|
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: 677.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 1 MDRIIQSPGKYIQGANVIARLGDYLKPMANNWLVVGDKFVLGFAEETLRKSLTDAGLSVEIAPFSGECSQNEIDRLRAVA 80
Cdd:PRK09423 1 MDRIFISPSKYVQGKGALARLGEYLKPLGKRALVIADEFVLGIVGDRVEASLKEAGLTVVFEVFNGECSDNEIDRLVAIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 81 EKSQCGAVLGIGGGKTLDTAKALAHFMNVPVAIAPTIASTDAPCSALSVIYTDAGEFDRYLLLPHNPNMVIVDTQIVAGA 160
Cdd:PRK09423 81 EENGCDVVIGIGGGKTLDTAKAVADYLGVPVVIVPTIASTDAPTSALSVIYTEEGEFERYLFLPKNPDLVLVDTAIIAKA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 161 PARLLAAGIGDALATWFEARACSRSGATTMAGGKCTQAALALAELCYNTLIEEGEKAMLAAEQHVVTPALERVIEANTYL 240
Cdd:PRK09423 161 PARFLAAGIGDALATWFEARACSRSGGTTMAGGKPTLAALALAELCYETLLEDGLKAKLAVEAKVVTPALENVIEANTLL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 241 SGVGFESGGLAAAHAIHNGLTAIPDAHHYYHGEKVAFGTLTQLVLENAPVEEIETVAALCHSVGLPITLAQLDIKQDIPA 320
Cdd:PRK09423 241 SGLGFESGGLAAAHAIHNGLTALEDTHHLTHGEKVAFGTLTQLVLENRPKEEIEEVIDFCHAVGLPTTLADLGLKEDSDE 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 446296183 321 KMRTVAEASCAEGETIHNMPGGATPDEVYAALLVADQYGQRFLQEW 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: 603.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 8 PGKYIQGANVIARLGDYLKPMANNWLVVGDKFVLGFAEETLRKSLTDAGLSVEIAPFSGECSQNEIDRLRAVAEKSQCGA 87
Cdd:cd08170 1 PSRYVQGPGALDRLGEYLAPLGKKALVIADPFVLDLVGERLEESLEKAGLEVVFEVFGGECSREEIERLAAIARANGADV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 88 VLGIGGGKTLDTAKALAHFMNVPVAIAPTIASTDAPCSALSVIYTDAGEFDRYLLLPHNPNMVIVDTQIVAGAPARLLAA 167
Cdd:cd08170 81 VIGIGGGKTIDTAKAVADYLGLPVVIVPTIASTDAPCSALSVIYTEDGEFDEYLFLPRNPDLVLVDTEIIAKAPVRFLVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 168 GIGDALATWFEARACSRSGATTMAGGKCTQAALALAELCYNTLIEEGEKAMLAAEQHVVTPALERVIEANTYLSGVGFES 247
Cdd:cd08170 161 GMGDALATYFEARACARSGAPNMAGGRPTLAALALAELCYDTLLEYGVAAKAAVEAGVVTPALEAVIEANTLLSGLGFES 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 248 GGLAAAHAIHNGLTAIPDAHHYYHGEKVAFGTLTQLVLENAPVEEIETVAALCHSVGLPITLAQLDIKQDIPAKMRTVAE 327
Cdd:cd08170 241 GGLAAAHAIHNGLTALPETHHLLHGEKVAFGTLVQLVLEGRPDEEIEEVIRFCRSVGLPVTLADLGLEDVTDEELRKVAE 320
|
330 340 350
....*....|....*....|....*....|.
gi 446296183 328 ASCAEGETIHNMPGGATPDEVYAALLVADQY 358
Cdd:cd08170 321 AACAPGETIHNMPFPVTPEDVVDAILAADAL 351
|
|
| GldA |
COG0371 |
Glycerol dehydrogenase or related enzyme, iron-containing ADH family [Energy production and ... |
3-355 |
1.38e-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: 497.00 E-value: 1.38e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 3 RIIQSPGKYIQGANVIARLGDYLKPMANNWLVVGDKFVLGFAEETLRKSLTDAGLSVEIAPFSGECSQNEIDRLRAVAEK 82
Cdd:COG0371 1 RVIILPRRYVQGEGALDELGEYLADLGKRALIITGPTALKAAGDRLEESLEDAGIEVEVEVFGGECSEEEIERLAEEAKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 83 SQCGAVLGIGGGKTLDTAKALAHFMNVPVAIAPTIASTDAPCSALSVIYTDAGEFDRYLLLPHNPNMVIVDTQIVAGAPA 162
Cdd:COG0371 81 QGADVIIGVGGGKALDTAKAVAYRLGLPVVSVPTIASTDAPASPLSVIYTEDGAFDGYSFLAKNPDLVLVDTDIIAKAPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 163 RLLAAGIGDALATWFEARACSRSGAtTMAGGKCTQAALALAELCYNTLIEEGEKAMLAAEQHVVTPALERVIEANTYLSG 242
Cdd:COG0371 161 RLLAAGIGDALAKWYEARDWSLAHR-DLAGEYYTEAAVALARLCAETLLEYGEAAIKAVEAGVVTPALERVVEANLLLSG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 243 VGF----ESGGLAAAHAIHNGLTAIPDAHHYYHGEKVAFGTLTQLVLENAPvEEIETVAALCHSVGLPITLAQLDIKQDI 318
Cdd:COG0371 240 LAMgigsSRPGSGAAHAIHNGLTALPETHHALHGEKVAFGTLVQLVLEGRP-EEIEELLDFLRSVGLPTTLADLGLDDET 318
|
330 340 350
....*....|....*....|....*....|....*..
gi 446296183 319 PAKMRTVAEASCAEGETIHNMPGGATPDEVYAALLVA 355
Cdd:COG0371 319 EEELLTVAEAARPERYTILNLPFEVTPEAVEAAILAT 355
|
|
| GlyDH-like |
cd08550 |
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins. ... |
8-353 |
1.49e-144 |
|
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: 413.09 E-value: 1.49e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 8 PGKYIQGANVIARLGDYLKPMANNWLVVGDKFVLGFAEETLRKSLTDAGLSVEIAPFSGECSQNEIDRLRAVAEKSQCGA 87
Cdd:cd08550 1 PGRYIQEPGILAKAGEYIAPLGKKALIIGGKTALEAVGEKLEKSLEEAGIDYEVEVFGGECTEENIERLAEKAKEEGADV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 88 VLGIGGGKTLDTAKALAHFMNVPVAIAPTIASTDAPCSALSVIYTDAGEFDRYLLLPHNPNMVIVDTQIVAGAPARLLAA 167
Cdd:cd08550 81 IIGIGGGKVLDTAKAVADRLGLPVVTVPTIAATCAAWSALSVLYDEEGEFLGYSLLKRSPDLVLVDTDIIAAAPVRYLAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 168 GIGDALATWFEARACSRSGATTMAggkcTQAALALAELCYNTLIEEGEKAMLAAEQHVVTPALERVIEANTYLSGVGFES 247
Cdd:cd08550 161 GIGDTLAKWYEARPSSRGGPDDLA----LQAAVQLAKLAYDLLLEYGVQAVEDVRQGKVTPALEDVVDAIILLAGLVGSL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 248 GG----LAAAHAIHNGLTAIPDAHHYYHGEKVAFGTLTQLVLENAPVEEIETVAALCHSVGLPITLAQLDIKQDiPAKMR 323
Cdd:cd08550 237 GGggcrTAAAHAIHNGLTKLPETHGTLHGEKVAFGLLVQLALEGRSEEEIEELIEFLRRLGLPVTLEDLGLELT-EEELR 315
|
330 340 350
....*....|....*....|....*....|
gi 446296183 324 TVAEASCAEGETIHNMPGGATPDEVYAALL 353
Cdd:cd08550 316 KIAEYACDPPDMAHMLPFPVTPEMLAEAIL 345
|
|
| GlyDH-like |
cd08172 |
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins ... |
8-352 |
1.06e-106 |
|
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: 316.77 E-value: 1.06e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 8 PGKYIQGANVIARLGDYLKPM-ANNWLVVGDKFVLGFAEETLrKSLTDAGLSVEIapFSGECSQNEIDRLRAVAEKSQCG 86
Cdd:cd08172 1 PQEYICEEGALKELPELLSEFgIKRPLIIHGEKSWQAAKPYL-PKLFEIEYPVLR--YDGECSYEEIDRLAEEAKEHQAD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 87 AVLGIGGGKTLDTAKALAHFMNVPVAIAPTIASTDAPCSALSVIYTDAGEFDRYLLLPHNPNMVIVDTQIVAGAPARLLA 166
Cdd:cd08172 78 VIIGIGGGKVLDTAKAVADKLNIPLILIPTLASNCAAWTPLSVIYDEDGEFIGYDYFPRSAYLVLVDPRLLLDSPKDYFV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 167 AGIGDALATWFEARACSRSGATTMAggkCTQAALALAELCYNTLIEEGEKAMLAAEQHVVTPALERVIEANTYLSGV--G 244
Cdd:cd08172 158 AGIGDTLAKWYEADAILRQLEELPA---FLQLARQAAKLCRDILLKDSEQALADLEAGKLTPAFIKVVETIIALAGMvgG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 245 F--ESGGLAAAHAIHNGLTAIPDAHHYYHGEKVAFGTLTQLVLENApVEEIETVAALCHSVGLPITLAQLDIKQDIPAKM 322
Cdd:cd08172 235 FgdEYGRSAGAHAIHNGLTKLPETHHFLHGEKVAYGILVQLALEGK-WDEIKKLLPFYRRLGLPTSLADLGLTDDTEEAL 313
|
330 340 350
....*....|....*....|....*....|
gi 446296183 323 RTVAEASCAEGETIHNMPGGATPDEVYAAL 352
Cdd:cd08172 314 QKIAAFAASPEESIHLLPPDVTAEEVLQAI 343
|
|
| GlyDH-like |
cd08171 |
Glycerol dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins ... |
14-353 |
1.81e-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: 239.34 E-value: 1.81e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 14 GANVIARLGDYLKPMANNWLVVGDKFVLGFAEETLRKSLTDAGLSV-EIAPFSGECSQNEIDRLRAVAEKSQCGAVLGIG 92
Cdd:cd08171 7 GEDAYDAIPKICSPYGKKVVVIGGKKALAAAKPKLRAALEGSGLEItDFIWYGGEATYENVEKLKANPEVQEADMIFAVG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 93 GGKTLDTAKALAHFMNVPVAIAPTIASTDAPCSALSVIYTDAGEFDRYLLLPHNPNMVIVDTQIVAGAPARLLAAGIGDA 172
Cdd:cd08171 87 GGKAIDTVKVLADRLNKPVFTFPTIASNCAAVTAVSVMYNPDGSFKEYYFLKRPPVHTFIDTEIIAEAPEKYLWAGIGDT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 173 LATWFEARACSRSGATTMAggkcTQAALALAELCYNTLIEEGEKAMLAAEQHVVTPALERVIEANTYLSG-----VGFE- 246
Cdd:cd08171 167 LAKYYEVEFSARGDELDHT----NALGVAISKMCSEPLLKYGVQALEDCRANKVSDALEQVVLDIIVTTGlvsnlVEPDy 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 247 SGGLaaAHAIHNGLTAIPDA-HHYYHGEKVAFGTLTQLVLENApVEEIETVAALCHSVGLPITLAQLDIKqdiPAKMRTV 325
Cdd:cd08171 243 NSSL--AHALYYGLTTLPQIeEEHLHGEVVSYGVLVLLTVDGQ-FEELEKVYAFNKSIGLPTCLADLGLT---VEDLEKV 316
|
330 340
....*....|....*....|....*...
gi 446296183 326 AEAsCAEGETIHNMPGGATPDEVYAALL 353
Cdd:cd08171 317 LDK-ALKTKDLRHSPYPITKEMFEEAIK 343
|
|
| Fe-ADH |
pfam00465 |
Iron-containing alcohol dehydrogenase; |
8-348 |
1.04e-65 |
|
Iron-containing alcohol dehydrogenase;
Pssm-ID: 425696 [Multi-domain] Cd Length: 362 Bit Score: 212.08 E-value: 1.04e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 8 PGKYIQGANVIARLGDYLKPMANNWLVVGDKFVLGF-AEETLRKSLTDAGLSVEIAP-FSGECSQNEIDRLRAVAEKSQC 85
Cdd:pfam00465 1 PTRIVFGAGALAELGEELKRLGARALIVTDPGSLKSgLLDKVLASLEEAGIEVVVFDgVEPEPTLEEVDEAAALAREAGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 86 GAVLGIGGGKTLDTAKALAHFMN------------------VPVAIAPTIASTDAPCSALSVIYTDAGEFDRYLLLPH-N 146
Cdd:pfam00465 81 DVIIAVGGGSVIDTAKAIALLLTnpgdvwdylggkpltkpaLPLIAIPTTAGTGSEVTPLAVITDTETGEKLGIFSPKlL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 147 PNMVIVDTQIVAGAPARLLAAGIGDALATWFEARACSRSGATTMAggkCTQAALALAELCYNTLIEEGEKAmlaaeqhvv 226
Cdd:pfam00465 161 PDLAILDPELTLTLPPRLTAATGMDALAHAVEAYVSKGANPLTDA---LALEAIRLIAENLPRAVADGEDL--------- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 227 tPALERVIEANTyLSGVGFESGGLAAAHAIHNGLTAIPDAHH-YYHGEKVAFGT----------LTQLVL-------ENA 288
Cdd:pfam00465 229 -EARENMLLAST-LAGLAFSNAGLGAAHALAHALGGRYGIPHgLANAILLPYVLrfnapaapekLAQLARalgedsdEEA 306
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 289 PVEEIETVAALCHSVGLPITLAQLDIKQDipaKMRTVAEASCAEGeTIHNMPGGATPDEV 348
Cdd:pfam00465 307 AEEAIEALRELLRELGLPTTLSELGVTEE---DLDALAEAALRDR-SLANNPRPLTAEDI 362
|
|
| PRK10586 |
PRK10586 |
putative oxidoreductase; Provisional |
3-360 |
5.87e-54 |
|
putative oxidoreductase; Provisional
Pssm-ID: 182570 Cd Length: 362 Bit Score: 181.85 E-value: 5.87e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 3 RIIQSPGKYIQGANVIARLGDYLKPMA-NNWLVVGDKFVLGFAEETLRKSLTDAGlsVEIAPFSGECSQNEIDRLRAVAe 81
Cdd:PRK10586 7 RVVVGPANYFSHPGSIDHLHDFFTDEQlSRAVWIYGERAIAAAQPYLPPAFELPG--AKHILFRGHCSESDVAQLAAAS- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 82 KSQCGAVLGIGGGKTLDTAKALAHFMNVPVAIAPTIASTDAPCSALSVIYTDAGEFDRYLLLPHNPNMVIVDTQIVAGAP 161
Cdd:PRK10586 84 GDDRQVVIGVGGGALLDTAKALARRLGLPFVAIPTIAATCAAWTPLSVWYNDAGQALHFEIFDDANFLVLVEPRIILNAP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 162 ARLLAAGIGDALATWFEARACSRSGAT---TMAGGkcTQAALALAelcyNTLIEEGEKAMLAAEQHVVTPALERVIEAnt 238
Cdd:PRK10586 164 QEYLLAGIGDTLAKWYEAVVLAPQPETlplTVRLG--INNALAIR----DVLLNSSEQALADQQNGQLTQDFCDVVDA-- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 239 YLSGVGFeSGGL-------AAAHAIHNGLTAIPDAHHYYHGEKVAFGTLTQLVLenapVEEIETVAALC---HSVGLPIT 308
Cdd:PRK10586 236 IIAGGGM-VGGLgerytrvAAAHAVHNGLTVLPQTEKFLHGTKVAYGILVQSAL----LGQDDVLAQLIgayQRFHLPTT 310
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 446296183 309 LAQLDIKQDIPAKMRTVAEASCAEGETIHNMPGGATPDEVYAALLVADQYGQ 360
Cdd:PRK10586 311 LAELDVDINNQAEIDRVIAHTLRPVESIHYLPVTLTPDTLRAAFEKVESFKA 362
|
|
| DHQ_Fe-ADH |
cd07766 |
Dehydroquinate synthase-like (DHQ-like) and iron-containing alcohol dehydrogenases (Fe-ADH); ... |
8-320 |
1.35e-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: 1.35e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 8 PGKYIQGANVIARLGDYLKPMANNWLVVGDKFVLGFAEETLRKSLtDAGLSVEIAPFSGE-CSQNEIDRLRAVAEKSQCG 86
Cdd:cd07766 1 PTRIVFGEGAIAKLGEIKRRGFDRALVVSDEGVVKGVGEKVADSL-KKGLAVAIFDFVGEnPTFEEVKNAVERARAAEAD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 87 AVLGIGGGKTLDTAKALAHFMN--VPVAIAPTIASTDAPCSALSVIYTDAGEFdRYLLLPHNPNMVIVDTQIVAGAPARL 164
Cdd:cd07766 80 AVIAVGGGSTLDTAKAVAALLNrgIPFIIVPTTASTDSEVSPKSVITDKGGKN-KQVGPHYNPDVVFVDTDITKGLPPRQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 165 LAAGIGDALATWFEaracsrsgattmaggkctqaalalaelcyntlieegekamlaaeqhvvtpaLERVIEANTYLSGVG 244
Cdd:cd07766 159 VASGGVDALAHAVE---------------------------------------------------LEKVVEAATLAGMGL 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 245 FESGGLAAAHAIHNGLTAipdAHHYYHGEKVAFGTLTQLVLENAPVEE----IETVAALCHSVGLPITLAQLDI-KQDIP 319
Cdd:cd07766 188 FESPGLGLAHAIGHALTA---FEGIPHGEAVAVGLPYVLKVANDMNPEpeaaIEAVFKFLEDLGLPTHLADLGVsKEDIP 264
|
.
gi 446296183 320 A 320
Cdd:cd07766 265 K 265
|
|
| G1PDH-like |
cd08174 |
Glycerol-1-phosphate dehydrogenase-like; These glycerol-1-phosphate dehydrogenase-like ... |
14-317 |
6.17e-28 |
|
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: 111.84 E-value: 6.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 14 GANVIARLGDYLKPM---ANNWLVVGDKFVLGFAEETLRKSLTDAGLSVEIapfsgecSQNEIDRLRAVAEKSQCG---- 86
Cdd:cd08174 7 EEGALEHLGKYLADRnqgFGKVAIVTGEGIDELLGEDILESLEEAGEIVTV-------EENTDNSAEELAEKAFSLpkvd 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 87 AVLGIGGGKTLDTAKALAHFMNVPVAIAPTIASTDAPCSALSVIYTDAGefdRYLLLPHNPNMVIVDTQIVAGAPARLLA 166
Cdd:cd08174 80 AIVGIGGGKVLDVAKYAAFLSKLPFISVPTSLSNDGIASPVAVLKVDGK---RKSLGAKMPYGVIVDLDVIKSAPRRLIL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 167 AGIGD------ALATW-FEARAcsrsGATTMAGgkctqAALALAELCYNTLIEEGEKAMLAAEqhvvtpALERVIEANTy 239
Cdd:cd08174 157 AGIGDlisnitALYDWkLAEEK----GGEPVDD-----FAYLLSRTAADSLLNTPGKDIKDDE------FLKELAESLV- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 240 LSGVGFE--------SGglaAAHAI-HngltAIpDAHH---YYHGEKVAFGTLTQLVLENAPVEEIETVAALChsvGLPI 307
Cdd:cd08174 221 LSGIAMEiagssrpaSG---SEHLIsH----AL-DKLFpgpALHGIQVGLGTYFMSFLQGQRYEEIRDVLKRT---GFPL 289
|
330
....*....|
gi 446296183 308 TLAQLDIKQD 317
Cdd:cd08174 290 NPSDLGLTKE 299
|
|
| Gro1PDH |
cd08173 |
Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) catalyzes the reversible conversion between ... |
14-318 |
1.65e-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: 102.25 E-value: 1.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 14 GANVIARLGDYLKP--MANNWLVVGDKFVLGFAEETLRKSLTDAGLSVEIAPFSGECSQNEIDRLRAVAEKSQCGAVLGI 91
Cdd:cd08173 8 GHGAINKIGEVLKKllLGKRALIITGPNTYKIAGKRVEDLLESSGVEVVIVDIATIEEAAEVEKVKKLIKESKADFIIGV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 92 GGGKTLDTAKALAHFMNVPVAIAPTIASTDAPCSALSVIYTDAGefdRYLLLPHNPNMVIVDTQIVAGAPARLLAAGIGD 171
Cdd:cd08173 88 GGGKVIDVAKYAAYKLNLPFISIPTSASHDGIASPFASIKGGDK---PYSIKAKAPIAIIADTEIISKAPKRLLAAGCGD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 172 ALAT------WFEARacsrsgatTMAGGKCTQAALALAELCYNTLIEEGEKAMLAAEQHVVTpalerVIEAnTYLSGVgf 245
Cdd:cd08173 165 LISNitavkdWRLAH--------RLKGEYYSEYAASLALMSAKLIIENADLIKPGLEEGVRT-----VVKA-LISSGV-- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 246 eSGGLAA------------AHAIH-----NGLtaipdahhyyHGEKVAFGTLTQLVLENAPVEEIetVAALcHSVGLPIT 308
Cdd:cd08173 229 -AMSIAGssrpasgsehlfSHALDklapgPAL----------HGEQCGVGTIMMAYLHGGDWKEI--REAL-KKIGAPTT 294
|
330
....*....|
gi 446296183 309 LAQLDIKQDI 318
Cdd:cd08173 295 AKELGLDKEI 304
|
|
| Fe-ADH_2 |
pfam13685 |
Iron-containing alcohol dehydrogenase; |
14-276 |
3.12e-23 |
|
Iron-containing alcohol dehydrogenase;
Pssm-ID: 404557 [Multi-domain] Cd Length: 251 Bit Score: 96.99 E-value: 3.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 14 GANVIARLGDYLKPMA-NNWLVVGDKFVLGFAEETLRKSLTDAGLSVEIAPF-SGECSQNEIDRLRAVAEKSQCGAVLGI 91
Cdd:pfam13685 3 GPGALGRLGEYLAELGfRRVALVADANTYAAAGRKVAESLKRAGIEVETRLEvAGNADMETAEKLVGALRERDADAVVGV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 92 GGGKTLDTAKALAHFMNVPVAIAPTIASTDAPCSALSVIYTDaGEFDRYLLLPhnPNMVIVDTQIVAGAPARLLAAGIGD 171
Cdd:pfam13685 83 GGGTVIDLAKYAAFKLGKPFISVPTAASNDGFASPGASLTVD-GKKRSIPAAA--PFGVIADTDVIAAAPRRLLASGVGD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 172 ------ALATWFEARAcSRSGAttmaggkctQAALALAELCYNtlieegeKAMLAAEQHVVTPALERVIEANTyLSGVGF 245
Cdd:pfam13685 160 llakitAVADWELAHA-EEVAA---------PLALLSAAMVMN-------FADRPLRDPGDIEALAELLSALA-MGGAGS 221
|
250 260 270
....*....|....*....|....*....|.
gi 446296183 246 ESGGLAAAHAIHNGLTAIPDAHHyYHGEKVA 276
Cdd:pfam13685 222 SRPASGSEHLISHALDMIAPKQA-LHGEQVG 251
|
|
| EutG |
COG1454 |
Alcohol dehydrogenase, class IV [Energy production and conversion]; |
1-355 |
1.89e-22 |
|
Alcohol dehydrogenase, class IV [Energy production and conversion];
Pssm-ID: 441063 [Multi-domain] Cd Length: 381 Bit Score: 97.11 E-value: 1.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 1 MDRIIQSPGKYIQGANVIARLGDYLKPM-ANNWLVVGDKFV--LGFAEEtLRKSLTDAGLSVEIapFSG---ECSQNEID 74
Cdd:COG1454 1 MMFTFRLPTRIVFGAGALAELGEELKRLgAKRALIVTDPGLakLGLLDR-VLDALEAAGIEVVV--FDDvepNPTVETVE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 75 RLRAVAEKSQCGAVLGIGGGKTLDTAKALAHFMNVP-------------------VAIaPTIASTDAPCSALSVIYTDAG 135
Cdd:COG1454 78 AGAAAAREFGADVVIALGGGSAIDAAKAIALLATNPgdledylgikkvpgpplplIAI-PTTAGTGSEVTPFAVITDPET 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 136 E-----FDRYLLlphnPNMVIVDTQIVAGAPARLLAA-GIgDALATWFEArACSRsGATTMAggkctqAALALA--ELCY 207
Cdd:COG1454 157 GvkkgiADPELL----PDVAILDPELTLTLPPSLTAAtGM-DALTHAIEA-YVSK-GANPLT------DALALEaiRLIA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 208 NTL---IEEG------EKAMLAAeqhvvtpalervieantYLSGVGFESGGLAAAHAIHNGLTAIPDAHH---------- 268
Cdd:COG1454 224 RNLpraVADGddlearEKMALAS-----------------LLAGMAFANAGLGAVHALAHPLGGLFHVPHglanaillph 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 269 ---YY---HGEKVA-----FGTLTQLVLENAPVEEIETVAALCHSVGLPITLAQLDIKQ-DIPAkmrtVAEASCAEGETI 336
Cdd:COG1454 287 vlrFNapaAPERYAeiaraLGLDVGLSDEEAAEALIEAIRELLRDLGIPTRLSELGVTEeDLPE----LAELALADRCLA 362
|
410
....*....|....*....
gi 446296183 337 HNmPGGATPDEVYAALLVA 355
Cdd:COG1454 363 NN-PRPLTEEDIEAILRAA 380
|
|
| Fe-ADH |
cd08551 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains large ... |
8-350 |
2.67e-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: 96.75 E-value: 2.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 8 PGKYIQGANVIARLGDYLKPM-ANNWLVVGDKFV--LGFAEEtLRKSLTDAGLSVEIapFSG---ECSQNEIDRLRAVAE 81
Cdd:cd08551 1 PTRIVFGAGALARLGEELKALgGKKVLLVTDPGLvkAGLLDK-VLESLKAAGIEVEV--FDDvepNPTVETVEAAAELAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 82 KSQCGAVLGIGGGKTLDTAKALAHFMN------------------VPVAIAPTIASTDAPCSALSVIyTDAGE------F 137
Cdd:cd08551 78 EEGADLVIAVGGGSVLDTAKAIAVLATnggsirdyegigkvpkpgLPLIAIPTTAGTGSEVTPNAVI-TDPETgrkmgiV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 138 DRYLLlphnPNMVIVDTQIVAGAPARLLAA-GIgDALATWFEArACSRsGATTMaggkcTQA-ALALAELCYNTL----- 210
Cdd:cd08551 157 SPYLL----PDVAILDPELTLSLPPSVTAAtGM-DALTHAIEA-YTSK-KANPI-----SDAlALEAIRLIGKNLrrava 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 211 ----IEEGEKAMLAAeqhvvtpalervieantYLSGVGFESGGLAAAHAIHNGLTAIPDAHH-------------YY--- 270
Cdd:cd08551 225 dgsdLEAREAMLLAS-----------------LLAGIAFGNAGLGAVHALAYPLGGRYHIPHgvanaillpyvmeFNlpa 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 271 HGEK-----VAFGTLTQLVLENAPVEE-IETVAALCHSVGLPITLAQLDIKQ-DIPAkmrtVAEASCAEGETIHNMPGGA 343
Cdd:cd08551 288 CPEKyaeiaEALGEDVEGLSDEEAAEAaVEAVRELLRDLGIPTSLSELGVTEeDIPE----LAEDAMKSGRLLSNNPRPL 363
|
....*..
gi 446296183 344 TPDEVYA 350
Cdd:cd08551 364 TEEDIRE 370
|
|
| egsA |
PRK00843 |
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed |
3-171 |
2.26e-21 |
|
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed
Pssm-ID: 179139 Cd Length: 350 Bit Score: 93.80 E-value: 2.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 3 RIIQSPGKYIQGANVIARLGDYLKPMA--NNWLVVGDKFVLGFAEETLRKSLTDAGlSVEIApFSGECSQNEIDRLRAVA 80
Cdd:PRK00843 6 HWIQLPRDVVVGHGVLDDIGDVCSDLKltGRALIVTGPTTKKIAGDRVEENLEDAG-DVEVV-IVDEATMEEVEKVEEKA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 81 EKSQCGAVLGIGGGKTLDTAKALAHFMNVPVAIAPTIASTDAPCSALSVIYTDAGefdRYLLLPHNPNMVIVDTQIVAGA 160
Cdd:PRK00843 84 KDVNAGFLIGVGGGKVIDVAKLAAYRLGIPFISVPTAASHDGIASPRASIKGGGK---PVSVKAKPPLAVIADTEIIAKA 160
|
170
....*....|.
gi 446296183 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 |
1.67e-19 |
|
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: 88.01 E-value: 1.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 8 PGKYIQGANVIARLGDYLK-PMANNWLVVGDKFVLGFAEETLRKSLTDAGLSVeiapfsgecSQNEIDRLRAVAEKSQ-C 85
Cdd:cd08549 1 PRYTIVGDGAINKIEEILKkLNLKRVLIITGKNTKAKYCRFFYDQLKTVCDIV---------YYDNIDNLEDELKKYTfY 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 86 GAVLGIGGGKTLDTAKALAHFMNVPVAIAPTIASTDAPCS-ALSVIYTDAgefdRYLLLPHNPNMVIVDTQIVAGAPARL 164
Cdd:cd08549 72 DCVIGIGGGRSIDTGKYLAYKLKIPFISVPTSASNDGIASpIVSLRIPGV----KKTFMADAPIAIIADTEIIKKSPRRL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 165 LAAGIGD------ALATW-FEARacsrsgattMAGGKCTQAALALAELCYNTLIEEGEKAMLAAEQHvvtpaleRVIEAN 237
Cdd:cd08549 148 LSAGIGDlvsnitAVLDWkLAHK---------EKGEKYSEFAAILSKTSAKELVSYVLKASDLEEYH-------RVLVKA 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 238 TYLSGVGFESGGLAA---------AHAIHNGLTAIPDaHHYYHGEKVAFGTLTQLVL------ENAPVEE-IETVAAlch 301
Cdd:cd08549 212 LVGSGIAMAIAGSSRpasgsehlfSHALDKLKEEYLN-INVLHGEQVGVGTIIMSYLhekenkKLSGLHErIKMILK--- 287
|
330
....*....|....*..
gi 446296183 302 SVGLPITLAQLDIKQDI 318
Cdd:cd08549 288 KVGAPTTAKQLGIDEDL 304
|
|
| Fe-ADH-like |
cd14863 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
14-353 |
1.98e-19 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341485 [Multi-domain] Cd Length: 380 Bit Score: 88.36 E-value: 1.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 14 GANVIARLGDYLKPM-ANNWLVVGDKFV--LGFAEEtLRKSLTDAGLSVEIapFSG---ECSQNEIDRLRAVAEKSQCGA 87
Cdd:cd14863 11 GAGAVEQIGELLKELgCKKVLLVTDKGLkkAGIVDK-IIDLLEEAGIEVVV--FDDvepDPPDEIVDEAAEIAREEGADG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 88 VLGIGGGKTLDTAKALA-----------HFMNVPVAIA--------PTIASTDAPCSALSVIYTDagEFDRYLLLPHN-- 146
Cdd:cd14863 88 VIGIGGGSVLDTAKAIAvlltnpgpiidYALAGPPVPKpgipliaiPTTAGTGSEVTPIAVITDE--ENGVKKSLLGPfl 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 147 -PNMVIVDTQIVAGAPARLLAA-GIgDALATWFEARACSRSGATTMAggKCTQAalalAELCYNTL---IEEG------E 215
Cdd:cd14863 166 vPDLAILDPELTVGLPPSLTAAtGM-DALSHAIEAYTSKLANPMTDA--LALQA----IRLIVKNLpraVKDGdnlearE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 216 KAMLAAeqhvvtpalervieantYLSGVGFESGGLAAAHAIHNGLTAIpdaHHYYHGEKVAFGTLTqlVLE-NAPV---- 290
Cdd:cd14863 239 NMLLAS-----------------NLAGIAFNNAGTHIGHAIAHALGAL---YHIPHGLACALALPV--VLEfNAEAypek 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 291 --------------EEIETVAALCH--------SVGLPITLAQLDIKQDipaKMRTVAEAscAEGETIHNMPGGATPDEV 348
Cdd:cd14863 297 vkkiakalgvsfpgESDEELGEAVAdairefmkELGIPSLFEDYGIDKE---DLDKIAEA--VLKDPFAMFNPRPITEEE 371
|
....*
gi 446296183 349 YAALL 353
Cdd:cd14863 372 VAEIL 376
|
|
| Fe-ADH-like |
cd08196 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
5-352 |
1.28e-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: 341475 [Multi-domain] Cd Length: 367 Bit Score: 86.09 E-value: 1.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 5 IQSPGKYIQGANVIARLGDYLKPMA-NNWLVVGDKFvlgFAEETLRKSLTDAGLSVEIAPFSG---ECSQNEIDRLRAVA 80
Cdd:cd08196 3 YYQPVKIIFGEGILKELPDIIKELGgKRGLLVTDPS---FIKSGLAKRIVESLKGRIVAVFSDvepNPTVENVDKCARLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 81 EKSQCGAVLGIGGGKTLDTAKALAHFMN-------------------VPVAIAPTIASTDAPCSALSVI-YTDAGE---F 137
Cdd:cd08196 80 RENGADFVIAIGGGSVLDTAKAAACLAKtdgsiedylegkkkipkkgLPLIAIPTTAGTGSEVTPVAVLtDKEKGKkapL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 138 DRYLLLphnPNMVIVDTQIVAGAPARLLAA-GIgDALATWFEArACSRSgattmAGGKCTQAALALAELCYNTL---IEE 213
Cdd:cd08196 160 VSPGFY---PDIAIVDPELTYSMPPKVTAStGI-DALCHAIEA-YWSIN-----HQPISDALALEAAKLVLENLekaYNN 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 214 GEKAmlaaeqhvvtPALERVIEANTyLSGVGFESGGLAAAHAIHNGLTAIpdaHHYYHGEKVAFgTLTQLVLENAPVEE- 292
Cdd:cd08196 230 PNDK----------EAREKMALASL-LAGLAFSQTRTTASHACSYPLTSH---FGIPHGEACAL-TLPSFIRLNAEALPg 294
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446296183 293 -----------------IETVAALCHSVGLPITLAQLDIKQDipaKMRTVAEASCAEgETIHNMPGGATPDEVYAAL 352
Cdd:cd08196 295 rldelakqlgfkdaeelADKIEELKKRIGLRTRLSELGITEE---DLEEIVEESFHP-NRANNNPVEVTKEDLEKLL 367
|
|
| Fe-ADH-like |
cd14864 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
8-319 |
3.77e-16 |
|
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: 78.88 E-value: 3.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 8 PGKYIQGANVIARLGDYLKPMANNWLVVGDKFVLGFAE-ETLRKSLTDAGLSVEI-APFSGECSQNEIDRLRAVAEKSQC 85
Cdd:cd14864 4 PPNIVFGADSLERIGEEVKEYGSRFLLITDPVLKESGLaDKIVSSLEKAGISVIVfDEIPASATSDTIDEAAELARKAGA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 86 GAVLGIGGGKTLDTAKALA----------HFMN--------VPVAIAPTIASTDAPCSAlSVIYTDAGEFDRYLLLPHN- 146
Cdd:cd14864 84 DGIIAVGGGKVLDTAKAVAilanndggayDFLEgakpkkkpLPLIAVPTTPRSGFEFSD-RFPVVDSRSREVKLLKAQPg 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 147 -PNMVIVDTQIVAGAPARLLAAGIGDALATWFEARACSRSG-ATTMAGGKctqaALALAelcyntlieeGEKAMLAAEQH 224
Cdd:cd14864 163 lPKAVIVDPNLMASLTGNQTAAMALAALALAVEAYLSKKSNfFSDALALK----AIELV----------SENLDGALADP 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 225 VVTPALERVIEANtYLSGVGFESGGL----AAAHAIhNGLTAIPDAH-------HY--YHGEKVAFGTLTQLVLENAPVE 291
Cdd:cd14864 229 KNTPAEELLAQAG-CLAGLAASSSSPglatALALAV-NSRYKVSKSLvasillpHVieYAATSAPDKYAKIARALGEDVE 306
|
330 340 350
....*....|....*....|....*....|....*...
gi 446296183 292 EIETVAA----------LCHSVGLPITLAQLDIKQDIP 319
Cdd:cd14864 307 GASPEEAaiaavegvrrLIAQLNLPTRLKDLDLASSLE 344
|
|
| G1PDH |
cd08175 |
Glycerol-1-phosphate dehydrogenase (G1PDH) catalyzes the reversible reduction of ... |
14-317 |
1.23e-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: 74.08 E-value: 1.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 14 GANVIARLGDYLK--PMANNWLVVGDKFVLGFAEETLRKSLTDAGLSVEIAPFSGEcsQNEIDRLRAVAE-----KSQCG 86
Cdd:cd08175 7 GEGALKKLPEYLKelFGGKKVLVVADENTYAAAGEEVEAALEEAGVTVCLLIFPGE--GDLIADEAAVGKvllelEKDTD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 87 AVLGIGGGkTL-DTAKALAHFMNVPVAIAPTIASTDAPCSALSVIYTDaGEfdRYLLLPHNPNMVIVDTQIVAGAPARLL 165
Cdd:cd08175 85 LIIAVGSG-TInDLTKYAAYKLGIPYISVPTAPSMDGYTSSGAPIIVD-GV--KKTFPAHAPKAIFADLDVLANAPQRMI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 166 AAGIGD------ALATWFEARAcsrsgattmAGGK--CTQAAlalaelcynTLIEEGEKAMLAAEQHVVT---PALERVI 234
Cdd:cd08175 161 AAGFGDllgkytALADWKLSHL---------LGGEyyCPEVA---------DLVQEALEKCLDNAEGIAArdpEAIEALM 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 235 EANTyLSGVGFE--------SGglaAAH---------AIHNGLTAIpdahhyYHGEKVAFGTLTQL---VLENAP-VEEI 293
Cdd:cd08175 223 EALI-LSGLAMQlvgnsrpaSG---AEHhlshywemeFLRLGKPPV------LHGEKVGVGTLLIAalyILEQLPpPEEL 292
|
330 340
....*....|....*....|....
gi 446296183 294 EtvaALCHSVGLPITLAQLDIKQD 317
Cdd:cd08175 293 R---ELLRKAGAPTTPEDLGIDRD 313
|
|
| BDH |
cd08187 |
Butanol dehydrogenase catalyzes the conversion of butyraldehyde to butanol with the cofactor ... |
4-352 |
3.68e-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: 72.85 E-value: 3.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 4 IIQSPGKYIQGANVIARLGDYLKPMANNWLVV-GDKFV--LGFAEEtLRKSLTDAGlsVEIAPFSGECSQNEIDRLR--- 77
Cdd:cd08187 3 TFYNPTKIIFGKGAIEELGEEIKKYGKKVLLVyGGGSIkkNGLYDR-VVASLKEAG--IEVVEFGGVEPNPRLETVRegi 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 78 AVAEKSQCGAVLGIGGGKTLDTAKALAH----------FMN--------VPVAIAPTIASTDAPCSALSVIYTDAGEFDR 139
Cdd:cd08187 80 ELAREENVDFILAVGGGSVIDAAKAIAAgakydgdvwdFFTgkappekaLPVGTVLTLAATGSEMNGGAVITNEETKEKL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 140 YLLLPHN-PNMVIVDTQIVAGAPARLLAAGIGDALATWFEaracsrsgaTTMAGGKCTQAALALAELCYNTLIEEGEKA- 217
Cdd:cd08187 160 GFGSPLLrPKFSILDPELTYTLPKYQTAAGIVDIFSHVLE---------QYFTGTEDAPLQDRLAEGLLRTVIENGPKAl 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 218 ------------MLAAEQhvvtpalervieANTYLSGVGFESGglAAAHAIHNGLTAIPDAHH-------------YYHG 272
Cdd:cd08187 231 kdpddyearanlMWAATL------------ALNGLLGAGRGGD--WATHAIEHELSALYDITHgaglaivfpawmrYVLK 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 273 EKVA---------FGTLTQLVLENAPVEEIETVAALCHSVGLPITLAQLDIKQDIPAKMrtvAEAsCAEGETIHNMPGGA 343
Cdd:cd08187 297 KKPErfaqfarrvFGIDPGGDDEETALEGIEALEEFFKSIGLPTTLSELGIDEEDIEEM---AEK-AVRGGGLGGGFKPL 372
|
....*....
gi 446296183 344 TPDEVYAAL 352
Cdd:cd08187 373 TREDIEEIL 381
|
|
| Fe-ADH-like |
cd08191 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
7-355 |
5.14e-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: 5.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 7 SPGKYIQGANVIARLGDYLKPMANNWLVVGDKFVLGFAE-ETLRKSLTDAGLSVEIapFSGEC----SQNEIDRLRAVAE 81
Cdd:cd08191 3 SPSRLLFGPGARRALGRVAARLGSRVLIVTDPRLASTPLvAELLAALTAAGVAVEV--FDGGQpelpVSTVADAAAAARA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 82 kSQCGAVLGIGGGKTLDTAKA----LAH---------FMNVP------VAIaPTIASTDAPCSALSVIYTDAGEFDRYLL 142
Cdd:cd08191 81 -FDPDVVIGLGGGSNMDLAKVvallLAHggdprdyygEDRVPgpvlplIAV-PTTAGTGSEVTPVAVLTDPARGMKVGVS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 143 LPH-NPNMVIVDTQIVAGAPARLLA-AGIgDALATWFEA------RACSRSGATTMAGGK---CTQAALALAELCYNTLI 211
Cdd:cd08191 159 SPYlRPAVAIVDPELTLTCPPGVTAdSGI-DALTHAIESytardfPPFPRLDPDPVYVGKnplTDLLALEAIRLIGRHLP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 212 EegekamlAAEQHVVTPALERVIEANTyLSGVGFESGGLAAAHAIHNGLTAipdAHHYYHGEKV---------------- 275
Cdd:cd08191 238 R-------AVRDGDDLEARSGMALAAL-LAGLAFGTAGTAAAHALQYPIGA---LTHTSHGVGNglllpyvmrfnrpara 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 276 --------AFGTLTQLVLENAPVEEIETVAALCHSVGLPITLAQLDIKQ-DIPakmrTVAEASCAEGETIHNMPgGATPD 346
Cdd:cd08191 307 aelaeiarALGVTTAGTSEEAADRAIERVEELLARIGIPTTLADLGVTEaDLP----GLAEKALSVTRLIANNP-RPPTE 381
|
....*....
gi 446296183 347 EVYAALLVA 355
Cdd:cd08191 382 EDLLRILRA 390
|
|
| Fe-ADH-like |
cd08183 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
8-329 |
9.17e-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 domains. Proteins of this family have not been characterized.
Pssm-ID: 341462 [Multi-domain] Cd Length: 377 Bit Score: 68.68 E-value: 9.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 8 PGKYIQGANVIARLGDYLKPMANNWLVV-GDKFVLGFAEETLRKSLTDAGLSVEIAPFSGECSQNEIDRLRAVAEKSQCG 86
Cdd:cd08183 1 PPRIVFGRGSLQELGELAAELGKRALLVtGRSSLRSGRLARLLEALEAAGIEVALFSVSGEPTVETVDAAVALAREAGCD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 87 AVLGIGGGKTLDTAKALA----------HFMNV------------PVAIAPTIASTDAPCSALSVIYTDAGEF-----DR 139
Cdd:cd08183 81 VVIAIGGGSVIDAAKAIAalltnegsvlDYLEVvgkgrpltepplPFIAIPTTAGTGSEVTKNAVLSSPEHGVkvslrSP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 140 YLLlphnPNMVIVDTQIVAGAPARLLAAGIGDALATWFEARACSRSGATT----MAGgkCTQAALALAELCYN-TLIEEG 214
Cdd:cd08183 161 SML----PDVALVDPELTLSLPPEVTAASGLDALTQLIEPYVSRKANPLTdalaREG--LRLAARSLRRAYEDgEDLEAR 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 215 EKAMLAAeqhvvtpalervieantYLSGVGFESGGLAAAHAIHN---GLTAIP------------------------DAH 267
Cdd:cd08183 235 EDMALAS-----------------LLGGLALANAGLGAVHGLAGplgGMFGAPhgaicaallppvleanlralrerePDS 297
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446296183 268 HYYHGEKVAFGTLTQlvLENAPVEE-IETVAALCHSVGLPiTLAQLDIK-QDIPAkmrtVAEAS 329
Cdd:cd08183 298 PALARYRELAGILTG--DPDAAAEDgVEWLEELCEELGIP-RLSEYGLTeEDFPE----IVEKA 354
|
|
| Fe-ADH-like |
cd14862 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
7-327 |
1.96e-11 |
|
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: 64.55 E-value: 1.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 7 SPGKYIQGANVIARLGDYLKPMAnnwLVVGDKFV--LGFAEETLrKSLTDAGLSVEIapFSG---ECSQNEIDRLRAVAE 81
Cdd:cd14862 5 SSPKIVFGEDALSHLEQLSGKRA---LIVTDKVLvkLGLLKKVL-KRLLQAGFEVEV--FDEvepEPPLETVLKGAEAMR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 82 KSQCGAVLGIGGGKTLDTAKALAHFMNVP---------------------VAIaPTIASTDAPCSALSVIyTDAGEFdRY 140
Cdd:cd14862 79 EFEPDLIIALGGGSVMDAAKAAWVLYERPdldpedispldllglrkkaklIAI-PTTSGTGSEATWAIVL-TDTEEP-RK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 141 LLLPHN---PNMVIVDTQIVAGAPARLLAA-GIgDALATWFEARACSRSgaTTMAGGKCTQAalalAELCYNTLieegek 216
Cdd:cd14862 156 IAVANPelvPDVAILDPEFVLGMPPKLTAGtGL-DALAHAVEAYLSTWS--NDFSDALALKA----IELIFKYL------ 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 217 aMLAAEQHVVTPALERVIEANTyLSGVGFESGGLAAAHAIHNGLTAIPDAHH--------------YYHGEKVAFGTLTQ 282
Cdd:cd14862 223 -PRAYKDGDDLEAREKMHNAAT-IAGLAFGNSQAGLAHALGHSLGAVFHVPHgiavglflpyviefYAKVTDERYDLLKL 300
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 446296183 283 LVLENAPVEE-----IETVAALCHSVGLPITLAQLDI-KQDIPAKMRTVAE 327
Cdd:cd14862 301 LGIEARDEEEalkklVEAIRELYKEVGQPLSIKDLGIsEEEFEEKLDELVE 351
|
|
| Fe-ADH-like |
cd14861 |
Iron-containing alcohol dehydrogenases-like; This family contains proteins similar to ... |
14-329 |
9.76e-11 |
|
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: 62.53 E-value: 9.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 14 GANVIARLGDYLKPM-ANNWLVVGDKFV--LGFAEETLRkSLTDAGLSVEIapFSGECS---QNEIDRLRAVAEKSQCGA 87
Cdd:cd14861 9 GAGAIAELPEELKALgIRRPLLVTDPGLaaLGIVDRVLE-ALGAAGLSPAV--FSDVPPnptEADVEAGVAAYREGGCDG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 88 VLGIGGGKTLDTAKA----------LAHF-----------MNVPVAIA-PTIASTDAPCSALSVIY-TDAGE----FDRY 140
Cdd:cd14861 86 IIALGGGSAIDAAKAialmathpgpLWDYedgeggpaaitPAVPPLIAiPTTAGTGSEVGRAAVITdDDTGRkkiiFSPK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 141 LLlphnPNMVIVDTQIVAGAPARLLAA-GIgDALATWFEarACSRSGATTMAggkctqAALALAELCyntLIEEG-EKAM 218
Cdd:cd14861 166 LL----PKVAICDPELTLGLPPRLTAAtGM-DALTHCIE--AYLSPGFHPMA------DGIALEGLR---LISEWlPRAV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 219 -----LAAEQHVVTPALErvieantylSGVGFESgGLAAAHAIHNGLTAIPDAHHyyhgekvafGTLTQLVLE-----NA 288
Cdd:cd14861 230 adgsdLEARGEMMMAALM---------GAVAFQK-GLGAVHALAHALGALYGLHH---------GLLNAILLPyvlrfNR 290
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446296183 289 PVEE--------------------IETVAALCHSVGLPITLAQLDIKQDIPAKMRTVAEAS 329
Cdd:cd14861 291 PAVEdklarlaralglglggfddfIAWVEDLNERLGLPATLSELGVTEDDLDELAELALAD 351
|
|
| Fe-ADH-like |
cd08194 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
8-173 |
3.49e-10 |
|
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: 61.01 E-value: 3.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 8 PGKYIQGANVIARLGDYLKPM-ANNWLVVGDKFV--LGFAEEtLRKSLTDAGLSVEI-APFSGECSQNEIDRLRAVAEKS 83
Cdd:cd08194 1 PRTIIIGGGALEELGEEAASLgGKRALIVTDKVMvkLGLVDK-VTQLLAEAGIAYAVfDDVVSEPTDEMVEEGLALYKEG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 84 QCGAVLGIGGGKTLDTAKA----------LAHFMN--------VPVAIAPTIASTDAPCSALSVIyTDAgEFDRYLLLPH 145
Cdd:cd08194 80 GCDFIVALGGGSPIDTAKAiavlatnggpIRDYMGprkvdkpgLPLIAIPTTAGTGSEVTRFTVI-TDT-ETDVKMLLKG 157
|
170 180 190
....*....|....*....|....*....|..
gi 446296183 146 ---NPNMVIVDTQIVAGAPARLLAA-GIgDAL 173
Cdd:cd08194 158 palLPAVAIVDPELTLSMPPRVTAAtGI-DAL 188
|
|
| PRK10624 |
PRK10624 |
L-1,2-propanediol oxidoreductase; Provisional |
33-320 |
4.16e-10 |
|
L-1,2-propanediol oxidoreductase; Provisional
Pssm-ID: 182595 [Multi-domain] Cd Length: 382 Bit Score: 60.78 E-value: 4.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 33 LVVGDKFVLGF-AEETLRKSLTDAGLSVEIapFSGECSQNEIDRLRA-VAEKSQCGA--VLGIGGGKTLDTAKALAHFMN 108
Cdd:PRK10624 34 LIVTDKTLVKCgVVAKVTDVLDAAGLAYEI--YDGVKPNPTIEVVKEgVEVFKASGAdyLIAIGGGSPQDTCKAIGIISN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 109 --------------------VPVAIAPTIASTDAPCSALSVIyTDAGEFDRYLLL-PHN-PNMVIVDTQIVAGAPARLLA 166
Cdd:PRK10624 112 npefadvrslegvaptkkpsVPIIAIPTTAGTAAEVTINYVI-TDEEKRRKFVCVdPHDiPQVAFVDADMMDSMPPGLKA 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 167 AGIGDALATWFEaracsrsgattmagGKCTQAALALAELCYNTLIE--------------EGEKAMLAAEqhvvtpaler 232
Cdd:PRK10624 191 ATGVDALTHAIE--------------GYITRGAWALTDMLHLKAIEiiagalrgavagdkEAGEGMALGQ---------- 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 233 vieantYLSGVGFESGGLAAAHAIHNGLTAIPDAHH-------------Y---YHGEK-----VAFGTLTQ-LVLENAPV 290
Cdd:PRK10624 247 ------YIAGMGFSNVGLGLVHGMAHPLGAFYNTPHgvanaillphvmeYnadFTGEKyrdiaRAMGVKVEgMSLEEARN 320
|
330 340 350
....*....|....*....|....*....|.
gi 446296183 291 EEIETVAALCHSVGLPITLAQLDIK-QDIPA 320
Cdd:PRK10624 321 AAVEAVKALNRDVGIPPHLRDVGVKeEDIPA 351
|
|
| HEPD |
cd08182 |
Hydroxyethylphosphoate dehydrogenase (HEPD) catalyzes the reduction of phosphonoacetaldehyde ... |
8-352 |
5.01e-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: 5.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 8 PGKYIQGANVIARLGDYLKPM-ANNWLVVGDKfvlGFAEETLRKSLTDA-GLSVEIAPFSGECSQNEIDRLRAVAEK--- 82
Cdd:cd08182 1 PVKIIFGPGALAELKDLLGGLgARRVLLVTGP---SAVRESGAADILDAlGGRIPVVVFSDFSPNPDLEDLERGIELfre 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 83 SQCGAVLGIGGGKTLDTAKALAHFMNVP---------------------VAIaPTIASTDAPCSALSVIY-TDAGE---F 137
Cdd:cd08182 78 SGPDVIIAVGGGSVIDTAKAIAALLGSPgenllllrtgekapeenalplIAI-PTTAGTGSEVTPFATIWdEAEGKkysL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 138 DRYLLLPHnpnMVIVDTQIVAGAPARLLAAGIGDALATWFEARACSRSGATTMAggkctqAALALAELCYNTLieegeKA 217
Cdd:cd08182 157 AHPSLYPD---AAILDPELTLSLPLYLTASTGLDALSHAIESIWSVNANPESRA------YALRAIRLILENL-----PL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 218 MLAAEQHvvTPALERVIEAnTYLSGVGFESGGLAAAHAIHNGLTAipdAHHYYHGEKVAF-------------------- 277
Cdd:cd08182 223 LLENLPN--LEAREAMAEA-SLLAGLAISITKTTAAHAISYPLTS---RYGVPHGHACALtlpavlrynagaddecdddp 296
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446296183 278 -GTLTQLVLENAPVEE-IETVAALCHSVGLPITLAQLDIKQDipAKMRTVAEAScaEGETIHNMPGGATPDEVYAAL 352
Cdd:cd08182 297 rGREILLALGASDPAEaAERLRALLESLGLPTRLSEYGVTAE--DLEALAASVN--TPERLKNNPVRLSEEDLLRLL 369
|
|
| LPO |
cd08176 |
Lactadehyde:propanediol oxidoreductase (LPO) catalyzes the interconversion between ... |
14-320 |
1.90e-09 |
|
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: 58.71 E-value: 1.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 14 GANVIARLGDYLKPMA-NNWLVVGDKFVL--GFAEEtLRKSLTDAGLSVEIapFSG-------ECSQNEIdrlrAVAEKS 83
Cdd:cd08176 12 GWGAIEEIGEEAKKRGfKKALIVTDKGLVkfGIVDK-VTDVLKEAGIAYTV--FDEvkpnptiENVMAGV----AAYKES 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 84 QCGAVLGIGGGKTLDTAKALA-------------------HFMNVPVAIAPTIASTDAPCSALSVIyTDAGEFDRYLLL- 143
Cdd:cd08176 85 GADGIIAVGGGSSIDTAKAIGiivanpgadvrslegvaptKNPAVPIIAVPTTAGTGSEVTINYVI-TDTEKKRKFVCVd 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 144 PH-NPNMVIVDTQIVAGAPARLLAA-GIgDALATWFEARAcSRsGATTMAGGKCTQA----ALALAELCYNTLIEEGEKA 217
Cdd:cd08176 164 PHdIPTVAIVDPDLMSSMPKGLTAAtGM-DALTHAIEGYI-TK-GAWELSDMLALKAieliAKNLRKAVANPNNVEAREN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 218 MLAAEqhvvtpalervieantYLSGVGFESGGLAAAHAIHNGLTAIPDAHH-------------Y---YHGEK-----VA 276
Cdd:cd08176 241 MALAQ----------------YIAGMAFSNVGLGIVHSMAHPLSAFYDTPHgvanaillpyvmeFnapATGEKyrdiaRA 304
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 446296183 277 FG-TLTQLVLENAPVEEIETVAALCHSVGLPITLAQLDIKQ-DIPA 320
Cdd:cd08176 305 MGvDTTGMSDEEAAEAAVDAVKKLSKDVGIPQKLSELGVKEeDIEA 350
|
|
| Fe-ADH-like |
cd08189 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
12-328 |
2.90e-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 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: 57.86 E-value: 2.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 12 IQGANVIARLGDYLKPMA-NNWLVVGDKFV--LGFAEEtLRKSLTDAGLSVEIapFSG-----ECSQneIDRLRAVAEKS 83
Cdd:cd08189 9 FEGAGSLLQLPEALKKLGiKRVLIVTDKGLvkLGLLDP-LLDALKKAGIEYVV--FDGvvpdpTIDN--VEEGLALYKEN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 84 QCGAVLGIGGGKTLDTAKA--------------LAHFMNVP------VAIaPTIASTDAPCSALSVIyTDAGEFDRYL-- 141
Cdd:cd08189 84 GCDAIIAIGGGSVIDCAKViaaraanpkksvrkLKGLLKVRkklpplIAV-PTTAGTGSEATIAAVI-TDPETHEKYAin 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 142 ---LLPHnpnMVIVDTQIVAGAPARLLAA-GIgDALATWFEAR-ACSRSGATTMAGGKCTQAALALAELCYN--TLIEEG 214
Cdd:cd08189 162 dpkLIPD---AAVLDPELTLGLPPAITAAtGM-DALTHAVEAYiSRSATKETDEYALEAVKLIFENLPKAYEdgSDLEAR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 215 EKAMLAAeqhvvtpalervieantYLSGVGFESGGLAAAHAI-HN--GLTAIPdaHHY-----------YHGEKVA---- 276
Cdd:cd08189 238 ENMLLAS-----------------YYAGLAFTRAYVGYVHAIaHQlgGLYGVP--HGLanavvlphvleFYGPAAEkrla 298
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 277 -FGTLTQLVLENAPVEE-----IETVAALCHSVGLPITLAQLDiKQDIP--AKmRTVAEA 328
Cdd:cd08189 299 eLADAAGLGDSGESDSEkaeafIAAIRELNRRMGIPTTLEELK-EEDIPeiAK-RALKEA 356
|
|
| HOT |
cd08190 |
Hydroxyacid-oxoacid transhydrogenase (HOT) involved in gamma-hydroxybutyrate metabolism; This ... |
14-173 |
2.95e-08 |
|
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: 54.86 E-value: 2.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 14 GANVIARLGDYLKPM-ANNWLVVGDKFVLGF-AEETLRKSLTDAGLSVEIapFSG---ECSQNEIDRLRAVAEKSQCGAV 88
Cdd:cd08190 7 GPGATRELGMDLKRLgAKKVLVVTDPGLAKLgLVERVLESLEKAGIEVVV--YDGvrvEPTDESFEEAIEFAKEGDFDAF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 89 LGIGGGKTLDTAKAL-------AHFMN-----------VPVAIAPTIA-----STDAPCSALSVI-YTDA----GEFDRY 140
Cdd:cd08190 85 VAVGGGSVIDTAKAAnlyathpGDFLDyvnapigkgkpVPGPLKPLIAipttaGTGSETTGVAIFdLEELkvktGISSRY 164
|
170 180 190
....*....|....*....|....*....|...
gi 446296183 141 LLlphnPNMVIVDTQIVAGAPARLLAAGIGDAL 173
Cdd:cd08190 165 LR----PTLAIVDPLLTLTLPPRVTASSGFDVL 193
|
|
| HVD |
cd08193 |
5-hydroxyvalerate dehydrogenase (HVD) catalyzes the oxidation of 5-hydroxyvalerate to ... |
6-326 |
8.53e-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: 53.29 E-value: 8.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 6 QSPGKYIQGANVIARLGDYLKPM-ANNWLVVGDKFV--LGFAEeTLRKSLTDAGLSVEIapfsgeCSQNEIDR-----LR 77
Cdd:cd08193 2 QTVPRIICGAGAAARLGELLRELgARRVLLVTDPGLvkAGLAD-PALAALEAAGIAVTV------FDDVVADPpeavvEA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 78 AVAEKSQCGA--VLGIGGGKTLDTAKALAHFMN------------------VPVAIAPTIASTDAPCSALSVIYTDAGE- 136
Cdd:cd08193 75 AVEQAREAGAdgVIGFGGGSSMDVAKLVALLAGsdqplddiygvgkatgprLPLILVPTTAGTGSEVTPISIVTTGETEk 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 137 ---FDRYLLlphnPNMVIVDTQIVAGAPARLLAA-GIgDALATWFEARAcSRSGATTMAGGKCTQaalALAELCYN--TL 210
Cdd:cd08193 155 kgvVSPQLL----PDVALLDAELTLGLPPHVTAAtGI-DAMVHAIEAYT-SRHKKNPISDALARE---ALRLLGANlrRA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 211 IEEGEKamLAAEQHVVTPALervieantyLSGVGFESGGLAAAHAIhngltAIPDAHHYyhgeKVAFGTLTQLVLE---- 286
Cdd:cd08193 226 VEDGSD--LEAREAMLLGSM---------LAGQAFANAPVAAVHAL-----AYPLGGHF----HVPHGLSNALVLPhvlr 285
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446296183 287 -NAPVEE--------------------------IETVAALCHSVGLPITLAQLDIKQDIPAKMRTVA 326
Cdd:cd08193 286 fNLPAAEalyaelarallpglafgsdaaaaeafIDALEELVEASGLPTRLRDVGVTEEDLPMLAEDA 352
|
|
| Fe-ADH-like |
cd14865 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
6-355 |
9.57e-08 |
|
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: 53.31 E-value: 9.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 6 QSPGKYIQGANVIARLGDYLKPM-ANNWLVVGDKFV--LGFA---EETLRKSLTDAGLSVEIAPFSgecSQNEIDRLRAV 79
Cdd:cd14865 4 FNPTKIVSGAGALENLPAELARLgARRPLIVTDKGLaaAGLLkkvEDALGDAIEIVGVFDDVPPDS---SVAVVNEAAAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 80 AEKSQCGAVLGIGGGKTLDTAKA-----------LAHFMN--------VPVAIAPTIASTDAPCSALSVIY-TDAG---E 136
Cdd:cd14865 81 AREAGADGIIAVGGGSVIDTAKGvnillseggddLDDYGGanrltrplKPLIAIPTTAGTGSEVTLVAVIKdEEKKvklL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 137 F-DRYLLlphnPNMVIVDTQIVAGAPARLLAAGIGDALATWFEARACSRSGATTmaggkctqAALALA--ELCYNTLI-- 211
Cdd:cd14865 161 FvSPFLL----PDVAILDPRLTLSLPPKLTAATGMDALTHAIEAYTSLQKNPIS--------DALALQaiRLISENLPka 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 212 ------EEGEKAMLAAeqhvvtpalervieanTYLSGVGFESGGLAAAHAI-HngltAIPDAHHYYHGekVAFGTLTQLV 284
Cdd:cd14865 229 vkngkdLEARLALAIA----------------ATMAGIAFSNSMVGLVHAIaH----AVGAVAGVPHG--LANSILLPHV 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 285 LE------------------------NAPVEE-----IETVAALCHSVGLPITLAQLDIKQ-DIPAkmrtVAEASCAEGE 334
Cdd:cd14865 287 MRynldaaaeryaelalalaygvtpaGRRAEEaieaaIDLVRRLHELCGLPTRLRDVGVPEeQLEA----IAELALNDGA 362
|
410 420
....*....|....*....|.
gi 446296183 335 TIHNmPGGATPDEVYAALLVA 355
Cdd:cd14865 363 ILFN-PREVDPEDILAILEAA 382
|
|
| NADPH_BDH |
cd08179 |
NADPH-dependent butanol dehydrogenase involved in the butanol and ethanol formation pathway in ... |
88-348 |
1.50e-07 |
|
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: 52.58 E-value: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 88 VLGIGGGKTLDTAKALAHF--------------MNVP--------VAIaPTIASTDAPCSALSVIyTDAGEFDRYLLLPH 145
Cdd:cd08179 85 IIAIGGGSVIDAAKAMWVFyeypeltfedalvpFPLPelrkkarfIAI-PSTSGTGSEVTRASVI-TDTEKGIKYPLASF 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 146 N--PNMVIVDTQIVAGAPARLLAAGIGDALATWFEARACSRsgATTMaggkcTQA-ALALAELCYNTLIE--EGEKAMLA 220
Cdd:cd08179 163 EitPDVAILDPELTMTMPPHVTANTGMDALTHAIEAYVSTL--ANDF-----TDAlALGAILDIFENLPKsyNGGKDLEA 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 221 AEQ-HVVtpalervieanTYLSGVGFESGGLAAAHAI-HngltAIPDAHHYYHGEKVAFgtLTQLVLE-NAPVEE----- 292
Cdd:cd08179 236 REKmHNA-----------SCLAGMAFSNSGLGIVHSMaH----KGGAFFGIPHGLANAI--LLPYVIEfNSKDPEarary 298
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446296183 293 ----------------IETVAALCHSVGLPITLAQLDIKQDI-PAKMRTVAEASCAEGETIHNmPGGATPDEV 348
Cdd:cd08179 299 aalligltdeelvedlIEAIEELNKKLGIPLSFKEAGIDEDEfFAKLDEMAENAMNDACTGTN-PRKPTVEEM 370
|
|
| Fe-ADH_KdnB-like |
cd08184 |
Iron-containing alcohol dehydrogenase similar to Shewanella oneidensis KdnB required for Kdo8N ... |
8-161 |
3.80e-06 |
|
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: 48.42 E-value: 3.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 8 PGKYIQGANVIARLGDYLKPMANNwlvvGDKFVLGFAEETLRKSLTDAGL------SVEIAPFSGECSQNEIDRLRA--- 78
Cdd:cd08184 1 VPKYLFGRGSFDQLGELLAERRKS----NNDYVVFFIDDVFKGKPLLDRLplqngdLLIFVDTTDEPKTDQIDALRAqir 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 79 VAEKSQCGAVLGIGGGKTLDTAKALAHFMNVP-------------------VAIaPTIASTDAPCSALSV---------I 130
Cdd:cd08184 77 AENDKLPAAVVGIGGGSTMDIAKAVSNMLTNPgsaadyqgwdlvknpgiykIGV-PTLSGTGAEASRTAVltgpekklgI 155
|
170 180 190
....*....|....*....|....*....|.
gi 446296183 131 YTDAGEFDRylllphnpnmVIVDTQIVAGAP 161
Cdd:cd08184 156 NSDYTVFDQ----------VILDPELIATVP 176
|
|
| Fe-ADH-like |
cd17814 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
11-319 |
7.19e-06 |
|
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: 47.54 E-value: 7.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 11 YIQGANVIARLGDYLKPM-ANNWLVVGDKFVL--GFAEETLrKSLTDAGLSVEIapFSGEcSQN----EIDRLRAVAEKS 83
Cdd:cd17814 7 FIFGVGARKLAGRYAKNLgARKVLVVTDPGVIkaGWVDEVL-DSLEAEGLEYVV--FSDV-TPNprdfEVMEGAELYREE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 84 QCGAVLGIGGGKTLDTAKALA------------------HFMNVPVAIAPTIASTDAPCSALSVIyTDAGEFDRYLLLPH 145
Cdd:cd17814 83 GCDGIVAVGGGSPIDCAKGIGivvsngghildyegvdkvRRPLPPLICIPTTAGSSADVSQFAII-TDTERRVKMAIISK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 146 N--PNMVIVDTQIVAGAPARLLAAGIGDALATWFEARACSRSGATTMAggkctqAALALAELCYNTL---------IEEG 214
Cdd:cd17814 162 TlvPDVSLIDPETLTTMDPELTACTGMDALTHAIEAYVSNASSPLTDL------HALEAIRLISENLpkavadpddLEAR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 215 EKAMLAAEQhvvtpalervieantylSGVGFESGGLAAAHAI-HN--GLTAIPdahhyyHGE------------------ 273
Cdd:cd17814 236 EKMMLASLQ-----------------AGLAFSNASLGAVHAMaHSlgGLLDLP------HGEcnalllphvirfnfpaap 292
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 446296183 274 ------KVAFGT-LTQLVLENAPVEEIETVAALCHSVGLPITLAQLDIK-QDIP 319
Cdd:cd17814 293 eryrkiAEAMGLdVDGLDDEEVAERLIEAIRDLREDLGIPETLSELGVDeEDIP 346
|
|
| Fe-ADH-like |
cd08185 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
14-350 |
2.82e-05 |
|
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: 45.57 E-value: 2.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 14 GANVIARLGDYLKPMANNWLVVGDK---FVLGFAEEtLRKSLTDAGLSVEIapFSgECSQN----EIDRLRAVAEKSQCG 86
Cdd:cd08185 10 GAGKLNELGEEALRPGKKALIVTGKgssKKTGLLDR-VKKLLEKAGVEVVV--FD-KVEPNplttTVMEGAALAKEEGCD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 87 AVLGIGGGKTLDTAKALAhFMNVP------------------------VAIaPTIASTDAPCSALSVIyTDA------GE 136
Cdd:cd08185 86 FVIGLGGGSSMDAAKAIA-FMATNpgdiwdyifggtgkgpppekalpiIAI-PTTAGTGSEVDPWAVI-TNPetkekkGI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 137 FDRYLLlphnPNMVIVDTQIVAGAPARLLAA-GIgDALATWFEARACSRSGATTMaggkctqaALALaelcyntlieege 215
Cdd:cd08185 163 GHPALF----PKVSIVDPELMLTVPPRVTAYtGF-DALFHAFESYISKNANPFSD--------MLAL------------- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 216 KAM-LAAEQ--HVVT-----PALERVIEANTyLSGVGFESGGLAAAHAI--------HN-----GLTAI-PDAHHY---Y 270
Cdd:cd08185 217 EAIrLVAKYlpRAVKdgsdlEAREKMAWAST-LAGIVIANSGTTLPHGLehplsgyhPNiphgaGLAALyPAYFEFtieK 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 271 HGEK---VAFGTLTQLVLENAPVEEIETVAALCHSVGLPITLAQLDIKQ-DIPAKMRTVAEAScaeGETIHNMPGGATPD 346
Cdd:cd08185 296 APEKfafVARAEASGLSDAKAAEDFIEALRKLLKDIGLDDLLSDLGVTEeDIPWLAENAMETM---GGLFANNPVELTEE 372
|
....
gi 446296183 347 EVYA 350
Cdd:cd08185 373 DIVE 376
|
|
| PDDH |
cd08188 |
1,3-Propanediol (1,3-PD) dehydrogenase; This family includes 1,3-propanediol (1,3-PD) ... |
3-320 |
1.02e-04 |
|
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: 44.04 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 3 RIIQSPGKYIQGANVIARLGDYLKPM-ANNWLVVGDKFV--LGFAEETLrKSLTDAGLSVEIapFSG-----------EC 68
Cdd:cd08188 1 FRFYIPPVNLFGPGCLKEIGDELKKLgGKKALIVTDKGLvkLGLVKKVT-DVLEEAGIEYVI--FDGvqpnptvtnvnEG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 69 SqneidrlrAVAEKSQCGAVLGIGGGKTLDTAKALAHFMN-------------VPVAIAP-----TIASTDAPCSALSVI 130
Cdd:cd08188 78 L--------ELFKENGCDFIISVGGGSAHDCAKAIGILATnggeiedyegvdkSKKPGLPliainTTAGTASEVTRFAVI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 131 yTDAGEfdrylllphNPNMVIVDTQIVA-----------GAPARLLAA-GIgDALATWFEARACsrSGATTMaggkcTQA 198
Cdd:cd08188 150 -TDEER---------HVKMVIVDWNVTPtiavndpelmlGMPPSLTAAtGM-DALTHAIEAYVS--TGATPL-----TDA 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 199 -ALALAELCYNTL---IEEGE-----KAMLAAEqhvvtpalervieantYLSGVGFESGGLAAAHAIHNGLTAIPDAHH- 268
Cdd:cd08188 212 lALEAIRLIAENLpkaVANGKdlearENMAYAQ----------------FLAGMAFNNAGLGYVHAMAHQLGGFYNLPHg 275
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446296183 269 ---------------YYHGEKVA------FGTLTQLVLENAPVEEIETVAALCHSVGLPITLAQLDIKQ-DIPA 320
Cdd:cd08188 276 vcnaillphvmefnlPACPERFAdiaralGENTEGLSDEEAAEAAIEAIRKLSRRVGIPSGLKELGVKEeDFPL 349
|
|
| PPD-like |
cd08181 |
1,3-propanediol dehydrogenase-like (PPD); This family contains proteins similar to 1, ... |
7-120 |
2.81e-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: 42.57 E-value: 2.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 7 SPGKYIQGANVIARLGDYLKPMANNWLVVGDK---FVLGfAEETLRKSLTDAGLS------VEIAPfsgecSQNEIDRLR 77
Cdd:cd08181 3 MPTKVYFGKNCVEKHADELAALGKKALIVTGKhsaKKNG-SLDDVTEALEENGIEyfifdeVEENP-----SIETVEKGA 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 78 AVAEKSQCGAVLGIGGGKTLDTAKALAHFM-----------------NVPVAIAPTIAST 120
Cdd:cd08181 77 ELARKEGADFVIGIGGGSPLDAAKAIALLAankdgdedlfqngkynpPLPIVAIPTTAGT 136
|
|
| PRK15454 |
PRK15454 |
ethanolamine utilization ethanol dehydrogenase EutG; |
48-273 |
3.03e-04 |
|
ethanolamine utilization ethanol dehydrogenase EutG;
Pssm-ID: 185351 [Multi-domain] Cd Length: 395 Bit Score: 42.32 E-value: 3.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 48 LRKSLTDAGLSVEIAPF-SGECSQNEIDRLRAVAEKSQCGAVLGIGGGKTLDTAKALAHFMN------------------ 108
Cdd:PRK15454 69 LTRSLAVKGIAMTLWPCpVGEPCITDVCAAVAQLRESGCDGVIAFGGGSVLDAAKAVALLVTnpdstlaemsetsvlqpr 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 109 VPVAIAPTIASTDAPCSALSVIyTDAGEfDRYLLLPHN---PNMVIVDTQIVAGAPARLLAAGIGDALATWFEARACSRS 185
Cdd:PRK15454 149 LPLIAIPTTAGTGSETTNVTVI-IDAVS-GRKQVLAHAslmPDVAILDAALTEGVPSHVTAMTGIDALTHAIEAYSALNA 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 186 ---------GATTMAGGKCTQAAlalaelcyntlieeGEKAMLAAEQHVVTPALervieantyLSGVGFESGGLAAAHAI 256
Cdd:PRK15454 227 tpftdslaiGAIAMIGKSLPKAV--------------GYGHDLAARESMLLASC---------MAGMAFSSAGLGLCHAM 283
|
250
....*....|....*..
gi 446296183 257 HNGLTAipdAHHYYHGE 273
Cdd:PRK15454 284 AHQPGA---ALHIPHGL 297
|
|
| AAD_C |
cd08178 |
C-terminal alcohol dehydrogenase domain of the acetaldehyde dehydrogenase-alcohol ... |
33-179 |
4.82e-04 |
|
C-terminal alcohol dehydrogenase domain of the acetaldehyde dehydrogenase-alcohol dehydrogenase bifunctional two-domain protein (AAD); This alcohol dehydrogenase domain is located on the C-terminal of a bifunctional two-domain protein. The N-terminal of the protein contains an acetaldehyde-CoA dehydrogenase domain. This protein is involved in pyruvate metabolism whereby pyruvate is converted to acetyl-CoA and formate by pyruvate formate-lysase (PFL). Under anaerobic condition, acetyl-CoA is reduced to acetaldehyde and ethanol by this two-domain protein. Acetyl-CoA is first converted into an enzyme-bound thiohemiacetal by the N-terminal acetaldehyde dehydrogenase domain. The enzyme-bound thiohemiacetal is subsequently reduced by the C-terminal NAD+-dependent alcohol dehydrogenase domain. In E. coli, this protein is called AdhE and has been shown to have pyruvate formate-lyase (PFL) deactivase activity, which leads to the inactivation of PFL, a key enzyme in anaerobic metabolism. In Escherichia coli and Entamoeba histolytica, this enzyme forms homopolymeric peptides composed of more than 20 protomers associated in a helical rod-like structure.
Pssm-ID: 341457 [Multi-domain] Cd Length: 400 Bit Score: 41.79 E-value: 4.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 33 LVVGDK--FVLGFAEEtLRKSLTDAGLSVEIapFSG---ECSQNEIDRLRAVAEKSQCGAVLGIGGGKTLDTAKAL---- 103
Cdd:cd08178 27 FIVTDRvlYKLGYVDK-VLDVLEARGVETEV--FSDvepDPTLSTVRKGLEAMNAFKPDVIIALGGGSAMDAAKIMwlfy 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 104 -----------AHFMNV-------P--------VAIaPTIASTDAPCSALSVIyTDAGEFDRYLLLPHN--PNMVIVDTQ 155
Cdd:cd08178 104 ehpetkfedlaQRFMDIrkrvykfPklgkkaklVAI-PTTSGTGSEVTPFAVI-TDDKTGKKYPLADYAltPDMAIVDPE 181
|
170 180
....*....|....*....|....
gi 446296183 156 IVAGAPARLLAAGIGDALATWFEA 179
Cdd:cd08178 182 LVMTMPKRLTADTGIDALTHAIEA 205
|
|
| 4HBD_NAD |
cd14860 |
4-hydroxybutyrate dehydrogenase, also called gamma-hydroxybutyrate dehydrogenase, catalyzes ... |
65-273 |
5.25e-04 |
|
4-hydroxybutyrate dehydrogenase, also called gamma-hydroxybutyrate dehydrogenase, catalyzes the reduction of succinic simialdehyde to 4-hydroxybutyrate in the succinic degradation pathway; 4-hydroxybutyrate dehydrogenase (4HBD) is an iron-containing (type III) NAD-dependent alcohol dehydrogenase. It plays a role in the succinate metabolism biochemical pathway. It catalyzes the reduction of succinic simialdehide to 4-hydroxybutyrate in the succinate degradation pathway This succinate degradation pathway is present in some bacteria which can use succinate as sole carbon source.
Pssm-ID: 341482 Cd Length: 371 Bit Score: 41.82 E-value: 5.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 65 SGECSQNEIDRLRAVAEKSQCGAVLGIGGGKTLDTAKALAHFMNVPVA----------------IAPTIASTDAPCSALS 128
Cdd:cd14860 59 TGEPSDEMVEAIYKDIKKYGYKRVIAIGGGTVIDIAKLLALKGISPVLdlfdgkiplikekeliIVPTTCGTGSEVTNIS 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296183 129 VIY-----TDAGefdryllLPHN---PNMVIVDTQIVAGAPARLLAAGIGDALATWFEARACSRSGATT-MAGGKCTQAA 199
Cdd:cd14860 139 IVEltslgTKKG-------LAVDelyADKAVLIPELLKGLPYKVFATSSIDALIHAIESYLSPKATPYTeMFSYKAIEMI 211
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446296183 200 LAlaelCYNTLIEEGEKAMLaaeqhvvtPALERVIEANTYlSGVGFESGGLAAAHAIHNGLTAipdAHHYYHGE 273
Cdd:cd14860 212 LE----GYQEIAEKGEEARF--------PLLGDFLIASNY-AGIAFGNAGCAAVHALSYPLGG---KYHVPHGE 269
|
|
| |
