKAGWVDEVLDSLEAEGLEYVVFSDVTPNPRDFEVMEGAElYREEGC-DGIVAVGGGSPIDCA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 104 KAANLYASSpHSDFLDYvsapIGKGKpVSVPLKPLIAVPTTSGTGSETTGVAIFDYEHLKVKIGITSRAIKPTLGLIDPL 183
Cdd:cd17814 100 KGIGIVVSN-GGHILDY----EGVDK-VRRPLPPLICIPTTAGSSADVSQFAIITDTERRVKMAIISKTLVPDVSLIDPE 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 184 HTLHMPARVVANSGFDVLCHALESYTtlpyhlrspcpSNpitrpayqGSNPISDIWAIHALRIVAKYLKRAVRNPDDLEA 263
Cdd:cd17814 174 TLTTMDPELTACTGMDALTHAIEAYV-----------SN--------ASSPLTDLHALEAIRLISENLPKAVADPDDLEA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 264 RSHMHLASAFAGIGFGNAGVHLCHGMSYPISGLVKMykakdynvdhplvPHGLSVVLTSPAVFTFTAQMFPERHLEMAEI 343
Cdd:cd17814 235 REKMMLASLQAGLAFSNASLGAVHAMAHSLGGLLDL-------------PHGECNALLLPHVIRFNFPAAPERYRKIAEA 301
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119607307 344 LGADTRTARIQDAGLVLADTLRKFLFDLDVDDGLAAVGYSKADIPALVKGTLpqeR----VTKlaPCPQSEEDLAALF 417
Cdd:cd17814 302 MGLDVDGLDDEEVAERLIEAIRDLREDLGIPETLSELGVDEEDIPELAKRAM---KdpclVTN--PRRPTREDIEEIY 374
|
|
| Fe-ADH-like |
cd08194 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
4-391 |
3.36e-66 |
|
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: 215.86 E-value: 3.36e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 4 SNIRYGAAVTKEVGmasirDDLKNMGAKNVCLMTDKNLSKLPPVQVAMDSLVKNGIPFTVYDNVRVEPTDSSFMEAIEFA 83
Cdd:cd08194 2 RTIIIGGGALEELG-----EEAASLGGKRALIVTDKVMVKLGLVDKVTQLLAEAGIAYAVFDDVVSEPTDEMVEEGLALY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 84 QKGAFDAYVAVGGGSTMDTCKAANLYASSPhSDFLDYVSAPIGKGKPVsvplkPLIAVPTTSGTGSETTGVAIFDYEHLK 163
Cdd:cd08194 77 KEGGCDFIVALGGGSPIDTAKAIAVLATNG-GPIRDYMGPRKVDKPGL-----PLIAIPTTAGTGSEVTRFTVITDTETD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 164 VKIGITSRAIKPTLGLIDPLHTLHMPARVVANSGFDVLCHALESYttlpyhlrspcpsnpITRPAyqgsNPISDIWAIHA 243
Cdd:cd08194 151 VKMLLKGPALLPAVAIVDPELTLSMPPRVTAATGIDALTHAIEAY---------------VSRKA----QPLTDTLALSA 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 244 LRIVAKYLKRAVRNPDDLEARSHMHLASAFAGIGFGNAGVHLCHGMSYPISGLVkmykakdynvdHplVPHGLSVVLTSP 323
Cdd:cd08194 212 IKLIGRNLRRAYADGDDLEAREAMMLAALEAGIAFSNSSVALVHGMSRPIGALF-----------H--VPHGLSNAMLLP 278
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119607307 324 AVFTFTAQMFPERHLEMAEILGADTRTARIQDAGLVLADTLRKFLFDLDVdDGLAAVGYSKADIPALV 391
Cdd:cd08194 279 AVTEFSLPGAPERYAEIARAMGIATEGDSDEEAAEKLVEALERLCADLEI-PTLREYGIDEEEFEAAL 345
|
|
| Fe-ADH-like |
cd08196 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
5-417 |
9.43e-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: 341475 [Multi-domain] Cd Length: 367 Bit Score: 214.37 E-value: 9.43e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 5 NIRYGAAVTKEvgmasIRDDLKNMGAKNVCLMTDKNLSKLPPVQVAMDSLVKNGIpfTVYDNVRVEPTDSSFMEAIEFAQ 84
Cdd:cd08196 8 KIIFGEGILKE-----LPDIIKELGGKRGLLVTDPSFIKSGLAKRIVESLKGRIV--AVFSDVEPNPTVENVDKCARLAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 85 KGAFDAYVAVGGGSTMDTCKAANLYASSPHSdFLDYvsapIGKGKPVSVPLKPLIAVPTTSGTGSETTGVAIFDYEHLKV 164
Cdd:cd08196 81 ENGADFVIAIGGGSVLDTAKAAACLAKTDGS-IEDY----LEGKKKIPKKGLPLIAIPTTAGTGSEVTPVAVLTDKEKGK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 165 KIGITSRAIKPTLGLIDPLHTLHMPARVVANSGFDVLCHALESYTTLpyhlrspcpsnpitrpayqGSNPISDIWAIHAL 244
Cdd:cd08196 156 KAPLVSPGFYPDIAIVDPELTYSMPPKVTASTGIDALCHAIEAYWSI-------------------NHQPISDALALEAA 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 245 RIVAKYLKRAVRNPDDLEARSHMHLASAFAGIGFGNAGVHLCHGMSYPISGLvkmykakdYNvdhplVPHGLSVVLTSPA 324
Cdd:cd08196 217 KLVLENLEKAYNNPNDKEAREKMALASLLAGLAFSQTRTTASHACSYPLTSH--------FG-----IPHGEACALTLPS 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 325 VFTFTAQMFPERHLEMAEILGADTrtarIQDaglvLADTLRKFLFDLDVDDGLAAVGYSKADIPALVKGTLPQERVtKLA 404
Cdd:cd08196 284 FIRLNAEALPGRLDELAKQLGFKD----AEE----LADKIEELKKRIGLRTRLSELGITEEDLEEIVEESFHPNRA-NNN 354
|
410
....*....|...
gi 119607307 405 PCPQSEEDLAALF 417
Cdd:cd08196 355 PVEVTKEDLEKLL 367
|
|
| LPO |
cd08176 |
Lactadehyde:propanediol oxidoreductase (LPO) catalyzes the interconversion between ... |
21-392 |
2.29e-65 |
|
Lactadehyde:propanediol oxidoreductase (LPO) catalyzes the interconversion between L-lactaldehyde and L-1,2-propanediol in Escherichia coli and other enterobacteria; Lactadehyde:propanediol oxidoreductase (LPO) is a member of the group III iron-activated dehydrogenases which catalyze the interconversion between L-lactaldehyde and L-1,2-propanediol in Escherichia coli and other enterobacteria. L-fucose and L-rhamnose are used by Escherichia coli through an inducible pathway mediated by the fucose regulon comprising four linked operons fucO, fucA, fucPIK, and fucR. The fucA-encoded aldolase catalyzes the formation of dihydroxyacetone phosphate and L-lactaldehyde. Under anaerobic conditions, with NADH as a cofactor, lactaldehyde is converted by a fucO-encoded lactadehyde:propanediol oxidoreductase (LPO) to L-1,2-propanediol, which is excreted as a fermentation product. In mutant strains, E. coli adapted to grow on L-1,2-propanediol, FucO catalyzes the oxidation of the polyol to L-lactaldehyde. FucO is induced regardless of the respiratory conditions of the culture, remains fully active in the absence of oxygen. In the presence of oxygen, this enzyme becomes oxidatively inactivated by a metal-catalyzed oxidation mechanism. FucO is an iron-dependent metalloenzyme that is inactivated by other metals, such as zinc, copper, or cadmium. This enzyme can also reduce glycol aldehyde with similar efficiency. Beside L-1,2-propanediol, the enzyme is also able to oxidize methanol as an alternative substrate.
Pssm-ID: 341455 [Multi-domain] Cd Length: 378 Bit Score: 213.56 E-value: 2.29e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 21 IRDDLKNMGAKNVCLMTDKNLSKLPPVQVAMDSLVKNGIPFTVYDNVRVEPTDSSFMEAIEFAQKGAFDAYVAVGGGSTM 100
Cdd:cd08176 19 IGEEAKKRGFKKALIVTDKGLVKFGIVDKVTDVLKEAGIAYTVFDEVKPNPTIENVMAGVAAYKESGADGIIAVGGGSSI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 101 DTCKAANLYASSPHSDFLDYVSApigkgKPVSVPLKPLIAVPTTSGTGSETTGVA-IFDYEHlKVKIGITSRAIKPTLGL 179
Cdd:cd08176 99 DTAKAIGIIVANPGADVRSLEGV-----APTKNPAVPIIAVPTTAGTGSEVTINYvITDTEK-KRKFVCVDPHDIPTVAI 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 180 IDPLHTLHMPARVVANSGFDVLCHALESYTTLpyhlrspcpsnpitrpayqGSNPISDIWAIHALRIVAKYLKRAVRNPD 259
Cdd:cd08176 173 VDPDLMSSMPKGLTAATGMDALTHAIEGYITK-------------------GAWELSDMLALKAIELIAKNLRKAVANPN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 260 DLEARSHMHLASAFAGIGFGNAGVHLCHGMSYPISGLvkmykakdYNvdhplVPHGLSVVLTSPAVFTFTAQMFPERHLE 339
Cdd:cd08176 234 NVEARENMALAQYIAGMAFSNVGLGIVHSMAHPLSAF--------YD-----TPHGVANAILLPYVMEFNAPATGEKYRD 300
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 119607307 340 MAEILGADTRTARIQDAGLVLADTLRKFLFDLDVDDGLAAVGYSKADIPALVK 392
Cdd:cd08176 301 IARAMGVDTTGMSDEEAAEAAVDAVKKLSKDVGIPQKLSELGVKEEDIEALAE 353
|
|
| Fe-ADH-like |
cd14865 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
19-421 |
9.72e-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: 341487 [Multi-domain] Cd Length: 383 Bit Score: 204.31 E-value: 9.72e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 19 ASIRDDLKNMGAKNVCLMTDKNLSKLPPVQVAMDSLVKNGIPFTVYDNVrvePTDSSF---MEAIEFAQKGAFDAYVAVG 95
Cdd:cd14865 17 ENLPAELARLGARRPLIVTDKGLAAAGLLKKVEDALGDAIEIVGVFDDV---PPDSSVavvNEAAARAREAGADGIIAVG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 96 GGSTMDTCKAANLYASSPHSDFLDYVSAPIGKGkpvsvPLKPLIAVPTTSGTGSETTGVAIFDYEHLKVKIGITSRAIKP 175
Cdd:cd14865 94 GGSVIDTAKGVNILLSEGGDDLDDYGGANRLTR-----PLKPLIAIPTTAGTGSEVTLVAVIKDEEKKVKLLFVSPFLLP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 176 TLGLIDPLHTLHMPARVVANSGFDVLCHALESYTTLpyhlrspcpsnpitrpayqGSNPISDIWAIHALRIVAKYLKRAV 255
Cdd:cd14865 169 DVAILDPRLTLSLPPKLTAATGMDALTHAIEAYTSL-------------------QKNPISDALALQAIRLISENLPKAV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 256 RNPDDLEARSHMHLASAFAGIGFGNAGVHLCHGMSYPISGLVKmykakdynvdhplVPHGL--SVVLtsPAVFTFTAQMF 333
Cdd:cd14865 230 KNGKDLEARLALAIAATMAGIAFSNSMVGLVHAIAHAVGAVAG-------------VPHGLanSILL--PHVMRYNLDAA 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 334 PERHLEMAEIL--GADTRTARIQDAGLVLADTLRKFLFDLDVDDGLAAVGYSKADIPALVKGTLpQERVTKLAPCPQSEE 411
Cdd:cd14865 295 AERYAELALALayGVTPAGRRAEEAIEAAIDLVRRLHELCGLPTRLRDVGVPEEQLEAIAELAL-NDGAILFNPREVDPE 373
|
410
....*....|
gi 119607307 412 DLAALFEASM 421
Cdd:cd14865 374 DILAILEAAY 383
|
|
| Fe-ADH-like |
cd14862 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
16-417 |
1.28e-59 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341484 [Multi-domain] Cd Length: 375 Bit Score: 198.60 E-value: 1.28e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 16 VGMASIrDDLKNMGAKNVCLMTDKNLSKLPPVQVAMDSLVKNGIPFTVYDNVRVEPTDSSFMEAIEFAQKGAFDAYVAVG 95
Cdd:cd14862 11 FGEDAL-SHLEQLSGKRALIVTDKVLVKLGLLKKVLKRLLQAGFEVEVFDEVEPEPPLETVLKGAEAMREFEPDLIIALG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 96 GGSTMDTCKAANLYASSPHSDFLDYVSAPIGKGKPVSVplkpLIAVPTTSGTGSETTGVAIFDYEHLKVKIGITSRAIKP 175
Cdd:cd14862 90 GGSVMDAAKAAWVLYERPDLDPEDISPLDLLGLRKKAK----LIAIPTTSGTGSEATWAIVLTDTEEPRKIAVANPELVP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 176 TLGLIDPLHTLHMPARVVANSGFDVLCHALESYTTlpyhlrspcpsnpitrpayQGSNPISDIWAIHALRIVAKYLKRAV 255
Cdd:cd14862 166 DVAILDPEFVLGMPPKLTAGTGLDALAHAVEAYLS-------------------TWSNDFSDALALKAIELIFKYLPRAY 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 256 RNPDDLEARSHMHLASAFAGIGFGNAGVHLCHGMSYPISGLVKmykakdynvdhplVPHGLSVVLTSPAVFTFTAQmFPE 335
Cdd:cd14862 227 KDGDDLEAREKMHNAATIAGLAFGNSQAGLAHALGHSLGAVFH-------------VPHGIAVGLFLPYVIEFYAK-VTD 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 336 RHLEMAEILGADTRTAriQDAGLVLADTLRKFLFDLDVDDGLAAVGYSKAD----IPALVKGTLpQERVTKLAPCPQSEE 411
Cdd:cd14862 293 ERYDLLKLLGIEARDE--EEALKKLVEAIRELYKEVGQPLSIKDLGISEEEfeekLDELVEYAM-EDSCTITSPRPPSEE 369
|
....*.
gi 119607307 412 DLAALF 417
Cdd:cd14862 370 DLKKLF 375
|
|
| PDDH |
cd08188 |
1,3-Propanediol (1,3-PD) dehydrogenase; This family includes 1,3-propanediol (1,3-PD) ... |
21-418 |
9.11e-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: 191.19 E-value: 9.11e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 21 IRDDLKNMGAKNVCLMTDKNLSKLPPVQVAMDSLVKNGIPFTVYDNVRVEPTDSSFMEAIEFAQKGAFDAYVAVGGGSTM 100
Cdd:cd08188 19 IGDELKKLGGKKALIVTDKGLVKLGLVKKVTDVLEEAGIEYVIFDGVQPNPTVTNVNEGLELFKENGCDFIISVGGGSAH 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 101 DTCKAANLYASSPhSDFLDYvsapIGKGKpVSVPLKPLIAVPTTSGTGSETTGVAIFDYEHLKVKIGITSRAIKPTLGLI 180
Cdd:cd08188 99 DCAKAIGILATNG-GEIEDY----EGVDK-SKKPGLPLIAINTTAGTASEVTRFAVITDEERHVKMVIVDWNVTPTIAVN 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 181 DPLHTLHMPARVVANSGFDVLCHALESYTTLpyhlrspcpsnpitrpayqGSNPISDIWAIHALRIVAKYLKRAVRNPDD 260
Cdd:cd08188 173 DPELMLGMPPSLTAATGMDALTHAIEAYVST-------------------GATPLTDALALEAIRLIAENLPKAVANGKD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 261 LEARSHMHLASAFAGIGFGNAGVHLCHGMSYPISGLvkmykakdYNvdhplVPHGL--SVVLtsPAVFTFTAQMFPERHL 338
Cdd:cd08188 234 LEARENMAYAQFLAGMAFNNAGLGYVHAMAHQLGGF--------YN-----LPHGVcnAILL--PHVMEFNLPACPERFA 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 339 EMAEILGADTRTARIQDAGLVLADTLRKFLFDLDVDDGLAAVGYSKADIPALVKGTLpQERVTKLAPCPQSEEDLAALFE 418
Cdd:cd08188 299 DIARALGENTEGLSDEEAAEAAIEAIRKLSRRVGIPSGLKELGVKEEDFPLLAENAL-KDACGPTNPRQATKEDVIAIYR 377
|
|
| HVD |
cd08193 |
5-hydroxyvalerate dehydrogenase (HVD) catalyzes the oxidation of 5-hydroxyvalerate to ... |
3-419 |
6.37e-56 |
|
5-hydroxyvalerate dehydrogenase (HVD) catalyzes the oxidation of 5-hydroxyvalerate to 5-oxovalerate with NAD+ as cofactor; 5-hydroxyvalerate dehydrogenase (HVD) is an iron-containing (type III) NAD-dependent alcohol dehydrogenase. It plays a role in the cyclopentanol metabolism biochemical pathway. It catalyzes the oxidation of 5-hydroxyvalerate to 5-oxovalerate with NAD+ as cofactor. This cyclopentanol (cpn) degradation pathway is present in some bacteria which can use cyclopentanol as sole carbon source. In Comamonas sp. strain NCIMB 9872, this enzyme is encoded by the CpnD gene.
Pssm-ID: 341472 [Multi-domain] Cd Length: 379 Bit Score: 188.88 E-value: 6.37e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 3 VSNIRYGAAvtkevGMASIRDDLKNMGAKNVCLMTDKNLSKLPPVQVAMDSLVKNGIPFTVYDNVRVEPTDSSFMEAIEF 82
Cdd:cd08193 4 VPRIICGAG-----AAARLGELLRELGARRVLLVTDPGLVKAGLADPALAALEAAGIAVTVFDDVVADPPEAVVEAAVEQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 83 AQKGAFDAYVAVGGGSTMDTCKAANLYASSPHSdfldyVSAPIGKGKpVSVPLKPLIAVPTTSGTGSETTGVAIF-DYEH 161
Cdd:cd08193 79 AREAGADGVIGFGGGSSMDVAKLVALLAGSDQP-----LDDIYGVGK-ATGPRLPLILVPTTAGTGSEVTPISIVtTGET 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 162 LKVkiGITSRAIKPTLGLIDPLHTLHMPARVVANSGFDVLCHALESYTTlpYHLRspcpsnpitrpayqgsNPISDIWAI 241
Cdd:cd08193 153 EKK--GVVSPQLLPDVALLDAELTLGLPPHVTAATGIDAMVHAIEAYTS--RHKK----------------NPISDALAR 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 242 HALRIVAKYLKRAVRNPDDLEARSHMHLASAFAGIGFGNAGVHLCHGMSYPISGlvkMYKakdynvdhplVPHGLSVVLT 321
Cdd:cd08193 213 EALRLLGANLRRAVEDGSDLEAREAMLLGSMLAGQAFANAPVAAVHALAYPLGG---HFH----------VPHGLSNALV 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 322 SPAVFTFTAQMFPERHLEMAEILGADTRTARIQDAGLVLADTLRKFLFDLDVDDGLAAVGYSKADIPALVKGTLPQERVT 401
Cdd:cd08193 280 LPHVLRFNLPAAEALYAELARALLPGLAFGSDAAAAEAFIDALEELVEASGLPTRLRDVGVTEEDLPMLAEDAMKQTRLL 359
|
410
....*....|....*...
gi 119607307 402 KLAPCPQSEEDLAALFEA 419
Cdd:cd08193 360 VNNPREVTEEDALAIYQA 377
|
|
| Fe-ADH-like |
cd14861 |
Iron-containing alcohol dehydrogenases-like; This family contains proteins similar to ... |
6-421 |
7.22e-54 |
|
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: 183.48 E-value: 7.22e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 6 IRYGAAVTKEVGmasirDDLKNMGAKNVCLMTDKNLSKLPPVQVAMDSLVKNGIPFTVYDNVRVEPTDSSFMEAIEFAQK 85
Cdd:cd14861 6 IRFGAGAIAELP-----EELKALGIRRPLLVTDPGLAALGIVDRVLEALGAAGLSPAVFSDVPPNPTEADVEAGVAAYRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 86 GAFDAYVAVGGGSTMDTCKAANLYASSPHsDFLDYVSAPIGkGKPVSVPLKPLIAVPTTSGTGSETTGVAIFDYEHLKVK 165
Cdd:cd14861 81 GGCDGIIALGGGSAIDAAKAIALMATHPG-PLWDYEDGEGG-PAAITPAVPPLIAIPTTAGTGSEVGRAAVITDDDTGRK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 166 IGITSRAIKPTLGLIDPLHTLHMPARVVANSGFDVLCHALESYTTLPYHlrspcpsnpitrpayqgsnPISDIWAIHALR 245
Cdd:cd14861 159 KIIFSPKLLPKVAICDPELTLGLPPRLTAATGMDALTHCIEAYLSPGFH-------------------PMADGIALEGLR 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 246 IVAKYLKRAVRNPDDLEARSHMHLASAFAGIGFGNaGVHLCHGMSYPISGLVKMykakdynvdhplvPHGLSVVLTSPAV 325
Cdd:cd14861 220 LISEWLPRAVADGSDLEARGEMMMAALMGAVAFQK-GLGAVHALAHALGALYGL-------------HHGLLNAILLPYV 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 326 FTFTAQMFPERHLEMAEILGADTRTAriqDAglvLADTLRKFLFDLDVDDGLAAVGYSKADIPALVKGTLpQERVTKLAP 405
Cdd:cd14861 286 LRFNRPAVEDKLARLARALGLGLGGF---DD---FIAWVEDLNERLGLPATLSELGVTEDDLDELAELAL-ADPCHATNP 358
|
410
....*....|....*.
gi 119607307 406 CPQSEEDLAALFEASM 421
Cdd:cd14861 359 RPVTAEDYRALLREAL 374
|
|
| Fe-ADH-like |
cd08183 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
6-418 |
2.61e-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: 179.62 E-value: 2.61e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 6 IRYGAAVTKEVGmasirDDLKNMGaKNVCLMTDKNLSKLPPVQVAMDSLVKNGIPFTVYDNVRvEPTDSSFMEAIEFAQK 85
Cdd:cd08183 4 IVFGRGSLQELG-----ELAAELG-KRALLVTGRSSLRSGRLARLLEALEAAGIEVALFSVSG-EPTVETVDAAVALARE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 86 GAFDAYVAVGGGSTMDTCKAANLYASSPHS--DFLDYVsapiGKGKPVSVPLKPLIAVPTtsgtgsettgVA-------- 155
Cdd:cd08183 77 AGCDVVIAIGGGSVIDAAKAIAALLTNEGSvlDYLEVV----GKGRPLTEPPLPFIAIPT----------TAgtgsevtk 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 156 ---IFDYEHlKVKIGITSRAIKPTLGLIDPLHTLHMPARVVANSGFDVLCHALESYTtlpyhlrspcpSNpitrpayqGS 232
Cdd:cd08183 143 navLSSPEH-GVKVSLRSPSMLPDVALVDPELTLSLPPEVTAASGLDALTQLIEPYV-----------SR--------KA 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 233 NPISDIWAIHALRIVAKYLKRAVRNPDDLEARSHMHLASAFAGIGFGNAGVHLCHGMSYPISGlvkMYKAkdynvdhplv 312
Cdd:cd08183 203 NPLTDALAREGLRLAARSLRRAYEDGEDLEAREDMALASLLGGLALANAGLGAVHGLAGPLGG---MFGA---------- 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 313 PHGL--SVVLtsPAVFTFTAQ---------MFPERHLEMAEILgADTRTARIQDaglvLADTLRKFLFDLDVdDGLAAVG 381
Cdd:cd08183 270 PHGAicAALL--PPVLEANLRalrerepdsPALARYRELAGIL-TGDPDAAAED----GVEWLEELCEELGI-PRLSEYG 341
|
410 420 430
....*....|....*....|....*....|....*..
gi 119607307 382 YSKADIPALVKGTLpQERVTKLAPCPQSEEDLAALFE 418
Cdd:cd08183 342 LTEEDFPEIVEKAR-GSSSMKGNPIELSDEELLEILE 377
|
|
| HEPD |
cd08182 |
Hydroxyethylphosphoate dehydrogenase (HEPD) catalyzes the reduction of phosphonoacetaldehyde ... |
4-418 |
2.48e-49 |
|
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: 171.25 E-value: 2.48e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 4 SNIRYGAAVTKEVGmasirDDLKNMGAKNVCLMTDKNLSKLPPVQVAMDSLvKNGIPFTVYDNVRVEPTDSSFMEAIEFA 83
Cdd:cd08182 2 VKIIFGPGALAELK-----DLLGGLGARRVLLVTGPSAVRESGAADILDAL-GGRIPVVVFSDFSPNPDLEDLERGIELF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 84 QKGAFDAYVAVGGGSTMDTCKAANLYASSPHSDFLdyvsAPIGKGKPVSVPLKPLIAVPttsgtgsettGVA-------- 155
Cdd:cd08182 76 RESGPDVIIAVGGGSVIDTAKAIAALLGSPGENLL----LLRTGEKAPEENALPLIAIP----------TTAgtgsevtp 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 156 ---IFDyEHLKVKIGITSRAIKPTLGLIDPLHTLHMPARVVANSGFDVLCHALESYTTLpyhlrspcpsnpitrpayqGS 232
Cdd:cd08182 142 fatIWD-EAEGKKYSLAHPSLYPDAAILDPELTLSLPLYLTASTGLDALSHAIESIWSV-------------------NA 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 233 NPISDIWAIHALRIVAKYLKRAVRNPDDLEARSHMHLASAFAGIGFGNAGVHLCHGMSYPISglvkmykaKDYNvdhplV 312
Cdd:cd08182 202 NPESRAYALRAIRLILENLPLLLENLPNLEAREAMAEASLLAGLAISITKTTAAHAISYPLT--------SRYG-----V 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 313 PHGLSVVLTSPAVFTFTAQMFPERHlemaeilgADTRTARIQDAGLV-----LADTLRKFLFDLDVDDGLAAVGYSKADI 387
Cdd:cd08182 269 PHGHACALTLPAVLRYNAGADDECD--------DDPRGREILLALGAsdpaeAAERLRALLESLGLPTRLSEYGVTAEDL 340
|
410 420 430
....*....|....*....|....*....|.
gi 119607307 388 PALVKGTLPQERVtKLAPCPQSEEDLAALFE 418
Cdd:cd08182 341 EALAASVNTPERL-KNNPVRLSEEDLLRLLE 370
|
|
| NADPH_BDH |
cd08179 |
NADPH-dependent butanol dehydrogenase involved in the butanol and ethanol formation pathway in ... |
25-419 |
1.73e-48 |
|
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: 169.29 E-value: 1.73e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 25 LKNMGAKNVCLMTDKN-LSKLPPVQVAMDSLVKNGIPFTVYDNVRVEPTDSSFMEAIEFAQKGAFDAYVAVGGGSTMDTC 103
Cdd:cd08179 18 LKTLKGKRAFIVTGGGsMKRNGFLDKVEDYLKEAGMEVKVFEGVEPDPSVETVEKGAEAMREFEPDWIIAIGGGSVIDAA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 104 KAANLYASSPHSDFLDYVsapigkgKPVSVPLKP----LIAVPTTSGTGSETTGVAIF-DYEHlKVKIGITSRAIKPTLG 178
Cdd:cd08179 98 KAMWVFYEYPELTFEDAL-------VPFPLPELRkkarFIAIPSTSGTGSEVTRASVItDTEK-GIKYPLASFEITPDVA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 179 LIDPLHTLHMPARVVANSGFDVLCHALESYTtlpyhlrSPCPsnpitrpayqgsNPISDIWAIHALRIVAKYLKRAVRNP 258
Cdd:cd08179 170 ILDPELTMTMPPHVTANTGMDALTHAIEAYV-------STLA------------NDFTDALALGAILDIFENLPKSYNGG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 259 DDLEARSHMHLASAFAGIGFGNAGVHLCHGMSYPISGLVKmykakdynvdhplVPHGL--SVVLtsPAVFTFTAQMFPER 336
Cdd:cd08179 231 KDLEAREKMHNASCLAGMAFSNSGLGIVHSMAHKGGAFFG-------------IPHGLanAILL--PYVIEFNSKDPEAR 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 337 HLEMAEILGADTRTArIQDaglvLADTLRKFLFDLDVDDGLAAVGYS----KADIPALVKGTLpQERVTKLAPCPQSEED 412
Cdd:cd08179 296 ARYAALLIGLTDEEL-VED----LIEAIEELNKKLGIPLSFKEAGIDedefFAKLDEMAENAM-NDACTGTNPRKPTVEE 369
|
....*..
gi 119607307 413 LAALFEA 419
Cdd:cd08179 370 MKELLKA 376
|
|
| Fe-ADH-like |
cd08186 |
Iron-containing alcohol dehydrogenase; This family contains iron-containing alcohol ... |
19-421 |
3.07e-45 |
|
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: 160.89 E-value: 3.07e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 19 ASIRDDLKNMGAKNVCLMTDKNLSKLPPV-QVAMDSLVKNGIPFTVYDNVRVEPTDSSFMEAIEFAQKGAFDAYVAVGGG 97
Cdd:cd08186 12 AKIKDILKDLGIDKVIIVTGRSSYKKSGAwDDVEKALEENGIEYVVYDKVTPNPTVDQADEAAKLARDFGADAVIAIGGG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 98 STMDTCKAANLYASSPHS---DFLDYVSAPIGKgkpvsvplKPLIAVPTTSGTGSETTGVAIFDYEHLKVKIGITSRAIK 174
Cdd:cd08186 92 SPIDTAKSVAVLLAYGGKtarDLYGFRFAPERA--------LPLVAINLTHGTGSEVDRFAVATIPEKGYKPGIAYDCIY 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 175 PTLGLIDPLHTLHMPARVVANSGFDVLCHALESYTTLpyhlrspcpsnpitrpayqGSNPISDIWAIHALRIVAKYLKRA 254
Cdd:cd08186 164 PLYAIDDPRLTLTLPKEQTLYTSIDAFNHVYEAATTK-------------------VSSPYVITLAKEAIRLIAEYLPRA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 255 VRNPDDLEARSHMHLASAFAGIGFGNAGVHLCHGMSYPISGLVkmykakdynvdhPLVPHGLSVVLTSPAVFTFTAQMFP 334
Cdd:cd08186 225 LANPKDLEARYWLLYASMIAGIAIDNGLLHLTHALEHPLSGLK------------PELPHGLGLALLGPAVVKYIYKAVP 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 335 ErhlEMAEILgadtrtaRIQDAGLV--------LADTLRKFLFDLDVDDGLAAVGYSKADIPALVK---GTLPQERVTKL 403
Cdd:cd08186 293 E---TLADIL-------RPIVPGLKgtpdeaekAARGVEEFLFSVGFTEKLSDYGFTEDDVDRLVElafTTPSLDLLLSL 362
|
410
....*....|....*...
gi 119607307 404 APCPQSEEDLAALFEASM 421
Cdd:cd08186 363 APVEVTEEVVREIYEESL 380
|
|
| Fe-ADH-like |
cd08189 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
25-419 |
2.43e-43 |
|
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: 155.70 E-value: 2.43e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 25 LKNMGAKNVCLMTDKNLSKLPPVQVAMDSLVKNGIPFTVYDNVRVEPTDSSFMEAIEFAQKGAFDAYVAVGGGSTMDTCK 104
Cdd:cd08189 22 LKKLGIKRVLIVTDKGLVKLGLLDPLLDALKKAGIEYVVFDGVVPDPTIDNVEEGLALYKENGCDAIIAIGGGSVIDCAK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 105 AANLYASSPHSDFLDYVsapiGKGKpVSVPLKPLIAVPTTSGTGSETTGVA-IFDYEHlKVKIGITSRAIKPTLGLIDPL 183
Cdd:cd08189 102 VIAARAANPKKSVRKLK----GLLK-VRKKLPPLIAVPTTAGTGSEATIAAvITDPET-HEKYAINDPKLIPDAAVLDPE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 184 HTLHMPARVVANSGFDVLCHALESYttlpyhlrspcpsnpITRPAyqgsNPISDIWAIHALRIVAKYLKRAVRNPDDLEA 263
Cdd:cd08189 176 LTLGLPPAITAATGMDALTHAVEAY---------------ISRSA----TKETDEYALEAVKLIFENLPKAYEDGSDLEA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 264 RSHMHLASAFAGIGFGNAGVHLCHGMSYPISGLvkmykakdYNvdhplVPHGL--SVVLtsPAVFTFTAQMFPERHLEMA 341
Cdd:cd08189 237 RENMLLASYYAGLAFTRAYVGYVHAIAHQLGGL--------YG-----VPHGLanAVVL--PHVLEFYGPAAEKRLAELA 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 342 EILGADTRTARIQDAGLVLADTLRKFLFDLDVDDGLAAVgySKADIPALVKGTLpQErVTKLAPCPQ--SEEDLAALFEA 419
Cdd:cd08189 302 DAAGLGDSGESDSEKAEAFIAAIRELNRRMGIPTTLEEL--KEEDIPEIAKRAL-KE-ANPLYPVPRimDRKDCEELLRK 377
|
|
| PDD |
cd08180 |
1,3-propanediol dehydrogenase (PPD) catalyzes the reduction of 3-hydroxypropionaldehyde (3-HPA) ... |
23-418 |
2.75e-43 |
|
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: 154.19 E-value: 2.75e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 23 DDLKNMGAKNVCLMTDKNLSKLPPVQVAMDSLvKNGIPFTVYDNVRVEPTDSSFMEAIEFAQKGAFDAYVAVGGGSTMDT 102
Cdd:cd08180 15 ERLKELKGKRVFIVTDPFMVKSGMVDKVTDEL-DKSNEVEIFSDVVPDPSIEVVAKGLAKILEFKPDTIIALGGGSAIDA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 103 CKAANLYassphsdfldYVSAPIGKGKPvsvplkPLIAVPTTSGTGSETTGVA-IFDYEHlKVKIGITSRAIKPTLGLID 181
Cdd:cd08180 94 AKAIIYF----------ALKQKGNIKKP------LFIAIPTTSGTGSEVTSFAvITDPEK-GIKYPLVDDSMLPDIAILD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 182 PLHTLHMPARVVANSGFDVLCHALESYTTLpyhlrspcpsnpitrpayqGSNPISDIWAIHALRIVAKYLKRAVRNPDDL 261
Cdd:cd08180 157 PELVKSVPPKVTADTGMDVLTHALEAYVST-------------------NANDFTDALAEKAIKLVFENLPRAYRDGDDL 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 262 EARSHMHLASAFAGIGFGNAGVHLCHGMSYPISGLVKmykakdynvdhplVPHGLSVVLTSPAVFTFtaqmfperhlema 341
Cdd:cd08180 218 EAREKMHNASCMAGIAFNNAGLGINHSLAHALGGRFH-------------IPHGRANAILLPYVIEF------------- 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 342 eilgadtrtariqdaglvLADTLRKFLFDLDVDDGLAAVGYSKAD----IPALVKGTLpQERVTKLAPCPQSEEDLAALF 417
Cdd:cd08180 272 ------------------LIAAIRRLNKKLGIPSTLKELGIDEEEfekaIDEMAEAAL-ADRCTATNPRKPTAEDLIELL 332
|
.
gi 119607307 418 E 418
Cdd:cd08180 333 R 333
|
|
| PPD-like |
cd08181 |
1,3-propanediol dehydrogenase-like (PPD); This family contains proteins similar to 1, ... |
22-348 |
1.01e-41 |
|
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: 150.81 E-value: 1.01e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 22 RDDLKNMGaKNVCLMTDKNLSK-LPPVQVAMDSLVKNGIPFTVYDNVRVEPTDSSFMEAIEFAQKGAFDAYVAVGGGSTM 100
Cdd:cd08181 18 ADELAALG-KKALIVTGKHSAKkNGSLDDVTEALEENGIEYFIFDEVEENPSIETVEKGAELARKEGADFVIGIGGGSPL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 101 DTCKAANLYASSPHSDFLDYvsapigKGKPVSVPLkPLIAVPTTSGTGSETTGVAIFDYEHLKVKIGITSRAIKPTLGLI 180
Cdd:cd08181 97 DAAKAIALLAANKDGDEDLF------QNGKYNPPL-PIVAIPTTAGTGSEVTPYSILTDHEKGTKKSFGNPLIFPKLALL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 181 DPLHTLHMPARVVANSGFDVLCHALESYTTlpyhlrspcpsnpiTRpayqgSNPISDIWAIHALRIVAKYLKRAVRNPDD 260
Cdd:cd08181 170 DPKYTLSLPEELTIDTAVDALSHAIEGYLS--------------VK-----ATPLSDALALEALRLIGECLPNLLGDELD 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 261 LEARSHMHLASAFAGIGFGNAGVHLCHGMSYPISglvkmykakdYNVDhplVPHGLSVVLTSPAVFTFTAQMFPERHLEM 340
Cdd:cd08181 231 EEDREKLMYASTLAGMVIAQTGTTLPHGLGYPLT----------YFKG---IPHGRANGILLPAYLKLCEKQEPEKVDKI 297
|
....*...
gi 119607307 341 AEILGADT 348
Cdd:cd08181 298 LKLLGFGS 305
|
|
| PRK10624 |
PRK10624 |
L-1,2-propanediol oxidoreductase; Provisional |
21-421 |
1.27e-40 |
|
L-1,2-propanediol oxidoreductase; Provisional
Pssm-ID: 182595 [Multi-domain] Cd Length: 382 Bit Score: 148.61 E-value: 1.27e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 21 IRDDLKNMGAKNVCLMTDKNLSKLPPVQVAMDSLVKNGIPFTVYDNVRVEPTDSSFMEAIE-FAQKGAfDAYVAVGGGST 99
Cdd:PRK10624 21 LTDEVKRRGFKKALIVTDKTLVKCGVVAKVTDVLDAAGLAYEIYDGVKPNPTIEVVKEGVEvFKASGA-DYLIAIGGGSP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 100 MDTCKAANLYASSPhsDFLDYVS----APIGKgkpvsvPLKPLIAVPTTS-GTGSETTGVAIFDYEHLKVKIGITSRAIk 174
Cdd:PRK10624 100 QDTCKAIGIISNNP--EFADVRSlegvAPTKK------PSVPIIAIPTTAgTAAEVTINYVITDEEKRRKFVCVDPHDI- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 175 PTLGLIDPLHTLHMPARVVANSGFDVLCHALESYTTlpyhlrspcpsnpitrpayQGSNPISDIWAIHALRIVAKYLKRA 254
Cdd:PRK10624 171 PQVAFVDADMMDSMPPGLKAATGVDALTHAIEGYIT-------------------RGAWALTDMLHLKAIEIIAGALRGA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 255 VRNpdDLEARSHMHLASAFAGIGFGNAGVHLCHGMSYPISGLvkmykakdYNvdhplVPHGLSVVLTSPAVFTFTAQMFP 334
Cdd:PRK10624 232 VAG--DKEAGEGMALGQYIAGMGFSNVGLGLVHGMAHPLGAF--------YN-----TPHGVANAILLPHVMEYNADFTG 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 335 ERHLEMAEILGADTRTARIQDAGLVLADTLRKFLFDLDVDDGLAAVGYSKADIPALVKGTLpQERVTKLAPCPQSEEDLA 414
Cdd:PRK10624 297 EKYRDIARAMGVKVEGMSLEEARNAAVEAVKALNRDVGIPPHLRDVGVKEEDIPALAQAAF-DDVCTGGNPREATLEDIV 375
|
....*..
gi 119607307 415 ALFEASM 421
Cdd:PRK10624 376 ELYKKAW 382
|
|
| AAD_C |
cd08178 |
C-terminal alcohol dehydrogenase domain of the acetaldehyde dehydrogenase-alcohol ... |
25-386 |
4.12e-40 |
|
C-terminal alcohol dehydrogenase domain of the acetaldehyde dehydrogenase-alcohol dehydrogenase bifunctional two-domain protein (AAD); This alcohol dehydrogenase domain is located on the C-terminal of a bifunctional two-domain protein. The N-terminal of the protein contains an acetaldehyde-CoA dehydrogenase domain. This protein is involved in pyruvate metabolism whereby pyruvate is converted to acetyl-CoA and formate by pyruvate formate-lysase (PFL). Under anaerobic condition, acetyl-CoA is reduced to acetaldehyde and ethanol by this two-domain protein. Acetyl-CoA is first converted into an enzyme-bound thiohemiacetal by the N-terminal acetaldehyde dehydrogenase domain. The enzyme-bound thiohemiacetal is subsequently reduced by the C-terminal NAD+-dependent alcohol dehydrogenase domain. In E. coli, this protein is called AdhE and has been shown to have pyruvate formate-lyase (PFL) deactivase activity, which leads to the inactivation of PFL, a key enzyme in anaerobic metabolism. In Escherichia coli and Entamoeba histolytica, this enzyme forms homopolymeric peptides composed of more than 20 protomers associated in a helical rod-like structure.
Pssm-ID: 341457 [Multi-domain] Cd Length: 400 Bit Score: 147.72 E-value: 4.12e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 25 LKNMGAKNVCLMTDKNLSKLPPVQVAMDSLVKNGIPFTVYDNVRVEPTDSSFMEAIEfaQKGAF--DAYVAVGGGSTMDT 102
Cdd:cd08178 18 LELPGVKRAFIVTDRVLYKLGYVDKVLDVLEARGVETEVFSDVEPDPTLSTVRKGLE--AMNAFkpDVIIALGGGSAMDA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 103 CKAANLYASSPHSDFLDYVSAPIGKGKPVSVPLKP-----LIAVPTTSGTGSETTGVAIFDYEHLKVKIGITSRAIKPTL 177
Cdd:cd08178 96 AKIMWLFYEHPETKFEDLAQRFMDIRKRVYKFPKLgkkakLVAIPTTSGTGSEVTPFAVITDDKTGKKYPLADYALTPDM 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 178 GLIDPLHTLHMPARVVANSGFDVLCHALESYTtlpyhlrSPCpsnpitrpayqgSNPISDIWAIHALRIVAKYLKRAVRN 257
Cdd:cd08178 176 AIVDPELVMTMPKRLTADTGIDALTHAIEAYV-------SVM------------ASDYTDGLALQAIKLIFEYLPRSYNN 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 258 PDDLEARSHMHLASAFAGIGFGNAGVHLCHGMSYPISGLVKmykakdynvdhplVPHGLSVVLTSPAVFTFTAQ------ 331
Cdd:cd08178 237 GNDIEAREKMHNAATIAGMAFANAFLGICHSLAHKLGAAFH-------------IPHGRANAILLPHVIRYNATdpptkq 303
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119607307 332 -MFP--------ERHLEMAEILGADTRTariqDAGLV--LADTLRKFLFDLDVDDGLAAVGYSKAD 386
Cdd:cd08178 304 aAFPqykyyvakERYAEIADLLGLGGKT----PEEKVesLIKAIEDLKKDLGIPTSIREAGIDEAD 365
|
|
| BDH |
cd08187 |
Butanol dehydrogenase catalyzes the conversion of butyraldehyde to butanol with the cofactor ... |
51-418 |
2.27e-38 |
|
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: 142.57 E-value: 2.27e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 51 MDSLVKNGIPFTVYDNVRVEPTDSSFMEAIEFAQKGAFDAYVAVGGGSTMDTCKAANLYASSPHsDFLDYVSapigKGKP 130
Cdd:cd08187 50 VASLKEAGIEVVEFGGVEPNPRLETVREGIELAREENVDFILAVGGGSVIDAAKAIAAGAKYDG-DVWDFFT----GKAP 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 131 VSVPLkPLIAVPTTSGTGSETTGVAIFDYEHLKVKIGITSRAIKPTLGLIDPLHTLHMPARVVANSGFDVLCHALESYTT 210
Cdd:cd08187 125 PEKAL-PVGTVLTLAATGSEMNGGAVITNEETKEKLGFGSPLLRPKFSILDPELTYTLPKYQTAAGIVDIFSHVLEQYFT 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 211 LPYHlrspcpsnpitrpayqgsNPISDIWAIHALRIVAKYLKRAVRNPDDLEARSHMHLASAFA--GI-GFGNAGVHLCH 287
Cdd:cd08187 204 GTED------------------APLQDRLAEGLLRTVIENGPKALKDPDDYEARANLMWAATLAlnGLlGAGRGGDWATH 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 288 GMSYPISGLvkmykakdYNVDHplvPHGLSVVLtsPAVFTFTAQMFPERHLEMAE------ILGADTRTAriqDAGLvla 361
Cdd:cd08187 266 AIEHELSAL--------YDITH---GAGLAIVF--PAWMRYVLKKKPERFAQFARrvfgidPGGDDEETA---LEGI--- 326
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 119607307 362 DTLRKFLFDLDVDDGLAAVGYSKADIPALVKGTLPQERVTKLAPcPQSEEDLAALFE 418
Cdd:cd08187 327 EALEEFFKSIGLPTTLSELGIDEEDIEEMAEKAVRGGGLGGGFK-PLTREDIEEILK 382
|
|
| Fe-ADH-like |
cd14864 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
4-419 |
5.94e-35 |
|
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: 133.20 E-value: 5.94e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 4 SNIRYGAAVTKEVGmasirDDLKNMGAKNVcLMTDKNLSKLPPVQVAMDSLVKNGIPFTVYDNVRVEPTDSSFMEAIEFA 83
Cdd:cd14864 5 PNIVFGADSLERIG-----EEVKEYGSRFL-LITDPVLKESGLADKIVSSLEKAGISVIVFDEIPASATSDTIDEAAELA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 84 QKGAFDAYVAVGGGSTMDTCKAANLYASSPHsDFLDYVSAPIGKGKPVsvplkPLIAVPTTSGTGSETTGVAIF-DYEHL 162
Cdd:cd14864 79 RKAGADGIIAVGGGKVLDTAKAVAILANNDG-GAYDFLEGAKPKKKPL-----PLIAVPTTPRSGFEFSDRFPVvDSRSR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 163 KVKIgITSRAIKPTLGLIDPLHTLHMPARVVANSGFDVLCHALESYTTlpyhlrspcpsnpitrpayQGSNPISDIWAIH 242
Cdd:cd14864 153 EVKL-LKAQPGLPKAVIVDPNLMASLTGNQTAAMALAALALAVEAYLS-------------------KKSNFFSDALALK 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 243 ALRIVAKYLKRAVRNPDDLEARSHMHLASAFAGIGFGNAGVHLCHGMSYPISGLvkmykakdYNVDHPLVphgLSVVLts 322
Cdd:cd14864 213 AIELVSENLDGALADPKNTPAEELLAQAGCLAGLAASSSSPGLATALALAVNSR--------YKVSKSLV---ASILL-- 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 323 PAVFTFTAQMFPERHLEMAEILGADTRTARIQDAGLVLADTLRKFLFDLDVDDGLAAVGyskadipalVKGTLPQ----- 397
Cdd:cd14864 280 PHVIEYAATSAPDKYAKIARALGEDVEGASPEEAAIAAVEGVRRLIAQLNLPTRLKDLD---------LASSLEQlaaia 350
|
410 420
....*....|....*....|....
gi 119607307 398 --ERVTKLAPCPQSEEDLAALFEA 419
Cdd:cd14864 351 edAPKLNGLPRSMSSDDIFDILKA 374
|
|
| PRK13805 |
PRK13805 |
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional |
28-386 |
2.66e-33 |
|
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional
Pssm-ID: 237515 [Multi-domain] Cd Length: 862 Bit Score: 132.62 E-value: 2.66e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 28 MGAKNVCLMTDKNLSKLPPVQVAMDSL--VKNGIPFTVYDNVRVEPTDSSFMEAIEFAQkgAF--DAYVAVGGGSTMDTC 103
Cdd:PRK13805 478 DGKKRAFIVTDRFMVELGYVDKVTDVLkkRENGVEYEVFSEVEPDPTLSTVRKGAELMR--SFkpDTIIALGGGSPMDAA 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 104 KAANLYASSPHSDFLD------------YVSAPIG-KGKPVSVP--------LKPlIAVpttsgtgsettgvaIFDyEHL 162
Cdd:PRK13805 556 KIMWLFYEHPETDFEDlaqkfmdirkriYKFPKLGkKAKLVAIPttsgtgseVTP-FAV--------------ITD-DKT 619
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 163 KVKIGITSRAIKPTLGLIDPLHTLHMPARVVANSGFDVLCHALESYTTLPyhlrspcpsnpitrpayqgSNPISDIWAIH 242
Cdd:PRK13805 620 GVKYPLADYELTPDVAIVDPNLVMTMPKSLTADTGIDALTHALEAYVSVM-------------------ASDYTDGLALQ 680
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 243 ALRIVAKYLKRAVRN-PDDLEARSHMHLASAFAGIGFGNAGVHLCHGMSYPISGLVKmykakdynvdhplVPHGLSVVLT 321
Cdd:PRK13805 681 AIKLVFEYLPRSYKNgAKDPEAREKMHNASTIAGMAFANAFLGICHSMAHKLGAEFH-------------IPHGRANAIL 747
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 322 SPAVFTFTAQ------MFP--------ERHLEMAEILG--ADTRTARIQdaglVLADTLRKFLFDLDVDDGLAAVGYSKA 385
Cdd:PRK13805 748 LPHVIRYNATdppkqaAFPqyeypradERYAEIARHLGlpGSTTEEKVE----SLIKAIEELKAELGIPMSIKEAGVDEA 823
|
.
gi 119607307 386 D 386
Cdd:PRK13805 824 D 824
|
|
| PRK09860 |
PRK09860 |
putative alcohol dehydrogenase; Provisional |
16-421 |
2.30e-31 |
|
putative alcohol dehydrogenase; Provisional
Pssm-ID: 182118 [Multi-domain] Cd Length: 383 Bit Score: 123.53 E-value: 2.30e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 16 VGMASIRDDLKNM---GAKNVCLMTDKNLSKLPPVQVAMDSLVKNGIPFTVYDNVRVEPTDSSFMEAIEFAQKGAFDAYV 92
Cdd:PRK09860 14 IGADSLTDAMNMMadyGFTRTLIVTDNMLTKLGMAGDVQKALEERNIFSVIYDGTQPNPTTENVAAGLKLLKENNCDSVI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 93 AVGGGSTMDTCKAANLYASSpHSDFLDYvsapigKGKPVSV-PLKPLIAVPTTSGTGSETTGVAIFDYEHLKVKIGITSR 171
Cdd:PRK09860 94 SLGGGSPHDCAKGIALVAAN-GGDIRDY------EGVDRSAkPQLPMIAINTTAGTASEMTRFCIITDEARHIKMAIVDK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 172 AIKPTLGLIDPLHTLHMPARVVANSGFDVLCHALESYTTLpyhlrspcpsnpitrpayqGSNPISDIWAIHALRIVAKYL 251
Cdd:PRK09860 167 HVTPLLSVNDSSLMIGMPKSLTAATGMDALTHAIEAYVSI-------------------AATPITDACALKAVTMIAENL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 252 KRAVRNPDDLEARSHMHLASAFAGIGFGNAGVHLCHGMSYPISGLvkmykakdYNvdhplVPHGLSVVLTSPAVFTFTAQ 331
Cdd:PRK09860 228 PLAVEDGSNAKAREAMAYAQFLAGMAFNNASLGYVHAMAHQLGGF--------YN-----LPHGVCNAVLLPHVQVFNSK 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 332 MFPERHLEMAEILGADTRTARIQDAGLVLADTLRKFLFDLDVDDGLAAVGYSKADIPALVKGTLpQERVTKLAPCPQSEE 411
Cdd:PRK09860 295 VAAARLRDCAAAMGVNVTGKNDAEGAEACINAIRELAKKVDIPAGLRDLNVKEEDFAVLATNAL-KDACGFTNPIQATHE 373
|
410
....*....|
gi 119607307 412 DLAALFEASM 421
Cdd:PRK09860 374 EIVAIYRAAM 383
|
|
| Fe-ADH-like |
cd14866 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
6-419 |
3.07e-26 |
|
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: 108.86 E-value: 3.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 6 IRYGAAVtkevgMASIRDDLKNMGAKNVCLMTDKNLSKLPPVqvaMDsLVKNGI---PFTVYDNVRVEPTDSSFMEAIEF 82
Cdd:cd14866 8 LFSGRGA-----LARLGRELDRLGARRALVVCGSSVGANPDL---MD-PVRAALgdrLAGVFDGVRPHSPLETVEAAAEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 83 AQKGAFDAYVAVGGGSTMDTCKAANLYASSPhSDFLDYVSAPIGKGKPVS----VPLKPLIAVPTTSGTGSETTGVAIFD 158
Cdd:cd14866 79 LREADADAVVAVGGGSAIVTARAASILLAED-RDVRELCTRRAEDGLMVSprldAPKLPIFVVPTTPTTADVKAGSAVTD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 159 YEHLKvKIGITSRAIKPTLGLIDPLHTLHMPARVVANSGFDVLCHALESyttlpyhLRSPcpsnpitrpayqGSNPISDI 238
Cdd:cd14866 158 PPAGQ-RLALFDPKTRPAAVFYDPELLATAPASLVAGAAMNGFDMAVEG-------LYSR------------HADPLADA 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 239 WAIHALRIVAKYLKRAVrNPDDLEARSHMHLASAFAGIGFGNAGVHLCHGMSYPISGlvkmykakDYNVDHPLVpHglSV 318
Cdd:cd14866 218 TLMHALRLLADGLPRLA-DDDDPAARADLVLAAVLAGYGTDHTGGGVIHALGHAIGA--------RYGVQNGVV-H--AI 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 319 VLtsPAVFTFTAQMFPERHLEMAEILGADTRTAriQDAGLVLADTLRKFLFDLDVDDGLAAVGYSKADIPALVKGTLPQE 398
Cdd:cd14866 286 LL--PHVLRFNAPATDGRLDRLAEALGVADAGD--EASAAAVVDAVEALLDALGVPTRLRDLGVSREDLPAIAEAAMDDW 361
|
410 420
....*....|....*....|.
gi 119607307 399 RVTKLAPCPQSEEDLAALFEA 419
Cdd:cd14866 362 FMDNNPRPVPTAEELEALLEA 382
|
|
| PRK15454 |
PRK15454 |
ethanolamine utilization ethanol dehydrogenase EutG; |
29-420 |
3.31e-26 |
|
ethanolamine utilization ethanol dehydrogenase EutG;
Pssm-ID: 185351 [Multi-domain] Cd Length: 395 Bit Score: 108.96 E-value: 3.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 29 GAKNVCLMTDKNLSKLPPVQVAMDSLVKNGIPFTVYDNVRVEPTDSSFMEAIEFAQKGAFDAYVAVGGGSTMDTCKAANL 108
Cdd:PRK15454 48 GLKHLFVMADSFLHQAGMTAGLTRSLAVKGIAMTLWPCPVGEPCITDVCAAVAQLRESGCDGVIAFGGGSVLDAAKAVAL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 109 YASSPHSDFLDYVSapigkgKPVSVPLKPLIAVPTTSGTGSETTGVAIFDYEHLKVKIGITSRAIKPTLGLIDPLHTLHM 188
Cdd:PRK15454 128 LVTNPDSTLAEMSE------TSVLQPRLPLIAIPTTAGTGSETTNVTVIIDAVSGRKQVLAHASLMPDVAILDAALTEGV 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 189 PARVVANSGFDVLCHALESYTTLpyhlrspcpsnpitrpayqGSNPISDIWAIHALRIVAKYLKRAVRNPDDLEARSHMH 268
Cdd:PRK15454 202 PSHVTAMTGIDALTHAIEAYSAL-------------------NATPFTDSLAIGAIAMIGKSLPKAVGYGHDLAARESML 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 269 LASAFAGIGFGNAGVHLCHGMSY-PISGLvkmykakdynvdHplVPHGLSVVLTSPAVFTFTAQMFPERHLEMAEILgaD 347
Cdd:PRK15454 263 LASCMAGMAFSSAGLGLCHAMAHqPGAAL------------H--IPHGLANAMLLPTVMEFNRMVCRERFSQIGRAL--R 326
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119607307 348 TRTARIQDAglvlADTLRKFLFDLDVDDGLAAVGYSKADIPALVKGTLpQERVTKLAPCPQSEEDLAALFEAS 420
Cdd:PRK15454 327 TKKSDDRDA----INAVSELIAEVGIGKRLGDVGATSAHYGAWAQAAL-EDICLRSNPRTASLEQIVGLYAAA 394
|
|
| MAR-like |
cd08192 |
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic ... |
6-419 |
7.07e-26 |
|
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: 107.72 E-value: 7.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 6 IRYGAAVtkevgMASIRDDLKNMGAKNVCLMTDKNLSKLPPV--QVAM---DSLVkngipfTVYDNVRVEPTDSSFMEAI 80
Cdd:cd08192 4 VSYGPGA-----VEALLHELATLGASRVFIVTSKSLATKTDVikRLEEalgDRHV------GVFSGVRQHTPREDVLEAA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 81 EFAQKGAFDAYVAVGGGSTMDTCKAANLYASSPHSDFLDYVSAPIGKGKPVSV--PLKPLIAVPTTSGTGSETTGVAIFD 158
Cdd:cd08192 73 RAVREAGADLLVSLGGGSPIDAAKAVALALAEDVTDVDQLDALEDGKRIDPNVtgPTLPHIAIPTTLSGAEFTAGAGATD 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 159 yEHLKVKIGITSRAIKPTLGLIDPLHTLHMPARVVANSGFDVLCHALESYttlpYHLRSpcpsnpitrpayqgsNPISDI 238
Cdd:cd08192 153 -DDTGHKQGFAHPELGPDAVILDPELTLHTPERLWLSTGIRAVDHAVETL----CSPQA---------------TPFVDA 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 239 WAIHALRIVAKYLKRAVRNPDDLEARSHMHLASAFAGIGFGN-AGVHLCHGMSYPISGLvkmykakdYNvdhplVPHGLS 317
Cdd:cd08192 213 LALKALRLLFEGLPRSKADPEDLEARLKCQLAAWLSLFGLGSgVPMGASHAIGHQLGPL--------YG-----VPHGIT 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 318 VVLTSPAVFTFTAQMFPERHLEMAEILGADTRTARIQDAGlvLADTLRKFLFDLDVDDGLAAVGYSKADIPALVKGTLPQ 397
Cdd:cd08192 280 SCIMLPAVLRFNAPVNAERQRLIARALGLVTGGLGREAAD--AADAIDALIRELGLPRTLRDVGVGRDQLEKIAENALTD 357
|
410 420
....*....|....*....|..
gi 119607307 398 ERVTKLAPCPQSEEDLAALFEA 419
Cdd:cd08192 358 VWCRTNPRPITDKDDVLEILES 379
|
|
| 4HBD_NAD |
cd14860 |
4-hydroxybutyrate dehydrogenase, also called gamma-hydroxybutyrate dehydrogenase, catalyzes ... |
70-424 |
1.77e-25 |
|
4-hydroxybutyrate dehydrogenase, also called gamma-hydroxybutyrate dehydrogenase, catalyzes the reduction of succinic simialdehyde to 4-hydroxybutyrate in the succinic degradation pathway; 4-hydroxybutyrate dehydrogenase (4HBD) is an iron-containing (type III) NAD-dependent alcohol dehydrogenase. It plays a role in the succinate metabolism biochemical pathway. It catalyzes the reduction of succinic simialdehide to 4-hydroxybutyrate in the succinate degradation pathway This succinate degradation pathway is present in some bacteria which can use succinate as sole carbon source.
Pssm-ID: 341482 Cd Length: 371 Bit Score: 106.53 E-value: 1.77e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 70 EPTDSSFMEAIEFAQKGAFDAYVAVGGGSTMDTCKaanLYASSPHSDFLDYVS--APIGKGKPvsvplkpLIAVPTTSGT 147
Cdd:cd14860 61 EPSDEMVEAIYKDIKKYGYKRVIAIGGGTVIDIAK---LLALKGISPVLDLFDgkIPLIKEKE-------LIIVPTTCGT 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 148 GSETTGVAIFDYEHLKVKIGITSRAIKPTLGLIDP--LHTLhmPARVVANSGFDVLCHALESYTtlpyhlrSPcpsnpit 225
Cdd:cd14860 131 GSEVTNISIVELTSLGTKKGLAVDELYADKAVLIPelLKGL--PYKVFATSSIDALIHAIESYL-------SP------- 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 226 rpayqGSNPISDIWAIHALR-IVAKYLKRAVRNPDDL-EARSHMHLASAFAGIGFGNAGVHLCHGMSYPISGlvkMYKak 303
Cdd:cd14860 195 -----KATPYTEMFSYKAIEmILEGYQEIAEKGEEARfPLLGDFLIASNYAGIAFGNAGCAAVHALSYPLGG---KYH-- 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 304 dynvdhplVPHGLS--VVLTspAVFTFTAQMFPERHLE-----MAEILGADTRTAriqdaglvlADTLRKFLFDLDVDDG 376
Cdd:cd14860 265 --------VPHGEAnyAVFT--GVLKNYQEKNPDGEIKklnefLAKILGCDEEDV---------YDELEELLNKILPKKP 325
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 119607307 377 LAAVGYSKADIPALVKGTLP-QERVTKLAPCPQSEEDLAALFeasMKLY 424
Cdd:cd14860 326 LHEYGMKEEEIDEFADSVMEnQQRLLANNYVPLDREDVAEIY---KELY 371
|
|
| YqdH |
COG1979 |
Alcohol dehydrogenase YqhD, Fe-dependent ADH family [Energy production and conversion]; |
48-392 |
1.80e-23 |
|
Alcohol dehydrogenase YqhD, Fe-dependent ADH family [Energy production and conversion];
Pssm-ID: 441582 [Multi-domain] Cd Length: 387 Bit Score: 100.92 E-value: 1.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 48 QVaMDSLVKNGIPFTVYDNVRVEPTDSSFMEAIEFAQKGAFDAYVAVGGGSTMDTCK---AANLYAssphSDFLDYVSap 124
Cdd:COG1979 50 QV-KAALKEAGIEVVEFGGVEPNPRLETVRKGVELCKEEGIDFILAVGGGSVIDGAKaiaAGAKYD----GDPWDILT-- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 125 igKGKPVSVPLkPLIAVPTTSGTGSETTGVAIFDYEHLKVKIGITSRAIKPTLGLIDPLHTLHMPARVVANSGFDVLCHA 204
Cdd:COG1979 123 --GKAPVEKAL-PLGTVLTLPATGSEMNSGSVITNEETKEKLGFGSPLVFPKFSILDPELTYTLPKRQTANGIVDIFSHV 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 205 LESYTTLPyhlrspcpsnpitrpayqGSNPISDIWAIHALRIVAKYLKRAVRNPDDLEARSHMHLASAFAGIGFGNAGVH 284
Cdd:COG1979 200 MEQYFTYP------------------VDAPLQDRFAEGLLRTLIEEGPKALKDPEDYDARANLMWAATLALNGLIGAGVP 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 285 ---LCHGMSYPISGLvkmykakdYNVDHplvPHGLSVVLtsPAVFTFTAQMFPERHLEMAE-ILGADTRT--ARIQDAgl 358
Cdd:COG1979 262 qdwATHMIEHELSAL--------YDIDH---GAGLAIVL--PAWMRYVLEEKPEKFAQYAErVWGITEGDdeERALEG-- 326
|
330 340 350
....*....|....*....|....*....|....
gi 119607307 359 vlADTLRKFLFDLDVDDGLAAVGYSKADIPALVK 392
Cdd:COG1979 327 --IEATEEFFESLGLPTRLSEYGIDEEDIEEMAE 358
|
|
| MAR |
cd08177 |
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic ... |
78-419 |
1.02e-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: 80.63 E-value: 1.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 78 EAIEFAQKGAFDAYVAVGGGSTmdtckaanlyassphsdfldyvsapIGKGKPVSVPLK-PLIAVPTTSgtgsettgvA- 155
Cdd:cd08177 67 RALAAAREAGADGLVAIGGGSA-------------------------IGLAKAIALRTGlPIVAVPTTY---------Ag 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 156 -----IFDYEHLKVKIGITSRAIKPTLGLIDPLHTLHMPARVVANSGFDVLCHALESyttlpyhLRSPcpsnpitrpayq 230
Cdd:cd08177 113 semtpIWGETEDGVKTTGRDPRVLPRTVIYDPDLTLGLPAALSVASGLNALAHAVEA-------LYAP------------ 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 231 GSNPISDIWAIHALRIVAKYLKRAVRNPDDLEARSHMHLASAFAGIGFGNAG--VH--LCH--GMSYpisGLvkmykakd 304
Cdd:cd08177 174 DANPITSLLAEEGIRALARALPRLVADPSDLEARSDALYGAWLAGVVLGSVGmgLHhkLCHvlGGTF---DL-------- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 305 ynvdhplvPHGL--SVVLtsPAVFTFTAQMFPERHLEMAEILGADtrtariqDAGLVLADTLRkflfDLDVDDGLAAVGY 382
Cdd:cd08177 243 --------PHAEthAVVL--PHVLAYNAPAAPDAMARLARALGGG-------DAAGGLYDLAR----RLGAPTSLRDLGM 301
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 119607307 383 SKADIPALVkgtlpqERVTKLA---PCPQSEEDLAALFEA 419
Cdd:cd08177 302 PEDDIDRAA------DLALANPypnPRPVERDALRALLER 335
|
|
| PRK15138 |
PRK15138 |
alcohol dehydrogenase; |
53-403 |
2.22e-09 |
|
alcohol dehydrogenase;
Pssm-ID: 185092 [Multi-domain] Cd Length: 387 Bit Score: 58.65 E-value: 2.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 53 SLVKNGIPFTVYD-----NVR----VEPTDS--SFMEAIEFAQKGAFDAYVAVGGGSTMDTCK----AANLYASSPHSDF 117
Cdd:PRK15138 40 SVKKTGVLDQVLDalkgmDVLefggIEPNPTyeTLMKAVKLVREEKITFLLAVGGGSVLDGTKfiaaAANYPENIDPWHI 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 118 LDYVSAPIGKGkpvsVPLKPLIAVPTTSGTGSETtgvAIFDYEHLKVKIGITSRAIKPTLGLIDPLHTLHMPARVVANSG 197
Cdd:PRK15138 120 LETGGKEIKSA----IPMGSVLTLPATGSESNAG---AVISRKTTGDKQAFHSPHVQPVFAVLDPVYTYTLPPRQVANGV 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 198 FDVLCHALESYTTLPYHLRspcpsnpitrpayqgsnpISDIWAIHALRIVAKYLKRAVRNPDDLEARSHMHLASAFAGIG 277
Cdd:PRK15138 193 VDAFVHTVEQYVTYPVDAK------------------IQDRFAEGILLTLIEEGPKALKEPENYDVRANVMWAATQALNG 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 278 FGNAGVH---LCHGMSYPISGLvkmykakdYNVDHplvPHGLSVVLtsPAVFTFTAQMFPERHLEMAEI---LGADTRTA 351
Cdd:PRK15138 255 LIGAGVPqdwATHMLGHELTAM--------HGLDH---AQTLAIVL--PALWNEKRDTKRAKLLQYAERvwnITEGSDDE 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 119607307 352 RIQDAglvLADTlRKFLFDLDVDDGLAAVGYSKADIPALVKgTLPQERVTKL 403
Cdd:PRK15138 322 RIDAA---IAAT-RNFFEQMGVPTRLSDYGLDGSSIPALLK-KLEEHGMTQL 368
|
|
| DHQ_Fe-ADH |
cd07766 |
Dehydroquinate synthase-like (DHQ-like) and iron-containing alcohol dehydrogenases (Fe-ADH); ... |
19-206 |
3.81e-09 |
|
Dehydroquinate synthase-like (DHQ-like) and iron-containing alcohol dehydrogenases (Fe-ADH); This superfamily consists of two subgroups: the dehydroquinate synthase (DHQS)-like, and a large metal-containing alcohol dehydrogenases (ADH), known as iron-containing alcohol dehydrogenases. Dehydroquinate synthase (DHQS) catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate-7-phosphate (DAHP) to dehydroquinate (DHQ) in the second step of the shikimate pathway. This pathway involves seven sequential enzymatic steps in the conversion of erythrose 4-phosphate and phosphoenolpyruvate into chorismate for subsequent synthesis of aromatic compounds. Dehydroquinate synthase-like group includes dehydroquinate synthase, 2-deoxy-scyllo-inosose synthase, and 2-epi-5-epi-valiolone synthase. The alcohol dehydrogenases (ADHs) in this superfamily contain a dehydroquinate synthase-like protein structural fold and mostly contain iron. They are distinct from other alcohol dehydrogenases which contains different protein domains. There are several distinct families of alcohol dehydrogenases: Zinc-containing long-chain alcohol dehydrogenases; insect-type, or short-chain alcohol dehydrogenases; iron-containing alcohol dehydrogenases, and others. The iron-containing family has a Rossmann fold-like topology that resembles the fold of the zinc-dependent alcohol dehydrogenases, but lacks sequence homology, and differs in strand arrangement. ADH catalyzes the reversible oxidation of alcohol to acetaldehyde with the simultaneous reduction of NAD(P)+ to NAD(P)H.
Pssm-ID: 341447 [Multi-domain] Cd Length: 271 Bit Score: 57.37 E-value: 3.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 19 ASIRDDLKNMGAKnVCLMTDKNLSKLppVQVAMDSLVKNGIPFTVYDNVRVEPTDSSFMEAIEFAQKGAFDAYVAVGGGS 98
Cdd:cd07766 12 AKLGEIKRRGFDR-ALVVSDEGVVKG--VGEKVADSLKKGLAVAIFDFVGENPTFEEVKNAVERARAAEADAVIAVGGGS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 99 TMDTCKAANLyassphsdfldyvsapigkgkpVSVPLKPLIAVPTTSGTGSETTGVAIFDYEHLKVKIGITsrAIKPTLG 178
Cdd:cd07766 89 TLDTAKAVAA----------------------LLNRGIPFIIVPTTASTDSEVSPKSVITDKGGKNKQVGP--HYNPDVV 144
|
170 180
....*....|....*....|....*...
gi 119607307 179 LIDPLHTLHMPARVVANSGFDVLCHALE 206
Cdd:cd07766 145 FVDTDITKGLPPRQVASGGVDALAHAVE 172
|
|
| G1PDH-like |
cd08174 |
Glycerol-1-phosphate dehydrogenase-like; These glycerol-1-phosphate dehydrogenase-like ... |
27-141 |
4.53e-07 |
|
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: 51.37 E-value: 4.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 27 NMGAKNVCLMTDKNLSKLPPVQVAmDSLVKNGIPFTVYDNvrvepTDSSFMEAIEFAQKG-AFDAYVAVGGGSTMDTCK- 104
Cdd:cd08174 22 NQGFGKVAIVTGEGIDELLGEDIL-ESLEEAGEIVTVEEN-----TDNSAEELAEKAFSLpKVDAIVGIGGGKVLDVAKy 95
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 119607307 105 AANL----YASSPHSDFLDYVSAPI----GKGKPVSVPLKPLIAV 141
Cdd:cd08174 96 AAFLsklpFISVPTSLSNDGIASPVavlkVDGKRKSLGAKMPYGV 140
|
|
| Fe-ADH_2 |
pfam13685 |
Iron-containing alcohol dehydrogenase; |
25-290 |
3.73e-05 |
|
Iron-containing alcohol dehydrogenase;
Pssm-ID: 404557 [Multi-domain] Cd Length: 251 Bit Score: 44.99 E-value: 3.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 25 LKNMGAKNVCLMTDKNLSKLPPVQVAmDSLVKNGIPFTVYDNVRVEPTDSSFMEAIEFAQKGAFDAYVAVGGGSTMDTCK 104
Cdd:pfam13685 14 LAELGFRRVALVADANTYAAAGRKVA-ESLKRAGIEVETRLEVAGNADMETAEKLVGALRERDADAVVGVGGGTVIDLAK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 105 aanlyassphsdfldYVSAPIGkgkpvsvplKPLIAVPTTSGTGSETTGVAIFDYEHLKVKIGitsrAIKPTLGLIDPLH 184
Cdd:pfam13685 93 ---------------YAAFKLG---------KPFISVPTAASNDGFASPGASLTVDGKKRSIP----AAAPFGVIADTDV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 185 TLHMPARVVAnSGFDVLchaLESYTTLPYHlrspcpsnpitrpAYQGSNPISDIWAIHALRIVAKYLKRAVRNPDDLEAR 264
Cdd:pfam13685 145 IAAAPRRLLA-SGVGDL---LAKITAVADW-------------ELAHAEEVAAPLALLSAAMVMNFADRPLRDPGDIEAL 207
|
250 260
....*....|....*....|....*.
gi 119607307 265 SHMHLASAFAGIGFGNAGVHLCHGMS 290
Cdd:pfam13685 208 AELLSALAMGGAGSSRPASGSEHLIS 233
|
|
| Fe-ADH_KdnB-like |
cd08184 |
Iron-containing alcohol dehydrogenase similar to Shewanella oneidensis KdnB required for Kdo8N ... |
3-343 |
1.93e-04 |
|
Iron-containing alcohol dehydrogenase similar to Shewanella oneidensis KdnB required for Kdo8N biosynthesis; This family contains iron-containing alcohol dehydrogenase-like proteins, many of which have not been characterized. Their specific function is unknown. The protein structure represents a dehydroquinate synthase-like fold and belongs to the iron-containing alcohol dehydrogenase-like superfamily. It is distinct from other alcohol dehydrogenases which contain different protein domains. Alcohol dehydrogenase catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron or zinc ions. This family also includes Shewanella oneidensis KdnB which is required for biosynthesis of 8-Amino-3,8-dideoxy-D-manno-octulosonic acid (Kdo8N), a unique amino sugar that has thus far only been observed on the lipopolysaccharides of marine bacteria belonging to the genus Shewanella, and thought to be important for the integrity of the bacterial cell outer membrane. KdnB requires NAD(P) and zinc ion for activity.
Pssm-ID: 341463 [Multi-domain] Cd Length: 348 Bit Score: 43.41 E-value: 1.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 3 VSNIRYGAAVTKEVGmaSIRDDLKNMGAKNVCLMTDKNLSKLPPVqvamDSLVKNGIPFTVYDNVRVEPTDS---SFMEA 79
Cdd:cd08184 1 VPKYLFGRGSFDQLG--ELLAERRKSNNDYVVFFIDDVFKGKPLL----DRLPLQNGDLLIFVDTTDEPKTDqidALRAQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 80 IEFAQKGAFDAYVAVGGGSTMDTCKA-ANLYA---SSPHSDFLDYVsapigKGKPVsvplkPLIAVPTTSGTGSETTGVA 155
Cdd:cd08184 75 IRAENDKLPAAVVGIGGGSTMDIAKAvSNMLTnpgSAADYQGWDLV-----KNPGI-----YKIGVPTLSGTGAEASRTA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 156 IFDYEHLkvKIGITSRAIKPTLGLIDPLHTLHMPARVVANSGFDVLCHALESyttlpyhlrspcpsnpitrpaYQGS--N 233
Cdd:cd08184 145 VLTGPEK--KLGINSDYTVFDQVILDPELIATVPRDQYFYTGMDCYIHCVES---------------------LNGTyrN 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 234 PISDIWAIHALRIVAK-YLKRAVRNPDDLEarsHMHLASAFAGIGFGNAGVHLCHGMSYPISGLVKMykakdynvdhplv 312
Cdd:cd08184 202 AFGDAYAEKALELCRDvFLSDDMMSPENRE---KLMVASYLGGSSIANSQVGVCHALSYGLSVVLGT------------- 265
|
330 340 350
....*....|....*....|....*....|....
gi 119607307 313 PHGLSVVLtspaVFTFTAQMFPERHLE---MAEI 343
Cdd:cd08184 266 HHGVANCI----VFNVLEEFYPEGVKEfreMLEK 295
|
|
| GldA |
COG0371 |
Glycerol dehydrogenase or related enzyme, iron-containing ADH family [Energy production and ... |
31-106 |
8.86e-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: 41.31 E-value: 8.86e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119607307 31 KNVCLMTDKNLSKL--PPVQvamDSLVKNGIPFTVYdNVRVEPTDSSFMEAIEFAQKGAFDAYVAVGGGSTMDTCKAA 106
Cdd:COG0371 28 KRALIITGPTALKAagDRLE---ESLEDAGIEVEVE-VFGGECSEEEIERLAEEAKEQGADVIIGVGGGKALDTAKAV 101
|
|
| Gro1PDH |
cd08173 |
Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) catalyzes the reversible conversion between ... |
20-141 |
1.32e-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: 40.61 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607307 20 SIRDDLKNMG-AKNVCLMTDKNLSKLPpVQVAMDSLVKNGIPFTVYDNVRVEpTDSSFMEAIEFAQKGAFDAYVAVGGGS 98
Cdd:cd08173 14 KIGEVLKKLLlGKRALIITGPNTYKIA-GKRVEDLLESSGVEVVIVDIATIE-EAAEVEKVKKLIKESKADFIIGVGGGK 91
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 119607307 99 TMDTCKaanlYASSPHSdfLDYVSAP---------------IGKGKPVSVPLKPLIAV 141
Cdd:cd08173 92 VIDVAK----YAAYKLN--LPFISIPtsashdgiaspfasiKGGDKPYSIKAKAPIAI 143
|
|
| |
