|
Name |
Accession |
Description |
Interval |
E-value |
| gldA |
PRK09423 |
glycerol dehydrogenase; Provisional |
1-366 |
0e+00 |
|
glycerol dehydrogenase; Provisional
Pssm-ID: 181843 Cd Length: 366 Bit Score: 661.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 1 MDRIIQSPGKYIQGADVITRLGSYLKPLAERWLIVGDKFVLGFAQGALEKSFQDAGLALEIAPFGGECSQNEIDRLRVVA 80
Cdd:PRK09423 1 MDRIFISPSKYVQGKGALARLGEYLKPLGKRALVIADEFVLGIVGDRVEASLKEAGLTVVFEVFNGECSDNEIDRLVAIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 81 EKAQCAAVLGIGGGKTLDTAKALAHFMGVPVAIAPTIASTDAPCSALSVIYTDAGEFDRYLLLPNNPDRVIVDTKIVAGA 160
Cdd:PRK09423 81 EENGCDVVIGIGGGKTLDTAKAVADYLGVPVVIVPTIASTDAPTSALSVIYTEEGEFERYLFLPKNPDLVLVDTAIIAKA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 161 PARLLAAGIGDALATWFEARACSRSGATTMAGGQCTQAALTLAELCFNTLIEEGEKAMLAAEQHVVTPALERVIEANTYL 240
Cdd:PRK09423 161 PARFLAAGIGDALATWFEARACSRSGGTTMAGGKPTLAALALAELCYETLLEDGLKAKLAVEAKVVTPALENVIEANTLL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 241 SGVGFESGGLAAAHAIHNGLTAIPDAHHYYHGEKVAFGTLTQLVLENAPVDEIETVAALCHSVGLPITLAQLDIKQDIQA 320
Cdd:PRK09423 241 SGLGFESGGLAAAHAIHNGLTALEDTHHLTHGEKVAFGTLTQLVLENRPKEEIEEVIDFCHAVGLPTTLADLGLKEDSDE 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 949719653 321 KMRIVAEAACAEGETIHNMPGGATPDQVYAALLVADQYGQRYLQEW 366
Cdd:PRK09423 321 ELRKVAEAACAEGETIHNMPFKVTPEDVAAAILAADAYGQRYKQEW 366
|
|
| GlyDH |
cd08170 |
Glycerol dehydrogenases (GlyDH) catalyzes oxidation of glycerol to dihydroxyacetone in ... |
8-358 |
0e+00 |
|
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: 589.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 8 PGKYIQGADVITRLGSYLKPLAERWLIVGDKFVLGFAQGALEKSFQDAGLALEIAPFGGECSQNEIDRLRVVAEKAQCAA 87
Cdd:cd08170 1 PSRYVQGPGALDRLGEYLAPLGKKALVIADPFVLDLVGERLEESLEKAGLEVVFEVFGGECSREEIERLAAIARANGADV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 88 VLGIGGGKTLDTAKALAHFMGVPVAIAPTIASTDAPCSALSVIYTDAGEFDRYLLLPNNPDRVIVDTKIVAGAPARLLAA 167
Cdd:cd08170 81 VIGIGGGKTIDTAKAVADYLGLPVVIVPTIASTDAPCSALSVIYTEDGEFDEYLFLPRNPDLVLVDTEIIAKAPVRFLVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 168 GIGDALATWFEARACSRSGATTMAGGQCTQAALTLAELCFNTLIEEGEKAMLAAEQHVVTPALERVIEANTYLSGVGFES 247
Cdd:cd08170 161 GMGDALATYFEARACARSGAPNMAGGRPTLAALALAELCYDTLLEYGVAAKAAVEAGVVTPALEAVIEANTLLSGLGFES 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 248 GGLAAAHAIHNGLTAIPDAHHYYHGEKVAFGTLTQLVLENAPVDEIETVAALCHSVGLPITLAQLDIKQDIQAKMRIVAE 327
Cdd:cd08170 241 GGLAAAHAIHNGLTALPETHHLLHGEKVAFGTLVQLVLEGRPDEEIEEVIRFCRSVGLPVTLADLGLEDVTDEELRKVAE 320
|
330 340 350
....*....|....*....|....*....|.
gi 949719653 328 AACAEGETIHNMPGGATPDQVYAALLVADQY 358
Cdd:cd08170 321 AACAPGETIHNMPFPVTPEDVVDAILAADAL 351
|
|
| GldA |
COG0371 |
Glycerol dehydrogenase or related enzyme, iron-containing ADH family [Energy production and ... |
3-355 |
1.02e-171 |
|
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: 481.97 E-value: 1.02e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 3 RIIQSPGKYIQGADVITRLGSYLKPLAERWLIVGDKFVLGFAQGALEKSFQDAGLALEIAPFGGECSQNEIDRLRVVAEK 82
Cdd:COG0371 1 RVIILPRRYVQGEGALDELGEYLADLGKRALIITGPTALKAAGDRLEESLEDAGIEVEVEVFGGECSEEEIERLAEEAKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 83 AQCAAVLGIGGGKTLDTAKALAHFMGVPVAIAPTIASTDAPCSALSVIYTDAGEFDRYLLLPNNPDRVIVDTKIVAGAPA 162
Cdd:COG0371 81 QGADVIIGVGGGKALDTAKAVAYRLGLPVVSVPTIASTDAPASPLSVIYTEDGAFDGYSFLAKNPDLVLVDTDIIAKAPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 163 RLLAAGIGDALATWFEARACSRSGAtTMAGGQCTQAALTLAELCFNTLIEEGEKAMLAAEQHVVTPALERVIEANTYLSG 242
Cdd:COG0371 161 RLLAAGIGDALAKWYEARDWSLAHR-DLAGEYYTEAAVALARLCAETLLEYGEAAIKAVEAGVVTPALERVVEANLLLSG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 243 VGF----ESGGLAAAHAIHNGLTAIPDAHHYYHGEKVAFGTLTQLVLENAPvDEIETVAALCHSVGLPITLAQLDIKQDI 318
Cdd:COG0371 240 LAMgigsSRPGSGAAHAIHNGLTALPETHHALHGEKVAFGTLVQLVLEGRP-EEIEELLDFLRSVGLPTTLADLGLDDET 318
|
330 340 350
....*....|....*....|....*....|....*..
gi 949719653 319 QAKMRIVAEAACAEGETIHNMPGGATPDQVYAALLVA 355
Cdd:COG0371 319 EEELLTVAEAARPERYTILNLPFEVTPEAVEAAILAT 355
|
|
| GlyDH-like |
cd08550 |
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins. ... |
8-353 |
1.01e-141 |
|
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins. Glycerol dehydrogenases (GlyDH) is a key enzyme in the glycerol dissimilation pathway. In anaerobic conditions, many microorganisms utilize glycerol as a source of carbon through coupled oxidative and reductive pathways. One of the pathways involves the oxidation of glycerol to dihydroxyacetone with the reduction of NAD+ to NADH catalyzed by glycerol dehydrogenases. Dihydroxyacetone is then phosphorylated by dihydroxyacetone kinase and enters the glycolytic pathway for further degradation. The activity of GlyDH is zinc-dependent; the zinc ion plays a role in stabilizing an alkoxide intermediate at the active site. Some subfamilies have yet to be characterized.
Pssm-ID: 341480 [Multi-domain] Cd Length: 347 Bit Score: 405.77 E-value: 1.01e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 8 PGKYIQGADVITRLGSYLKPLAERWLIVGDKFVLGFAQGALEKSFQDAGLALEIAPFGGECSQNEIDRLRVVAEKAQCAA 87
Cdd:cd08550 1 PGRYIQEPGILAKAGEYIAPLGKKALIIGGKTALEAVGEKLEKSLEEAGIDYEVEVFGGECTEENIERLAEKAKEEGADV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 88 VLGIGGGKTLDTAKALAHFMGVPVAIAPTIASTDAPCSALSVIYTDAGEFDRYLLLPNNPDRVIVDTKIVAGAPARLLAA 167
Cdd:cd08550 81 IIGIGGGKVLDTAKAVADRLGLPVVTVPTIAATCAAWSALSVLYDEEGEFLGYSLLKRSPDLVLVDTDIIAAAPVRYLAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 168 GIGDALATWFEARACSRSGATTMAggqcTQAALTLAELCFNTLIEEGEKAMLAAEQHVVTPALERVIEANTYLSGVGFES 247
Cdd:cd08550 161 GIGDTLAKWYEARPSSRGGPDDLA----LQAAVQLAKLAYDLLLEYGVQAVEDVRQGKVTPALEDVVDAIILLAGLVGSL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 248 GG----LAAAHAIHNGLTAIPDAHHYYHGEKVAFGTLTQLVLENAPVDEIETVAALCHSVGLPITLAQLDIKQDiQAKMR 323
Cdd:cd08550 237 GGggcrTAAAHAIHNGLTKLPETHGTLHGEKVAFGLLVQLALEGRSEEEIEELIEFLRRLGLPVTLEDLGLELT-EEELR 315
|
330 340 350
....*....|....*....|....*....|
gi 949719653 324 IVAEAACAEGETIHNMPGGATPDQVYAALL 353
Cdd:cd08550 316 KIAEYACDPPDMAHMLPFPVTPEMLAEAIL 345
|
|
| GlyDH-like |
cd08172 |
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins ... |
8-352 |
1.10e-105 |
|
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins that have yet to be characterized, but show sequence homology with glycerol dehydrogenase. 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: 341451 [Multi-domain] Cd Length: 346 Bit Score: 314.07 E-value: 1.10e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 8 PGKYIQGADVITRLGSYLKPL-AERWLIVGDKFVLGFAQGALEKSFQDAglaLEIAPFGGECSQNEIDRLRVVAEKAQCA 86
Cdd:cd08172 1 PQEYICEEGALKELPELLSEFgIKRPLIIHGEKSWQAAKPYLPKLFEIE---YPVLRYDGECSYEEIDRLAEEAKEHQAD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 87 AVLGIGGGKTLDTAKALAHFMGVPVAIAPTIASTDAPCSALSVIYTDAGEFDRYLLLPNNPDRVIVDTKIVAGAPARLLA 166
Cdd:cd08172 78 VIIGIGGGKVLDTAKAVADKLNIPLILIPTLASNCAAWTPLSVIYDEDGEFIGYDYFPRSAYLVLVDPRLLLDSPKDYFV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 167 AGIGDALATWFEARACSRSGATTMAggqCTQAALTLAELCFNTLIEEGEKAMLAAEQHVVTPALERVIEANTYLSGV--G 244
Cdd:cd08172 158 AGIGDTLAKWYEADAILRQLEELPA---FLQLARQAAKLCRDILLKDSEQALADLEAGKLTPAFIKVVETIIALAGMvgG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 245 F--ESGGLAAAHAIHNGLTAIPDAHHYYHGEKVAFGTLTQLVLENApVDEIETVAALCHSVGLPITLAQLDIKQDIQAKM 322
Cdd:cd08172 235 FgdEYGRSAGAHAIHNGLTKLPETHHFLHGEKVAYGILVQLALEGK-WDEIKKLLPFYRRLGLPTSLADLGLTDDTEEAL 313
|
330 340 350
....*....|....*....|....*....|
gi 949719653 323 RIVAEAACAEGETIHNMPGGATPDQVYAAL 352
Cdd:cd08172 314 QKIAAFAASPEESIHLLPPDVTAEEVLQAI 343
|
|
| GlyDH-like |
cd08171 |
Glycerol dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins ... |
14-353 |
3.73e-74 |
|
Glycerol dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins that have yet to be characterized, but show sequence homology with glycerol dehydrogenase. 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: 341450 Cd Length: 345 Bit Score: 233.57 E-value: 3.73e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 14 GADVITRLGSYLKPLAERWLIVGDKFVLGFAQGALEKSFQDAGLalEIA---PFGGECSQNEIDRLRVVAEKAQCAAVLG 90
Cdd:cd08171 7 GEDAYDAIPKICSPYGKKVVVIGGKKALAAAKPKLRAALEGSGL--EITdfiWYGGEATYENVEKLKANPEVQEADMIFA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 91 IGGGKTLDTAKALAHFMGVPVAIAPTIASTDAPCSALSVIYTDAGEFDRYLLLPNNPDRVIVDTKIVAGAPARLLAAGIG 170
Cdd:cd08171 85 VGGGKAIDTVKVLADRLNKPVFTFPTIASNCAAVTAVSVMYNPDGSFKEYYFLKRPPVHTFIDTEIIAEAPEKYLWAGIG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 171 DALATWFEARACSRSGATTMAggqcTQAALTLAELCFNTLIEEGEKAMLAAEQHVVTPALERVIEANTYLSG-----VGF 245
Cdd:cd08171 165 DTLAKYYEVEFSARGDELDHT----NALGVAISKMCSEPLLKYGVQALEDCRANKVSDALEQVVLDIIVTTGlvsnlVEP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 246 E-SGGLaaAHAIHNGLTAIPDA-HHYYHGEKVAFGTLTQLVLENApVDEIETVAALCHSVGLPITLAQLDIKQDiqaKMR 323
Cdd:cd08171 241 DyNSSL--AHALYYGLTTLPQIeEEHLHGEVVSYGVLVLLTVDGQ-FEELEKVYAFNKSIGLPTCLADLGLTVE---DLE 314
|
330 340 350
....*....|....*....|....*....|
gi 949719653 324 IVAEAAcAEGETIHNMPGGATPDQVYAALL 353
Cdd:cd08171 315 KVLDKA-LKTKDLRHSPYPITKEMFEEAIK 343
|
|
| Fe-ADH |
pfam00465 |
Iron-containing alcohol dehydrogenase; |
8-348 |
2.08e-62 |
|
Iron-containing alcohol dehydrogenase;
Pssm-ID: 425696 [Multi-domain] Cd Length: 362 Bit Score: 203.60 E-value: 2.08e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 8 PGKYIQGADVITRLGSYLKPLAERWLIVGDKFVLGFaqGALEK---SFQDAGLALEIAP-FGGECSQNEIDRLRVVAEKA 83
Cdd:pfam00465 1 PTRIVFGAGALAELGEELKRLGARALIVTDPGSLKS--GLLDKvlaSLEEAGIEVVVFDgVEPEPTLEEVDEAAALAREA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 84 QCAAVLGIGGGKTLDTAKALAHFMG------------------VPVAIAPTIASTDAPCSALSVIY-TDAGEFDRYLLLP 144
Cdd:pfam00465 79 GADVIIAVGGGSVIDTAKAIALLLTnpgdvwdylggkpltkpaLPLIAIPTTAGTGSEVTPLAVITdTETGEKLGIFSPK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 145 NNPDRVIVDTKIVAGAPARLLAAGIGDALATWFEARACSRsgATTMAGGQCTQAALTLAElCFNTLIEEGEKAmlaaeqh 224
Cdd:pfam00465 159 LLPDLAILDPELTLTLPPRLTAATGMDALAHAVEAYVSKG--ANPLTDALALEAIRLIAE-NLPRAVADGEDL------- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 225 vvtPALERVIEANTyLSGVGFESGGLAAAHAIHNGLTAIPDAHH-YYHGEKVAFGT----------LTQLVL-------E 286
Cdd:pfam00465 229 ---EARENMLLAST-LAGLAFSNAGLGAAHALAHALGGRYGIPHgLANAILLPYVLrfnapaapekLAQLARalgedsdE 304
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 949719653 287 NAPVDEIETVAALCHSVGLPITLAQLDIKQDiqaKMRIVAEAACAEGeTIHNMPGGATPDQV 348
Cdd:pfam00465 305 EAAEEAIEALRELLRELGLPTTLSELGVTEE---DLDALAEAALRDR-SLANNPRPLTAEDI 362
|
|
| PRK10586 |
PRK10586 |
putative oxidoreductase; Provisional |
3-360 |
1.34e-52 |
|
putative oxidoreductase; Provisional
Pssm-ID: 182570 Cd Length: 362 Bit Score: 178.00 E-value: 1.34e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 3 RIIQSPGKYIQGADVITRLGSYLKPLA-ERWLIVGDKFVLGFAQGALEKSFQDAGLalEIAPFGGECSQNEIDRLrVVAE 81
Cdd:PRK10586 7 RVVVGPANYFSHPGSIDHLHDFFTDEQlSRAVWIYGERAIAAAQPYLPPAFELPGA--KHILFRGHCSESDVAQL-AAAS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 82 KAQCAAVLGIGGGKTLDTAKALAHFMGVPVAIAPTIASTDAPCSALSVIYTDAGEFDRYLLLPNNPDRVIVDTKIVAGAP 161
Cdd:PRK10586 84 GDDRQVVIGVGGGALLDTAKALARRLGLPFVAIPTIAATCAAWTPLSVWYNDAGQALHFEIFDDANFLVLVEPRIILNAP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 162 ARLLAAGIGDALATWFEARACSRSGAT---TMAGGqcTQAALTLAelcfNTLIEEGEKAMLAAEQHVVTPALERVIEAnt 238
Cdd:PRK10586 164 QEYLLAGIGDTLAKWYEAVVLAPQPETlplTVRLG--INNALAIR----DVLLNSSEQALADQQNGQLTQDFCDVVDA-- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 239 YLSGVGFeSGGL-------AAAHAIHNGLTAIPDAHHYYHGEKVAFGTLTQLVLenapVDEIETVAALC---HSVGLPIT 308
Cdd:PRK10586 236 IIAGGGM-VGGLgerytrvAAAHAVHNGLTVLPQTEKFLHGTKVAYGILVQSAL----LGQDDVLAQLIgayQRFHLPTT 310
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 949719653 309 LAQLDIKQDIQAKMRIVAEAACAEGETIHNMPGGATPDQVYAALLVADQYGQ 360
Cdd:PRK10586 311 LAELDVDINNQAEIDRVIAHTLRPVESIHYLPVTLTPDTLRAAFEKVESFKA 362
|
|
| DHQ_Fe-ADH |
cd07766 |
Dehydroquinate synthase-like (DHQ-like) and iron-containing alcohol dehydrogenases (Fe-ADH); ... |
8-330 |
1.39e-50 |
|
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: 170.24 E-value: 1.39e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 8 PGKYIQGADVITRLGSYLKPLAERWLIVGDKFVLGFAQGALEKSFqDAGLALEIAPF-GGECSQNEIDRLRVVAEKAQCA 86
Cdd:cd07766 1 PTRIVFGEGAIAKLGEIKRRGFDRALVVSDEGVVKGVGEKVADSL-KKGLAVAIFDFvGENPTFEEVKNAVERARAAEAD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 87 AVLGIGGGKTLDTAKALAH--FMGVPVAIAPTIASTDAPCSALSVIYTDAGEFdRYLLLPNNPDRVIVDTKIVAGAPARL 164
Cdd:cd07766 80 AVIAVGGGSTLDTAKAVAAllNRGIPFIIVPTTASTDSEVSPKSVITDKGGKN-KQVGPHYNPDVVFVDTDITKGLPPRQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 165 LAAGIGDALATWFEaracsrsgattmaggqctqaaltlaelcfntlieegekamlaaeqhvvtpaLERVIEANTYLSGVG 244
Cdd:cd07766 159 VASGGVDALAHAVE---------------------------------------------------LEKVVEAATLAGMGL 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 245 FESGGLAAAHAIHNGLTAipdAHHYYHGEKVAFGTLTQLVLENAPVDE----IETVAALCHSVGLPITLAQLDI-KQDIQ 319
Cdd:cd07766 188 FESPGLGLAHAIGHALTA---FEGIPHGEAVAVGLPYVLKVANDMNPEpeaaIEAVFKFLEDLGLPTHLADLGVsKEDIP 264
|
330
....*....|.
gi 949719653 320 AkmriVAEAAC 330
Cdd:cd07766 265 K----LAEKAL 271
|
|
| G1PDH-like |
cd08174 |
Glycerol-1-phosphate dehydrogenase-like; These glycerol-1-phosphate dehydrogenase-like ... |
14-317 |
1.19e-23 |
|
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: 99.90 E-value: 1.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 14 GADVITRLGSYLKPL---AERWLIVGDKFVLGFAQGALEKSFQDAGLALEIapfggecSQNEIDRLRVVAEKAQCA---- 86
Cdd:cd08174 7 EEGALEHLGKYLADRnqgFGKVAIVTGEGIDELLGEDILESLEEAGEIVTV-------EENTDNSAEELAEKAFSLpkvd 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 87 AVLGIGGGKTLDTAKALAHFMGVPVAIAPTIASTDAPCSALSVIYTDAGefdRYLLLPNNPDRVIVDTKIVAGAPARLLA 166
Cdd:cd08174 80 AIVGIGGGKVLDVAKYAAFLSKLPFISVPTSLSNDGIASPVAVLKVDGK---RKSLGAKMPYGVIVDLDVIKSAPRRLIL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 167 AGIGD------ALATW-FEARAcsrsGATTMAGgqctqAALTLAELCFNTLIEEGEKAMLAAEqhvvtpALERVIEANTy 239
Cdd:cd08174 157 AGIGDlisnitALYDWkLAEEK----GGEPVDD-----FAYLLSRTAADSLLNTPGKDIKDDE------FLKELAESLV- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 240 LSGVGFE--------SGglaAAHAI-HngltAIpDAHH---YYHGEKVAFGTLTQLVLENAPVDEIETVAALChsvGLPI 307
Cdd:cd08174 221 LSGIAMEiagssrpaSG---SEHLIsH----AL-DKLFpgpALHGIQVGLGTYFMSFLQGQRYEEIRDVLKRT---GFPL 289
|
330
....*....|
gi 949719653 308 TLAQLDIKQD 317
Cdd:cd08174 290 NPSDLGLTKE 299
|
|
| Fe-ADH |
cd08551 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains large ... |
8-350 |
3.42e-20 |
|
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: 90.58 E-value: 3.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 8 PGKYIQGADVITRLGSYLKPL-AERWLIVGDKFV--LGFAQgALEKSFQDAGLALEIapFGG---ECSQNEIDRLRVVAE 81
Cdd:cd08551 1 PTRIVFGAGALARLGEELKALgGKKVLLVTDPGLvkAGLLD-KVLESLKAAGIEVEV--FDDvepNPTVETVEAAAELAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 82 KAQCAAVLGIGGGKTLDTAKALAHFM------------------GVPVAIAPTIASTDAPCSALSVIyTDAGE------F 137
Cdd:cd08551 78 EEGADLVIAVGGGSVLDTAKAIAVLAtnggsirdyegigkvpkpGLPLIAIPTTAGTGSEVTPNAVI-TDPETgrkmgiV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 138 DRYLLlpnnPDRVIVDTKIVAGAPARLLAA-GIgDALATWFEArACSRsGATTMAGGQCTQAaltlAELCFNTL------ 210
Cdd:cd08551 157 SPYLL----PDVAILDPELTLSLPPSVTAAtGM-DALTHAIEA-YTSK-KANPISDALALEA----IRLIGKNLrravad 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 211 ---IEEGEKAMLAAeqhvvtpalervieantYLSGVGFESGGLAAAHAIHNGLTAIpdaHHYYHGekVAFGTLTQLVLE- 286
Cdd:cd08551 226 gsdLEAREAMLLAS-----------------LLAGIAFGNAGLGAVHALAYPLGGR---YHIPHG--VANAILLPYVMEf 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 287 NAPVDE--------------------------IETVAALCHSVGLPITLAQLDIKQDIQAKMrivAEAACAEGETIHNMP 340
Cdd:cd08551 284 NLPACPekyaeiaealgedveglsdeeaaeaaVEAVRELLRDLGIPTSLSELGVTEEDIPEL---AEDAMKSGRLLSNNP 360
|
410
....*....|
gi 949719653 341 GGATPDQVYA 350
Cdd:cd08551 361 RPLTEEDIRE 370
|
|
| EutG |
COG1454 |
Alcohol dehydrogenase, class IV [Energy production and conversion]; |
1-355 |
7.44e-20 |
|
Alcohol dehydrogenase, class IV [Energy production and conversion];
Pssm-ID: 441063 [Multi-domain] Cd Length: 381 Bit Score: 89.79 E-value: 7.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 1 MDRIIQSPGKYIQGADVITRLGSYLKPL-AERWLIVGDKFV--LGFAQgALEKSFQDAGLALEIapFGG---ECSQNEID 74
Cdd:COG1454 1 MMFTFRLPTRIVFGAGALAELGEELKRLgAKRALIVTDPGLakLGLLD-RVLDALEAAGIEVVV--FDDvepNPTVETVE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 75 RLRVVAEKAQCAAVLGIGGGKTLDTAKALA----------HFMGVP---------VAIaPTIASTDAPCSALSVIYTDAG 135
Cdd:COG1454 78 AGAAAAREFGADVVIALGGGSAIDAAKAIAllatnpgdleDYLGIKkvpgpplplIAI-PTTAGTGSEVTPFAVITDPET 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 136 E-----FDRYLLlpnnPDRVIVDTKIVAGAPARLLAA-GIgDALATWFEArACSRsGATTMAGGQCTQAaltlAELCFNT 209
Cdd:COG1454 157 GvkkgiADPELL----PDVAILDPELTLTLPPSLTAAtGM-DALTHAIEA-YVSK-GANPLTDALALEA----IRLIARN 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 210 L---IEEG------EKAMLAAeqhvvtpalervieantYLSGVGFESGGLAAAHAIHNGLTAIPDAHH------------ 268
Cdd:COG1454 226 LpraVADGddlearEKMALAS-----------------LLAGMAFANAGLGAVHALAHPLGGLFHVPHglanaillphvl 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 269 -YY---HGEKVA-----FGTLTQLVLENAPVDEIETVAALCHSVGLPITLAQLDIKQ-DIQAkmriVAEAACAEGETIHN 338
Cdd:COG1454 289 rFNapaAPERYAeiaraLGLDVGLSDEEAAEALIEAIRELLRDLGIPTRLSELGVTEeDLPE----LAELALADRCLANN 364
|
410
....*....|....*..
gi 949719653 339 mPGGATPDQVYAALLVA 355
Cdd:COG1454 365 -PRPLTEEDIEAILRAA 380
|
|
| Fe-ADH_2 |
pfam13685 |
Iron-containing alcohol dehydrogenase; |
14-276 |
3.62e-19 |
|
Iron-containing alcohol dehydrogenase;
Pssm-ID: 404557 [Multi-domain] Cd Length: 251 Bit Score: 85.82 E-value: 3.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 14 GADVITRLGSYLKPLA-ERWLIVGDKFVLGFAQGALEKSFQDAGLALEIAPF-GGECSQNEIDRLRVVAEKAQCAAVLGI 91
Cdd:pfam13685 3 GPGALGRLGEYLAELGfRRVALVADANTYAAAGRKVAESLKRAGIEVETRLEvAGNADMETAEKLVGALRERDADAVVGV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 92 GGGKTLDTAKALAHFMGVPVAIAPTIASTDAPCSALSVIYTDAgefdRYLLLP-NNPDRVIVDTKIVAGAPARLLAAGIG 170
Cdd:pfam13685 83 GGGTVIDLAKYAAFKLGKPFISVPTAASNDGFASPGASLTVDG----KKRSIPaAAPFGVIADTDVIAAAPRRLLASGVG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 171 D------ALATWFEARAcSRSGAttmaggqctQAALTLAELCFNtlieegeKAMLAAEQHVVTPALERVIEANTyLSGVG 244
Cdd:pfam13685 159 DllakitAVADWELAHA-EEVAA---------PLALLSAAMVMN-------FADRPLRDPGDIEALAELLSALA-MGGAG 220
|
250 260 270
....*....|....*....|....*....|..
gi 949719653 245 FESGGLAAAHAIHNGLTAIPDAHHyYHGEKVA 276
Cdd:pfam13685 221 SSRPASGSEHLISHALDMIAPKQA-LHGEQVG 251
|
|
| egsA |
PRK00843 |
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed |
3-171 |
2.38e-18 |
|
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed
Pssm-ID: 179139 Cd Length: 350 Bit Score: 84.95 E-value: 2.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 3 RIIQSPGKYIQGADVITRLGSYLKPLA--ERWLIVGDKFVLGFAQGALEKSFQDAGLALEIapFGGECSQNEIDRLRVVA 80
Cdd:PRK00843 6 HWIQLPRDVVVGHGVLDDIGDVCSDLKltGRALIVTGPTTKKIAGDRVEENLEDAGDVEVV--IVDEATMEEVEKVEEKA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 81 EKAQCAAVLGIGGGKTLDTAKALAHFMGVPVAIAPTIASTDAPCSALSVIYTDAGefdRYLLLPNNPDRVIVDTKIVAGA 160
Cdd:PRK00843 84 KDVNAGFLIGVGGGKVIDVAKLAAYRLGIPFISVPTAASHDGIASPRASIKGGGK---PVSVKAKPPLAVIADTEIIAKA 160
|
170
....*....|.
gi 949719653 161 PARLLAAGIGD 171
Cdd:PRK00843 161 PYRLLAAGCGD 171
|
|
| G1PDH_related |
cd08549 |
Glycerol-1-phosphate dehydrogenase and related proteins; This family contains bacterial and ... |
8-318 |
6.41e-18 |
|
Glycerol-1-phosphate dehydrogenase and related proteins; This family contains bacterial and archeal glycerol-1-phosphate dehydrogenase-like oxidoreductases. These proteins have similarity with 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. It also contains archaeal Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) that plays an important role in the formation of the enantiomeric configuration of the glycerophosphate backbone (sn-glycerol-1-phosphate) of archaeal ether lipids.
Pssm-ID: 341479 [Multi-domain] Cd Length: 331 Bit Score: 83.77 E-value: 6.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 8 PGKYIQGADVITRLGSYLK-PLAERWLIVGDKFVLGFAQGALEKSFQDAglaLEIAPFggecsqNEIDRLRVVAEKAQCA 86
Cdd:cd08549 1 PRYTIVGDGAINKIEEILKkLNLKRVLIITGKNTKAKYCRFFYDQLKTV---CDIVYY------DNIDNLEDELKKYTFY 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 87 -AVLGIGGGKTLDTAKALAHFMGVPVAIAPTIASTDAPCS-ALSVIYTDAgefdRYLLLPNNPDRVIVDTKIVAGAPARL 164
Cdd:cd08549 72 dCVIGIGGGRSIDTGKYLAYKLKIPFISVPTSASNDGIASpIVSLRIPGV----KKTFMADAPIAIIADTEIIKKSPRRL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 165 LAAGIGD------ALATW-FEARacsrsgattMAGGQCTQAALTLAELCFNTLIEEGEKAMLAAEQHvvtpaleRVIEAN 237
Cdd:cd08549 148 LSAGIGDlvsnitAVLDWkLAHK---------EKGEKYSEFAAILSKTSAKELVSYVLKASDLEEYH-------RVLVKA 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 238 TYLSGVGFESGGLAA---------AHAIHNGLTAIPDaHHYYHGEKVAFGTLTQLVL------ENAPVDE-IETVAAlch 301
Cdd:cd08549 212 LVGSGIAMAIAGSSRpasgsehlfSHALDKLKEEYLN-INVLHGEQVGVGTIIMSYLhekenkKLSGLHErIKMILK--- 287
|
330
....*....|....*..
gi 949719653 302 SVGLPITLAQLDIKQDI 318
Cdd:cd08549 288 KVGAPTTAKQLGIDEDL 304
|
|
| Gro1PDH |
cd08173 |
Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) catalyzes the reversible conversion between ... |
14-174 |
7.52e-18 |
|
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: 83.37 E-value: 7.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 14 GADVITRLGSYLKPLAE--RWLIVGDKFVLGFAQGALEKSFQDAGLALEIapfggeCSQNEIDRLRVVAEKAQCAA---- 87
Cdd:cd08173 8 GHGAINKIGEVLKKLLLgkRALIITGPNTYKIAGKRVEDLLESSGVEVVI------VDIATIEEAAEVEKVKKLIKeska 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 88 --VLGIGGGKTLDTAKALAHFMGVPVAIAPTIASTDAPCSALSVIYTDAGefdRYLLLPNNPDRVIVDTKIVAGAPARLL 165
Cdd:cd08173 82 dfIIGVGGGKVIDVAKYAAYKLNLPFISIPTSASHDGIASPFASIKGGDK---PYSIKAKAPIAIIADTEIISKAPKRLL 158
|
....*....
gi 949719653 166 AAGIGDALA 174
Cdd:cd08173 159 AAGCGDLIS 167
|
|
| Fe-ADH-like |
cd14863 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
14-353 |
1.98e-15 |
|
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: 76.81 E-value: 1.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 14 GADVITRLGSYLKPL-AERWLIVGDKFV--LGFAQGALEkSFQDAGLA----LEIAPfggECSQNEIDRLRVVAEKAQCA 86
Cdd:cd14863 11 GAGAVEQIGELLKELgCKKVLLVTDKGLkkAGIVDKIID-LLEEAGIEvvvfDDVEP---DPPDEIVDEAAEIAREEGAD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 87 AVLGIGGGKTLDTAKALA-----------HFMGVPVAIA--------PTIASTDAPCSALSVIYTDAGEFDRYLLLPN-N 146
Cdd:cd14863 87 GVIGIGGGSVLDTAKAIAvlltnpgpiidYALAGPPVPKpgipliaiPTTAGTGSEVTPIAVITDEENGVKKSLLGPFlV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 147 PDRVIVDTKIVAGAPARLLAA-GIgDALATWFEARACSRSGATTMAggqctqAALTLAELCFNTL---IEEG------EK 216
Cdd:cd14863 167 PDLAILDPELTVGLPPSLTAAtGM-DALSHAIEAYTSKLANPMTDA------LALQAIRLIVKNLpraVKDGdnlearEN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 217 AMLAAeqhvvtpalervieantYLSGVGFESGGLAAAHAIHNGLTAIpdaHHYYHGEKVAFGTLTqlVLE-NAPV----- 290
Cdd:cd14863 240 MLLAS-----------------NLAGIAFNNAGTHIGHAIAHALGAL---YHIPHGLACALALPV--VLEfNAEAypekv 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 291 -------------DEIETVAALCH--------SVGLPITLAQLDIKQDiqAKMRIVAEAAcaeGETIHNMPGGATPDQVY 349
Cdd:cd14863 298 kkiakalgvsfpgESDEELGEAVAdairefmkELGIPSLFEDYGIDKE--DLDKIAEAVL---KDPFAMFNPRPITEEEV 372
|
....
gi 949719653 350 AALL 353
Cdd:cd14863 373 AEIL 376
|
|
| Fe-ADH-like |
cd08196 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
5-352 |
1.19e-14 |
|
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: 74.15 E-value: 1.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 5 IQSPGKYIQGADVITRLGSYLKPLA-ERWLIVGDKFVLgfAQGALEKSFQDAGLAL-----EIAPfggECSQNEIDRLRV 78
Cdd:cd08196 3 YYQPVKIIFGEGILKELPDIIKELGgKRGLLVTDPSFI--KSGLAKRIVESLKGRIvavfsDVEP---NPTVENVDKCAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 79 VAEKAQCAAVLGIGGGKTLDTAKALA----------HFM---------GVPVAIAPTIASTDAPCSALSVIyTDAGEFDR 139
Cdd:cd08196 78 LARENGADFVIAIGGGSVLDTAKAAAclaktdgsieDYLegkkkipkkGLPLIAIPTTAGTGSEVTPVAVL-TDKEKGKK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 140 YLLLPNN--PDRVIVDTKIVAGAPARLLAA-GIgDALATWFEArACSRSgattmAGGQCTQAALTLAELCFNTL---IEE 213
Cdd:cd08196 157 APLVSPGfyPDIAIVDPELTYSMPPKVTAStGI-DALCHAIEA-YWSIN-----HQPISDALALEAAKLVLENLekaYNN 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 214 GEKAmlaaeqhvvtPALERVIEANTyLSGVGFESGGLAAAHAIHNGLTAIpdaHHYYHGEKVAFgTLTQLVLENAPVDE- 292
Cdd:cd08196 230 PNDK----------EAREKMALASL-LAGLAFSQTRTTASHACSYPLTSH---FGIPHGEACAL-TLPSFIRLNAEALPg 294
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 949719653 293 -----------------IETVAALCHSVGLPITLAQLDIKQDiqaKMRIVAEAACAEgETIHNMPGGATPDQVYAAL 352
Cdd:cd08196 295 rldelakqlgfkdaeelADKIEELKKRIGLRTRLSELGITEE---DLEEIVEESFHP-NRANNNPVEVTKEDLEKLL 367
|
|
| Fe-ADH-like |
cd14864 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
8-329 |
1.87e-14 |
|
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: 73.87 E-value: 1.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 8 PGKYIQGADVITRLGSYLKPLAERWLIVGDKFVLGF-AQGALEKSFQDAGLalEIAPF---GGECSQNEIDRLRVVAEKA 83
Cdd:cd14864 4 PPNIVFGADSLERIGEEVKEYGSRFLLITDPVLKESgLADKIVSSLEKAGI--SVIVFdeiPASATSDTIDEAAELARKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 84 QCAAVLGIGGGKTLDTAKALA----------HFMG--------VPVAIAPTIASTDAPCSAlSVIYTDAGEFDRYLL--L 143
Cdd:cd14864 82 GADGIIAVGGGKVLDTAKAVAilanndggayDFLEgakpkkkpLPLIAVPTTPRSGFEFSD-RFPVVDSRSREVKLLkaQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 144 PNNPDRVIVDTKIVAGAPARLLAAGIGDALATWFEARACSRSGATTmaggqctqaaltlaelcfNTLIEEGEKAML---- 219
Cdd:cd14864 161 PGLPKAVIVDPNLMASLTGNQTAAMALAALALAVEAYLSKKSNFFS------------------DALALKAIELVSenld 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 220 -AAEQHVVTPALERVIEANtYLSGVGFESGGL----AAAHAIhNGLTAIPDAH-------HY--YHGEKVAFGTLTQLVL 285
Cdd:cd14864 223 gALADPKNTPAEELLAQAG-CLAGLAASSSSPglatALALAV-NSRYKVSKSLvasillpHVieYAATSAPDKYAKIARA 300
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 949719653 286 ENAPVDEIETVAA----------LCHSVGLPITLAQLDIKQDIQAKMRIVAEAA 329
Cdd:cd14864 301 LGEDVEGASPEEAaiaavegvrrLIAQLNLPTRLKDLDLASSLEQLAAIAEDAP 354
|
|
| G1PDH |
cd08175 |
Glycerol-1-phosphate dehydrogenase (G1PDH) catalyzes the reversible reduction of ... |
14-317 |
2.16e-13 |
|
Glycerol-1-phosphate dehydrogenase (G1PDH) catalyzes the reversible reduction of dihydroxyacetone phosphate (DHAP) to glycerol-1-phosphate (G1P) in an NADH-dependent manner; Glycerol-1-phosphate dehydrogenase (G1PDH) 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 a Ni++ ion. In Bacillus subtilis, it has been described as AraM gene in L-arabinose (ara) operon. AraM protein forms homodimer.
Pssm-ID: 341454 Cd Length: 340 Bit Score: 70.23 E-value: 2.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 14 GADVITRLGSYLKPL--AERWLIVGDKFVLGFAQGALEKSFQDAGLALEIAPFggecsqneIDRLRVVAE---------- 81
Cdd:cd08175 7 GEGALKKLPEYLKELfgGKKVLVVADENTYAAAGEEVEAALEEAGVTVCLLIF--------PGEGDLIADeaavgkvlle 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 82 -KAQCAAVLGIGGGkTL-DTAKALAHFMGVPVAIAPTIASTDAPCSALSVIytdagefdryllLPNN---------PDRV 150
Cdd:cd08175 79 lEKDTDLIIAVGSG-TInDLTKYAAYKLGIPYISVPTAPSMDGYTSSGAPI------------IVDGvkktfpahaPKAI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 151 IVDTKIVAGAPARLLAAGIGD------ALATWFEARAcsrsgattmAGGQ--CTQAAltlaelcfnTLIEEGEKAMLAAE 222
Cdd:cd08175 146 FADLDVLANAPQRMIAAGFGDllgkytALADWKLSHL---------LGGEyyCPEVA---------DLVQEALEKCLDNA 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 223 QHVVT---PALERVIEANTyLSGVGFE--------SGglaAAH---------AIHNGLTAIpdahhyYHGEKVAFGTLTQ 282
Cdd:cd08175 208 EGIAArdpEAIEALMEALI-LSGLAMQlvgnsrpaSG---AEHhlshywemeFLRLGKPPV------LHGEKVGVGTLLI 277
|
330 340 350
....*....|....*....|....*....|....*...
gi 949719653 283 L---VLENAPvdEIETVAALCHSVGLPITLAQLDIKQD 317
Cdd:cd08175 278 AalyILEQLP--PPEELRELLRKAGAPTTPEDLGIDRD 313
|
|
| Fe-ADH-like |
cd14862 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
7-329 |
2.50e-12 |
|
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: 67.25 E-value: 2.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 7 SPGKYIQGADVITRLGSYLKplaERWLIVGDKFV--LGFAQGALEKsFQDAGLALEIapFGG---ECSQNEIDRLRVVAE 81
Cdd:cd14862 5 SSPKIVFGEDALSHLEQLSG---KRALIVTDKVLvkLGLLKKVLKR-LLQAGFEVEV--FDEvepEPPLETVLKGAEAMR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 82 KAQCAAVLGIGGGKTLDTAKALAHFMGVP---------------------VAIaPTIASTDAPCSALSVIyTDAGEFdRY 140
Cdd:cd14862 79 EFEPDLIIALGGGSVMDAAKAAWVLYERPdldpedispldllglrkkaklIAI-PTTSGTGSEATWAIVL-TDTEEP-RK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 141 LLLPNN---PDRVIVDTKIVAGAPARLLAA-GIgDALATWFEARACSRSgaTTMAGGQCTQAaltlAELCFNTLieegek 216
Cdd:cd14862 156 IAVANPelvPDVAILDPEFVLGMPPKLTAGtGL-DALAHAVEAYLSTWS--NDFSDALALKA----IELIFKYL------ 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 217 aMLAAEQHVVTPALERVIEANTyLSGVGFESGGLAAAHAIHNGLTAIPDAHH--------------YYHGEKVAFGTLTQ 282
Cdd:cd14862 223 -PRAYKDGDDLEAREKMHNAAT-IAGLAFGNSQAGLAHALGHSLGAVFHVPHgiavglflpyviefYAKVTDERYDLLKL 300
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 949719653 283 LVLENAPVDE-----IETVAALCHSVGLPITLAQLDI-KQDIQAKMRIVAEAA 329
Cdd:cd14862 301 LGIEARDEEEalkklVEAIRELYKEVGQPLSIKDLGIsEEEFEEKLDELVEYA 353
|
|
| BDH |
cd08187 |
Butanol dehydrogenase catalyzes the conversion of butyraldehyde to butanol with the cofactor ... |
4-337 |
1.76e-11 |
|
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: 64.76 E-value: 1.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 4 IIQSPGKYIQGADVITRLGSYLKPLAERWLIV-GDKFVlgFAQGALEK---SFQDAGLalEIAPFGGECSQNEIDRLRVV 79
Cdd:cd08187 3 TFYNPTKIIFGKGAIEELGEEIKKYGKKVLLVyGGGSI--KKNGLYDRvvaSLKEAGI--EVVEFGGVEPNPRLETVREG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 80 AEKA---QCAAVLGIGGGKTLDTAKALA-----------HFMG-------VPVAIAPTIASTDAPCSALSVI-YTDAGE- 136
Cdd:cd08187 79 IELAreeNVDFILAVGGGSVIDAAKAIAagakydgdvwdFFTGkappekaLPVGTVLTLAATGSEMNGGAVItNEETKEk 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 137 --FDRYLLLPnnpdRV-IVDTKIVAGAPARLLAAGIGDALA----TWFearacsrsgattmagGQCTQAALT--LAELCF 207
Cdd:cd08187 159 lgFGSPLLRP----KFsILDPELTYTLPKYQTAAGIVDIFShvleQYF---------------TGTEDAPLQdrLAEGLL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 208 NTLIEEGEKA-------------MLAAEQhvvtpalervieANTYLSGVGFESGglAAAHAIHNGLTAIPDAHH------ 268
Cdd:cd08187 220 RTVIENGPKAlkdpddyearanlMWAATL------------ALNGLLGAGRGGD--WATHAIEHELSALYDITHgaglai 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 269 -------YYHGEKVA---------FGTLTQLVLENAPVDEIETVAALCHSVGLPITLAQLDIKQDIQAKMrivAEAACAE 332
Cdd:cd08187 286 vfpawmrYVLKKKPErfaqfarrvFGIDPGGDDEETALEGIEALEEFFKSIGLPTTLSELGIDEEDIEEM---AEKAVRG 362
|
....*
gi 949719653 333 GETIH 337
Cdd:cd08187 363 GGLGG 367
|
|
| HEPD |
cd08182 |
Hydroxyethylphosphoate dehydrogenase (HEPD) catalyzes the reduction of phosphonoacetaldehyde ... |
8-352 |
1.82e-10 |
|
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: 61.47 E-value: 1.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 8 PGKYIQGADVITRLGSYLKPL-AERWLIVGDKfvLGFAQGALEKSFQDAGLALEIAPFGGECSQNEIDRLRVVAEKAQ-- 84
Cdd:cd08182 1 PVKIIFGPGALAELKDLLGGLgARRVLLVTGP--SAVRESGAADILDALGGRIPVVVFSDFSPNPDLEDLERGIELFRes 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 85 -CAAVLGIGGGKTLDTAKALAHFMGVP---------------------VAIaPTIASTDAPCSALSVIY-TDAGE---FD 138
Cdd:cd08182 79 gPDVIIAVGGGSVIDTAKAIAALLGSPgenllllrtgekapeenalplIAI-PTTAGTGSEVTPFATIWdEAEGKkysLA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 139 RYLLLpnnPDRVIVDTKIVAGAPARLLAAGIGDALATWFEARACSRSGATTMAggqctqAALTLAELCFNTLieegeKAM 218
Cdd:cd08182 158 HPSLY---PDAAILDPELTLSLPLYLTASTGLDALSHAIESIWSVNANPESRA------YALRAIRLILENL-----PLL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 219 LAAEQHvvTPALERVIEAnTYLSGVGFESGGLAAAHAIHNGLTAipdAHHYYHGEKVAFgTLTQLVLENAPVDE------ 292
Cdd:cd08182 224 LENLPN--LEAREAMAEA-SLLAGLAISITKTTAAHAISYPLTS---RYGVPHGHACAL-TLPAVLRYNAGADDecdddp 296
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 949719653 293 -----------------IETVAALCHSVGLPITLAQLDIKQDiqAKMRIVAEAacAEGETIHNMPGGATPDQVYAAL 352
Cdd:cd08182 297 rgreillalgasdpaeaAERLRALLESLGLPTRLSEYGVTAE--DLEALAASV--NTPERLKNNPVRLSEEDLLRLL 369
|
|
| Fe-ADH-like |
cd08191 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
7-341 |
1.87e-09 |
|
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: 58.78 E-value: 1.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 7 SPGKYIQGADVITRLGSYLKPLAERWLIVGDKFVL---GFAQgaLEKSFQDAGLALEIapFGGECsqnEIDRLRVVAEKA 83
Cdd:cd08191 3 SPSRLLFGPGARRALGRVAARLGSRVLIVTDPRLAstpLVAE--LLAALTAAGVAVEV--FDGGQ---PELPVSTVADAA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 84 QCAA------VLGIGGGKTLDTAKALA----------HFMG--------VPVAIAPTIASTDAPCSALSVIY-----TDA 134
Cdd:cd08191 76 AAARafdpdvVIGLGGGSNMDLAKVVAlllahggdprDYYGedrvpgpvLPLIAVPTTAGTGSEVTPVAVLTdpargMKV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 135 GEFDRYLLlpnnPDRVIVDTKIVAGAPARLLA-AGIgDAL--------ATWFEARACSR-----SGATTMAggqcTQAAL 200
Cdd:cd08191 156 GVSSPYLR----PAVAIVDPELTLTCPPGVTAdSGI-DALthaiesytARDFPPFPRLDpdpvyVGKNPLT----DLLAL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 201 TLAELCFNTLIEegekamlAAEQHVVTPALERVIEANTyLSGVGFESGGLAAAHAIHNGLTAipdAHHYYHGEKV----- 275
Cdd:cd08191 227 EAIRLIGRHLPR-------AVRDGDDLEARSGMALAAL-LAGLAFGTAGTAAAHALQYPIGA---LTHTSHGVGNglllp 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 276 -------------------AFGTLTQLVLENAPVDEIETVAALCHSVGLPITLAQLDIKqdiQAKMRIVAEAACAEGETI 336
Cdd:cd08191 296 yvmrfnrparaaelaeiarALGVTTAGTSEEAADRAIERVEELLARIGIPTTLADLGVT---EADLPGLAEKALSVTRLI 372
|
....*
gi 949719653 337 HNMPG 341
Cdd:cd08191 373 ANNPR 377
|
|
| Fe-ADH-like |
cd08183 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
8-104 |
3.18e-09 |
|
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: 57.90 E-value: 3.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 8 PGKYIQGADVITRLGSYLKPLAERWLIV-GDKFVLGFAQGALEKSFQDAGLALEIAPFGGECSQNEIDRLRVVAEKAQCA 86
Cdd:cd08183 1 PPRIVFGRGSLQELGELAAELGKRALLVtGRSSLRSGRLARLLEALEAAGIEVALFSVSGEPTVETVDAAVALAREAGCD 80
|
90
....*....|....*...
gi 949719653 87 AVLGIGGGKTLDTAKALA 104
Cdd:cd08183 81 VVIAIGGGSVIDAAKAIA 98
|
|
| Fe-ADH-like |
cd08194 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
8-173 |
3.77e-09 |
|
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: 57.54 E-value: 3.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 8 PGKYIQGADVITRLGSYLKPL-AERWLIVGDKFV--LGFAQgALEKSFQDAGLALEI-APFGGECSQNEIDRLRVVAEKA 83
Cdd:cd08194 1 PRTIIIGGGALEELGEEAASLgGKRALIVTDKVMvkLGLVD-KVTQLLAEAGIAYAVfDDVVSEPTDEMVEEGLALYKEG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 84 QCAAVLGIGGGKTLDTAKA----------LAHFMG--------VPVAIAPTIASTDAPCSALSVIyTDAgEFDRYLLLPN 145
Cdd:cd08194 80 GCDFIVALGGGSPIDTAKAiavlatnggpIRDYMGprkvdkpgLPLIAIPTTAGTGSEVTRFTVI-TDT-ETDVKMLLKG 157
|
170 180 190
....*....|....*....|....*....|..
gi 949719653 146 ---NPDRVIVDTKIVAGAPARLLAA-GIgDAL 173
Cdd:cd08194 158 palLPAVAIVDPELTLSMPPRVTAAtGI-DAL 188
|
|
| Fe-ADH-like |
cd14865 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
6-355 |
3.91e-09 |
|
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: 57.55 E-value: 3.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 6 QSPGKYIQGADVITRLGSYLKPL-AERWLIVGDKFV--LGFA---QGALEKSFQDAGLALEIAPfggECSQNEIDRLRVV 79
Cdd:cd14865 4 FNPTKIVSGAGALENLPAELARLgARRPLIVTDKGLaaAGLLkkvEDALGDAIEIVGVFDDVPP---DSSVAVVNEAAAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 80 AEKAQCAAVLGIGGGKTLDTAKA-----------LAHFMG--------VPVAIAPTIASTDAPCSALSVIY-TDAG---E 136
Cdd:cd14865 81 AREAGADGIIAVGGGSVIDTAKGvnillseggddLDDYGGanrltrplKPLIAIPTTAGTGSEVTLVAVIKdEEKKvklL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 137 F-DRYLLlpnnPDRVIVDTKIVAGAPARLLAAGIGDALATWFEARACSRSGATTMAggqctqAALTLAELCFNTLI---- 211
Cdd:cd14865 161 FvSPFLL----PDVAILDPRLTLSLPPKLTAATGMDALTHAIEAYTSLQKNPISDA------LALQAIRLISENLPkavk 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 212 ----EEGEKAMLAAeqhvvtpalervieanTYLSGVGFESGGLAAAHAI-HngltAIPDAHHYYHGekVAFGTLTQLVLE 286
Cdd:cd14865 231 ngkdLEARLALAIA----------------ATMAGIAFSNSMVGLVHAIaH----AVGAVAGVPHG--LANSILLPHVMR 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 287 -NAPVDE----------------------------IETVAALCHSVGLPITLAQLDIKQDiqaKMRIVAEAACAEGETIH 337
Cdd:cd14865 289 yNLDAAAeryaelalalaygvtpagrraeeaieaaIDLVRRLHELCGLPTRLRDVGVPEE---QLEAIAELALNDGAILF 365
|
410
....*....|....*...
gi 949719653 338 NmPGGATPDQVYAALLVA 355
Cdd:cd14865 366 N-PREVDPEDILAILEAA 382
|
|
| Fe-ADH-like |
cd14861 |
Iron-containing alcohol dehydrogenases-like; This family contains proteins similar to ... |
14-329 |
4.56e-09 |
|
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: 57.52 E-value: 4.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 14 GADVITRLGSYLKPL-AERWLIVGDKFV--LGFAQGALEkSFQDAGLALEIapFGGECS---QNEIDRLRVVAEKAQCAA 87
Cdd:cd14861 9 GAGAIAELPEELKALgIRRPLLVTDPGLaaLGIVDRVLE-ALGAAGLSPAV--FSDVPPnptEADVEAGVAAYREGGCDG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 88 VLGIGGGKTLDTAKA----------LAHF-----------MGVPVAIA-PTIASTDAPCSALSVIY-TDAGE----FDRY 140
Cdd:cd14861 86 IIALGGGSAIDAAKAialmathpgpLWDYedgeggpaaitPAVPPLIAiPTTAGTGSEVGRAAVITdDDTGRkkiiFSPK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 141 LLlpnnPDRVIVDTKIVAGAPARLLAA-GIgDALATWFEarACSRSGATTMAGGqctqAALTLAELCFNTLieegEKAM- 218
Cdd:cd14861 166 LL----PKVAICDPELTLGLPPRLTAAtGM-DALTHCIE--AYLSPGFHPMADG----IALEGLRLISEWL----PRAVa 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 219 ----LAAEQHVVTPALErvieantylSGVGFESgGLAAAHAIHNGLTAIPDAHH--------------YYHGEKVAFGTL 280
Cdd:cd14861 231 dgsdLEARGEMMMAALM---------GAVAFQK-GLGAVHALAHALGALYGLHHgllnaillpyvlrfNRPAVEDKLARL 300
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 949719653 281 TQ-LVLENAPVDEIET-VAALCHSVGLPITLAQLDIKQDIQAkmRIVAEAA 329
Cdd:cd14861 301 ARaLGLGLGGFDDFIAwVEDLNERLGLPATLSELGVTEDDLD--ELAELAL 349
|
|
| NADPH_BDH |
cd08179 |
NADPH-dependent butanol dehydrogenase involved in the butanol and ethanol formation pathway in ... |
88-348 |
2.69e-08 |
|
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: 54.89 E-value: 2.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 88 VLGIGGGKTLDTAKALAHF--------------MGVP--------VAIaPTIASTDAPCSALSVIyTDAGEFDRYLLLPN 145
Cdd:cd08179 85 IIAIGGGSVIDAAKAMWVFyeypeltfedalvpFPLPelrkkarfIAI-PSTSGTGSEVTRASVI-TDTEKGIKYPLASF 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 146 N--PDRVIVDTKIVAGAPARLLAAGIGDALATWFEARACSRsgATTMAGGQCTQAALTLAE---LCFNtlieeGEKAMLA 220
Cdd:cd08179 163 EitPDVAILDPELTMTMPPHVTANTGMDALTHAIEAYVSTL--ANDFTDALALGAILDIFEnlpKSYN-----GGKDLEA 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 221 AEQ-HVVtpalervieanTYLSGVGFESGGLAAAHAI-HngltAIPDAHHYYHGEKVAFgtLTQLVLE-NAPVDE----- 292
Cdd:cd08179 236 REKmHNA-----------SCLAGMAFSNSGLGIVHSMaH----KGGAFFGIPHGLANAI--LLPYVIEfNSKDPEarary 298
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 949719653 293 ----------------IETVAALCHSVGLPITLAQLDIKQDI-QAKMRIVAEAACAEGETIHNmPGGATPDQV 348
Cdd:cd08179 299 aalligltdeelvedlIEAIEELNKKLGIPLSFKEAGIDEDEfFAKLDEMAENAMNDACTGTN-PRKPTVEEM 370
|
|
| LPO |
cd08176 |
Lactadehyde:propanediol oxidoreductase (LPO) catalyzes the interconversion between ... |
81-331 |
9.84e-08 |
|
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: 53.32 E-value: 9.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 81 EKAQCAAVLGIGGGKTLDTAKAL----AH-------FMGV-------PVAIA-PTIASTDAPCSALSVIyTDAGEFDRYL 141
Cdd:cd08176 82 KESGADGIIAVGGGSSIDTAKAIgiivANpgadvrsLEGVaptknpaVPIIAvPTTAGTGSEVTINYVI-TDTEKKRKFV 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 142 LL-PN-NPDRVIVDTKIVAGAPARLLAA-GIgDALATWFEARAcSRsGATTMAGGQCTQA----ALTLAELCFNTLIEEG 214
Cdd:cd08176 161 CVdPHdIPTVAIVDPDLMSSMPKGLTAAtGM-DALTHAIEGYI-TK-GAWELSDMLALKAieliAKNLRKAVANPNNVEA 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 215 EKAMLAAEqhvvtpalervieantYLSGVGFESGGLAAAHAIHNGLTAIPDAHH-------------Y---YHGEK---- 274
Cdd:cd08176 238 RENMALAQ----------------YIAGMAFSNVGLGIVHSMAHPLSAFYDTPHgvanaillpyvmeFnapATGEKyrdi 301
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 275 -VAFG-TLTQLVLENAPVDEIETVAALCHSVGLPITLAQLDIKQ-DIQAkmriVAEAACA 331
Cdd:cd08176 302 aRAMGvDTTGMSDEEAAEAAVDAVKKLSKDVGIPQKLSELGVKEeDIEA----LAEDALN 357
|
|
| HVD |
cd08193 |
5-hydroxyvalerate dehydrogenase (HVD) catalyzes the oxidation of 5-hydroxyvalerate to ... |
6-173 |
5.87e-07 |
|
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: 50.97 E-value: 5.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 6 QSPGKYIQGADVITRLGSYLKPL-AERWLIVGDKFV--LGFAQGALEkSFQDAGLALEIapfggeCSQNEID-RLRVV-- 79
Cdd:cd08193 2 QTVPRIICGAGAAARLGELLRELgARRVLLVTDPGLvkAGLADPALA-ALEAAGIAVTV------FDDVVADpPEAVVea 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 80 ----AEKAQCAAVLGIGGGKTLDTAK----------ALAHFMGV--------PVAIAPTIASTDAPCSALSVIYTDAGE- 136
Cdd:cd08193 75 aveqAREAGADGVIGFGGGSSMDVAKlvallagsdqPLDDIYGVgkatgprlPLILVPTTAGTGSEVTPISIVTTGETEk 154
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 949719653 137 ---FDRYLLlpnnPDRVIVDTKIVAGAPARLLAA-GIgDAL 173
Cdd:cd08193 155 kgvVSPQLL----PDVALLDAELTLGLPPHVTAAtGI-DAM 190
|
|
| Fe-ADH-like |
cd08189 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
12-328 |
1.46e-06 |
|
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: 49.77 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 12 IQGADVITRLGSYLKPLA-ERWLIVGDKFV--LGFAQGALEkSFQDAGLALEIapFGG-----ECSQneIDRLRVVAEKA 83
Cdd:cd08189 9 FEGAGSLLQLPEALKKLGiKRVLIVTDKGLvkLGLLDPLLD-ALKKAGIEYVV--FDGvvpdpTIDN--VEEGLALYKEN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 84 QCAAVLGIGGGKTLDTAKALA-----------HFMGV-------PVAIA-PTIASTDAPCSALSVIyTDAGEFDRYLLLP 144
Cdd:cd08189 84 GCDAIIAIGGGSVIDCAKVIAaraanpkksvrKLKGLlkvrkklPPLIAvPTTAGTGSEATIAAVI-TDPETHEKYAIND 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 145 NN--PDRVIVDTKIVAGAPARLLAA-GIgDALATWFEARACsrsgatTMAGGQCTQAALTLAELCFNTL---------IE 212
Cdd:cd08189 163 PKliPDAAVLDPELTLGLPPAITAAtGM-DALTHAVEAYIS------RSATKETDEYALEAVKLIFENLpkayedgsdLE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 213 EGEKAMLAAeqhvvtpalervieantYLSGVGFESGGLAAAHAI-HN--GLTAIPdaHHY-----------YHGEKVA-- 276
Cdd:cd08189 236 ARENMLLAS-----------------YYAGLAFTRAYVGYVHAIaHQlgGLYGVP--HGLanavvlphvleFYGPAAEkr 296
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 949719653 277 ---FGTLTQLVLENAPVDE-----IETVAALCHSVGLPITLAQLDiKQDIqAKM--RIVAEA 328
Cdd:cd08189 297 laeLADAAGLGDSGESDSEkaeafIAAIRELNRRMGIPTTLEELK-EEDI-PEIakRALKEA 356
|
|
| Fe-ADH_KdnB-like |
cd08184 |
Iron-containing alcohol dehydrogenase similar to Shewanella oneidensis KdnB required for Kdo8N ... |
8-161 |
2.28e-05 |
|
Iron-containing alcohol dehydrogenase similar to Shewanella oneidensis KdnB required for Kdo8N biosynthesis; This family contains iron-containing alcohol dehydrogenase-like proteins, many of which have not been characterized. Their specific function is unknown. The protein structure represents a dehydroquinate synthase-like fold and belongs to the iron-containing alcohol dehydrogenase-like superfamily. It is distinct from other alcohol dehydrogenases which contain different protein domains. Alcohol dehydrogenase catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron or zinc ions. This family also includes Shewanella oneidensis KdnB which is required for biosynthesis of 8-Amino-3,8-dideoxy-D-manno-octulosonic acid (Kdo8N), a unique amino sugar that has thus far only been observed on the lipopolysaccharides of marine bacteria belonging to the genus Shewanella, and thought to be important for the integrity of the bacterial cell outer membrane. KdnB requires NAD(P) and zinc ion for activity.
Pssm-ID: 341463 [Multi-domain] Cd Length: 348 Bit Score: 45.72 E-value: 2.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 8 PGKYIQGADVITRLGSYLKPLAERwlivGDKFVLGFaqgaLEKSFQDAGLALEIAPFGG----------ECSQNEID--R 75
Cdd:cd08184 1 VPKYLFGRGSFDQLGELLAERRKS----NNDYVVFF----IDDVFKGKPLLDRLPLQNGdllifvdttdEPKTDQIDalR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 76 LRVVAE-KAQCAAVLGIGGGKTLDTAKALAHFM------------------GVPVAIAPTIASTDAPCSALSVIyTDAGe 136
Cdd:cd08184 73 AQIRAEnDKLPAAVVGIGGGSTMDIAKAVSNMLtnpgsaadyqgwdlvknpGIYKIGVPTLSGTGAEASRTAVL-TGPE- 150
|
170 180
....*....|....*....|....*....
gi 949719653 137 fdRYLLLpNNP----DRVIVDTKIVAGAP 161
Cdd:cd08184 151 --KKLGI-NSDytvfDQVILDPELIATVP 176
|
|
| HOT |
cd08190 |
Hydroxyacid-oxoacid transhydrogenase (HOT) involved in gamma-hydroxybutyrate metabolism; This ... |
14-173 |
1.09e-04 |
|
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: 43.69 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 14 GADVITRLGSYLKPL-AERWLIVGDKFV--LGFAQGALEkSFQDAGLALEIapfggecsqneIDRLRV------------ 78
Cdd:cd08190 7 GPGATRELGMDLKRLgAKKVLVVTDPGLakLGLVERVLE-SLEKAGIEVVV-----------YDGVRVeptdesfeeaie 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 79 VAEKAQCAAVLGIGGGKTLDTAKAL-------AHFM---------GVPVA------IA-PTIASTDAPCSALSVI-YTDA 134
Cdd:cd08190 75 FAKEGDFDAFVAVGGGSVIDTAKAAnlyathpGDFLdyvnapigkGKPVPgplkplIAiPTTAGTGSETTGVAIFdLEEL 154
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 949719653 135 ----GEFDRYLLlpnnPDRVIVDTKIVAGAPARLLAAGIGDAL 173
Cdd:cd08190 155 kvktGISSRYLR----PTLAIVDPLLTLTLPPRVTASSGFDVL 193
|
|
| PRK15454 |
PRK15454 |
ethanolamine utilization ethanol dehydrogenase EutG; |
48-273 |
6.87e-04 |
|
ethanolamine utilization ethanol dehydrogenase EutG;
Pssm-ID: 185351 [Multi-domain] Cd Length: 395 Bit Score: 41.17 E-value: 6.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 48 LEKSFQDAGLALEIAPfggeCSQNE---IDRLRVVAE--KAQCAAVLGIGGGKTLDTAKALAHFMG-------------- 108
Cdd:PRK15454 69 LTRSLAVKGIAMTLWP----CPVGEpciTDVCAAVAQlrESGCDGVIAFGGGSVLDAAKAVALLVTnpdstlaemsetsv 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 109 ----VPVAIAPTIASTDAPCSALSVIyTDAGEFDRYLLLPNN--PDRVIVDTKIVAGAPARLLAAGIGDALATWFEARAC 182
Cdd:PRK15454 145 lqprLPLIAIPTTAGTGSETTNVTVI-IDAVSGRKQVLAHASlmPDVAILDAALTEGVPSHVTAMTGIDALTHAIEAYSA 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 183 SRS---------GATTMAGGQCTQAAltlaelcfntlieeGEKAMLAAEQHVVTPALervieantyLSGVGFESGGLAAA 253
Cdd:PRK15454 224 LNAtpftdslaiGAIAMIGKSLPKAV--------------GYGHDLAARESMLLASC---------MAGMAFSSAGLGLC 280
|
250 260
....*....|....*....|
gi 949719653 254 HAIHNGLTAipdAHHYYHGE 273
Cdd:PRK15454 281 HAMAHQPGA---ALHIPHGL 297
|
|
| PPD-like |
cd08181 |
1,3-propanediol dehydrogenase-like (PPD); This family contains proteins similar to 1, ... |
7-120 |
7.78e-04 |
|
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: 41.03 E-value: 7.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 7 SPGKYIQGADVITRLGSYLKPLAERWLIVGDK---FVLGfAQGALEKSFQDAGLALEIapFGG---ECSQNEIDRLRVVA 80
Cdd:cd08181 3 MPTKVYFGKNCVEKHADELAALGKKALIVTGKhsaKKNG-SLDDVTEALEENGIEYFI--FDEveeNPSIETVEKGAELA 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 949719653 81 EKAQCAAVLGIGGGKTLDTAKALAHFM-----------------GVPVAIAPTIAST 120
Cdd:cd08181 80 RKEGADFVIGIGGGSPLDAAKAIALLAankdgdedlfqngkynpPLPIVAIPTTAGT 136
|
|
| Fe-ADH-like |
cd17814 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
11-317 |
8.85e-03 |
|
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: 37.91 E-value: 8.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 11 YIQGADVITRLGSYLKPL-AERWLIVGDKFVL--GFAQgALEKSFQDAGLALEIapFGGEcSQN----EIDRLRVVAEKA 83
Cdd:cd17814 7 FIFGVGARKLAGRYAKNLgARKVLVVTDPGVIkaGWVD-EVLDSLEAEGLEYVV--FSDV-TPNprdfEVMEGAELYREE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 84 QCAAVLGIGGGKTLDTAKALA----------HFMGV--------PVAIAPTIASTDAPCSALSVIyTDAGEFDRYLLLPN 145
Cdd:cd17814 83 GCDGIVAVGGGSPIDCAKGIGivvsngghilDYEGVdkvrrplpPLICIPTTAGSSADVSQFAII-TDTERRVKMAIISK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 146 N--PDRVIVDTKIVAGAPARLLAAGIGDALATWFEARACSRSGATTMAggqctqAALTLAELCFNTL---------IEEG 214
Cdd:cd17814 162 TlvPDVSLIDPETLTTMDPELTACTGMDALTHAIEAYVSNASSPLTDL------HALEAIRLISENLpkavadpddLEAR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949719653 215 EKAMLAAEQhvvtpalervieantylSGVGFESGGLAAAHAI-HN--GLTAIPdahhyyHGE------------------ 273
Cdd:cd17814 236 EKMMLASLQ-----------------AGLAFSNASLGAVHAMaHSlgGLLDLP------HGEcnalllphvirfnfpaap 292
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 949719653 274 ------KVAFGT-LTQLVLENAPVDEIETVAALCHSVGLPITLAQLDIKQD 317
Cdd:cd17814 293 eryrkiAEAMGLdVDGLDDEEVAERLIEAIRDLREDLGIPETLSELGVDEE 343
|
|
| |
