|
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: 676.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 1 MDRIIQSPGKYIQGAGAIKRLGDYLKPLAERWLVVGDKFVLGFAEEMLRKSLADAGLAAEIAPFGGECSHNEINRLRDIA 80
Cdd:PRK09423 1 MDRIFISPSKYVQGKGALARLGEYLKPLGKRALVIADEFVLGIVGDRVEASLKEAGLTVVFEVFNGECSDNEIDRLVAIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 81 GNAKCTAVLGIGGGKTLDTAKALAHFMNVPVAIAPTIASTDAPCSALSVIYTDEGEFDSYLMLPRNPNMVIVDTQIVAGA 160
Cdd:PRK09423 81 EENGCDVVIGIGGGKTLDTAKAVADYLGVPVVIVPTIASTDAPTSALSVIYTEEGEFERYLFLPKNPDLVLVDTAIIAKA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 161 PARLLAAGIGDALATWFEARACSRSGATTMAGGKCTQAALALAELCYNTLLEEGEKAMLAAEQHVVTPALERVVEANTYL 240
Cdd:PRK09423 161 PARFLAAGIGDALATWFEARACSRSGGTTMAGGKPTLAALALAELCYETLLEDGLKAKLAVEAKVVTPALENVIEANTLL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 241 SGVGFESGGLAAAHAIHNGMTAIPDAHHYYHGEKVAFGTLTQLVLENAPVDEIETVAALCHSVGLPITLAQLDIKGDIPT 320
Cdd:PRK09423 241 SGLGFESGGLAAAHAIHNGLTALEDTHHLTHGEKVAFGTLTQLVLENRPKEEIEEVIDFCHAVGLPTTLADLGLKEDSDE 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 839824880 321 KMRLVAEAACAEGETIHNMPGGVDSDQVYAALLVADQYGQRFLQEW 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: 601.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 8 PGKYIQGAGAIKRLGDYLKPLAERWLVVGDKFVLGFAEEMLRKSLADAGLAAEIAPFGGECSHNEINRLRDIAGNAKCTA 87
Cdd:cd08170 1 PSRYVQGPGALDRLGEYLAPLGKKALVIADPFVLDLVGERLEESLEKAGLEVVFEVFGGECSREEIERLAAIARANGADV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 88 VLGIGGGKTLDTAKALAHFMNVPVAIAPTIASTDAPCSALSVIYTDEGEFDSYLMLPRNPNMVIVDTQIVAGAPARLLAA 167
Cdd:cd08170 81 VIGIGGGKTIDTAKAVADYLGLPVVIVPTIASTDAPCSALSVIYTEDGEFDEYLFLPRNPDLVLVDTEIIAKAPVRFLVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 168 GIGDALATWFEARACSRSGATTMAGGKCTQAALALAELCYNTLLEEGEKAMLAAEQHVVTPALERVVEANTYLSGVGFES 247
Cdd:cd08170 161 GMGDALATYFEARACARSGAPNMAGGRPTLAALALAELCYDTLLEYGVAAKAAVEAGVVTPALEAVIEANTLLSGLGFES 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 248 GGLAAAHAIHNGMTAIPDAHHYYHGEKVAFGTLTQLVLENAPVDEIETVAALCHSVGLPITLAQLDIKGDIPTKMRLVAE 327
Cdd:cd08170 241 GGLAAAHAIHNGLTALPETHHLLHGEKVAFGTLVQLVLEGRPDEEIEEVIRFCRSVGLPVTLADLGLEDVTDEELRKVAE 320
|
330 340 350
....*....|....*....|....*....|.
gi 839824880 328 AACAEGETIHNMPGGVDSDQVYAALLVADQY 358
Cdd:cd08170 321 AACAPGETIHNMPFPVTPEDVVDAILAADAL 351
|
|
| GldA |
COG0371 |
Glycerol dehydrogenase or related enzyme, iron-containing ADH family [Energy production and ... |
3-355 |
3.53e-177 |
|
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: 495.84 E-value: 3.53e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 3 RIIQSPGKYIQGAGAIKRLGDYLKPLAERWLVVGDKFVLGFAEEMLRKSLADAGLAAEIAPFGGECSHNEINRLRDIAGN 82
Cdd:COG0371 1 RVIILPRRYVQGEGALDELGEYLADLGKRALIITGPTALKAAGDRLEESLEDAGIEVEVEVFGGECSEEEIERLAEEAKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 83 AKCTAVLGIGGGKTLDTAKALAHFMNVPVAIAPTIASTDAPCSALSVIYTDEGEFDSYLMLPRNPNMVIVDTQIVAGAPA 162
Cdd:COG0371 81 QGADVIIGVGGGKALDTAKAVAYRLGLPVVSVPTIASTDAPASPLSVIYTEDGAFDGYSFLAKNPDLVLVDTDIIAKAPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 163 RLLAAGIGDALATWFEARACSRSGAtTMAGGKCTQAALALAELCYNTLLEEGEKAMLAAEQHVVTPALERVVEANTYLSG 242
Cdd:COG0371 161 RLLAAGIGDALAKWYEARDWSLAHR-DLAGEYYTEAAVALARLCAETLLEYGEAAIKAVEAGVVTPALERVVEANLLLSG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 243 VGF----ESGGLAAAHAIHNGMTAIPDAHHYYHGEKVAFGTLTQLVLENAPvDEIETVAALCHSVGLPITLAQLDIKGDI 318
Cdd:COG0371 240 LAMgigsSRPGSGAAHAIHNGLTALPETHHALHGEKVAFGTLVQLVLEGRP-EEIEELLDFLRSVGLPTTLADLGLDDET 318
|
330 340 350
....*....|....*....|....*....|....*..
gi 839824880 319 PTKMRLVAEAACAEGETIHNMPGGVDSDQVYAALLVA 355
Cdd:COG0371 319 EEELLTVAEAARPERYTILNLPFEVTPEAVEAAILAT 355
|
|
| GlyDH-like |
cd08550 |
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins. ... |
8-353 |
4.74e-145 |
|
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: 414.24 E-value: 4.74e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 8 PGKYIQGAGAIKRLGDYLKPLAERWLVVGDKFVLGFAEEMLRKSLADAGLAAEIAPFGGECSHNEINRLRDIAGNAKCTA 87
Cdd:cd08550 1 PGRYIQEPGILAKAGEYIAPLGKKALIIGGKTALEAVGEKLEKSLEEAGIDYEVEVFGGECTEENIERLAEKAKEEGADV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 88 VLGIGGGKTLDTAKALAHFMNVPVAIAPTIASTDAPCSALSVIYTDEGEFDSYLMLPRNPNMVIVDTQIVAGAPARLLAA 167
Cdd:cd08550 81 IIGIGGGKVLDTAKAVADRLGLPVVTVPTIAATCAAWSALSVLYDEEGEFLGYSLLKRSPDLVLVDTDIIAAAPVRYLAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 168 GIGDALATWFEARACSRSGATTMAggkcTQAALALAELCYNTLLEEGEKAMLAAEQHVVTPALERVVEANTYLSGVGFES 247
Cdd:cd08550 161 GIGDTLAKWYEARPSSRGGPDDLA----LQAAVQLAKLAYDLLLEYGVQAVEDVRQGKVTPALEDVVDAIILLAGLVGSL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 248 GG----LAAAHAIHNGMTAIPDAHHYYHGEKVAFGTLTQLVLENAPVDEIETVAALCHSVGLPITLAQLDIKgDIPTKMR 323
Cdd:cd08550 237 GGggcrTAAAHAIHNGLTKLPETHGTLHGEKVAFGLLVQLALEGRSEEEIEELIEFLRRLGLPVTLEDLGLE-LTEEELR 315
|
330 340 350
....*....|....*....|....*....|
gi 839824880 324 LVAEAACAEGETIHNMPGGVDSDQVYAALL 353
Cdd:cd08550 316 KIAEYACDPPDMAHMLPFPVTPEMLAEAIL 345
|
|
| GlyDH-like |
cd08172 |
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins ... |
8-352 |
4.06e-111 |
|
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: 327.94 E-value: 4.06e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 8 PGKYIQGAGAIKRLGDYLKPL-AERWLVVGDKFVLGFAEEMLRKSLADAglaAEIAPFGGECSHNEINRLRDIAGNAKCT 86
Cdd:cd08172 1 PQEYICEEGALKELPELLSEFgIKRPLIIHGEKSWQAAKPYLPKLFEIE---YPVLRYDGECSYEEIDRLAEEAKEHQAD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 87 AVLGIGGGKTLDTAKALAHFMNVPVAIAPTIASTDAPCSALSVIYTDEGEFDSYLMLPRNPNMVIVDTQIVAGAPARLLA 166
Cdd:cd08172 78 VIIGIGGGKVLDTAKAVADKLNIPLILIPTLASNCAAWTPLSVIYDEDGEFIGYDYFPRSAYLVLVDPRLLLDSPKDYFV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 167 AGIGDALATWFEARACSRSGATTMAggkCTQAALALAELCYNTLLEEGEKAMLAAEQHVVTPALERVVEANTYLSGV--G 244
Cdd:cd08172 158 AGIGDTLAKWYEADAILRQLEELPA---FLQLARQAAKLCRDILLKDSEQALADLEAGKLTPAFIKVVETIIALAGMvgG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 245 F--ESGGLAAAHAIHNGMTAIPDAHHYYHGEKVAFGTLTQLVLENApVDEIETVAALCHSVGLPITLAQLDIKGDIPTKM 322
Cdd:cd08172 235 FgdEYGRSAGAHAIHNGLTKLPETHHFLHGEKVAYGILVQLALEGK-WDEIKKLLPFYRRLGLPTSLADLGLTDDTEEAL 313
|
330 340 350
....*....|....*....|....*....|
gi 839824880 323 RLVAEAACAEGETIHNMPGGVDSDQVYAAL 352
Cdd:cd08172 314 QKIAAFAASPEESIHLLPPDVTAEEVLQAI 343
|
|
| GlyDH-like |
cd08171 |
Glycerol dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins ... |
14-353 |
2.79e-76 |
|
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: 238.96 E-value: 2.79e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 14 GAGAIKRLGDYLKPLAERWLVVGDKFVLGFAEEMLRKSLADAGLaaEIA---PFGGECSHNEINRLRDIAGNAKCTAVLG 90
Cdd:cd08171 7 GEDAYDAIPKICSPYGKKVVVIGGKKALAAAKPKLRAALEGSGL--EITdfiWYGGEATYENVEKLKANPEVQEADMIFA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 91 IGGGKTLDTAKALAHFMNVPVAIAPTIASTDAPCSALSVIYTDEGEFDSYLMLPRNPNMVIVDTQIVAGAPARLLAAGIG 170
Cdd:cd08171 85 VGGGKAIDTVKVLADRLNKPVFTFPTIASNCAAVTAVSVMYNPDGSFKEYYFLKRPPVHTFIDTEIIAEAPEKYLWAGIG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 171 DALATWFEARACSRSGATTMAggkcTQAALALAELCYNTLLEEGEKAMLAAEQHVVTPALERVVEANTYLSG-----VGF 245
Cdd:cd08171 165 DTLAKYYEVEFSARGDELDHT----NALGVAISKMCSEPLLKYGVQALEDCRANKVSDALEQVVLDIIVTTGlvsnlVEP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 246 E-SGGLaaAHAIHNGMTAIPDA-HHYYHGEKVAFGTLTQLVLENApVDEIETVAALCHSVGLPITLAQLDIKGDiptKMR 323
Cdd:cd08171 241 DyNSSL--AHALYYGLTTLPQIeEEHLHGEVVSYGVLVLLTVDGQ-FEELEKVYAFNKSIGLPTCLADLGLTVE---DLE 314
|
330 340 350
....*....|....*....|....*....|
gi 839824880 324 LVAEAAcAEGETIHNMPGGVDSDQVYAALL 353
Cdd:cd08171 315 KVLDKA-LKTKDLRHSPYPITKEMFEEAIK 343
|
|
| Fe-ADH |
pfam00465 |
Iron-containing alcohol dehydrogenase; |
8-348 |
2.63e-66 |
|
Iron-containing alcohol dehydrogenase;
Pssm-ID: 425696 [Multi-domain] Cd Length: 362 Bit Score: 213.62 E-value: 2.63e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 8 PGKYIQGAGAIKRLGDYLKPLAERWLVVGDKFVLGF-AEEMLRKSLADAGLAAEIAP-FGGECSHNEINRLRDIAGNAKC 85
Cdd:pfam00465 1 PTRIVFGAGALAELGEELKRLGARALIVTDPGSLKSgLLDKVLASLEEAGIEVVVFDgVEPEPTLEEVDEAAALAREAGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 86 TAVLGIGGGKTLDTAKALAHFMN------------------VPVAIAPTIASTDAPCSALSVIY-TDEGEFDSYLMLPRN 146
Cdd:pfam00465 81 DVIIAVGGGSVIDTAKAIALLLTnpgdvwdylggkpltkpaLPLIAIPTTAGTGSEVTPLAVITdTETGEKLGIFSPKLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 147 PNMVIVDTQIVAGAPARLLAAGIGDALATWFEARACSRSGATTMAggkCTQAALALAELCYNTLLEEGEKAmlaaeqhvv 226
Cdd:pfam00465 161 PDLAILDPELTLTLPPRLTAATGMDALAHAVEAYVSKGANPLTDA---LALEAIRLIAENLPRAVADGEDL--------- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 227 tPALERVVEANTyLSGVGFESGGLAAAHAIHNGMTAIPDAHH-YYHGEKVAFGT----------LTQLVL-------ENA 288
Cdd:pfam00465 229 -EARENMLLAST-LAGLAFSNAGLGAAHALAHALGGRYGIPHgLANAILLPYVLrfnapaapekLAQLARalgedsdEEA 306
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 839824880 289 PVDEIETVAALCHSVGLPITLAQLDI-KGDIPTkmrlVAEAACAEGeTIHNMPGGVDSDQV 348
Cdd:pfam00465 307 AEEAIEALRELLRELGLPTTLSELGVtEEDLDA----LAEAALRDR-SLANNPRPLTAEDI 362
|
|
| PRK10586 |
PRK10586 |
putative oxidoreductase; Provisional |
3-360 |
6.58e-55 |
|
putative oxidoreductase; Provisional
Pssm-ID: 182570 Cd Length: 362 Bit Score: 184.16 E-value: 6.58e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 3 RIIQSPGKYIQGAGAIKRLGDYLKPLA-ERWLVVGDKFVLGFAEEMLRKSLADAGlaAEIAPFGGECSHNEINRLRDIAG 81
Cdd:PRK10586 7 RVVVGPANYFSHPGSIDHLHDFFTDEQlSRAVWIYGERAIAAAQPYLPPAFELPG--AKHILFRGHCSESDVAQLAAASG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 82 NAkCTAVLGIGGGKTLDTAKALAHFMNVPVAIAPTIASTDAPCSALSVIYTDEGEFDSYLMLPRNPNMVIVDTQIVAGAP 161
Cdd:PRK10586 85 DD-RQVVIGVGGGALLDTAKALARRLGLPFVAIPTIAATCAAWTPLSVWYNDAGQALHFEIFDDANFLVLVEPRIILNAP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 162 ARLLAAGIGDALATWFEARACSRSGAT---TMAGGkcTQAALALAelcyNTLLEEGEKAMLAAEQHVVTPALERVVEAnt 238
Cdd:PRK10586 164 QEYLLAGIGDTLAKWYEAVVLAPQPETlplTVRLG--INNALAIR----DVLLNSSEQALADQQNGQLTQDFCDVVDA-- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 239 YLSGVGFeSGGL-------AAAHAIHNGMTAIPDAHHYYHGEKVAFGTLTQLVLenapVDEIETVAALC---HSVGLPIT 308
Cdd:PRK10586 236 IIAGGGM-VGGLgerytrvAAAHAVHNGLTVLPQTEKFLHGTKVAYGILVQSAL----LGQDDVLAQLIgayQRFHLPTT 310
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 839824880 309 LAQLDIKGDIPTKMRLVAEAACAEGETIHNMPGGVDSDQVYAALLVADQYGQ 360
Cdd:PRK10586 311 LAELDVDINNQAEIDRVIAHTLRPVESIHYLPVTLTPDTLRAAFEKVESFKA 362
|
|
| DHQ_Fe-ADH |
cd07766 |
Dehydroquinate synthase-like (DHQ-like) and iron-containing alcohol dehydrogenases (Fe-ADH); ... |
8-330 |
2.82e-54 |
|
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: 179.87 E-value: 2.82e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 8 PGKYIQGAGAIKRLGDYLKPLAERWLVVGDKFVLGFAEEMLRKSLaDAGLAAEIAPF-GGECSHNEINRLRDIAGNAKCT 86
Cdd:cd07766 1 PTRIVFGEGAIAKLGEIKRRGFDRALVVSDEGVVKGVGEKVADSL-KKGLAVAIFDFvGENPTFEEVKNAVERARAAEAD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 87 AVLGIGGGKTLDTAKALAHFMN--VPVAIAPTIASTDAPCSALSVIYTDEGEFdSYLMLPRNPNMVIVDTQIVAGAPARL 164
Cdd:cd07766 80 AVIAVGGGSTLDTAKAVAALLNrgIPFIIVPTTASTDSEVSPKSVITDKGGKN-KQVGPHYNPDVVFVDTDITKGLPPRQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 165 LAAGIGDALATWFEaracsrsgattmaggkctqaalalaelcyntlleegekamlaaeqhvvtpaLERVVEANTYLSGVG 244
Cdd:cd07766 159 VASGGVDALAHAVE---------------------------------------------------LEKVVEAATLAGMGL 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 245 FESGGLAAAHAIHNGMTAipdAHHYYHGEKVAFGTLTQLVLENAPVDE----IETVAALCHSVGLPITLAQLDIKG-DIP 319
Cdd:cd07766 188 FESPGLGLAHAIGHALTA---FEGIPHGEAVAVGLPYVLKVANDMNPEpeaaIEAVFKFLEDLGLPTHLADLGVSKeDIP 264
|
330
....*....|.
gi 839824880 320 TkmrlVAEAAC 330
Cdd:cd07766 265 K----LAEKAL 271
|
|
| G1PDH-like |
cd08174 |
Glycerol-1-phosphate dehydrogenase-like; These glycerol-1-phosphate dehydrogenase-like ... |
14-317 |
1.06e-26 |
|
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: 108.38 E-value: 1.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 14 GAGAIKRLGDYLKPL---AERWLVVGDKFVLGFAEEMLRKSLADAGLAAEIapfgGECSHNEINRLRDIAGNAKCT-AVL 89
Cdd:cd08174 7 EEGALEHLGKYLADRnqgFGKVAIVTGEGIDELLGEDILESLEEAGEIVTV----EENTDNSAEELAEKAFSLPKVdAIV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 90 GIGGGKTLDTAKALAHFMNVPVAIAPTIASTDAPCSALSVIYTDeGEFDSylmLP-RNPNMVIVDTQIVAGAPARLLAAG 168
Cdd:cd08174 83 GIGGGKVLDVAKYAAFLSKLPFISVPTSLSNDGIASPVAVLKVD-GKRKS---LGaKMPYGVIVDLDVIKSAPRRLILAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 169 IGD------ALATW-FEARAcsrsGATTMAGgkctqAALALAELCYNTLLEEGEKAMLAAEqhvvtpALERVVEANTyLS 241
Cdd:cd08174 159 IGDlisnitALYDWkLAEEK----GGEPVDD-----FAYLLSRTAADSLLNTPGKDIKDDE------FLKELAESLV-LS 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 242 GVGFE--------SGglaAAHAI-HngmtAIpDAHH---YYHGEKVAFGTLTQLVLENAPVDEIETVAALChsvGLPITL 309
Cdd:cd08174 223 GIAMEiagssrpaSG---SEHLIsH----AL-DKLFpgpALHGIQVGLGTYFMSFLQGQRYEEIRDVLKRT---GFPLNP 291
|
....*...
gi 839824880 310 AQLDIKGD 317
Cdd:cd08174 292 SDLGLTKE 299
|
|
| Fe-ADH_2 |
pfam13685 |
Iron-containing alcohol dehydrogenase; |
14-276 |
1.26e-24 |
|
Iron-containing alcohol dehydrogenase;
Pssm-ID: 404557 [Multi-domain] Cd Length: 251 Bit Score: 100.84 E-value: 1.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 14 GAGAIKRLGDYLKPLA-ERWLVVGDKFVLGFAEEMLRKSLADAGLAAEIAPF-GGECSHNEINRLRDIAGNAKCTAVLGI 91
Cdd:pfam13685 3 GPGALGRLGEYLAELGfRRVALVADANTYAAAGRKVAESLKRAGIEVETRLEvAGNADMETAEKLVGALRERDADAVVGV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 92 GGGKTLDTAKALAHFMNVPVAIAPTIASTDAPCSALSVIYTDeGEFDSylmLPRN-PNMVIVDTQIVAGAPARLLAAGIG 170
Cdd:pfam13685 83 GGGTVIDLAKYAAFKLGKPFISVPTAASNDGFASPGASLTVD-GKKRS---IPAAaPFGVIADTDVIAAAPRRLLASGVG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 171 DALATWfEARACSRSGATTMAGGKCTQAALALAELCYNTLLEEGEKamlaaeqhvvTPALERVVEANTyLSGVGFESGGL 250
Cdd:pfam13685 159 DLLAKI-TAVADWELAHAEEVAAPLALLSAAMVMNFADRPLRDPGD----------IEALAELLSALA-MGGAGSSRPAS 226
|
250 260
....*....|....*....|....*.
gi 839824880 251 AAAHAIHNGMTAIPDAHHyYHGEKVA 276
Cdd:pfam13685 227 GSEHLISHALDMIAPKQA-LHGEQVG 251
|
|
| Gro1PDH |
cd08173 |
Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) catalyzes the reversible conversion between ... |
14-174 |
7.01e-24 |
|
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: 100.71 E-value: 7.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 14 GAGAIKRLGDYLKPLAE--RWLVVGDKFVLGFAEEMLRKSLADAGLAAEIAPFGGECSHNEINRLRDIAGNAKCTAVLGI 91
Cdd:cd08173 8 GHGAINKIGEVLKKLLLgkRALIITGPNTYKIAGKRVEDLLESSGVEVVIVDIATIEEAAEVEKVKKLIKESKADFIIGV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 92 GGGKTLDTAKALAHFMNVPVAIAPTIASTDAPCSALSVIYTDEGefdSYLMLPRNPNMVIVDTQIVAGAPARLLAAGIGD 171
Cdd:cd08173 88 GGGKVIDVAKYAAYKLNLPFISIPTSASHDGIASPFASIKGGDK---PYSIKAKAPIAIIADTEIISKAPKRLLAAGCGD 164
|
...
gi 839824880 172 ALA 174
Cdd:cd08173 165 LIS 167
|
|
| Fe-ADH |
cd08551 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains large ... |
8-340 |
3.48e-22 |
|
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: 96.36 E-value: 3.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 8 PGKYIQGAGAIKRLGDYLKPL-AERWLVVGDKFV--LGFAEEMLrKSLADAGLAAEIapFGG---ECSHNEINRLRDIAG 81
Cdd:cd08551 1 PTRIVFGAGALARLGEELKALgGKKVLLVTDPGLvkAGLLDKVL-ESLKAAGIEVEV--FDDvepNPTVETVEAAAELAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 82 NAKCTAVLGIGGGKTLDTAKALAHFMN------------------VPVAIAPTIASTDAPCSALSVIyTDEGE-----FD 138
Cdd:cd08551 78 EEGADLVIAVGGGSVLDTAKAIAVLATnggsirdyegigkvpkpgLPLIAIPTTAGTGSEVTPNAVI-TDPETgrkmgIV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 139 SYLMLPRnpnMVIVDTQIVAGAPARLLAA-GIgDALATWFEArACSRsGATTMaggkcTQA-ALALAELCYNTL------ 210
Cdd:cd08551 157 SPYLLPD---VAILDPELTLSLPPSVTAAtGM-DALTHAIEA-YTSK-KANPI-----SDAlALEAIRLIGKNLrravad 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 211 ---LEEGEKAMLAAeqhvvtpalervveantYLSGVGFESGGLAAAHAIHNGMTAIpdaHHYYHGekVAFGTLTQLVLE- 286
Cdd:cd08551 226 gsdLEAREAMLLAS-----------------LLAGIAFGNAGLGAVHALAYPLGGR---YHIPHG--VANAILLPYVMEf 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 287 NAPVDE--------------------------IETVAALCHSVGLPITLAQLDIK-GDIPTkmrlVAEAACAEGETIHNM 339
Cdd:cd08551 284 NLPACPekyaeiaealgedveglsdeeaaeaaVEAVRELLRDLGIPTSLSELGVTeEDIPE----LAEDAMKSGRLLSNN 359
|
.
gi 839824880 340 P 340
Cdd:cd08551 360 P 360
|
|
| EutG |
COG1454 |
Alcohol dehydrogenase, class IV [Energy production and conversion]; |
1-355 |
1.52e-21 |
|
Alcohol dehydrogenase, class IV [Energy production and conversion];
Pssm-ID: 441063 [Multi-domain] Cd Length: 381 Bit Score: 94.42 E-value: 1.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 1 MDRIIQSPGKYIQGAGAIKRLGDYLKPL-AERWLVVGDKFV--LGFAEEmLRKSLADAGLAAEIapFGG---ECSHNEIN 74
Cdd:COG1454 1 MMFTFRLPTRIVFGAGALAELGEELKRLgAKRALIVTDPGLakLGLLDR-VLDALEAAGIEVVV--FDDvepNPTVETVE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 75 RLRDIAGNAKCTAVLGIGGGKTLDTAKALAHFMNVP-------------------VAIaPTIASTDAPCSALSVIYTDEG 135
Cdd:COG1454 78 AGAAAAREFGADVVIALGGGSAIDAAKAIALLATNPgdledylgikkvpgpplplIAI-PTTAGTGSEVTPFAVITDPET 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 136 E----FDSYLMLPRnpnMVIVDTQIVAGAPARLLAA-GIgDALATWFEArACSRsGATTMAggkctqAALALA--ELCYN 208
Cdd:COG1454 157 GvkkgIADPELLPD---VAILDPELTLTLPPSLTAAtGM-DALTHAIEA-YVSK-GANPLT------DALALEaiRLIAR 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 209 TL---------LEEGEKAMLAAeqhvvtpalervveantYLSGVGFESGGLAAAHAIHNGMTAIPDAHH----------- 268
Cdd:COG1454 225 NLpravadgddLEAREKMALAS-----------------LLAGMAFANAGLGAVHALAHPLGGLFHVPHglanaillphv 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 269 --YY---HGEKVA-----FGTLTQLVLENAPVDEIETVAALCHSVGLPITLAQLDIK-GDIPTkmrlVAEAACAEGETIH 337
Cdd:COG1454 288 lrFNapaAPERYAeiaraLGLDVGLSDEEAAEALIEAIRELLRDLGIPTRLSELGVTeEDLPE----LAELALADRCLAN 363
|
410
....*....|....*...
gi 839824880 338 NmPGGVDSDQVYAALLVA 355
Cdd:COG1454 364 N-PRPLTEEDIEAILRAA 380
|
|
| egsA |
PRK00843 |
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed |
3-171 |
2.35e-21 |
|
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed
Pssm-ID: 179139 Cd Length: 350 Bit Score: 93.80 E-value: 2.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 3 RIIQSPGKYIQGAGAIKRLGDYLKPLA--ERWLVVGDKFVLGFAEEMLRKSLADAGLAAEIapFGGECSHNEINRLRDIA 80
Cdd:PRK00843 6 HWIQLPRDVVVGHGVLDDIGDVCSDLKltGRALIVTGPTTKKIAGDRVEENLEDAGDVEVV--IVDEATMEEVEKVEEKA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 81 GNAKCTAVLGIGGGKTLDTAKALAHFMNVPVAIAPTIASTDAPCSALSVIYTDEGefdSYLMLPRNPNMVIVDTQIVAGA 160
Cdd:PRK00843 84 KDVNAGFLIGVGGGKVIDVAKLAAYRLGIPFISVPTAASHDGIASPRASIKGGGK---PVSVKAKPPLAVIADTEIIAKA 160
|
170
....*....|.
gi 839824880 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 |
1.97e-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: 84.92 E-value: 1.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 8 PGKYIQGAGAIKRLGDYLK-PLAERWLVVGDKFVLGFAEEMLRKSLADAglaAEIAPFggecshNEINRLRD-IAGNAKC 85
Cdd:cd08549 1 PRYTIVGDGAINKIEEILKkLNLKRVLIITGKNTKAKYCRFFYDQLKTV---CDIVYY------DNIDNLEDeLKKYTFY 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 86 TAVLGIGGGKTLDTAKALAHFMNVPVAIAPTIASTD---APCSALSViytdEGEFdsYLMLPRNPNMVIVDTQIVAGAPA 162
Cdd:cd08549 72 DCVIGIGGGRSIDTGKYLAYKLKIPFISVPTSASNDgiaSPIVSLRI----PGVK--KTFMADAPIAIIADTEIIKKSPR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 163 RLLAAGIGD------ALATW-FEARacsrsgattMAGGKCTQAALALAELCYNTLLEEGEKAMLAAEQHVVtpalerVVE 235
Cdd:cd08549 146 RLLSAGIGDlvsnitAVLDWkLAHK---------EKGEKYSEFAAILSKTSAKELVSYVLKASDLEEYHRV------LVK 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 236 ANTYlSGVGFESGGLA--AAHAIHNGMTAIPDAHHYY------HGEKVAFGTLTQLVL------ENAPVDE-IETVAAlc 300
Cdd:cd08549 211 ALVG-SGIAMAIAGSSrpASGSEHLFSHALDKLKEEYlninvlHGEQVGVGTIIMSYLhekenkKLSGLHErIKMILK-- 287
|
330
....*....|....*...
gi 839824880 301 hSVGLPITLAQLDIKGDI 318
Cdd:cd08549 288 -KVGAPTTAKQLGIDEDL 304
|
|
| Fe-ADH-like |
cd14863 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
14-300 |
2.00e-18 |
|
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: 85.66 E-value: 2.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 14 GAGAIKRLGDYLKPL-AERWLVVGDKFV--LGFAEEMlRKSLADAGLAA----EIAPfggECSHNEINRLRDIAGNAKCT 86
Cdd:cd14863 11 GAGAVEQIGELLKELgCKKVLLVTDKGLkkAGIVDKI-IDLLEEAGIEVvvfdDVEP---DPPDEIVDEAAEIAREEGAD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 87 AVLGIGGGKTLDTAKALA-----------HFMNVPVAIA--------PTIASTDAPCSALSVIY-TDEGEFDSYLMLPRN 146
Cdd:cd14863 87 GVIGIGGGSVLDTAKAIAvlltnpgpiidYALAGPPVPKpgipliaiPTTAGTGSEVTPIAVITdEENGVKKSLLGPFLV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 147 PNMVIVDTQIVAGAPARLLAA-GIgDALATWFEARACSRSGATTMAggKCTQAalalAELCYNTL---------LEEGEK 216
Cdd:cd14863 167 PDLAILDPELTVGLPPSLTAAtGM-DALSHAIEAYTSKLANPMTDA--LALQA----IRLIVKNLpravkdgdnLEAREN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 217 AMLAAeqhvvtpalervveantYLSGVGFESGGLAAAHAI-HngmtAIPDAHHYYHGEKVAFGTLTqlVLE-NAPV--DE 292
Cdd:cd14863 240 MLLAS-----------------NLAGIAFNNAGTHIGHAIaH----ALGALYHIPHGLACALALPV--VLEfNAEAypEK 296
|
....*...
gi 839824880 293 IETVAALC 300
Cdd:cd14863 297 VKKIAKAL 304
|
|
| Fe-ADH-like |
cd14864 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
8-355 |
9.95e-18 |
|
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: 83.50 E-value: 9.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 8 PGKYIQGAGAIKRLGDYLKPLAERWLVVGDKFVLGFAE-EMLRKSLADAGLaaEIAPF---GGECSHNEINRLRDIAGNA 83
Cdd:cd14864 4 PPNIVFGADSLERIGEEVKEYGSRFLLITDPVLKESGLaDKIVSSLEKAGI--SVIVFdeiPASATSDTIDEAAELARKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 84 KCTAVLGIGGGKTLDTAKALA----------HFMN--------VPVAIAPTIASTDAPCSAlSVIYTDEGEFDSYLMLPR 145
Cdd:cd14864 82 GADGIIAVGGGKVLDTAKAVAilanndggayDFLEgakpkkkpLPLIAVPTTPRSGFEFSD-RFPVVDSRSREVKLLKAQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 146 N--PNMVIVDTQIVAGAPARLLAAGIGDALATWFEARACSRSG-ATTMAGGKctqaALALAelcyntlleeGEKAMLAAE 222
Cdd:cd14864 161 PglPKAVIVDPNLMASLTGNQTAAMALAALALAVEAYLSKKSNfFSDALALK----AIELV----------SENLDGALA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 223 QHVVTPALERVVEANtYLSGVGFESGGL----AAAHAIhNGMTAIPDAH-------HY--YHGEKVAFGTLTQLVLENAP 289
Cdd:cd14864 227 DPKNTPAEELLAQAG-CLAGLAASSSSPglatALALAV-NSRYKVSKSLvasillpHVieYAATSAPDKYAKIARALGED 304
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 839824880 290 VDEIETVAA----------LCHSVGLPITLAQLDIKGDIPTkmrlVAEAACAEGEtIHNMPGGVDSDQVYAALLVA 355
Cdd:cd14864 305 VEGASPEEAaiaavegvrrLIAQLNLPTRLKDLDLASSLEQ----LAAIAEDAPK-LNGLPRSMSSDDIFDILKAA 375
|
|
| Fe-ADH-like |
cd08196 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
5-352 |
1.50e-17 |
|
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: 83.01 E-value: 1.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 5 IQSPGKYIQGAGAIKRLGDYLKPLA-ERWLVVGDKFvlgFAEEMLRKSLADAGLAAEIAPFGG---ECSHNEINRLRDIA 80
Cdd:cd08196 3 YYQPVKIIFGEGILKELPDIIKELGgKRGLLVTDPS---FIKSGLAKRIVESLKGRIVAVFSDvepNPTVENVDKCARLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 81 GNAKCTAVLGIGGGKTLDTAKALAHFMN-------------------VPVAIAPTIASTDAPCSALSVIYTDE----GEF 137
Cdd:cd08196 80 RENGADFVIAIGGGSVLDTAKAAACLAKtdgsiedylegkkkipkkgLPLIAIPTTAGTGSEVTPVAVLTDKEkgkkAPL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 138 DSYLMLprnPNMVIVDTQIVAGAPARLLAA-GIgDALATWFEArACSRSgattmAGGKCTQAALALAELCYNTLL---EE 213
Cdd:cd08196 160 VSPGFY---PDIAIVDPELTYSMPPKVTAStGI-DALCHAIEA-YWSIN-----HQPISDALALEAAKLVLENLEkayNN 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 214 GEKAmlaaeqhvvtPALERVVEANTyLSGVGFESGGLAAAHAIHNGMTAIpdaHHYYHGEKVAFgTLTQLVLENAPVDE- 292
Cdd:cd08196 230 PNDK----------EAREKMALASL-LAGLAFSQTRTTASHACSYPLTSH---FGIPHGEACAL-TLPSFIRLNAEALPg 294
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 839824880 293 -----------------IETVAALCHSVGLPITLAQLDIKgdiPTKMRLVAEAACAEgETIHNMPGGVDSDQVYAAL 352
Cdd:cd08196 295 rldelakqlgfkdaeelADKIEELKKRIGLRTRLSELGIT---EEDLEEIVEESFHP-NRANNNPVEVTKEDLEKLL 367
|
|
| BDH |
cd08187 |
Butanol dehydrogenase catalyzes the conversion of butyraldehyde to butanol with the cofactor ... |
4-337 |
2.64e-14 |
|
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: 73.24 E-value: 2.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 4 IIQSPGKYIQGAGAIKRLGDYLKPLAERWLVV-GDKFV--LGFAEEmLRKSLADAGLaaEIAPFGGECS---HNEINRLR 77
Cdd:cd08187 3 TFYNPTKIIFGKGAIEELGEEIKKYGKKVLLVyGGGSIkkNGLYDR-VVASLKEAGI--EVVEFGGVEPnprLETVREGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 78 DIAGNAKCTAVLGIGGGKTLDTAKALAH----------FMN--------VPVAIAPTIASTDAPCSALSVIyTDEGE--- 136
Cdd:cd08187 80 ELAREENVDFILAVGGGSVIDAAKAIAAgakydgdvwdFFTgkappekaLPVGTVLTLAATGSEMNGGAVI-TNEETkek 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 137 --FDSYLMLPRnpnMVIVDTQIVAGAPARLLAAGIGDALATWFEaracsrsgaTTMAGGKCTQAALALAELCYNTLLEEG 214
Cdd:cd08187 159 lgFGSPLLRPK---FSILDPELTYTLPKYQTAAGIVDIFSHVLE---------QYFTGTEDAPLQDRLAEGLLRTVIENG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 215 EKA-------------MLAAEQhvvtpalervveANTYLSGVGFESGglAAAHAIHNGMTAIPDAHH------------- 268
Cdd:cd08187 227 PKAlkdpddyearanlMWAATL------------ALNGLLGAGRGGD--WATHAIEHELSALYDITHgaglaivfpawmr 292
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 839824880 269 YYHGEKVA---------FGTLTQLVLENAPVDEIETVAALCHSVGLPITLAQLDIKGDIPTKMrlvAEAACAEGETIH 337
Cdd:cd08187 293 YVLKKKPErfaqfarrvFGIDPGGDDEETALEGIEALEEFFKSIGLPTTLSELGIDEEDIEEM---AEKAVRGGGLGG 367
|
|
| Fe-ADH-like |
cd08183 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
8-329 |
4.55e-14 |
|
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: 72.53 E-value: 4.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 8 PGKYIQGAGAIKRLGDYLKPLAERWLVV--GDKFVLGFAEEMLRkSLADAGLAAEIAPFGGECSHNEINRLRDIAGNAKC 85
Cdd:cd08183 1 PPRIVFGRGSLQELGELAAELGKRALLVtgRSSLRSGRLARLLE-ALEAAGIEVALFSVSGEPTVETVDAAVALAREAGC 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 86 TAVLGIGGGKTLDTAKALA----------HFMNV------------PVAIAPTIASTDAPCSALSVIYTDEGEFD----S 139
Cdd:cd08183 80 DVVIAIGGGSVIDAAKAIAalltnegsvlDYLEVvgkgrpltepplPFIAIPTTAGTGSEVTKNAVLSSPEHGVKvslrS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 140 YLMLPRnpnMVIVDTQIVAGAPARLLAAGIGDALATWFEARACSRSGATT----MAGgkCTQAALALAELCYN-TLLEEG 214
Cdd:cd08183 160 PSMLPD---VALVDPELTLSLPPEVTAASGLDALTQLIEPYVSRKANPLTdalaREG--LRLAARSLRRAYEDgEDLEAR 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 215 EKAMLAAeqhvvtpalervveantYLSGVGFESGGLAAAHAIHN---GMTAIP------------------------DAH 267
Cdd:cd08183 235 EDMALAS-----------------LLGGLALANAGLGAVHGLAGplgGMFGAPhgaicaallppvleanlralrerePDS 297
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 839824880 268 HYYHGEKVAFGTLTQLVLENAPvDEIETVAALCHSVGLPiTLAQLDIKG-DIPtkmRLVAEAA 329
Cdd:cd08183 298 PALARYRELAGILTGDPDAAAE-DGVEWLEELCEELGIP-RLSEYGLTEeDFP---EIVEKAR 355
|
|
| G1PDH |
cd08175 |
Glycerol-1-phosphate dehydrogenase (G1PDH) catalyzes the reversible reduction of ... |
14-314 |
7.85e-14 |
|
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: 71.77 E-value: 7.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 14 GAGAIKRLGDYLKPL--AERWLVVGDKFVLGFAEEMLRKSLADAGLAAEIAPFGGE-----CSHNEINRLRDIAGNAkcT 86
Cdd:cd08175 7 GEGALKKLPEYLKELfgGKKVLVVADENTYAAAGEEVEAALEEAGVTVCLLIFPGEgdliaDEAAVGKVLLELEKDT--D 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 87 AVLGIGGGkTL-DTAKALAHFMNVPVAIAPTIASTDAPCSALSVIyTDEGEFDSYLMLPrnPNMVIVDTQIVAGAPARLL 165
Cdd:cd08175 85 LIIAVGSG-TInDLTKYAAYKLGIPYISVPTAPSMDGYTSSGAPI-IVDGVKKTFPAHA--PKAIFADLDVLANAPQRMI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 166 AAGIGD------ALATWFEARAcsrsgattmAGGK--CTQAAlalaelcynTLLEEGEKAMLAAEQHVVT---PALERVV 234
Cdd:cd08175 161 AAGFGDllgkytALADWKLSHL---------LGGEyyCPEVA---------DLVQEALEKCLDNAEGIAArdpEAIEALM 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 235 EANTyLSGVGFE--------SGG---LaaAHAIHngMTAIpDAHHYY--HGEKVAFGTLTQL---VLENAPvdEIETVAA 298
Cdd:cd08175 223 EALI-LSGLAMQlvgnsrpaSGAehhL--SHYWE--MEFL-RLGKPPvlHGEKVGVGTLLIAalyILEQLP--PPEELRE 294
|
330
....*....|....*.
gi 839824880 299 LCHSVGLPITLAQLDI 314
Cdd:cd08175 295 LLRKAGAPTTPEDLGI 310
|
|
| Fe-ADH-like |
cd08191 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
7-355 |
5.38e-13 |
|
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: 69.56 E-value: 5.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 7 SPGKYIQGAGAIKRLGDYLKPLAERWLVVGDKFVL---GFAEemLRKSLADAGLAAEIapFGGECSHNEINRLRDIAGNA 83
Cdd:cd08191 3 SPSRLLFGPGARRALGRVAARLGSRVLIVTDPRLAstpLVAE--LLAALTAAGVAVEV--FDGGQPELPVSTVADAAAAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 84 ---KCTAVLGIGGGKTLDTAKA----LAH---------FMNVP------VAIaPTIASTDAPCSALSVIYTDEGEFDSYL 141
Cdd:cd08191 79 rafDPDVVIGLGGGSNMDLAKVvallLAHggdprdyygEDRVPgpvlplIAV-PTTAGTGSEVTPVAVLTDPARGMKVGV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 142 MLPR-NPNMVIVDTQIVAGAPARLLA-AGIgDALATWFEARACSRSGATtmaggkctqaALALAELCY--NTLLEE--GE 215
Cdd:cd08191 158 SSPYlRPAVAIVDPELTLTCPPGVTAdSGI-DALTHAIESYTARDFPPF----------PRLDPDPVYvgKNPLTDllAL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 216 KAMLAAEQHvvtpaLERVV------EANT------YLSGVGFESGGLAAAHAIHngmTAIPDAHHYYHGEKV-------- 275
Cdd:cd08191 227 EAIRLIGRH-----LPRAVrdgddlEARSgmalaaLLAGLAFGTAGTAAAHALQ---YPIGALTHTSHGVGNglllpyvm 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 276 ----------------AFGTLTQLVLENAPVDEIETVAALCHSVGLPITLAQLDIK-GDIPTkmrlVAEAACAEGETIHN 338
Cdd:cd08191 299 rfnrparaaelaeiarALGVTTAGTSEEAADRAIERVEELLARIGIPTTLADLGVTeADLPG----LAEKALSVTRLIAN 374
|
410
....*....|....*..
gi 839824880 339 MPGGVDSDQVYAALLVA 355
Cdd:cd08191 375 NPRPPTEEDLLRILRAA 391
|
|
| Fe-ADH-like |
cd08194 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
8-173 |
8.90e-12 |
|
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: 65.63 E-value: 8.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 8 PGKYIQGAGAIKRLGDYLKPL-AERWLVVGDKFV--LGFAEEmLRKSLADAGLAAEI-APFGGECSHNEINRLRDIAGNA 83
Cdd:cd08194 1 PRTIIIGGGALEELGEEAASLgGKRALIVTDKVMvkLGLVDK-VTQLLAEAGIAYAVfDDVVSEPTDEMVEEGLALYKEG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 84 KCTAVLGIGGGKTLDTAKA----------LAHFMN--------VPVAIAPTIASTDAPCSALSVIyTDEgEFDSYLMLPR 145
Cdd:cd08194 80 GCDFIVALGGGSPIDTAKAiavlatnggpIRDYMGprkvdkpgLPLIAIPTTAGTGSEVTRFTVI-TDT-ETDVKMLLKG 157
|
170 180 190
....*....|....*....|....*....|..
gi 839824880 146 ---NPNMVIVDTQIVAGAPARLLAA-GIgDAL 173
Cdd:cd08194 158 palLPAVAIVDPELTLSMPPRVTAAtGI-DAL 188
|
|
| HEPD |
cd08182 |
Hydroxyethylphosphoate dehydrogenase (HEPD) catalyzes the reduction of phosphonoacetaldehyde ... |
8-352 |
5.19e-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: 60.32 E-value: 5.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 8 PGKYIQGAGAIKRLGDYLKPL-AERWLVVGDKfvlGFAEEMLRKSLADA-GLAAEIAPFGGECSHNEINRLRDIA---GN 82
Cdd:cd08182 1 PVKIIFGPGALAELKDLLGGLgARRVLLVTGP---SAVRESGAADILDAlGGRIPVVVFSDFSPNPDLEDLERGIelfRE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 83 AKCTAVLGIGGGKTLDTAKALAHFMNVP---------------------VAIaPTIASTDAPCSALSVIY-TDEGE---F 137
Cdd:cd08182 78 SGPDVIIAVGGGSVIDTAKAIAALLGSPgenllllrtgekapeenalplIAI-PTTAGTGSEVTPFATIWdEAEGKkysL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 138 DSYLMLPRnpnMVIVDTQIVAGAPARLLAAGIGDALATWFEARACSRSGATTMAGGKctqAALALAELCYNTLLEEGEKA 217
Cdd:cd08182 157 AHPSLYPD---AAILDPELTLSLPLYLTASTGLDALSHAIESIWSVNANPESRAYAL---RAIRLILENLPLLLENLPNL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 218 mlaaeqhvvtPALERVVEAnTYLSGVGFESGGLAAAHAIHNGMTAipdAHHYYHGEKVAFgTLTQLVLENAPVDE----- 292
Cdd:cd08182 231 ----------EAREAMAEA-SLLAGLAISITKTTAAHAISYPLTS---RYGVPHGHACAL-TLPAVLRYNAGADDecddd 295
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 839824880 293 ------------------IETVAALCHSVGLPITLAQLDIKGDipTKMRLVAEAacAEGETIHNMPGGVDSDQVYAAL 352
Cdd:cd08182 296 prgreillalgasdpaeaAERLRALLESLGLPTRLSEYGVTAE--DLEALAASV--NTPERLKNNPVRLSEEDLLRLL 369
|
|
| Fe-ADH-like |
cd14861 |
Iron-containing alcohol dehydrogenases-like; This family contains proteins similar to ... |
14-329 |
9.96e-10 |
|
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: 59.45 E-value: 9.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 14 GAGAIKRLGDYLKPL-AERWLVVGDKFV--LGFAEEMLRkSLADAGLAAEIapFGGECSH---NEINRLRDIAGNAKCTA 87
Cdd:cd14861 9 GAGAIAELPEELKALgIRRPLLVTDPGLaaLGIVDRVLE-ALGAAGLSPAV--FSDVPPNpteADVEAGVAAYREGGCDG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 88 VLGIGGGKTLDTAKA----------LAHF-----------MNVPVAIA-PTIASTDAPCSALSVIYTDEGE-----FDSY 140
Cdd:cd14861 86 IIALGGGSAIDAAKAialmathpgpLWDYedgeggpaaitPAVPPLIAiPTTAGTGSEVGRAAVITDDDTGrkkiiFSPK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 141 LMlprnPNMVIVDTQIVAGAPARLLAA-GIgDALATWFEarACSRSGATTMAGGkctqAALALAELCYNTLleegEKAM- 218
Cdd:cd14861 166 LL----PKVAICDPELTLGLPPRLTAAtGM-DALTHCIE--AYLSPGFHPMADG----IALEGLRLISEWL----PRAVa 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 219 ----LAAEQHVVTPALErvveantylSGVGFESgGLAAAHAIHNGMTAIPDAHH--------------YYHGEKVAFGTL 280
Cdd:cd14861 231 dgsdLEARGEMMMAALM---------GAVAFQK-GLGAVHALAHALGALYGLHHgllnaillpyvlrfNRPAVEDKLARL 300
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 839824880 281 TQ-LVLENAPVDEIET-VAALCHSVGLPITLAQLDIK-GDIPtkmRLVAEAA 329
Cdd:cd14861 301 ARaLGLGLGGFDDFIAwVEDLNERLGLPATLSELGVTeDDLD---ELAELAL 349
|
|
| Fe-ADH-like |
cd14862 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
7-329 |
1.62e-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: 341484 [Multi-domain] Cd Length: 375 Bit Score: 58.78 E-value: 1.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 7 SPGKYIQGAGAIKRLGDYLKplaERWLVVGDKFV--LGFAEEMLrKSLADAGLAAEIapFGG---ECSHNEINRLRDIAG 81
Cdd:cd14862 5 SSPKIVFGEDALSHLEQLSG---KRALIVTDKVLvkLGLLKKVL-KRLLQAGFEVEV--FDEvepEPPLETVLKGAEAMR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 82 NAKCTAVLGIGGGKTLDTAKALAHFMNVP---------------------VAIaPTIASTDAPCSALSVIyTDEGEFDSY 140
Cdd:cd14862 79 EFEPDLIIALGGGSVMDAAKAAWVLYERPdldpedispldllglrkkaklIAI-PTTSGTGSEATWAIVL-TDTEEPRKI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 141 LMLPRN--PNMVIVDTQIVAGAPARLLAA-GIgDALATWFEARACSRSgaTTMAGGKCTQAalalAELCYNTLleegeka 217
Cdd:cd14862 157 AVANPElvPDVAILDPEFVLGMPPKLTAGtGL-DALAHAVEAYLSTWS--NDFSDALALKA----IELIFKYL------- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 218 MLAAEQHVVTPALERVVEANTyLSGVGFESGGLAAAHAIHNGMTAIPDAHH--------------YYHGEKVAFGTLTQL 283
Cdd:cd14862 223 PRAYKDGDDLEAREKMHNAAT-IAGLAFGNSQAGLAHALGHSLGAVFHVPHgiavglflpyviefYAKVTDERYDLLKLL 301
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 839824880 284 VLENAPVDE-----IETVAALCHSVGLPITLAQLDI-KGDIPTKMRLVAEAA 329
Cdd:cd14862 302 GIEARDEEEalkklVEAIRELYKEVGQPLSIKDLGIsEEEFEEKLDELVEYA 353
|
|
| Fe-ADH-like |
cd14865 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
6-355 |
2.49e-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: 58.32 E-value: 2.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 6 QSPGKYIQGAGAIKRLGDYLKPL-AERWLVVGDKFV--LGFA---EEMLRKSLADAGLAAEIAPfggECSHNEINRLRDI 79
Cdd:cd14865 4 FNPTKIVSGAGALENLPAELARLgARRPLIVTDKGLaaAGLLkkvEDALGDAIEIVGVFDDVPP---DSSVAVVNEAAAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 80 AGNAKCTAVLGIGGGKTLDTAKA-----------LAHFMN--------VPVAIAPTIASTDAPCSALSVIYTDEG----E 136
Cdd:cd14865 81 AREAGADGIIAVGGGSVIDTAKGvnillseggddLDDYGGanrltrplKPLIAIPTTAGTGSEVTLVAVIKDEEKkvklL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 137 F-DSYLMlprnPNMVIVDTQIVAGAPARLLAAGIGDALATWFEARACSRSGATTmaggkctqAALALA--ELCYNTLL-- 211
Cdd:cd14865 161 FvSPFLL----PDVAILDPRLTLSLPPKLTAATGMDALTHAIEAYTSLQKNPIS--------DALALQaiRLISENLPka 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 212 ------EEGEKAMLAAeqhvvtpalervveanTYLSGVGFESGGLAAAHAI-HngmtAIPDAHHYYHGekVAFGTLTQLV 284
Cdd:cd14865 229 vkngkdLEARLALAIA----------------ATMAGIAFSNSMVGLVHAIaH----AVGAVAGVPHG--LANSILLPHV 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 285 LE-NAPVDE----------------------------IETVAALCHSVGLPITLAQLDIKGDiptKMRLVAEAACAEGET 335
Cdd:cd14865 287 MRyNLDAAAeryaelalalaygvtpagrraeeaieaaIDLVRRLHELCGLPTRLRDVGVPEE---QLEAIAELALNDGAI 363
|
410 420
....*....|....*....|
gi 839824880 336 IHNmPGGVDSDQVYAALLVA 355
Cdd:cd14865 364 LFN-PREVDPEDILAILEAA 382
|
|
| HVD |
cd08193 |
5-hydroxyvalerate dehydrogenase (HVD) catalyzes the oxidation of 5-hydroxyvalerate to ... |
6-173 |
1.37e-08 |
|
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: 55.98 E-value: 1.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 6 QSPGKYIQGAGAIKRLGDYLKPL-AERWLVVGDKFV--LGFAEEmLRKSLADAGLAAEI-------APfggecSHNeINR 75
Cdd:cd08193 2 QTVPRIICGAGAAARLGELLRELgARRVLLVTDPGLvkAGLADP-ALAALEAAGIAVTVfddvvadPP-----EAV-VEA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 76 LRDIAGNAKCTAVLGIGGGKTLDTAKALAHFMN------------------VPVAIAPTIASTDAPCSALSVIYTDEGE- 136
Cdd:cd08193 75 AVEQAREAGADGVIGFGGGSSMDVAKLVALLAGsdqplddiygvgkatgprLPLILVPTTAGTGSEVTPISIVTTGETEk 154
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 839824880 137 ---FDSYLMlprnPNMVIVDTQIVAGAPARLLAA-GIgDAL 173
Cdd:cd08193 155 kgvVSPQLL----PDVALLDAELTLGLPPHVTAAtGI-DAM 190
|
|
| LPO |
cd08176 |
Lactadehyde:propanediol oxidoreductase (LPO) catalyzes the interconversion between ... |
14-331 |
1.84e-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: 55.63 E-value: 1.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 14 GAGAIKRLGDYLKPLA-ERWLVVGDKFVL--GFAEEMlRKSLADAGLAAEIapFGGECSHNEINRLRDIAG---NAKCTA 87
Cdd:cd08176 12 GWGAIEEIGEEAKKRGfKKALIVTDKGLVkfGIVDKV-TDVLKEAGIAYTV--FDEVKPNPTIENVMAGVAaykESGADG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 88 VLGIGGGKTLDTAKALA-------------------HFMNVPVAIAPTIASTDAPCSALSVIyTDEGE------FDSYLM 142
Cdd:cd08176 89 IIAVGGGSSIDTAKAIGiivanpgadvrslegvaptKNPAVPIIAVPTTAGTGSEVTINYVI-TDTEKkrkfvcVDPHDI 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 143 lprnPNMVIVDTQIVAGAPARLLAA-GIgDALATWFEARAcSRsGATTMAGGKCTQA----ALALAELCYNTLLEEGEKA 217
Cdd:cd08176 168 ----PTVAIVDPDLMSSMPKGLTAAtGM-DALTHAIEGYI-TK-GAWELSDMLALKAieliAKNLRKAVANPNNVEAREN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 218 MLAAEqhvvtpalervveantYLSGVGFESGGLAAAHAIHNGMTAIPDAHH-------------Y---YHGEK-----VA 276
Cdd:cd08176 241 MALAQ----------------YIAGMAFSNVGLGIVHSMAHPLSAFYDTPHgvanaillpyvmeFnapATGEKyrdiaRA 304
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 839824880 277 FG-TLTQLVLENAPVDEIETVAALCHSVGLPITLAQLDIK-GDIPtkmrLVAEAACA 331
Cdd:cd08176 305 MGvDTTGMSDEEAAEAAVDAVKKLSKDVGIPQKLSELGVKeEDIE----ALAEDALN 357
|
|
| Fe-ADH-like |
cd08189 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
12-333 |
2.35e-08 |
|
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: 55.17 E-value: 2.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 12 IQGAGAIKRLGDYLKPLA-ERWLVVGDKFV--LGFAEEMLrKSLADAGLAAEIapFGG-------ECSHNEINRLRDiag 81
Cdd:cd08189 9 FEGAGSLLQLPEALKKLGiKRVLIVTDKGLvkLGLLDPLL-DALKKAGIEYVV--FDGvvpdptiDNVEEGLALYKE--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 82 nAKCTAVLGIGGGKTLDTAKA--------------LAHFMNVP------VAIaPTIASTDAPCSALSVIyTDEGEFDSYL 141
Cdd:cd08189 83 -NGCDAIIAIGGGSVIDCAKViaaraanpkksvrkLKGLLKVRkklpplIAV-PTTAGTGSEATIAAVI-TDPETHEKYA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 142 MLPRN--PNMVIVDTQIVAGAPARLLAA-GIgDALATWFEAR-ACSRSGATTMAGGKCTQAALALAELCYN--TLLEEGE 215
Cdd:cd08189 160 INDPKliPDAAVLDPELTLGLPPAITAAtGM-DALTHAVEAYiSRSATKETDEYALEAVKLIFENLPKAYEdgSDLEARE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 216 KAMLAAeqhvvtpalervveantYLSGVGFESGGLAAAHAI-HN--GMTAIPdaHHY-----------YHGEKVA----- 276
Cdd:cd08189 239 NMLLAS-----------------YYAGLAFTRAYVGYVHAIaHQlgGLYGVP--HGLanavvlphvleFYGPAAEkrlae 299
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 839824880 277 FGTLTQLVLENAPVDE-----IETVAALCHSVGLPITLAQLDiKGDIPTkmrlVAEAACAEG 333
Cdd:cd08189 300 LADAAGLGDSGESDSEkaeafIAAIRELNRRMGIPTTLEELK-EEDIPE----IAKRALKEA 356
|
|
| PRK10624 |
PRK10624 |
L-1,2-propanediol oxidoreductase; Provisional |
1-332 |
6.03e-08 |
|
L-1,2-propanediol oxidoreductase; Provisional
Pssm-ID: 182595 [Multi-domain] Cd Length: 382 Bit Score: 53.85 E-value: 6.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 1 MDRIIQSPGKYIqGAGAIKRLGDYLKPLA-ERWLVVGDKFVLGF-AEEMLRKSLADAGLAAEIapFGGECSHNEINRLRD 78
Cdd:PRK10624 2 ANRMILNETAYF-GRGAIGALTDEVKRRGfKKALIVTDKTLVKCgVVAKVTDVLDAAGLAYEI--YDGVKPNPTIEVVKE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 79 iaGNAKCTA-----VLGIGGGKTLDTAKALAHFMN--------------------VPVAIAPTIASTDAPCSALSVIyTD 133
Cdd:PRK10624 79 --GVEVFKAsgadyLIAIGGGSPQDTCKAIGIISNnpefadvrslegvaptkkpsVPIIAIPTTAGTAAEVTINYVI-TD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 134 EGEFDSYLMLPRN--PNMVIVDTQIVAGAPARLLAAGIGDALATWFEaracsrsgattmagGKCTQAALALAELCYntll 211
Cdd:PRK10624 156 EEKRRKFVCVDPHdiPQVAFVDADMMDSMPPGLKAATGVDALTHAIE--------------GYITRGAWALTDMLH---- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 212 eegEKAMlaaeqHVVTPALERVVEANT----------YLSGVGFESGGLAAAHAIHNGMTAIPDAHH------------- 268
Cdd:PRK10624 218 ---LKAI-----EIIAGALRGAVAGDKeagegmalgqYIAGMGFSNVGLGLVHGMAHPLGAFYNTPHgvanaillphvme 289
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 839824880 269 Y---YHGEK-----VAFGTLTQ-LVLENAPVDEIETVAALCHSVGLPITLAQLDIK-GDIPtkmrLVAEAACAE 332
Cdd:PRK10624 290 YnadFTGEKyrdiaRAMGVKVEgMSLEEARNAAVEAVKALNRDVGIPPHLRDVGVKeEDIP----ALAQAAFDD 359
|
|
| PDDH |
cd08188 |
1,3-Propanediol (1,3-PD) dehydrogenase; This family includes 1,3-propanediol (1,3-PD) ... |
3-338 |
4.27e-07 |
|
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: 51.36 E-value: 4.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 3 RIIQSPGKYIQGAGAIKRLGDYLKPL-AERWLVVGDKFV--LGFAEeMLRKSLADAGLAAEIapFGG-------ECSHNE 72
Cdd:cd08188 1 FRFYIPPVNLFGPGCLKEIGDELKKLgGKKALIVTDKGLvkLGLVK-KVTDVLEEAGIEYVI--FDGvqpnptvTNVNEG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 73 INRLRDiagnAKCTAVLGIGGGKTLDTAKALAHFMN-------------VPVAIAP-----TIASTDAPCSALSVIyTDE 134
Cdd:cd08188 78 LELFKE----NGCDFIISVGGGSAHDCAKAIGILATnggeiedyegvdkSKKPGLPliainTTAGTASEVTRFAVI-TDE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 135 GefdsylmlpRNPNMVIVDTQIVA-----------GAPARLLAA-GIgDALATWFEARACsrSGATTMaggkcTQaALAL 202
Cdd:cd08188 153 E---------RHVKMVIVDWNVTPtiavndpelmlGMPPSLTAAtGM-DALTHAIEAYVS--TGATPL-----TD-ALAL 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 203 aelcyntlleegeKAMLAAEQHvvtpaLERVV------EANT------YLSGVGFESGGLAAAHAIhngmtaipdAH--- 267
Cdd:cd08188 215 -------------EAIRLIAEN-----LPKAVangkdlEAREnmayaqFLAGMAFNNAGLGYVHAM---------AHqlg 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 268 -HYY--HGekVAFGTLTQLVLE-NAPVDE--------------------------IETVAALCHSVGLPITLAQLDIK-G 316
Cdd:cd08188 268 gFYNlpHG--VCNAILLPHVMEfNLPACPerfadiaralgenteglsdeeaaeaaIEAIRKLSRRVGIPSGLKELGVKeE 345
|
410 420
....*....|....*....|..
gi 839824880 317 DIPtkmrLVAEAACAEGETIHN 338
Cdd:cd08188 346 DFP----LLAENALKDACGPTN 363
|
|
| Fe-ADH-like |
cd17814 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
11-320 |
6.85e-07 |
|
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: 50.62 E-value: 6.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 11 YIQGAGAIKRLGDYLKPL-AERWLVVGDKFVL--GFAEEMLrKSLADAGLAAEIapFGGEcSHN----EINRLRDIAGNA 83
Cdd:cd17814 7 FIFGVGARKLAGRYAKNLgARKVLVVTDPGVIkaGWVDEVL-DSLEAEGLEYVV--FSDV-TPNprdfEVMEGAELYREE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 84 KCTAVLGIGGGKTLDTAKALA------------------HFMNVPVAIAPTIASTDAPCSALSVIyTDEGEFDSYLMLPR 145
Cdd:cd17814 83 GCDGIVAVGGGSPIDCAKGIGivvsngghildyegvdkvRRPLPPLICIPTTAGSSADVSQFAII-TDTERRVKMAIISK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 146 N--PNMVIVDTQIVAGAPARLLAAGIGDALATWFEARACSRSGATTMAggkctqAALALAELCYNTL---------LEEG 214
Cdd:cd17814 162 TlvPDVSLIDPETLTTMDPELTACTGMDALTHAIEAYVSNASSPLTDL------HALEAIRLISENLpkavadpddLEAR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 215 EKAMLAAEQhvvtpalervveantylSGVGFESGGLAAAHAI-HN--GMTAIPdahhyyHGE------------------ 273
Cdd:cd17814 236 EKMMLASLQ-----------------AGLAFSNASLGAVHAMaHSlgGLLDLP------HGEcnalllphvirfnfpaap 292
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 839824880 274 ------KVAFGT-LTQLVLENAPVDEIETVAALCHSVGLPITLAQLDIK-GDIPT 320
Cdd:cd17814 293 eryrkiAEAMGLdVDGLDDEEVAERLIEAIRDLREDLGIPETLSELGVDeEDIPE 347
|
|
| Fe-ADH-like |
cd08185 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
14-320 |
9.43e-07 |
|
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: 50.19 E-value: 9.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 14 GAGAIKRLGDYLKPLAERWLVVGDK---FVLGFAEEmLRKSLADAGLAAEIapFggecshNEI--NRLRD-------IAG 81
Cdd:cd08185 10 GAGKLNELGEEALRPGKKALIVTGKgssKKTGLLDR-VKKLLEKAGVEVVV--F------DKVepNPLTTtvmegaaLAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 82 NAKCTAVLGIGGGKTLDTAKALAhFMNVP------------------------VAIaPTIASTDAPCSALSVIyTDE--G 135
Cdd:cd08185 81 EEGCDFVIGLGGGSSMDAAKAIA-FMATNpgdiwdyifggtgkgpppekalpiIAI-PTTAGTGSEVDPWAVI-TNPetK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 136 E---FDSYLMLPRnpnMVIVDTQIVAGAPARLLAA-GIgDALATWFEARACSRSGATTMaggkctqaALALaelcyntll 211
Cdd:cd08185 158 EkkgIGHPALFPK---VSIVDPELMLTVPPRVTAYtGF-DALFHAFESYISKNANPFSD--------MLAL--------- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 212 eegeKAMlaaeqHVVTPALERVVE-------------ANTyLSGVGFESGGLAAAHAIHNGMTAI-PDAHH--------- 268
Cdd:cd08185 217 ----EAI-----RLVAKYLPRAVKdgsdlearekmawAST-LAGIVIANSGTTLPHGLEHPLSGYhPNIPHgaglaalyp 286
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 839824880 269 -YY------HGEK---VAFGTLTQLVLENAPVDEIETVAALCHSVGLPITLAQLDI-KGDIPT 320
Cdd:cd08185 287 aYFeftiekAPEKfafVARAEASGLSDAKAAEDFIEALRKLLKDIGLDDLLSDLGVtEEDIPW 349
|
|
| Fe-ADH_KdnB-like |
cd08184 |
Iron-containing alcohol dehydrogenase similar to Shewanella oneidensis KdnB required for Kdo8N ... |
8-161 |
1.06e-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: 46.88 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 8 PGKYIQGAGAIKRLGDYLKPLAERwlvvGDKFVLGFAEEMLRKSladaGLAAEIAPFGG----------ECSHNEINRLR 77
Cdd:cd08184 1 VPKYLFGRGSFDQLGELLAERRKS----NNDYVVFFIDDVFKGK----PLLDRLPLQNGdllifvdttdEPKTDQIDALR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 78 DI---AGNAKCTAVLGIGGGKTLDTAKALAHFMNVP-------------------VAIaPTIASTDAPCSALSV------ 129
Cdd:cd08184 73 AQiraENDKLPAAVVGIGGGSTMDIAKAVSNMLTNPgsaadyqgwdlvknpgiykIGV-PTLSGTGAEASRTAVltgpek 151
|
170 180 190
....*....|....*....|....*....|....*
gi 839824880 130 ---IYTDEGEFDSylmlprnpnmVIVDTQIVAGAP 161
Cdd:cd08184 152 klgINSDYTVFDQ----------VILDPELIATVP 176
|
|
| PPD-like |
cd08181 |
1,3-propanediol dehydrogenase-like (PPD); This family contains proteins similar to 1, ... |
7-178 |
7.63e-05 |
|
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: 44.11 E-value: 7.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 7 SPGKYIQGAGAIKRLGDYLKPLAERWLVVGDK---FVLGFAEEmLRKSLADAGLAAEIapFGG---ECSHNEINRLRDIA 80
Cdd:cd08181 3 MPTKVYFGKNCVEKHADELAALGKKALIVTGKhsaKKNGSLDD-VTEALEENGIEYFI--FDEveeNPSIETVEKGAELA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 81 GNAKCTAVLGIGGGKTLDTAKALAHFM-----------------NVPVAIAPTIASTDAPCSALSVIYTDEGEFDSYLML 143
Cdd:cd08181 80 RKEGADFVIGIGGGSPLDAAKAIALLAankdgdedlfqngkynpPLPIVAIPTTAGTGSEVTPYSILTDHEKGTKKSFGN 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 839824880 144 PRN-PNMVIVDTQIVAGAPARLLAAGIGDALATWFE 178
Cdd:cd08181 160 PLIfPKLALLDPKYTLSLPEELTIDTAVDALSHAIE 195
|
|
| HOT |
cd08190 |
Hydroxyacid-oxoacid transhydrogenase (HOT) involved in gamma-hydroxybutyrate metabolism; This ... |
14-118 |
8.26e-05 |
|
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: 44.07 E-value: 8.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 14 GAGAIKRLGDYLKPL-AERWLVVGDKFVLGF-AEEMLRKSLADAGLAAEIapFGG---ECSHNEINRLRDIAGNAKCTAV 88
Cdd:cd08190 7 GPGATRELGMDLKRLgAKKVLVVTDPGLAKLgLVERVLESLEKAGIEVVV--YDGvrvEPTDESFEEAIEFAKEGDFDAF 84
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 839824880 89 LGIGGGKTLDTAKAL-------AHFMN-----------VPVAIAPTIA 118
Cdd:cd08190 85 VAVGGGSVIDTAKAAnlyathpGDFLDyvnapigkgkpVPGPLKPLIA 132
|
|
| NADPH_BDH |
cd08179 |
NADPH-dependent butanol dehydrogenase involved in the butanol and ethanol formation pathway in ... |
88-338 |
1.79e-04 |
|
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: 42.95 E-value: 1.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 88 VLGIGGGKTLDTAKALAHF--------------MNVP--------VAIaPTIASTDAPCSALSVIyTDEGEFDSYLMLPR 145
Cdd:cd08179 85 IIAIGGGSVIDAAKAMWVFyeypeltfedalvpFPLPelrkkarfIAI-PSTSGTGSEVTRASVI-TDTEKGIKYPLASF 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 146 N--PNMVIVDTQIVAGAPARLLAAGIGDALATWFEARACSRsgATTMaggkcTQA-ALALAELCYNTLLE--EGEKAMLA 220
Cdd:cd08179 163 EitPDVAILDPELTMTMPPHVTANTGMDALTHAIEAYVSTL--ANDF-----TDAlALGAILDIFENLPKsyNGGKDLEA 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 221 AEQ-HVVtpalervveanTYLSGVGFESGGLAAAHAI-HngmtAIPDAHHYYHGEKVAFgtLTQLVLE-NAPVDE----- 292
Cdd:cd08179 236 REKmHNA-----------SCLAGMAFSNSGLGIVHSMaH----KGGAFFGIPHGLANAI--LLPYVIEfNSKDPEarary 298
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 839824880 293 ----------------IETVAALCHSVGLPITLAQLDIKGDI-PTKMRLVAEAACAEGETIHN 338
Cdd:cd08179 299 aalligltdeelvedlIEAIEELNKKLGIPLSFKEAGIDEDEfFAKLDEMAENAMNDACTGTN 361
|
|
| PRK15454 |
PRK15454 |
ethanolamine utilization ethanol dehydrogenase EutG; |
48-273 |
9.87e-04 |
|
ethanolamine utilization ethanol dehydrogenase EutG;
Pssm-ID: 185351 [Multi-domain] Cd Length: 395 Bit Score: 40.78 E-value: 9.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 48 LRKSLADAGLAAEI--APFGGECSHN---EINRLRDiagnAKCTAVLGIGGGKTLDTAKALAHFMN-------------- 108
Cdd:PRK15454 69 LTRSLAVKGIAMTLwpCPVGEPCITDvcaAVAQLRE----SGCDGVIAFGGGSVLDAAKAVALLVTnpdstlaemsetsv 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 109 ----VPVAIAPTIASTDAPCSALSVIYTD-EGEFDSYLMLPRNPNMVIVDTQIVAGAPARLLAAGIGDALATWFEARACS 183
Cdd:PRK15454 145 lqprLPLIAIPTTAGTGSETTNVTVIIDAvSGRKQVLAHASLMPDVAILDAALTEGVPSHVTAMTGIDALTHAIEAYSAL 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 184 RS---------GATTMAGGKCTQAAlalaelcyntlleeGEKAMLAAEQHVVTPALervveantyLSGVGFESGGLAAAH 254
Cdd:PRK15454 225 NAtpftdslaiGAIAMIGKSLPKAV--------------GYGHDLAARESMLLASC---------MAGMAFSSAGLGLCH 281
|
250
....*....|....*....
gi 839824880 255 AIHNGMTAipdAHHYYHGE 273
Cdd:PRK15454 282 AMAHQPGA---ALHIPHGL 297
|
|
| Fe-ADH-like |
cd08186 |
Iron-containing alcohol dehydrogenase; This family contains iron-containing alcohol ... |
14-104 |
6.53e-03 |
|
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: 38.40 E-value: 6.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 839824880 14 GAGAIKRLGDYLKPLA-ERWLVVGDK--FVLGFAEEMLRKSLADAGLAAEI------APfggecSHNEINRLRDIAGNAK 84
Cdd:cd08186 7 GVGAIAKIKDILKDLGiDKVIIVTGRssYKKSGAWDDVEKALEENGIEYVVydkvtpNP-----TVDQADEAAKLARDFG 81
|
90 100
....*....|....*....|
gi 839824880 85 CTAVLGIGGGKTLDTAKALA 104
Cdd:cd08186 82 ADAVIAIGGGSPIDTAKSVA 101
|
|
| |
