|
Name |
Accession |
Description |
Interval |
E-value |
| HOT |
cd08190 |
Hydroxyacid-oxoacid transhydrogenase (HOT) involved in gamma-hydroxybutyrate metabolism; This ... |
51-464 |
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: 720.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 51 VSNIRYGAAVTKEVGMDLKNMGAKNVCLMTDKNLSKLPPVQVAMDSLVKNGIPFTVYDNVRVEPTDSSFMEAIEFAQKGA 130
Cdd:cd08190 1 ASNIRFGPGATRELGMDLKRLGAKKVLVVTDPGLAKLGLVERVLESLEKAGIEVVVYDGVRVEPTDESFEEAIEFAKEGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 131 FDAYVAVGGGSTMDTCKAANLYASSPhSDFLDYVSAPIGKGKPVSVPLKPLIAVPTTSGTGSETTGVAIFDYEHLKVKIG 210
Cdd:cd08190 81 FDAFVAVGGGSVIDTAKAANLYATHP-GDFLDYVNAPIGKGKPVPGPLKPLIAIPTTAGTGSETTGVAIFDLEELKVKTG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 211 ITSRAIKPTLGLIDPLHTLHMPARVVANSGFDVLCHALESYTTLPYHLRsPCPSNPITRPAYQGSNPISDIWAIHALRIV 290
Cdd:cd08190 160 ISSRYLRPTLAIVDPLLTLTLPPRVTASSGFDVLCHALESYTARPYNAR-PRPANPDERPAYQGSNPISDVWAEKAIELI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 291 AKYLKRAVRNPDDLEARSHMHLASAFAGIGFGNAGVHLCHGMSYPISGLVKMYKAKDYNVDHPLVPHGLSVVLTSPAVFT 370
Cdd:cd08190 239 GKYLRRAVNDGDDLEARSNMLLASTLAGIGFGNAGVHLPHAMAYPIAGLVKDYRPPGYPVDHPHVPHGLSVALTAPAVFR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 371 FTAQMFPERHLEMAEILGADTRTARIQDAGLVLADTLRKFLFDLDVDDGLAAVGYSKADIPALVKGTLPQERVTKLAPCP 450
Cdd:cd08190 319 FTAPACPERHLEAAELLGADTSGASDRDAGEVLADALIKLMRDIGIPNGLSALGYSEDDIPALVEGTLPQQRLLKLNPRP 398
|
410
....*....|....
gi 133922590 451 QSEEDLAALFEASM 464
Cdd:cd08190 399 VTEEDLEEIFEDAL 412
|
|
| EutG |
COG1454 |
Alcohol dehydrogenase, class IV [Energy production and conversion]; |
54-464 |
2.70e-109 |
|
Alcohol dehydrogenase, class IV [Energy production and conversion];
Pssm-ID: 441063 [Multi-domain] Cd Length: 381 Bit Score: 328.23 E-value: 2.70e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 54 IRYGAAVTKEVGMDLKNMGAKNVCLMTDKNLSKLPPVQVAMDSLVKNGIPFTVYDNVRVEPTDSSFMEAIEFAQKGAFDA 133
Cdd:COG1454 11 IVFGAGALAELGEELKRLGAKRALIVTDPGLAKLGLLDRVLDALEAAGIEVVVFDDVEPNPTVETVEAGAAAAREFGADV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 134 YVAVGGGSTMDTCKAANLYASSPHsDFLDYVSApigkgKPVSVPLKPLIAVP----------TtsgtgsettgVAIFDYE 203
Cdd:COG1454 91 VIALGGGSAIDAAKAIALLATNPG-DLEDYLGI-----KKVPGPPLPLIAIPttagtgsevtP----------FAVITDP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 204 HLKVKIGITSRAIKPTLGLIDPLHTLHMPARVVANSGFDVLCHALESYTTLpyhlrspcpsnpitrpayqGSNPISDIWA 283
Cdd:COG1454 155 ETGVKKGIADPELLPDVAILDPELTLTLPPSLTAATGMDALTHAIEAYVSK-------------------GANPLTDALA 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 284 IHALRIVAKYLKRAVRNPDDLEARSHMHLASAFAGIGFGNAGVHLCHGMSYPISGLvkmykakdYNvdhplVPHGLSVVL 363
Cdd:COG1454 216 LEAIRLIARNLPRAVADGDDLEAREKMALASLLAGMAFANAGLGAVHALAHPLGGL--------FH-----VPHGLANAI 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 364 TSPAVFTFTAQMFPERHLEMAEILGADTrTARIQDAGLVLADTLRKFLFDLDVDDGLAAVGYSKADIPALVKGTLpQERV 443
Cdd:COG1454 283 LLPHVLRFNAPAAPERYAEIARALGLDV-GLSDEEAAEALIEAIRELLRDLGIPTRLSELGVTEEDLPELAELAL-ADRC 360
|
410 420
....*....|....*....|.
gi 133922590 444 TKLAPCPQSEEDLAALFEASM 464
Cdd:COG1454 361 LANNPRPLTEEDIEAILRAAY 381
|
|
| Fe-ADH |
cd08551 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains large ... |
52-460 |
5.24e-105 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains large metal-containing alcohol dehydrogenases (ADH), known as iron-containing alcohol dehydrogenases. They contain a dehydroquinate synthase-like protein structural fold and mostly contain iron. They are distinct from other alcohol dehydrogenases which contains different protein domains. There are several distinct families of alcohol dehydrogenases: Zinc-containing long-chain alcohol dehydrogenases, insect-type, or short-chain alcohol dehydrogenases, iron-containing alcohol dehydrogenases, among others. The iron-containing family has a Rossmann fold-like topology that resembles the fold of the zinc-dependent alcohol dehydrogenases, but lacks sequence homology, and differs in strand arrangement. ADH catalyzes the reversible oxidation of alcohol to acetaldehyde with the simultaneous reduction of NAD(P)+ to NAD(P)H.
Pssm-ID: 341481 [Multi-domain] Cd Length: 372 Bit Score: 317.08 E-value: 5.24e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 52 SNIRYGAAVTKEVGMDLKNMGAKNVCLMTDKNLSKLPPVQVAMDSLVKNGIPFTVYDNVRVEPTDSSFMEAIEFAQKGAF 131
Cdd:cd08551 2 TRIVFGAGALARLGEELKALGGKKVLLVTDPGLVKAGLLDKVLESLKAAGIEVEVFDDVEPNPTVETVEAAAELAREEGA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 132 DAYVAVGGGSTMDTCKAANLYASSPHSDfLDYVSapigkGKPVSVPLKPLIAVPttsgtgsettGVAIFDYEHLKVKIGI 211
Cdd:cd08551 82 DLVIAVGGGSVLDTAKAIAVLATNGGSI-RDYEG-----IGKVPKPGLPLIAIPttagtgsevtPNAVITDPETGRKMGI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 212 TSRAIKPTLGLIDPLHTLHMPARVVANSGFDVLCHALESYTTLPyhlrspcpsnpitrpayqgSNPISDIWAIHALRIVA 291
Cdd:cd08551 156 VSPYLLPDVAILDPELTLSLPPSVTAATGMDALTHAIEAYTSKK-------------------ANPISDALALEAIRLIG 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 292 KYLKRAVRNPDDLEARSHMHLASAFAGIGFGNAGVHLCHGMSYPISGlvkMYKakdynvdhplVPHGLSVVLTSPAVFTF 371
Cdd:cd08551 217 KNLRRAVADGSDLEAREAMLLASLLAGIAFGNAGLGAVHALAYPLGG---RYH----------IPHGVANAILLPYVMEF 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 372 TAQMFPERHLEMAEILGADTRTARIQDAGLVLADTLRKFLFDLDVDDGLAAVGYSKADIPALVKGTLPQERVTKLAPCPQ 451
Cdd:cd08551 284 NLPACPEKYAEIAEALGEDVEGLSDEEAAEAAVEAVRELLRDLGIPTSLSELGVTEEDIPELAEDAMKSGRLLSNNPRPL 363
|
....*....
gi 133922590 452 SEEDLAALF 460
Cdd:cd08551 364 TEEDIREIY 372
|
|
| Fe-ADH |
pfam00465 |
Iron-containing alcohol dehydrogenase; |
52-456 |
1.05e-94 |
|
Iron-containing alcohol dehydrogenase;
Pssm-ID: 425696 [Multi-domain] Cd Length: 362 Bit Score: 290.27 E-value: 1.05e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 52 SNIRYGAAVTKEVGMDLKNMGAKnVCLMTDKNLSKLPPVQVAMDSLVKNGIPFTVYDNVRVEPTDSSFMEAIEFAQKGAF 131
Cdd:pfam00465 2 TRIVFGAGALAELGEELKRLGAR-ALIVTDPGSLKSGLLDKVLASLEEAGIEVVVFDGVEPEPTLEEVDEAAALAREAGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 132 DAYVAVGGGSTMDTCKAANLYASSPHSDFLDYvsapigKGKPVSVPLKPLIAVPTTSGTGSETTGVAIFDYEHLKVKIGI 211
Cdd:pfam00465 81 DVIIAVGGGSVIDTAKAIALLLTNPGDVWDYL------GGKPLTKPALPLIAIPTTAGTGSEVTPLAVITDTETGEKLGI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 212 TSRAIKPTLGLIDPLHTLHMPARVVANSGFDVLCHALESYTTlpyhlrspcpsnpitrpayQGSNPISDIWAIHALRIVA 291
Cdd:pfam00465 155 FSPKLLPDLAILDPELTLTLPPRLTAATGMDALAHAVEAYVS-------------------KGANPLTDALALEAIRLIA 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 292 KYLKRAVRNPDDLEARSHMHLASAFAGIGFGNAGVHLCHGMSYPISGLVKmykakdynvdhplVPHGLSVVLTSPAVFTF 371
Cdd:pfam00465 216 ENLPRAVADGEDLEARENMLLASTLAGLAFSNAGLGAAHALAHALGGRYG-------------IPHGLANAILLPYVLRF 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 372 TAQMFPERHLEMAEILGADTRTARIQDAglvlADTLRKFLFDLDVDDGLAAVGYSKADIPALVKGTLpQERVTKLAPCPQ 451
Cdd:pfam00465 283 NAPAAPEKLAQLARALGEDSDEEAAEEA----IEALRELLRELGLPTTLSELGVTEEDLDALAEAAL-RDRSLANNPRPL 357
|
....*
gi 133922590 452 SEEDL 456
Cdd:pfam00465 358 TAEDI 362
|
|
| Fe-ADH-like |
cd14863 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
54-462 |
1.91e-82 |
|
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: 259.39 E-value: 1.91e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 54 IRYGAAVTKEVGMDLKNMGAKNVCLMTDKNLSKLPPVQVAMDSLVKNGIPFTVYDNVRVEPTDSSFMEAIEFAQKGAFDA 133
Cdd:cd14863 8 VIFGAGAVEQIGELLKELGCKKVLLVTDKGLKKAGIVDKIIDLLEEAGIEVVVFDDVEPDPPDEIVDEAAEIAREEGADG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 134 YVAVGGGSTMDTCKAANLYASSPHSDfLDYvsapIGKGKPVSVPLKPLIAVPTTSGTGSETTGVAIFDYEHLKVKIGITS 213
Cdd:cd14863 88 VIGIGGGSVLDTAKAIAVLLTNPGPI-IDY----ALAGPPVPKPGIPLIAIPTTAGTGSEVTPIAVITDEENGVKKSLLG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 214 RAIKPTLGLIDPLHTLHMPARVVANSGFDVLCHALESYTTlpyhlrspcpsnpitrpayQGSNPISDIWAIHALRIVAKY 293
Cdd:cd14863 163 PFLVPDLAILDPELTVGLPPSLTAATGMDALSHAIEAYTS-------------------KLANPMTDALALQAIRLIVKN 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 294 LKRAVRNPDDLEARSHMHLASAFAGIGFGNAGVHLCHGMSYPISGLvkmykakdYNvdhplVPHGLSVVLTSPAVFTFTA 373
Cdd:cd14863 224 LPRAVKDGDNLEARENMLLASNLAGIAFNNAGTHIGHAIAHALGAL--------YH-----IPHGLACALALPVVLEFNA 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 374 QMFPERHLEMAEILGADTRTARIQDAGLVLADTLRKFLFDLDVDDGLAAVGYSKADIPALVKGTLpQERVTKLAPCPQSE 453
Cdd:cd14863 291 EAYPEKVKKIAKALGVSFPGESDEELGEAVADAIREFMKELGIPSLFEDYGIDKEDLDKIAEAVL-KDPFAMFNPRPITE 369
|
....*....
gi 133922590 454 EDLAALFEA 462
Cdd:cd14863 370 EEVAEILEA 378
|
|
| Fe-ADH-like |
cd08185 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
53-461 |
1.98e-76 |
|
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol dehydrogenase-like (ADH) proteins. Alcohol dehydrogenase catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase fold and is a member of the iron-containing alcohol dehydrogenase-like family. They are distinct from other alcohol dehydrogenases which contain different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341464 [Multi-domain] Cd Length: 379 Bit Score: 243.94 E-value: 1.98e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 53 NIRYGAAVTKEVGmDLKNMGAKNVCLMTDKNLSKLPPV-QVAMDSLVKNGIPFTVYDNVRVEPTDSSFMEAIEFAQKGAF 131
Cdd:cd08185 6 RILFGAGKLNELG-EEALRPGKKALIVTGKGSSKKTGLlDRVKKLLEKAGVEVVVFDKVEPNPLTTTVMEGAALAKEEGC 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 132 DAYVAVGGGSTMDTCKAANLYASSPHsDFLDYVSAPIGKGKPVSVPLkPLIAVPTTSGTGSETTGVAIFDYEHLKVKIGI 211
Cdd:cd08185 85 DFVIGLGGGSSMDAAKAIAFMATNPG-DIWDYIFGGTGKGPPPEKAL-PIIAIPTTAGTGSEVDPWAVITNPETKEKKGI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 212 TSRAIKPTLGLIDPLHTLHMPARVVANSGFDVLCHALESYTtlpyhlrspcpSNpitrpayqGSNPISDIWAIHALRIVA 291
Cdd:cd08185 163 GHPALFPKVSIVDPELMLTVPPRVTAYTGFDALFHAFESYI-----------SK--------NANPFSDMLALEAIRLVA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 292 KYLKRAVRNPDDLEARSHMHLASAFAGIGFGNAGVHLCHGMSYPISGLvkmykakdynvdHPLVPHGLSVVLTSPAVFTF 371
Cdd:cd08185 224 KYLPRAVKDGSDLEAREKMAWASTLAGIVIANSGTTLPHGLEHPLSGY------------HPNIPHGAGLAALYPAYFEF 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 372 TAQMFPER--HLEMAEILGADTrtariQDAGLVLADTLRKFLFDLDVDDGLAAVGYSKADIPALVkgtlpqERVTKLA-- 447
Cdd:cd08185 292 TIEKAPEKfaFVARAEASGLSD-----AKAAEDFIEALRKLLKDIGLDDLLSDLGVTEEDIPWLA------ENAMETMgg 360
|
410
....*....|....*....
gi 133922590 448 -----PCPQSEEDLAALFE 461
Cdd:cd08185 361 lfannPVELTEEDIVEIYE 379
|
|
| Fe-ADH-like |
cd08191 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
52-464 |
5.75e-75 |
|
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contain different protein domain. Proteins of this family have not been characterized.
Pssm-ID: 341470 [Multi-domain] Cd Length: 392 Bit Score: 240.59 E-value: 5.75e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 52 SNIRYGAAVTKEVGMDLKNMGAKnVCLMTDKNLSKLPPVQVAMDSLVKNGIPFTVYDNVRVEPTDSSFMEAIEFAQKGAF 131
Cdd:cd08191 5 SRLLFGPGARRALGRVAARLGSR-VLIVTDPRLASTPLVAELLAALTAAGVAVEVFDGGQPELPVSTVADAAAAARAFDP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 132 DAYVAVGGGSTMDTCKAANLYASSPhSDFLDYvsapIGKGKpVSVPLKPLIAVPTTSGTGSETTGVAIFDYEHLKVKIGI 211
Cdd:cd08191 84 DVVIGLGGGSNMDLAKVVALLLAHG-GDPRDY----YGEDR-VPGPVLPLIAVPTTAGTGSEVTPVAVLTDPARGMKVGV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 212 TSRAIKPTLGLIDPLHTLHMPARVVANSGFDVLCHALESYTTLPyhlRSPCPSNPiTRPAYQGSNPISDIWAIHALRIVA 291
Cdd:cd08191 158 SSPYLRPAVAIVDPELTLTCPPGVTADSGIDALTHAIESYTARD---FPPFPRLD-PDPVYVGKNPLTDLLALEAIRLIG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 292 KYLKRAVRNPDDLEARSHMHLASAFAGIGFGNAGVHLCHGMSYPISGLVkmykakdynvdHplVPHGLSVVLTSPAVFTF 371
Cdd:cd08191 234 RHLPRAVRDGDDLEARSGMALAALLAGLAFGTAGTAAAHALQYPIGALT-----------H--TSHGVGNGLLLPYVMRF 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 372 TAQMFPERHLEMAEILGADTrTARIQDAGLVLADTLRKFLFDLDVDDGLAAVGYSKADIPALVKGTLPQERVTKLAPCPQ 451
Cdd:cd08191 301 NRPARAAELAEIARALGVTT-AGTSEEAADRAIERVEELLARIGIPTTLADLGVTEADLPGLAEKALSVTRLIANNPRPP 379
|
410
....*....|...
gi 133922590 452 SEEDLAALFEASM 464
Cdd:cd08191 380 TEEDLLRILRAAF 392
|
|
| Fe-ADH-like |
cd17814 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
62-460 |
9.42e-70 |
|
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: 226.27 E-value: 9.42e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 62 KEVGMDLKNMGAKNVCLMTDKNLSKLPPVQVAMDSLVKNGIPFTVYDNVRVEPTDSSFMEAIE-FAQKGAfDAYVAVGGG 140
Cdd:cd17814 15 KLAGRYAKNLGARKVLVVTDPGVIKAGWVDEVLDSLEAEGLEYVVFSDVTPNPRDFEVMEGAElYREEGC-DGIVAVGGG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 141 STMDTCKAANLYASSpHSDFLDYvsapIGKGKpVSVPLKPLIAVPTTSGTGSETTGVAIFDYEHLKVKIGITSRAIKPTL 220
Cdd:cd17814 94 SPIDCAKGIGIVVSN-GGHILDY----EGVDK-VRRPLPPLICIPTTAGSSADVSQFAIITDTERRVKMAIISKTLVPDV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 221 GLIDPLHTLHMPARVVANSGFDVLCHALESYTtlpyhlrspcpSNpitrpayqGSNPISDIWAIHALRIVAKYLKRAVRN 300
Cdd:cd17814 168 SLIDPETLTTMDPELTACTGMDALTHAIEAYV-----------SN--------ASSPLTDLHALEAIRLISENLPKAVAD 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 301 PDDLEARSHMHLASAFAGIGFGNAGVHLCHGMSYPISGLVKMykakdynvdhplvPHGLSVVLTSPAVFTFTAQMFPERH 380
Cdd:cd17814 229 PDDLEAREKMMLASLQAGLAFSNASLGAVHAMAHSLGGLLDL-------------PHGECNALLLPHVIRFNFPAAPERY 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 381 LEMAEILGADTRTARIQDAGLVLADTLRKFLFDLDVDDGLAAVGYSKADIPALVKGTLpqeR----VTKlaPCPQSEEDL 456
Cdd:cd17814 296 RKIAEAMGLDVDGLDDEEVAERLIEAIRDLREDLGIPETLSELGVDEEDIPELAKRAM---KdpclVTN--PRRPTREDI 370
|
....
gi 133922590 457 AALF 460
Cdd:cd17814 371 EEIY 374
|
|
| Fe-ADH-like |
cd08194 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
52-434 |
7.21e-68 |
|
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: 221.64 E-value: 7.21e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 52 SNIRYGAAVTKEVGMDLKNMGAKNVCLMTDKNLSKLPPVQVAMDSLVKNGIPFTVYDNVRVEPTDSSFMEAIEFAQKGAF 131
Cdd:cd08194 2 RTIIIGGGALEELGEEAASLGGKRALIVTDKVMVKLGLVDKVTQLLAEAGIAYAVFDDVVSEPTDEMVEEGLALYKEGGC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 132 DAYVAVGGGSTMDTCKAANLYASSPhSDFLDYVSAPIGKGKPVsvplkPLIAVPTTSGTGSETTGVAIFDYEHLKVKIGI 211
Cdd:cd08194 82 DFIVALGGGSPIDTAKAIAVLATNG-GPIRDYMGPRKVDKPGL-----PLIAIPTTAGTGSEVTRFTVITDTETDVKMLL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 212 TSRAIKPTLGLIDPLHTLHMPARVVANSGFDVLCHALESYttlpyhlrspcpsnpITRPAyqgsNPISDIWAIHALRIVA 291
Cdd:cd08194 156 KGPALLPAVAIVDPELTLSMPPRVTAATGIDALTHAIEAY---------------VSRKA----QPLTDTLALSAIKLIG 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 292 KYLKRAVRNPDDLEARSHMHLASAFAGIGFGNAGVHLCHGMSYPISGLVkmykakdynvdHplVPHGLSVVLTSPAVFTF 371
Cdd:cd08194 217 RNLRRAYADGDDLEAREAMMLAALEAGIAFSNSSVALVHGMSRPIGALF-----------H--VPHGLSNAMLLPAVTEF 283
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 133922590 372 TAQMFPERHLEMAEILGADTRTARIQDAGLVLADTLRKFLFDLDVdDGLAAVGYSKADIPALV 434
Cdd:cd08194 284 SLPGAPERYAEIARAMGIATEGDSDEEAAEKLVEALERLCADLEI-PTLREYGIDEEEFEAAL 345
|
|
| Fe-ADH-like |
cd08196 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
45-460 |
6.68e-67 |
|
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: 218.60 E-value: 6.68e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 45 YAFEMAVsNIRYGAAVTKEVGMDLKNMGAKNVCLMTDKNLSKLPPVQVAMDSLVKNGIpfTVYDNVRVEPTDSSFMEAIE 124
Cdd:cd08196 1 WSYYQPV-KIIFGEGILKELPDIIKELGGKRGLLVTDPSFIKSGLAKRIVESLKGRIV--AVFSDVEPNPTVENVDKCAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 125 FAQKGAFDAYVAVGGGSTMDTCKAANLYASSPHSdFLDYvsapIGKGKPVSVPLKPLIAVPTTSGTGSETTGVAIFDYEH 204
Cdd:cd08196 78 LARENGADFVIAIGGGSVLDTAKAAACLAKTDGS-IEDY----LEGKKKIPKKGLPLIAIPTTAGTGSEVTPVAVLTDKE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 205 LKVKIGITSRAIKPTLGLIDPLHTLHMPARVVANSGFDVLCHALESYTTLpyhlrspcpsnpitrpayqGSNPISDIWAI 284
Cdd:cd08196 153 KGKKAPLVSPGFYPDIAIVDPELTYSMPPKVTASTGIDALCHAIEAYWSI-------------------NHQPISDALAL 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 285 HALRIVAKYLKRAVRNPDDLEARSHMHLASAFAGIGFGNAGVHLCHGMSYPISGLvkmykakdYNvdhplVPHGLSVVLT 364
Cdd:cd08196 214 EAAKLVLENLEKAYNNPNDKEAREKMALASLLAGLAFSQTRTTASHACSYPLTSH--------FG-----IPHGEACALT 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 365 SPAVFTFTAQMFPERHLEMAEILGADTrtarIQDaglvLADTLRKFLFDLDVDDGLAAVGYSKADIPALVKGTLPQERVt 444
Cdd:cd08196 281 LPSFIRLNAEALPGRLDELAKQLGFKD----AEE----LADKIEELKKRIGLRTRLSELGITEEDLEEIVEESFHPNRA- 351
|
410
....*....|....*.
gi 133922590 445 KLAPCPQSEEDLAALF 460
Cdd:cd08196 352 NNNPVEVTKEDLEKLL 367
|
|
| LPO |
cd08176 |
Lactadehyde:propanediol oxidoreductase (LPO) catalyzes the interconversion between ... |
56-435 |
8.41e-67 |
|
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: 218.57 E-value: 8.41e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 56 YGAAVTKEVGMDLKNMGAKNVCLMTDKNLSKLPPVQVAMDSLVKNGIPFTVYDNVRVEPTDSSFMEAIEFAQKGAFDAYV 135
Cdd:cd08176 11 FGWGAIEEIGEEAKKRGFKKALIVTDKGLVKFGIVDKVTDVLKEAGIAYTVFDEVKPNPTIENVMAGVAAYKESGADGII 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 136 AVGGGSTMDTCKAANLYASSPHSDFLDYVSApigkgKPVSVPLKPLIAVPTTSGTGSETTGVA-IFDYEHlKVKIGITSR 214
Cdd:cd08176 91 AVGGGSSIDTAKAIGIIVANPGADVRSLEGV-----APTKNPAVPIIAVPTTAGTGSEVTINYvITDTEK-KRKFVCVDP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 215 AIKPTLGLIDPLHTLHMPARVVANSGFDVLCHALESYTTLpyhlrspcpsnpitrpayqGSNPISDIWAIHALRIVAKYL 294
Cdd:cd08176 165 HDIPTVAIVDPDLMSSMPKGLTAATGMDALTHAIEGYITK-------------------GAWELSDMLALKAIELIAKNL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 295 KRAVRNPDDLEARSHMHLASAFAGIGFGNAGVHLCHGMSYPISGLvkmykakdYNvdhplVPHGLSVVLTSPAVFTFTAQ 374
Cdd:cd08176 226 RKAVANPNNVEARENMALAQYIAGMAFSNVGLGIVHSMAHPLSAF--------YD-----TPHGVANAILLPYVMEFNAP 292
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 133922590 375 MFPERHLEMAEILGADTRTARIQDAGLVLADTLRKFLFDLDVDDGLAAVGYSKADIPALVK 435
Cdd:cd08176 293 ATGEKYRDIARAMGVDTTGMSDEEAAEAAVDAVKKLSKDVGIPQKLSELGVKEEDIEALAE 353
|
|
| Fe-ADH-like |
cd14865 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
54-464 |
2.69e-63 |
|
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: 209.70 E-value: 2.69e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 54 IRYGAAVTKEVGMDLKNMGAKNVCLMTDKNLSKLPPVQVAMDSLVKNGIPFTVYDNVrvePTDSSF---MEAIEFAQKGA 130
Cdd:cd14865 9 IVSGAGALENLPAELARLGARRPLIVTDKGLAAAGLLKKVEDALGDAIEIVGVFDDV---PPDSSVavvNEAAARAREAG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 131 FDAYVAVGGGSTMDTCKAANLYASSPHSDFLDYVSAPIGKGkpvsvPLKPLIAVPTTSGTGSETTGVAIFDYEHLKVKIG 210
Cdd:cd14865 86 ADGIIAVGGGSVIDTAKGVNILLSEGGDDLDDYGGANRLTR-----PLKPLIAIPTTAGTGSEVTLVAVIKDEEKKVKLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 211 ITSRAIKPTLGLIDPLHTLHMPARVVANSGFDVLCHALESYTTLpyhlrspcpsnpitrpayqGSNPISDIWAIHALRIV 290
Cdd:cd14865 161 FVSPFLLPDVAILDPRLTLSLPPKLTAATGMDALTHAIEAYTSL-------------------QKNPISDALALQAIRLI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 291 AKYLKRAVRNPDDLEARSHMHLASAFAGIGFGNAGVHLCHGMSYPISGLVKmykakdynvdhplVPHGL--SVVLtsPAV 368
Cdd:cd14865 222 SENLPKAVKNGKDLEARLALAIAATMAGIAFSNSMVGLVHAIAHAVGAVAG-------------VPHGLanSILL--PHV 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 369 FTFTAQMFPERHLEMAEIL--GADTRTARIQDAGLVLADTLRKFLFDLDVDDGLAAVGYSKADIPALVKGTLpQERVTKL 446
Cdd:cd14865 287 MRYNLDAAAERYAELALALayGVTPAGRRAEEAIEAAIDLVRRLHELCGLPTRLRDVGVPEEQLEAIAELAL-NDGAILF 365
|
410
....*....|....*...
gi 133922590 447 APCPQSEEDLAALFEASM 464
Cdd:cd14865 366 NPREVDPEDILAILEAAY 383
|
|
| Fe-ADH-like |
cd14862 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
68-460 |
1.38e-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: 199.76 E-value: 1.38e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 68 LKNMGAKNVCLMTDKNLSKLPPVQVAMDSLVKNGIPFTVYDNVRVEPTDSSFMEAIEFAQKGAFDAYVAVGGGSTMDTCK 147
Cdd:cd14862 19 LEQLSGKRALIVTDKVLVKLGLLKKVLKRLLQAGFEVEVFDEVEPEPPLETVLKGAEAMREFEPDLIIALGGGSVMDAAK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 148 AANLYASSPHSDFLDYVSAPIGKGKPVSVplkpLIAVPTTSGTGSETTGVAIFDYEHLKVKIGITSRAIKPTLGLIDPLH 227
Cdd:cd14862 99 AAWVLYERPDLDPEDISPLDLLGLRKKAK----LIAIPTTSGTGSEATWAIVLTDTEEPRKIAVANPELVPDVAILDPEF 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 228 TLHMPARVVANSGFDVLCHALESYTtlpyhlrspCPSnpitrpayqgSNPISDIWAIHALRIVAKYLKRAVRNPDDLEAR 307
Cdd:cd14862 175 VLGMPPKLTAGTGLDALAHAVEAYL---------STW----------SNDFSDALALKAIELIFKYLPRAYKDGDDLEAR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 308 SHMHLASAFAGIGFGNAGVHLCHGMSYPISGLVKmykakdynvdhplVPHGLSVVLTSPAVFTFTAQmFPERHLEMAEIL 387
Cdd:cd14862 236 EKMHNAATIAGLAFGNSQAGLAHALGHSLGAVFH-------------VPHGIAVGLFLPYVIEFYAK-VTDERYDLLKLL 301
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 133922590 388 GADTRTAriQDAGLVLADTLRKFLFDLDVDDGLAAVGYSKAD----IPALVKGTLpQERVTKLAPCPQSEEDLAALF 460
Cdd:cd14862 302 GIEARDE--EEALKKLVEAIRELYKEVGQPLSIKDLGISEEEfeekLDELVEYAM-EDSCTITSPRPPSEEDLKKLF 375
|
|
| PDDH |
cd08188 |
1,3-Propanediol (1,3-PD) dehydrogenase; This family includes 1,3-propanediol (1,3-PD) ... |
57-461 |
2.89e-58 |
|
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: 196.20 E-value: 2.89e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 57 GAAVTKEVGMDLKNMGAKNVCLMTDKNLSKLPPVQVAMDSLVKNGIPFTVYDNVRVEPTDSSFMEAIEFAQKGAFDAYVA 136
Cdd:cd08188 12 GPGCLKEIGDELKKLGGKKALIVTDKGLVKLGLVKKVTDVLEEAGIEYVIFDGVQPNPTVTNVNEGLELFKENGCDFIIS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 137 VGGGSTMDTCKAANLYASSPhSDFLDYvsapIGKGKpVSVPLKPLIAVPTTSGTGSETTGVAIFDYEHLKVKIGITSRAI 216
Cdd:cd08188 92 VGGGSAHDCAKAIGILATNG-GEIEDY----EGVDK-SKKPGLPLIAINTTAGTASEVTRFAVITDEERHVKMVIVDWNV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 217 KPTLGLIDPLHTLHMPARVVANSGFDVLCHALESYTTLpyhlrspcpsnpitrpayqGSNPISDIWAIHALRIVAKYLKR 296
Cdd:cd08188 166 TPTIAVNDPELMLGMPPSLTAATGMDALTHAIEAYVST-------------------GATPLTDALALEAIRLIAENLPK 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 297 AVRNPDDLEARSHMHLASAFAGIGFGNAGVHLCHGMSYPISGLvkmykakdYNvdhplVPHGL--SVVLtsPAVFTFTAQ 374
Cdd:cd08188 227 AVANGKDLEARENMAYAQFLAGMAFNNAGLGYVHAMAHQLGGF--------YN-----LPHGVcnAILL--PHVMEFNLP 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 375 MFPERHLEMAEILGADTRTARIQDAGLVLADTLRKFLFDLDVDDGLAAVGYSKADIPALVKGTLpQERVTKLAPCPQSEE 454
Cdd:cd08188 292 ACPERFADIARALGENTEGLSDEEAAEAAIEAIRKLSRRVGIPSGLKELGVKEEDFPLLAENAL-KDACGPTNPRQATKE 370
|
....*..
gi 133922590 455 DLAALFE 461
Cdd:cd08188 371 DVIAIYR 377
|
|
| HVD |
cd08193 |
5-hydroxyvalerate dehydrogenase (HVD) catalyzes the oxidation of 5-hydroxyvalerate to ... |
51-462 |
2.88e-57 |
|
5-hydroxyvalerate dehydrogenase (HVD) catalyzes the oxidation of 5-hydroxyvalerate to 5-oxovalerate with NAD+ as cofactor; 5-hydroxyvalerate dehydrogenase (HVD) is an iron-containing (type III) NAD-dependent alcohol dehydrogenase. It plays a role in the cyclopentanol metabolism biochemical pathway. It catalyzes the oxidation of 5-hydroxyvalerate to 5-oxovalerate with NAD+ as cofactor. This cyclopentanol (cpn) degradation pathway is present in some bacteria which can use cyclopentanol as sole carbon source. In Comamonas sp. strain NCIMB 9872, this enzyme is encoded by the CpnD gene.
Pssm-ID: 341472 [Multi-domain] Cd Length: 379 Bit Score: 193.88 E-value: 2.88e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 51 VSNIRYGAAVTKEVGMDLKNMGAKNVCLMTDKNLSKLPPVQVAMDSLVKNGIPFTVYDNVRVEPTDSSFMEAIEFAQKGA 130
Cdd:cd08193 4 VPRIICGAGAAARLGELLRELGARRVLLVTDPGLVKAGLADPALAALEAAGIAVTVFDDVVADPPEAVVEAAVEQAREAG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 131 FDAYVAVGGGSTMDTCKAANLYASSPHSdfldyVSAPIGKGKpVSVPLKPLIAVPTTSGTGSETTGVAIF-DYEHLKVki 209
Cdd:cd08193 84 ADGVIGFGGGSSMDVAKLVALLAGSDQP-----LDDIYGVGK-ATGPRLPLILVPTTAGTGSEVTPISIVtTGETEKK-- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 210 GITSRAIKPTLGLIDPLHTLHMPARVVANSGFDVLCHALESYTTlpYHLRspcpsnpitrpayqgsNPISDIWAIHALRI 289
Cdd:cd08193 156 GVVSPQLLPDVALLDAELTLGLPPHVTAATGIDAMVHAIEAYTS--RHKK----------------NPISDALAREALRL 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 290 VAKYLKRAVRNPDDLEARSHMHLASAFAGIGFGNAGVHLCHGMSYPISGlvkMYKakdynvdhplVPHGLSVVLTSPAVF 369
Cdd:cd08193 218 LGANLRRAVEDGSDLEAREAMLLGSMLAGQAFANAPVAAVHALAYPLGG---HFH----------VPHGLSNALVLPHVL 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 370 TFTAQMFPERHLEMAEILGADTRTARIQDAGLVLADTLRKFLFDLDVDDGLAAVGYSKADIPALVKGTLPQERVTKLAPC 449
Cdd:cd08193 285 RFNLPAAEALYAELARALLPGLAFGSDAAAAEAFIDALEELVEASGLPTRLRDVGVTEEDLPMLAEDAMKQTRLLVNNPR 364
|
410
....*....|...
gi 133922590 450 PQSEEDLAALFEA 462
Cdd:cd08193 365 EVTEEDALAIYQA 377
|
|
| Fe-ADH-like |
cd14861 |
Iron-containing alcohol dehydrogenases-like; This family contains proteins similar to ... |
54-464 |
1.92e-55 |
|
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: 188.87 E-value: 1.92e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 54 IRYGAAVTKEVGMDLKNMGAKNVCLMTDKNLSKLPPVQVAMDSLVKNGIPFTVYDNVRVEPTDSSFMEAIEFAQKGAFDA 133
Cdd:cd14861 6 IRFGAGAIAELPEELKALGIRRPLLVTDPGLAALGIVDRVLEALGAAGLSPAVFSDVPPNPTEADVEAGVAAYREGGCDG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 134 YVAVGGGSTMDTCKAANLYASSPHsDFLDYVSAPIGkGKPVSVPLKPLIAVPTTSGTGSETTGVAIFDYEHLKVKIGITS 213
Cdd:cd14861 86 IIALGGGSAIDAAKAIALMATHPG-PLWDYEDGEGG-PAAITPAVPPLIAIPTTAGTGSEVGRAAVITDDDTGRKKIIFS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 214 RAIKPTLGLIDPLHTLHMPARVVANSGFDVLCHALESYTTLPYHlrspcpsnpitrpayqgsnPISDIWAIHALRIVAKY 293
Cdd:cd14861 164 PKLLPKVAICDPELTLGLPPRLTAATGMDALTHCIEAYLSPGFH-------------------PMADGIALEGLRLISEW 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 294 LKRAVRNPDDLEARSHMHLASAFAGIGFGNaGVHLCHGMSYPISGLVKMykakdynvdhplvPHGLSVVLTSPAVFTFTA 373
Cdd:cd14861 225 LPRAVADGSDLEARGEMMMAALMGAVAFQK-GLGAVHALAHALGALYGL-------------HHGLLNAILLPYVLRFNR 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 374 QMFPERHLEMAEILGADTRTAriqDAglvLADTLRKFLFDLDVDDGLAAVGYSKADIPALVKGTLpQERVTKLAPCPQSE 453
Cdd:cd14861 291 PAVEDKLARLARALGLGLGGF---DD---FIAWVEDLNERLGLPATLSELGVTEDDLDELAELAL-ADPCHATNPRPVTA 363
|
410
....*....|.
gi 133922590 454 EDLAALFEASM 464
Cdd:cd14861 364 EDYRALLREAL 374
|
|
| Fe-ADH-like |
cd08183 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
54-461 |
7.96e-54 |
|
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: 184.63 E-value: 7.96e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 54 IRYGAAVTKEVGMDLKNMGaKNVCLMTDKNLSKLPPVQVAMDSLVKNGIPFTVYDNVRvEPTDSSFMEAIEFAQKGAFDA 133
Cdd:cd08183 4 IVFGRGSLQELGELAAELG-KRALLVTGRSSLRSGRLARLLEALEAAGIEVALFSVSG-EPTVETVDAAVALAREAGCDV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 134 YVAVGGGSTMDTCKAANLYASSPHS--DFLDYVsapiGKGKPVSVPLKPLIAVPTtsgtgsettgVA-----------IF 200
Cdd:cd08183 82 VIAIGGGSVIDAAKAIAALLTNEGSvlDYLEVV----GKGRPLTEPPLPFIAIPT----------TAgtgsevtknavLS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 201 DYEHlKVKIGITSRAIKPTLGLIDPLHTLHMPARVVANSGFDVLCHALESYTtlpyhlrspcpSNpitrpayqGSNPISD 280
Cdd:cd08183 148 SPEH-GVKVSLRSPSMLPDVALVDPELTLSLPPEVTAASGLDALTQLIEPYV-----------SR--------KANPLTD 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 281 IWAIHALRIVAKYLKRAVRNPDDLEARSHMHLASAFAGIGFGNAGVHLCHGMSYPISGlvkMYKAkdynvdhplvPHGL- 359
Cdd:cd08183 208 ALAREGLRLAARSLRRAYEDGEDLEAREDMALASLLGGLALANAGLGAVHGLAGPLGG---MFGA----------PHGAi 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 360 -SVVLtsPAVFTFTAQ---------MFPERHLEMAEILgADTRTARIQDaglvLADTLRKFLFDLDVdDGLAAVGYSKAD 429
Cdd:cd08183 275 cAALL--PPVLEANLRalrerepdsPALARYRELAGIL-TGDPDAAAED----GVEWLEELCEELGI-PRLSEYGLTEED 346
|
410 420 430
....*....|....*....|....*....|..
gi 133922590 430 IPALVKGTLpQERVTKLAPCPQSEEDLAALFE 461
Cdd:cd08183 347 FPEIVEKAR-GSSSMKGNPIELSDEELLEILE 377
|
|
| HEPD |
cd08182 |
Hydroxyethylphosphoate dehydrogenase (HEPD) catalyzes the reduction of phosphonoacetaldehyde ... |
52-461 |
3.46e-50 |
|
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: 174.72 E-value: 3.46e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 52 SNIRYGAAVTKEVGMDLKNMGAKNVCLMTDKNLSKLPPVQVAMDSLvKNGIPFTVYDNVRVEPTDSSFMEAIEFAQKGAF 131
Cdd:cd08182 2 VKIIFGPGALAELKDLLGGLGARRVLLVTGPSAVRESGAADILDAL-GGRIPVVVFSDFSPNPDLEDLERGIELFRESGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 132 DAYVAVGGGSTMDTCKAANLYASSPHSDFLdyvsAPIGKGKPVSVPLKPLIAVPttsgtgsettGVA-----------IF 200
Cdd:cd08182 81 DVIIAVGGGSVIDTAKAIAALLGSPGENLL----LLRTGEKAPEENALPLIAIP----------TTAgtgsevtpfatIW 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 201 DyEHLKVKIGITSRAIKPTLGLIDPLHTLHMPARVVANSGFDVLCHALESYTTLpyhlrspcpsnpitrpayqGSNPISD 280
Cdd:cd08182 147 D-EAEGKKYSLAHPSLYPDAAILDPELTLSLPLYLTASTGLDALSHAIESIWSV-------------------NANPESR 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 281 IWAIHALRIVAKYLKRAVRNPDDLEARSHMHLASAFAGIGFGNAGVHLCHGMSYPISglvkmykaKDYNvdhplVPHGLS 360
Cdd:cd08182 207 AYALRAIRLILENLPLLLENLPNLEAREAMAEASLLAGLAISITKTTAAHAISYPLT--------SRYG-----VPHGHA 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 361 VVLTSPAVFTFTAQMFPERHlemaeilgADTRTARIQDAGLV-----LADTLRKFLFDLDVDDGLAAVGYSKADIPALVK 435
Cdd:cd08182 274 CALTLPAVLRYNAGADDECD--------DDPRGREILLALGAsdpaeAAERLRALLESLGLPTRLSEYGVTAEDLEALAA 345
|
410 420
....*....|....*....|....*.
gi 133922590 436 GTLPQERVtKLAPCPQSEEDLAALFE 461
Cdd:cd08182 346 SVNTPERL-KNNPVRLSEEDLLRLLE 370
|
|
| NADPH_BDH |
cd08179 |
NADPH-dependent butanol dehydrogenase involved in the butanol and ethanol formation pathway in ... |
68-462 |
1.03e-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: 171.22 E-value: 1.03e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 68 LKNMGAKNVCLMTDKN-LSKLPPVQVAMDSLVKNGIPFTVYDNVRVEPTDSSFMEAIEFAQKGAFDAYVAVGGGSTMDTC 146
Cdd:cd08179 18 LKTLKGKRAFIVTGGGsMKRNGFLDKVEDYLKEAGMEVKVFEGVEPDPSVETVEKGAEAMREFEPDWIIAIGGGSVIDAA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 147 KAANLYASSPHSDFLDYVsapigkgKPVSVPLKP----LIAVPTTSGTGSETTGVAIF-DYEHlKVKIGITSRAIKPTLG 221
Cdd:cd08179 98 KAMWVFYEYPELTFEDAL-------VPFPLPELRkkarFIAIPSTSGTGSEVTRASVItDTEK-GIKYPLASFEITPDVA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 222 LIDPLHTLHMPARVVANSGFDVLCHALESYTtlpyhlrSPCPsnpitrpayqgsNPISDIWAIHALRIVAKYLKRAVRNP 301
Cdd:cd08179 170 ILDPELTMTMPPHVTANTGMDALTHAIEAYV-------STLA------------NDFTDALALGAILDIFENLPKSYNGG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 302 DDLEARSHMHLASAFAGIGFGNAGVHLCHGMSYPISGLVKmykakdynvdhplVPHGL--SVVLtsPAVFTFTAQMFPER 379
Cdd:cd08179 231 KDLEAREKMHNASCLAGMAFSNSGLGIVHSMAHKGGAFFG-------------IPHGLanAILL--PYVIEFNSKDPEAR 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 380 HLEMAEILGADTRTArIQDaglvLADTLRKFLFDLDVDDGLAAVGYS----KADIPALVKGTLpQERVTKLAPCPQSEED 455
Cdd:cd08179 296 ARYAALLIGLTDEEL-VED----LIEAIEELNKKLGIPLSFKEAGIDedefFAKLDEMAENAM-NDACTGTNPRKPTVEE 369
|
....*..
gi 133922590 456 LAALFEA 462
Cdd:cd08179 370 MKELLKA 376
|
|
| Fe-ADH-like |
cd08186 |
Iron-containing alcohol dehydrogenase; This family contains iron-containing alcohol ... |
68-464 |
5.21e-44 |
|
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: 158.58 E-value: 5.21e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 68 LKNMGAKNVCLMTDKNLSKLPPV-QVAMDSLVKNGIPFTVYDNVRVEPTDSSFMEAIEFAQKGAFDAYVAVGGGSTMDTC 146
Cdd:cd08186 18 LKDLGIDKVIIVTGRSSYKKSGAwDDVEKALEENGIEYVVYDKVTPNPTVDQADEAAKLARDFGADAVIAIGGGSPIDTA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 147 KAANLYASSPHS---DFLDYVSAPIGKgkpvsvplKPLIAVPTTSGTGSETTGVAIFDYEHLKVKIGITSRAIKPTLGLI 223
Cdd:cd08186 98 KSVAVLLAYGGKtarDLYGFRFAPERA--------LPLVAINLTHGTGSEVDRFAVATIPEKGYKPGIAYDCIYPLYAID 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 224 DPLHTLHMPARVVANSGFDVLCHALESYTTLpyhlrspcpsnpitrpayqGSNPISDIWAIHALRIVAKYLKRAVRNPDD 303
Cdd:cd08186 170 DPRLTLTLPKEQTLYTSIDAFNHVYEAATTK-------------------VSSPYVITLAKEAIRLIAEYLPRALANPKD 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 304 LEARSHMHLASAFAGIGFGNAGVHLCHGMSYPISGLVkmykakdynvdhPLVPHGLSVVLTSPAVFTFTAQMFPErhlEM 383
Cdd:cd08186 231 LEARYWLLYASMIAGIAIDNGLLHLTHALEHPLSGLK------------PELPHGLGLALLGPAVVKYIYKAVPE---TL 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 384 AEILgadtrtaRIQDAGLV--------LADTLRKFLFDLDVDDGLAAVGYSKADIPALVK---GTLPQERVTKLAPCPQS 452
Cdd:cd08186 296 ADIL-------RPIVPGLKgtpdeaekAARGVEEFLFSVGFTEKLSDYGFTEDDVDRLVElafTTPSLDLLLSLAPVEVT 368
|
410
....*....|..
gi 133922590 453 EEDLAALFEASM 464
Cdd:cd08186 369 EEVVREIYEESL 380
|
|
| PDD |
cd08180 |
1,3-propanediol dehydrogenase (PPD) catalyzes the reduction of 3-hydroxypropionaldehyde (3-HPA) ... |
68-461 |
1.61e-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: 156.11 E-value: 1.61e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 68 LKNMGAKNVCLMTDKNLSKLPPVQVAMDSLvKNGIPFTVYDNVRVEPTDSSFMEAIEFAQKGAFDAYVAVGGGSTMDTCK 147
Cdd:cd08180 17 LKELKGKRVFIVTDPFMVKSGMVDKVTDEL-DKSNEVEIFSDVVPDPSIEVVAKGLAKILEFKPDTIIALGGGSAIDAAK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 148 AANLYassphsdfldYVSAPIGKGKPvsvplkPLIAVPTTSGTGSETTGVA-IFDYEHlKVKIGITSRAIKPTLGLIDPL 226
Cdd:cd08180 96 AIIYF----------ALKQKGNIKKP------LFIAIPTTSGTGSEVTSFAvITDPEK-GIKYPLVDDSMLPDIAILDPE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 227 HTLHMPARVVANSGFDVLCHALESYTTLpyhlrspcpsnpitrpayqGSNPISDIWAIHALRIVAKYLKRAVRNPDDLEA 306
Cdd:cd08180 159 LVKSVPPKVTADTGMDVLTHALEAYVST-------------------NANDFTDALAEKAIKLVFENLPRAYRDGDDLEA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 307 RSHMHLASAFAGIGFGNAGVHLCHGMSYPISGLVKmykakdynvdhplVPHGLSVVLTSPAVFTFtaqmfperhlemaei 386
Cdd:cd08180 220 REKMHNASCMAGIAFNNAGLGINHSLAHALGGRFH-------------IPHGRANAILLPYVIEF--------------- 271
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 133922590 387 lgadtrtariqdaglvLADTLRKFLFDLDVDDGLAAVGYSKAD----IPALVKGTLpQERVTKLAPCPQSEEDLAALFE 461
Cdd:cd08180 272 ----------------LIAAIRRLNKKLGIPSTLKELGIDEEEfekaIDEMAEAAL-ADRCTATNPRKPTAEDLIELLR 333
|
|
| Fe-ADH-like |
cd08189 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
68-462 |
2.34e-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: 156.86 E-value: 2.34e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 68 LKNMGAKNVCLMTDKNLSKLPPVQVAMDSLVKNGIPFTVYDNVRVEPTDSSFMEAIEFAQKGAFDAYVAVGGGSTMDTCK 147
Cdd:cd08189 22 LKKLGIKRVLIVTDKGLVKLGLLDPLLDALKKAGIEYVVFDGVVPDPTIDNVEEGLALYKENGCDAIIAIGGGSVIDCAK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 148 AANLYASSPHSDFLDYVsapiGKGKpVSVPLKPLIAVPTTSGTGSETTGVA-IFDYEHlKVKIGITSRAIKPTLGLIDPL 226
Cdd:cd08189 102 VIAARAANPKKSVRKLK----GLLK-VRKKLPPLIAVPTTAGTGSEATIAAvITDPET-HEKYAINDPKLIPDAAVLDPE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 227 HTLHMPARVVANSGFDVLCHALESYttlpyhlrspcpsnpITRPAyqgsNPISDIWAIHALRIVAKYLKRAVRNPDDLEA 306
Cdd:cd08189 176 LTLGLPPAITAATGMDALTHAVEAY---------------ISRSA----TKETDEYALEAVKLIFENLPKAYEDGSDLEA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 307 RSHMHLASAFAGIGFGNAGVHLCHGMSYPISGLvkmykakdYNvdhplVPHGL--SVVLtsPAVFTFTAQMFPERHLEMA 384
Cdd:cd08189 237 RENMLLASYYAGLAFTRAYVGYVHAIAHQLGGL--------YG-----VPHGLanAVVL--PHVLEFYGPAAEKRLAELA 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 385 EILGADTRTARIQDAGLVLADTLRKFLFDLDVDDGLAAVgySKADIPALVKGTLpQErVTKLAPCPQ--SEEDLAALFEA 462
Cdd:cd08189 302 DAAGLGDSGESDSEKAEAFIAAIRELNRRMGIPTTLEEL--KEEDIPEIAKRAL-KE-ANPLYPVPRimDRKDCEELLRK 377
|
|
| PPD-like |
cd08181 |
1,3-propanediol dehydrogenase-like (PPD); This family contains proteins similar to 1, ... |
47-391 |
1.48e-42 |
|
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: 154.28 E-value: 1.48e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 47 FEMAVsNIRYGAAVTKEVGMDLKNMGaKNVCLMTDKNLSK-LPPVQVAMDSLVKNGIPFTVYDNVRVEPTDSSFMEAIEF 125
Cdd:cd08181 1 FYMPT-KVYFGKNCVEKHADELAALG-KKALIVTGKHSAKkNGSLDDVTEALEENGIEYFIFDEVEENPSIETVEKGAEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 126 AQKGAFDAYVAVGGGSTMDTCKAANLYASSPHSDFLDYvsapigKGKPVSVPLkPLIAVPTTSGTGSETTGVAIFDYEHL 205
Cdd:cd08181 79 ARKEGADFVIGIGGGSPLDAAKAIALLAANKDGDEDLF------QNGKYNPPL-PIVAIPTTAGTGSEVTPYSILTDHEK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 206 KVKIGITSRAIKPTLGLIDPLHTLHMPARVVANSGFDVLCHALESYTTlpyhlrspcpsnpiTRpayqgSNPISDIWAIH 285
Cdd:cd08181 152 GTKKSFGNPLIFPKLALLDPKYTLSLPEELTIDTAVDALSHAIEGYLS--------------VK-----ATPLSDALALE 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 286 ALRIVAKYLKRAVRNPDDLEARSHMHLASAFAGIGFGNAGVHLCHGMSYPISglvkmykakdYNVDhplVPHGLSVVLTS 365
Cdd:cd08181 213 ALRLIGECLPNLLGDELDEEDREKLMYASTLAGMVIAQTGTTLPHGLGYPLT----------YFKG---IPHGRANGILL 279
|
330 340
....*....|....*....|....*.
gi 133922590 366 PAVFTFTAQMFPERHLEMAEILGADT 391
Cdd:cd08181 280 PAYLKLCEKQEPEKVDKILKLLGFGS 305
|
|
| PRK10624 |
PRK10624 |
L-1,2-propanediol oxidoreductase; Provisional |
56-464 |
1.54e-41 |
|
L-1,2-propanediol oxidoreductase; Provisional
Pssm-ID: 182595 [Multi-domain] Cd Length: 382 Bit Score: 152.07 E-value: 1.54e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 56 YGAAVTKEVGMDLKNMGAKNVCLMTDKNLSKLPPVQVAMDSLVKNGIPFTVYDNVRVEPTDSSFMEAIE-FAQKGAfDAY 134
Cdd:PRK10624 13 FGRGAIGALTDEVKRRGFKKALIVTDKTLVKCGVVAKVTDVLDAAGLAYEIYDGVKPNPTIEVVKEGVEvFKASGA-DYL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 135 VAVGGGSTMDTCKAANLYASSPhsDFLDYVS----APIGKgkpvsvPLKPLIAVPTTS-GTGSETTGVAIFDYEHLKVKI 209
Cdd:PRK10624 92 IAIGGGSPQDTCKAIGIISNNP--EFADVRSlegvAPTKK------PSVPIIAIPTTAgTAAEVTINYVITDEEKRRKFV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 210 GITSRAIkPTLGLIDPLHTLHMPARVVANSGFDVLCHALESYTTlpyhlrspcpsnpitrpayQGSNPISDIWAIHALRI 289
Cdd:PRK10624 164 CVDPHDI-PQVAFVDADMMDSMPPGLKAATGVDALTHAIEGYIT-------------------RGAWALTDMLHLKAIEI 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 290 VAKYLKRAVRNpdDLEARSHMHLASAFAGIGFGNAGVHLCHGMSYPISGLvkmykakdYNvdhplVPHGLSVVLTSPAVF 369
Cdd:PRK10624 224 IAGALRGAVAG--DKEAGEGMALGQYIAGMGFSNVGLGLVHGMAHPLGAF--------YN-----TPHGVANAILLPHVM 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 370 TFTAQMFPERHLEMAEILGADTRTARIQDAGLVLADTLRKFLFDLDVDDGLAAVGYSKADIPALVKGTLpQERVTKLAPC 449
Cdd:PRK10624 289 EYNADFTGEKYRDIARAMGVKVEGMSLEEARNAAVEAVKALNRDVGIPPHLRDVGVKEEDIPALAQAAF-DDVCTGGNPR 367
|
410
....*....|....*
gi 133922590 450 PQSEEDLAALFEASM 464
Cdd:PRK10624 368 EATLEDIVELYKKAW 382
|
|
| AAD_C |
cd08178 |
C-terminal alcohol dehydrogenase domain of the acetaldehyde dehydrogenase-alcohol ... |
68-429 |
3.13e-40 |
|
C-terminal alcohol dehydrogenase domain of the acetaldehyde dehydrogenase-alcohol dehydrogenase bifunctional two-domain protein (AAD); This alcohol dehydrogenase domain is located on the C-terminal of a bifunctional two-domain protein. The N-terminal of the protein contains an acetaldehyde-CoA dehydrogenase domain. This protein is involved in pyruvate metabolism whereby pyruvate is converted to acetyl-CoA and formate by pyruvate formate-lysase (PFL). Under anaerobic condition, acetyl-CoA is reduced to acetaldehyde and ethanol by this two-domain protein. Acetyl-CoA is first converted into an enzyme-bound thiohemiacetal by the N-terminal acetaldehyde dehydrogenase domain. The enzyme-bound thiohemiacetal is subsequently reduced by the C-terminal NAD+-dependent alcohol dehydrogenase domain. In E. coli, this protein is called AdhE and has been shown to have pyruvate formate-lyase (PFL) deactivase activity, which leads to the inactivation of PFL, a key enzyme in anaerobic metabolism. In Escherichia coli and Entamoeba histolytica, this enzyme forms homopolymeric peptides composed of more than 20 protomers associated in a helical rod-like structure.
Pssm-ID: 341457 [Multi-domain] Cd Length: 400 Bit Score: 148.87 E-value: 3.13e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 68 LKNMGAKNVCLMTDKNLSKLPPVQVAMDSLVKNGIPFTVYDNVRVEPTDSSFMEAIEfaQKGAF--DAYVAVGGGSTMDT 145
Cdd:cd08178 18 LELPGVKRAFIVTDRVLYKLGYVDKVLDVLEARGVETEVFSDVEPDPTLSTVRKGLE--AMNAFkpDVIIALGGGSAMDA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 146 CKAANLYASSPHSDFLDYVSAPIGKGKPVSVPLKP-----LIAVPTTSGTGSETTGVA-IFDyEHLKVKIGITSRAIKPT 219
Cdd:cd08178 96 AKIMWLFYEHPETKFEDLAQRFMDIRKRVYKFPKLgkkakLVAIPTTSGTGSEVTPFAvITD-DKTGKKYPLADYALTPD 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 220 LGLIDPLHTLHMPARVVANSGFDVLCHALESYTtlpyhlrSPCpsnpitrpayqgSNPISDIWAIHALRIVAKYLKRAVR 299
Cdd:cd08178 175 MAIVDPELVMTMPKRLTADTGIDALTHAIEAYV-------SVM------------ASDYTDGLALQAIKLIFEYLPRSYN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 300 NPDDLEARSHMHLASAFAGIGFGNAGVHLCHGMSYPISGLVKmykakdynvdhplVPHGLSVVLTSPAVFTFTAQ----- 374
Cdd:cd08178 236 NGNDIEAREKMHNAATIAGMAFANAFLGICHSLAHKLGAAFH-------------IPHGRANAILLPHVIRYNATdpptk 302
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 133922590 375 --MFP--------ERHLEMAEILGADTRTariqDAGLV--LADTLRKFLFDLDVDDGLAAVGYSKAD 429
Cdd:cd08178 303 qaAFPqykyyvakERYAEIADLLGLGGKT----PEEKVesLIKAIEDLKKDLGIPTSIREAGIDEAD 365
|
|
| BDH |
cd08187 |
Butanol dehydrogenase catalyzes the conversion of butyraldehyde to butanol with the cofactor ... |
94-461 |
1.38e-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: 144.11 E-value: 1.38e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 94 MDSLVKNGIPFTVYDNVRVEPTDSSFMEAIEFAQKGAFDAYVAVGGGSTMDTCKAANLYASSPHsDFLDYVSapigKGKP 173
Cdd:cd08187 50 VASLKEAGIEVVEFGGVEPNPRLETVREGIELAREENVDFILAVGGGSVIDAAKAIAAGAKYDG-DVWDFFT----GKAP 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 174 VSVPLkPLIAVPTTSGTGSETTGVAIFDYEHLKVKIGITSRAIKPTLGLIDPLHTLHMPARVVANSGFDVLCHALESYTT 253
Cdd:cd08187 125 PEKAL-PVGTVLTLAATGSEMNGGAVITNEETKEKLGFGSPLLRPKFSILDPELTYTLPKYQTAAGIVDIFSHVLEQYFT 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 254 LPYHlrspcpsnpitrpayqgsNPISDIWAIHALRIVAKYLKRAVRNPDDLEARSHMHLASAFA--GI-GFGNAGVHLCH 330
Cdd:cd08187 204 GTED------------------APLQDRLAEGLLRTVIENGPKALKDPDDYEARANLMWAATLAlnGLlGAGRGGDWATH 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 331 GMSYPISGLvkmykakdYNVDHplvPHGLSVVLtsPAVFTFTAQMFPERHLEMAE------ILGADTRTAriqDAGLvla 404
Cdd:cd08187 266 AIEHELSAL--------YDITH---GAGLAIVF--PAWMRYVLKKKPERFAQFARrvfgidPGGDDEETA---LEGI--- 326
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 133922590 405 DTLRKFLFDLDVDDGLAAVGYSKADIPALVKGTLPQERVTKLAPcPQSEEDLAALFE 461
Cdd:cd08187 327 EALEEFFKSIGLPTTLSELGIDEEDIEEMAEKAVRGGGLGGGFK-PLTREDIEEILK 382
|
|
| Fe-ADH-like |
cd14864 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
52-462 |
5.02e-37 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341486 [Multi-domain] Cd Length: 376 Bit Score: 139.74 E-value: 5.02e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 52 SNIRYGAAVTKEVGMDLKNMGAKNVcLMTDKNLSKLPPVQVAMDSLVKNGIPFTVYDNVRVEPTDSSFMEAIEFAQKGAF 131
Cdd:cd14864 5 PNIVFGADSLERIGEEVKEYGSRFL-LITDPVLKESGLADKIVSSLEKAGISVIVFDEIPASATSDTIDEAAELARKAGA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 132 DAYVAVGGGSTMDTCKAANLYASSPHsDFLDYVSAPIGKGKPVsvplkPLIAVPTTSGTGSETTGVAIF-DYEHLKVKIg 210
Cdd:cd14864 84 DGIIAVGGGKVLDTAKAVAILANNDG-GAYDFLEGAKPKKKPL-----PLIAVPTTPRSGFEFSDRFPVvDSRSREVKL- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 211 ITSRAIKPTLGLIDPLHTLHMPARVVANSGFDVLCHALESYTTlpyhlrspcpsnpitrpayQGSNPISDIWAIHALRIV 290
Cdd:cd14864 157 LKAQPGLPKAVIVDPNLMASLTGNQTAAMALAALALAVEAYLS-------------------KKSNFFSDALALKAIELV 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 291 AKYLKRAVRNPDDLEARSHMHLASAFAGIGFGNAGVHLCHGMSYPISGLvkmykakdYNVDHPLVphgLSVVLtsPAVFT 370
Cdd:cd14864 218 SENLDGALADPKNTPAEELLAQAGCLAGLAASSSSPGLATALALAVNSR--------YKVSKSLV---ASILL--PHVIE 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 371 FTAQMFPERHLEMAEILGADTRTARIQDAGLVLADTLRKFLFDLDVDDGLAAVGyskadipalVKGTLPQ-------ERV 443
Cdd:cd14864 285 YAATSAPDKYAKIARALGEDVEGASPEEAAIAAVEGVRRLIAQLNLPTRLKDLD---------LASSLEQlaaiaedAPK 355
|
410
....*....|....*....
gi 133922590 444 TKLAPCPQSEEDLAALFEA 462
Cdd:cd14864 356 LNGLPRSMSSDDIFDILKA 374
|
|
| PRK13805 |
PRK13805 |
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional |
71-429 |
1.79e-33 |
|
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional
Pssm-ID: 237515 [Multi-domain] Cd Length: 862 Bit Score: 134.16 E-value: 1.79e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 71 MGAKNVCLMTDKNLSKLPPVQVAMDSL--VKNGIPFTVYDNVRVEPTDSSFMEAIEFAQkgAF--DAYVAVGGGSTMDTC 146
Cdd:PRK13805 478 DGKKRAFIVTDRFMVELGYVDKVTDVLkkRENGVEYEVFSEVEPDPTLSTVRKGAELMR--SFkpDTIIALGGGSPMDAA 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 147 KAANLYASSPHSDFLD------------YVSAPIG-KGKPVSVP--------LKPlIAVpttsgtgsettgvaIFDyEHL 205
Cdd:PRK13805 556 KIMWLFYEHPETDFEDlaqkfmdirkriYKFPKLGkKAKLVAIPttsgtgseVTP-FAV--------------ITD-DKT 619
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 206 KVKIGITSRAIKPTLGLIDPLHTLHMPARVVANSGFDVLCHALESYTTLPyhlrspcpsnpitrpayqgSNPISDIWAIH 285
Cdd:PRK13805 620 GVKYPLADYELTPDVAIVDPNLVMTMPKSLTADTGIDALTHALEAYVSVM-------------------ASDYTDGLALQ 680
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 286 ALRIVAKYLKRAVRN-PDDLEARSHMHLASAFAGIGFGNAGVHLCHGMSYPISGLVKmykakdynvdhplVPHGLSVVLT 364
Cdd:PRK13805 681 AIKLVFEYLPRSYKNgAKDPEAREKMHNASTIAGMAFANAFLGICHSMAHKLGAEFH-------------IPHGRANAIL 747
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 365 SPAVFTFTAQ------MFP--------ERHLEMAEILG--ADTRTARIQdaglVLADTLRKFLFDLDVDDGLAAVGYSKA 428
Cdd:PRK13805 748 LPHVIRYNATdppkqaAFPqyeypradERYAEIARHLGlpGSTTEEKVE----SLIKAIEELKAELGIPMSIKEAGVDEA 823
|
.
gi 133922590 429 D 429
Cdd:PRK13805 824 D 824
|
|
| PRK09860 |
PRK09860 |
putative alcohol dehydrogenase; Provisional |
57-464 |
2.11e-29 |
|
putative alcohol dehydrogenase; Provisional
Pssm-ID: 182118 [Multi-domain] Cd Length: 383 Bit Score: 118.52 E-value: 2.11e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 57 GAAVTKEVGMDLKNMGAKNVCLMTDKNLSKLPPVQVAMDSLVKNGIPFTVYDNVRVEPTDSSFMEAIEFAQKGAFDAYVA 136
Cdd:PRK09860 15 GADSLTDAMNMMADYGFTRTLIVTDNMLTKLGMAGDVQKALEERNIFSVIYDGTQPNPTTENVAAGLKLLKENNCDSVIS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 137 VGGGSTMDTCKAANLYASSpHSDFLDYvsapigKGKPVSV-PLKPLIAVPTTSGTGSETTGVAIFDYEHLKVKIGITSRA 215
Cdd:PRK09860 95 LGGGSPHDCAKGIALVAAN-GGDIRDY------EGVDRSAkPQLPMIAINTTAGTASEMTRFCIITDEARHIKMAIVDKH 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 216 IKPTLGLIDPLHTLHMPARVVANSGFDVLCHALESYTTLpyhlrspcpsnpitrpayqGSNPISDIWAIHALRIVAKYLK 295
Cdd:PRK09860 168 VTPLLSVNDSSLMIGMPKSLTAATGMDALTHAIEAYVSI-------------------AATPITDACALKAVTMIAENLP 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 296 RAVRNPDDLEARSHMHLASAFAGIGFGNAGVHLCHGMSYPISGLvkmykakdYNvdhplVPHGLSVVLTSPAVFTFTAQM 375
Cdd:PRK09860 229 LAVEDGSNAKAREAMAYAQFLAGMAFNNASLGYVHAMAHQLGGF--------YN-----LPHGVCNAVLLPHVQVFNSKV 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 376 FPERHLEMAEILGADTRTARIQDAGLVLADTLRKFLFDLDVDDGLAAVGYSKADIPALVKGTLpQERVTKLAPCPQSEED 455
Cdd:PRK09860 296 AAARLRDCAAAMGVNVTGKNDAEGAEACINAIRELAKKVDIPAGLRDLNVKEEDFAVLATNAL-KDACGFTNPIQATHEE 374
|
....*....
gi 133922590 456 LAALFEASM 464
Cdd:PRK09860 375 IVAIYRAAM 383
|
|
| Fe-ADH-like |
cd14866 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
47-462 |
1.23e-27 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341488 [Multi-domain] Cd Length: 384 Bit Score: 113.48 E-value: 1.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 47 FEMAVSNIRYGAAVTKEVGMDLKNMGAKNVCLMTDKNLSKLPPVqvaMDsLVKNGI---PFTVYDNVRVEPTDSSFMEAI 123
Cdd:cd14866 1 HDYPPLRLFSGRGALARLGRELDRLGARRALVVCGSSVGANPDL---MD-PVRAALgdrLAGVFDGVRPHSPLETVEAAA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 124 EFAQKGAFDAYVAVGGGSTMDTCKAANLYASSPhSDFLDYVSAPIGKGKPVS----VPLKPLIAVPTTSGTGSETTGVAI 199
Cdd:cd14866 77 EALREADADAVVAVGGGSAIVTARAASILLAED-RDVRELCTRRAEDGLMVSprldAPKLPIFVVPTTPTTADVKAGSAV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 200 FDYEHLKvKIGITSRAIKPTLGLIDPLHTLHMPARVVANSGFDVLCHALESyttlpyhLRSPcpsnpitrpayqGSNPIS 279
Cdd:cd14866 156 TDPPAGQ-RLALFDPKTRPAAVFYDPELLATAPASLVAGAAMNGFDMAVEG-------LYSR------------HADPLA 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 280 DIWAIHALRIVAKYLKRAVrNPDDLEARSHMHLASAFAGIGFGNAGVHLCHGMSYPISGlvkmykakDYNVDHPLVpHgl 359
Cdd:cd14866 216 DATLMHALRLLADGLPRLA-DDDDPAARADLVLAAVLAGYGTDHTGGGVIHALGHAIGA--------RYGVQNGVV-H-- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 360 SVVLtsPAVFTFTAQMFPERHLEMAEILGADTRTAriQDAGLVLADTLRKFLFDLDVDDGLAAVGYSKADIPALVKGTLP 439
Cdd:cd14866 284 AILL--PHVLRFNAPATDGRLDRLAEALGVADAGD--EASAAAVVDAVEALLDALGVPTRLRDLGVSREDLPAIAEAAMD 359
|
410 420
....*....|....*....|...
gi 133922590 440 QERVTKLAPCPQSEEDLAALFEA 462
Cdd:cd14866 360 DWFMDNNPRPVPTAEELEALLEA 382
|
|
| PRK15454 |
PRK15454 |
ethanolamine utilization ethanol dehydrogenase EutG; |
57-463 |
1.18e-26 |
|
ethanolamine utilization ethanol dehydrogenase EutG;
Pssm-ID: 185351 [Multi-domain] Cd Length: 395 Bit Score: 110.89 E-value: 1.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 57 GAAVTKEVGMDLKNMGAKNVCLMTDKNLSKLPPVQVAMDSLVKNGIPFTVYDNVRVEPTDSSFMEAIEFAQKGAFDAYVA 136
Cdd:PRK15454 33 GPGAVSSCGQQAQTRGLKHLFVMADSFLHQAGMTAGLTRSLAVKGIAMTLWPCPVGEPCITDVCAAVAQLRESGCDGVIA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 137 VGGGSTMDTCKAANLYASSPHSDFLDYVSapigkgKPVSVPLKPLIAVPTTSGTGSETTGVAIFDYEHLKVKIGITSRAI 216
Cdd:PRK15454 113 FGGGSVLDAAKAVALLVTNPDSTLAEMSE------TSVLQPRLPLIAIPTTAGTGSETTNVTVIIDAVSGRKQVLAHASL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 217 KPTLGLIDPLHTLHMPARVVANSGFDVLCHALESYTTLpyhlrspcpsnpitrpayqGSNPISDIWAIHALRIVAKYLKR 296
Cdd:PRK15454 187 MPDVAILDAALTEGVPSHVTAMTGIDALTHAIEAYSAL-------------------NATPFTDSLAIGAIAMIGKSLPK 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 297 AVRNPDDLEARSHMHLASAFAGIGFGNAGVHLCHGMSY-PISGLvkmykakdynvdHplVPHGLSVVLTSPAVFTFTAQM 375
Cdd:PRK15454 248 AVGYGHDLAARESMLLASCMAGMAFSSAGLGLCHAMAHqPGAAL------------H--IPHGLANAMLLPTVMEFNRMV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 376 FPERHLEMAEILgaDTRTARIQDAglvlADTLRKFLFDLDVDDGLAAVGYSKADIPALVKGTLpQERVTKLAPCPQSEED 455
Cdd:PRK15454 314 CRERFSQIGRAL--RTKKSDDRDA----INAVSELIAEVGIGKRLGDVGATSAHYGAWAQAAL-EDICLRSNPRTASLEQ 386
|
....*...
gi 133922590 456 LAALFEAS 463
Cdd:PRK15454 387 IVGLYAAA 394
|
|
| MAR-like |
cd08192 |
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic ... |
54-462 |
1.19e-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: 110.80 E-value: 1.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 54 IRYGAAVTKEVGMDLKNMGAKNVCLMTDKNLSKLPPV--QVAM---DSLVkngipfTVYDNVRVEPTDSSFMEAIEFAQK 128
Cdd:cd08192 4 VSYGPGAVEALLHELATLGASRVFIVTSKSLATKTDVikRLEEalgDRHV------GVFSGVRQHTPREDVLEAARAVRE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 129 GAFDAYVAVGGGSTMDTCKAANLYASSPHSDFLDYVSAPIGKGKPVSV--PLKPLIAVPTTSGTGSETTGVAIFDyEHLK 206
Cdd:cd08192 78 AGADLLVSLGGGSPIDAAKAVALALAEDVTDVDQLDALEDGKRIDPNVtgPTLPHIAIPTTLSGAEFTAGAGATD-DDTG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 207 VKIGITSRAIKPTLGLIDPLHTLHMPARVVANSGFDVLCHALESYttlpYHLRSpcpsnpitrpayqgsNPISDIWAIHA 286
Cdd:cd08192 157 HKQGFAHPELGPDAVILDPELTLHTPERLWLSTGIRAVDHAVETL----CSPQA---------------TPFVDALALKA 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 287 LRIVAKYLKRAVRNPDDLEARSHMHLASAFAGIGFGN-AGVHLCHGMSYPISGLvkmykakdYNvdhplVPHGLSVVLTS 365
Cdd:cd08192 218 LRLLFEGLPRSKADPEDLEARLKCQLAAWLSLFGLGSgVPMGASHAIGHQLGPL--------YG-----VPHGITSCIML 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 366 PAVFTFTAQMFPERHLEMAEILGADTRTARIQDAGlvLADTLRKFLFDLDVDDGLAAVGYSKADIPALVKGTLPQERVTK 445
Cdd:cd08192 285 PAVLRFNAPVNAERQRLIARALGLVTGGLGREAAD--AADAIDALIRELGLPRTLRDVGVGRDQLEKIAENALTDVWCRT 362
|
410
....*....|....*..
gi 133922590 446 LAPCPQSEEDLAALFEA 462
Cdd:cd08192 363 NPRPITDKDDVLEILES 379
|
|
| 4HBD_NAD |
cd14860 |
4-hydroxybutyrate dehydrogenase, also called gamma-hydroxybutyrate dehydrogenase, catalyzes ... |
113-467 |
1.45e-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: 107.30 E-value: 1.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 113 EPTDSSFMEAIEFAQKGAFDAYVAVGGGSTMDTCKaanLYASSPHSDFLDYVS--APIGKGKPvsvplkpLIAVPTTSGT 190
Cdd:cd14860 61 EPSDEMVEAIYKDIKKYGYKRVIAIGGGTVIDIAK---LLALKGISPVLDLFDgkIPLIKEKE-------LIIVPTTCGT 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 191 GSETTGVAIFDYEHLKVKIGITSRAIKPTLGLIDP--LHTLhmPARVVANSGFDVLCHALESYTtlpyhlrSPcpsnpit 268
Cdd:cd14860 131 GSEVTNISIVELTSLGTKKGLAVDELYADKAVLIPelLKGL--PYKVFATSSIDALIHAIESYL-------SP------- 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 269 rpayqGSNPISDIWAIHALR-IVAKYLKRAVRNPDDL-EARSHMHLASAFAGIGFGNAGVHLCHGMSYPISGlvkMYKak 346
Cdd:cd14860 195 -----KATPYTEMFSYKAIEmILEGYQEIAEKGEEARfPLLGDFLIASNYAGIAFGNAGCAAVHALSYPLGG---KYH-- 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 347 dynvdhplVPHGLS--VVLTspAVFTFTAQMFPERHLE-----MAEILGADTRTAriqdaglvlADTLRKFLFDLDVDDG 419
Cdd:cd14860 265 --------VPHGEAnyAVFT--GVLKNYQEKNPDGEIKklnefLAKILGCDEEDV---------YDELEELLNKILPKKP 325
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 133922590 420 LAAVGYSKADIPALVKGTLP-QERVTKLAPCPQSEEDLAALFeasMKLY 467
Cdd:cd14860 326 LHEYGMKEEEIDEFADSVMEnQQRLLANNYVPLDREDVAEIY---KELY 371
|
|
| YqdH |
COG1979 |
Alcohol dehydrogenase YqhD, Fe-dependent ADH family [Energy production and conversion]; |
91-435 |
1.27e-23 |
|
Alcohol dehydrogenase YqhD, Fe-dependent ADH family [Energy production and conversion];
Pssm-ID: 441582 [Multi-domain] Cd Length: 387 Bit Score: 102.07 E-value: 1.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 91 QVaMDSLVKNGIPFTVYDNVRVEPTDSSFMEAIEFAQKGAFDAYVAVGGGSTMDTCK---AANLYAssphSDFLDYVSap 167
Cdd:COG1979 50 QV-KAALKEAGIEVVEFGGVEPNPRLETVRKGVELCKEEGIDFILAVGGGSVIDGAKaiaAGAKYD----GDPWDILT-- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 168 igKGKPVSVPLkPLIAVPTTSGTGSETTGVAIFDYEHLKVKIGITSRAIKPTLGLIDPLHTLHMPARVVANSGFDVLCHA 247
Cdd:COG1979 123 --GKAPVEKAL-PLGTVLTLPATGSEMNSGSVITNEETKEKLGFGSPLVFPKFSILDPELTYTLPKRQTANGIVDIFSHV 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 248 LESYTTLPyhlrspcpsnpitrpayqGSNPISDIWAIHALRIVAKYLKRAVRNPDDLEARSHMHLASAFAGIGFGNAGVH 327
Cdd:COG1979 200 MEQYFTYP------------------VDAPLQDRFAEGLLRTLIEEGPKALKDPEDYDARANLMWAATLALNGLIGAGVP 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 328 ---LCHGMSYPISGLvkmykakdYNVDHplvPHGLSVVLtsPAVFTFTAQMFPERHLEMAE-ILGADTRT--ARIQDAgl 401
Cdd:COG1979 262 qdwATHMIEHELSAL--------YDIDH---GAGLAIVL--PAWMRYVLEEKPEKFAQYAErVWGITEGDdeERALEG-- 326
|
330 340 350
....*....|....*....|....*....|....
gi 133922590 402 vlADTLRKFLFDLDVDDGLAAVGYSKADIPALVK 435
Cdd:COG1979 327 --IEATEEFFESLGLPTRLSEYGIDEEDIEEMAE 358
|
|
| MAR |
cd08177 |
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic ... |
121-462 |
6.20e-17 |
|
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: 81.78 E-value: 6.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 121 EAIEFAQKGAFDAYVAVGGGSTmdtckaanlyassphsdfldyvsapIGKGKPVSVPLK-PLIAVPTTSgtgsettgvA- 198
Cdd:cd08177 67 RALAAAREAGADGLVAIGGGSA-------------------------IGLAKAIALRTGlPIVAVPTTY---------Ag 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 199 -----IFDYEHLKVKIGITSRAIKPTLGLIDPLHTLHMPARVVANSGFDVLCHALESyttlpyhLRSPcpsnpitrpayq 273
Cdd:cd08177 113 semtpIWGETEDGVKTTGRDPRVLPRTVIYDPDLTLGLPAALSVASGLNALAHAVEA-------LYAP------------ 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 274 GSNPISDIWAIHALRIVAKYLKRAVRNPDDLEARSHMHLASAFAGIGFGNAG--VH--LCH--GMSYpisGLvkmykakd 347
Cdd:cd08177 174 DANPITSLLAEEGIRALARALPRLVADPSDLEARSDALYGAWLAGVVLGSVGmgLHhkLCHvlGGTF---DL-------- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 348 ynvdhplvPHGL--SVVLtsPAVFTFTAQMFPERHLEMAEILGADtrtariqDAGLVLADTLRkflfDLDVDDGLAAVGY 425
Cdd:cd08177 243 --------PHAEthAVVL--PHVLAYNAPAAPDAMARLARALGGG-------DAAGGLYDLAR----RLGAPTSLRDLGM 301
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 133922590 426 SKADIPALVkgtlpqERVTKLA---PCPQSEEDLAALFEA 462
Cdd:cd08177 302 PEDDIDRAA------DLALANPypnPRPVERDALRALLER 335
|
|
| DHQ_Fe-ADH |
cd07766 |
Dehydroquinate synthase-like (DHQ-like) and iron-containing alcohol dehydrogenases (Fe-ADH); ... |
53-435 |
2.59e-10 |
|
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: 60.84 E-value: 2.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 53 NIRYGAAVTKEVGMDLKNMGAKnVCLMTDKNLSKLppVQVAMDSLVKNGIPFTVYDNVRVEPTDSSFMEAIEFAQKGAFD 132
Cdd:cd07766 3 RIVFGEGAIAKLGEIKRRGFDR-ALVVSDEGVVKG--VGEKVADSLKKGLAVAIFDFVGENPTFEEVKNAVERARAAEAD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 133 AYVAVGGGSTMDTCKAANLyassphsdfldyvsapigkgkpVSVPLKPLIAVPTTSGTGSETTGVAIFDYEHLKVKIGIT 212
Cdd:cd07766 80 AVIAVGGGSTLDTAKAVAA----------------------LLNRGIPFIIVPTTASTDSEVSPKSVITDKGGKNKQVGP 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 213 srAIKPTLGLIDPLHTLHMPARVVANSGFDVLCHALEsyttlpyhlrspcpsnpitrpayqgsnpisdiwaihalrivak 292
Cdd:cd07766 138 --HYNPDVVFVDTDITKGLPPRQVASGGVDALAHAVE------------------------------------------- 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 293 yLKRAVrnpddlearshmhLASAFAGIGFGNA-GVHLCHGMSYPISGLvkmykakdynvdHPLvPHGLSVVLTSPAVFTF 371
Cdd:cd07766 173 -LEKVV-------------EAATLAGMGLFESpGLGLAHAIGHALTAF------------EGI-PHGEAVAVGLPYVLKV 225
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 133922590 372 TAQMFPERHLEMAEilgadtrtariqdaglvladtLRKFLFDLDVDDGLAAVGYSKADIPALVK 435
Cdd:cd07766 226 ANDMNPEPEAAIEA---------------------VFKFLEDLGLPTHLADLGVSKEDIPKLAE 268
|
|
| PRK15138 |
PRK15138 |
alcohol dehydrogenase; |
96-446 |
2.25e-09 |
|
alcohol dehydrogenase;
Pssm-ID: 185092 [Multi-domain] Cd Length: 387 Bit Score: 59.04 E-value: 2.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 96 SLVKNGIPFTVYD-----NVR----VEPTDS--SFMEAIEFAQKGAFDAYVAVGGGSTMDTCK----AANLYASSPHSDF 160
Cdd:PRK15138 40 SVKKTGVLDQVLDalkgmDVLefggIEPNPTyeTLMKAVKLVREEKITFLLAVGGGSVLDGTKfiaaAANYPENIDPWHI 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 161 LDYVSAPIGKGkpvsVPLKPLIAVPTTSGTGSETtgvAIFDYEHLKVKIGITSRAIKPTLGLIDPLHTLHMPARVVANSG 240
Cdd:PRK15138 120 LETGGKEIKSA----IPMGSVLTLPATGSESNAG---AVISRKTTGDKQAFHSPHVQPVFAVLDPVYTYTLPPRQVANGV 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 241 FDVLCHALESYTTLPYHLRspcpsnpitrpayqgsnpISDIWAIHALRIVAKYLKRAVRNPDDLEARSHMHLASAFAGIG 320
Cdd:PRK15138 193 VDAFVHTVEQYVTYPVDAK------------------IQDRFAEGILLTLIEEGPKALKEPENYDVRANVMWAATQALNG 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 321 FGNAGVH---LCHGMSYPISGLvkmykakdYNVDHplvPHGLSVVLtsPAVFTFTAQMFPERHLEMAEI---LGADTRTA 394
Cdd:PRK15138 255 LIGAGVPqdwATHMLGHELTAM--------HGLDH---AQTLAIVL--PALWNEKRDTKRAKLLQYAERvwnITEGSDDE 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 133922590 395 RIQDAglvLADTlRKFLFDLDVDDGLAAVGYSKADIPALVKgTLPQERVTKL 446
Cdd:PRK15138 322 RIDAA---IAAT-RNFFEQMGVPTRLSDYGLDGSSIPALLK-KLEEHGMTQL 368
|
|
| G1PDH-like |
cd08174 |
Glycerol-1-phosphate dehydrogenase-like; These glycerol-1-phosphate dehydrogenase-like ... |
70-184 |
3.00e-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: 52.14 E-value: 3.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 70 NMGAKNVCLMTDKNLSKLPPVQVAmDSLVKNGIPFTVYDNvrvepTDSSFMEAIEFAQKG-AFDAYVAVGGGSTMDTCK- 147
Cdd:cd08174 22 NQGFGKVAIVTGEGIDELLGEDIL-ESLEEAGEIVTVEEN-----TDNSAEELAEKAFSLpKVDAIVGIGGGKVLDVAKy 95
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 133922590 148 AANL----YASSPHSDFLDYVSAPI----GKGKPVSVPLKPLIAV 184
Cdd:cd08174 96 AAFLsklpFISVPTSLSNDGIASPVavlkVDGKRKSLGAKMPYGV 140
|
|
| Fe-ADH_2 |
pfam13685 |
Iron-containing alcohol dehydrogenase; |
68-333 |
2.15e-05 |
|
Iron-containing alcohol dehydrogenase;
Pssm-ID: 404557 [Multi-domain] Cd Length: 251 Bit Score: 45.76 E-value: 2.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 68 LKNMGAKNVCLMTDKNLSKLPPVQVAmDSLVKNGIPFTVYDNVRVEPTDSSFMEAIEFAQKGAFDAYVAVGGGSTMDTCK 147
Cdd:pfam13685 14 LAELGFRRVALVADANTYAAAGRKVA-ESLKRAGIEVETRLEVAGNADMETAEKLVGALRERDADAVVGVGGGTVIDLAK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 148 aanlyassphsdfldYVSAPIGkgkpvsvplKPLIAVPTTSGTGSETTGVAIFDYEHLKVKIGitsrAIKPtLGLI-DPL 226
Cdd:pfam13685 93 ---------------YAAFKLG---------KPFISVPTAASNDGFASPGASLTVDGKKRSIP----AAAP-FGVIaDTD 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 227 HTLHMPARVVAnSGF-DvlchALESYTTLPYHlrspcpsnpitrpAYQGSNPISDIWAIHALRIVAKYLKRAVRNPDDLE 305
Cdd:pfam13685 144 VIAAAPRRLLA-SGVgD----LLAKITAVADW-------------ELAHAEEVAAPLALLSAAMVMNFADRPLRDPGDIE 205
|
250 260
....*....|....*....|....*...
gi 133922590 306 ARSHMHLASAFAGIGFGNAGVHLCHGMS 333
Cdd:pfam13685 206 ALAELLSALAMGGAGSSRPASGSEHLIS 233
|
|
| GldA |
COG0371 |
Glycerol dehydrogenase or related enzyme, iron-containing ADH family [Energy production and ... |
52-149 |
1.07e-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: 44.39 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 52 SNIRYGAAVTKEVGMDLKNMGaKNVCLMTDKNLSKL--PPVQvamDSLVKNGIPFTVYdNVRVEPTDSSFMEAIEFAQKG 129
Cdd:COG0371 7 RRYVQGEGALDELGEYLADLG-KRALIITGPTALKAagDRLE---ESLEDAGIEVEVE-VFGGECSEEEIERLAEEAKEQ 81
|
90 100
....*....|....*....|
gi 133922590 130 AFDAYVAVGGGSTMDTCKAA 149
Cdd:COG0371 82 GADVIIGVGGGKALDTAKAV 101
|
|
| Gro1PDH |
cd08173 |
Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) catalyzes the reversible conversion between ... |
52-184 |
1.21e-04 |
|
Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) catalyzes the reversible conversion between dihydroxyacetone phosphate and glycerol-1-phosphate using either NADH or NADPH as a coenzyme; Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH, EC 1.1.1.261) plays an important role in the formation of the enantiomeric configuration of the glycerophosphate backbone (sn-glycerol-1-phosphate) of archaeal ether lipids. It catalyzes the reversible conversion between dihydroxyacetone phosphate and glycerol-1-phosphate using either NADH or NADPH as a coenzyme. The activity is zinc-dependent. One characteristic feature of archaea is that their cellular membrane has an ether linkage between the glycerol backbone and the hydrocarbon residues. The polar lipids of the members of Archaea consist of di- and tetra-ethers of glycerol with isoprenoid alcohols bound at the sn-2 and sn-3 positions of the glycerol moiety. The archaeal polar lipids have the enantiomeric configuration of a glycerophosphate backbone [sn-glycerol-1-phosphate (G-1-P)] that is the mirror image structure of the bacterial or eukaryal counterpart [sn-glycerol- 3-phosphate (G-3-P)]. The absolute stereochemistry of the glycerol moiety in all archaeal polar lipids is opposite to that of glycerol ester lipids in bacteria and eukarya.
Pssm-ID: 341452 Cd Length: 343 Bit Score: 44.08 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 52 SNIRYGAAVTKEVGMDLKNMG-AKNVCLMTDKNLSKLPpVQVAMDSLVKNGIPFTVYDNVRVEpTDSSFMEAIEFAQKGA 130
Cdd:cd08173 3 RNVVVGHGAINKIGEVLKKLLlGKRALIITGPNTYKIA-GKRVEDLLESSGVEVVIVDIATIE-EAAEVEKVKKLIKESK 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 133922590 131 FDAYVAVGGGSTMDTCKaanlYASSPHSdfLDYVSAP---------------IGKGKPVSVPLKPLIAV 184
Cdd:cd08173 81 ADFIIGVGGGKVIDVAK----YAAYKLN--LPFISIPtsashdgiaspfasiKGGDKPYSIKAKAPIAI 143
|
|
| Fe-ADH_KdnB-like |
cd08184 |
Iron-containing alcohol dehydrogenase similar to Shewanella oneidensis KdnB required for Kdo8N ... |
51-386 |
2.23e-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: 2.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 51 VSNIRYGAAVTKEVGMDLKNMGAKN---VCLMTDKNLSKLPPVqvamDSLVKNGIPFTVYDNVRVEPTDS---SFMEAIE 124
Cdd:cd08184 1 VPKYLFGRGSFDQLGELLAERRKSNndyVVFFIDDVFKGKPLL----DRLPLQNGDLLIFVDTTDEPKTDqidALRAQIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 125 FAQKGAFDAYVAVGGGSTMDTCKA-ANLYA---SSPHSDFLDYVsapigKGKPVsvplkPLIAVPTTSGTGSETTGVAIF 200
Cdd:cd08184 77 AENDKLPAAVVGIGGGSTMDIAKAvSNMLTnpgSAADYQGWDLV-----KNPGI-----YKIGVPTLSGTGAEASRTAVL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 201 DYEHLkvKIGITSRAIKPTLGLIDPLHTLHMPARVVANSGFDVLCHALESyttlpyhlrspcpsnpitrpaYQGS--NPI 278
Cdd:cd08184 147 TGPEK--KLGINSDYTVFDQVILDPELIATVPRDQYFYTGMDCYIHCVES---------------------LNGTyrNAF 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 133922590 279 SDIWAIHALRIVAK-YLKRAVRNPDDLEarsHMHLASAFAGIGFGNAGVHLCHGMSYPISGLVKMykakdynvdhplvPH 357
Cdd:cd08184 204 GDAYAEKALELCRDvFLSDDMMSPENRE---KLMVASYLGGSSIANSQVGVCHALSYGLSVVLGT-------------HH 267
|
330 340 350
....*....|....*....|....*....|..
gi 133922590 358 GLSVVLtspaVFTFTAQMFPERHLE---MAEI 386
Cdd:cd08184 268 GVANCI----VFNVLEEFYPEGVKEfreMLEK 295
|
|
| GlyDH |
cd08170 |
Glycerol dehydrogenases (GlyDH) catalyzes oxidation of glycerol to dihydroxyacetone in ... |
55-156 |
3.50e-03 |
|
Glycerol dehydrogenases (GlyDH) catalyzes oxidation of glycerol to dihydroxyacetone in glycerol dissmilation; Glycerol dehydrogenases (GlyDH) is a key enzyme in the glycerol dissimilation pathway. In anaerobic conditions, many microorganisms utilize glycerol as a source of carbon through coupled oxidative and reductive pathways. One of the pathways involves the oxidation of glycerol to dihydroxyacetone with the reduction of NAD+ to NADH catalyzed by glycerol dehydrogenases. Dihydroxyacetone is then phosphorylated by dihydroxyacetone kinase and enters the glycolytic pathway for further degradation. The activity of GlyDH is zinc-dependent; the zinc ion plays a role in stabilizing an alkoxide intermediate at the active site.
Pssm-ID: 341449 [Multi-domain] Cd Length: 351 Bit Score: 39.32 E-value: 3.50e-03
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gi 133922590 55 RY--GAAVTKEVGMDLKNMGaKNVCLMTDKNLSKLPPVQVAmDSLVKNGIPFTVYDnVRVEPTDSSFMEAIEFAQKGAFD 132
Cdd:cd08170 3 RYvqGPGALDRLGEYLAPLG-KKALVIADPFVLDLVGERLE-ESLEKAGLEVVFEV-FGGECSREEIERLAAIARANGAD 79
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90 100
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gi 133922590 133 AYVAVGGGSTMDTCKAANLYASSP 156
Cdd:cd08170 80 VVIGIGGGKTIDTAKAVADYLGLP 103
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