|
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: 676.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 1 MDRIIQSPGKYIQGADVINRLGEYLKPLAERWLVVGDKFVLGFAQSTVEKSFKDAGLVVEIAPFGGECSQNEIDRLRGIA 80
Cdd:PRK09423 1 MDRIFISPSKYVQGKGALARLGEYLKPLGKRALVIADEFVLGIVGDRVEASLKEAGLTVVFEVFNGECSDNEIDRLVAIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 81 ETAQCGAILGIGGGKTLDTAKALAHFMGVPVAIAPTIASTDAPCSALSVIYTDEGEFDRYLLLPNNPNMVIVDTKIVAGA 160
Cdd:PRK09423 81 EENGCDVVIGIGGGKTLDTAKAVADYLGVPVVIVPTIASTDAPTSALSVIYTEEGEFERYLFLPKNPDLVLVDTAIIAKA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 161 PARLLAAGIGDALATWFEARACSRSGATTMAGGKCTQAALALAELCYNTLLEEGEKAMLAAEQHVVTPALERVIEANTYL 240
Cdd:PRK09423 161 PARFLAAGIGDALATWFEARACSRSGGTTMAGGKPTLAALALAELCYETLLEDGLKAKLAVEAKVVTPALENVIEANTLL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 241 SGVGFESGGLAAAHAVHNGLTAIPDAHHYYHGEKVAFGTLTQLVLENAPVEEIETVAALSHAVGLPITLAQLDIKEDVPA 320
Cdd:PRK09423 241 SGLGFESGGLAAAHAIHNGLTALEDTHHLTHGEKVAFGTLTQLVLENRPKEEIEEVIDFCHAVGLPTTLADLGLKEDSDE 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 446296152 321 KMRIVAEAACAEGETIHNMPSGATPDQVYAALLVADQYGQRFLQEW 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: 599.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 8 PGKYIQGADVINRLGEYLKPLAERWLVVGDKFVLGFAQSTVEKSFKDAGLVVEIAPFGGECSQNEIDRLRGIAETAQCGA 87
Cdd:cd08170 1 PSRYVQGPGALDRLGEYLAPLGKKALVIADPFVLDLVGERLEESLEKAGLEVVFEVFGGECSREEIERLAAIARANGADV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 88 ILGIGGGKTLDTAKALAHFMGVPVAIAPTIASTDAPCSALSVIYTDEGEFDRYLLLPNNPNMVIVDTKIVAGAPARLLAA 167
Cdd:cd08170 81 VIGIGGGKTIDTAKAVADYLGLPVVIVPTIASTDAPCSALSVIYTEDGEFDEYLFLPRNPDLVLVDTEIIAKAPVRFLVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 168 GIGDALATWFEARACSRSGATTMAGGKCTQAALALAELCYNTLLEEGEKAMLAAEQHVVTPALERVIEANTYLSGVGFES 247
Cdd:cd08170 161 GMGDALATYFEARACARSGAPNMAGGRPTLAALALAELCYDTLLEYGVAAKAAVEAGVVTPALEAVIEANTLLSGLGFES 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 248 GGLAAAHAVHNGLTAIPDAHHYYHGEKVAFGTLTQLVLENAPVEEIETVAALSHAVGLPITLAQLDIKEDVPAKMRIVAE 327
Cdd:cd08170 241 GGLAAAHAIHNGLTALPETHHLLHGEKVAFGTLVQLVLEGRPDEEIEEVIRFCRSVGLPVTLADLGLEDVTDEELRKVAE 320
|
330 340 350
....*....|....*....|....*....|.
gi 446296152 328 AACAEGETIHNMPSGATPDQVYAALLVADQY 358
Cdd:cd08170 321 AACAPGETIHNMPFPVTPEDVVDAILAADAL 351
|
|
| GldA |
COG0371 |
Glycerol dehydrogenase or related enzyme, iron-containing ADH family [Energy production and ... |
3-355 |
3.38e-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: 496.23 E-value: 3.38e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 3 RIIQSPGKYIQGADVINRLGEYLKPLAERWLVVGDKFVLGFAQSTVEKSFKDAGLVVEIAPFGGECSQNEIDRLRGIAET 82
Cdd:COG0371 1 RVIILPRRYVQGEGALDELGEYLADLGKRALIITGPTALKAAGDRLEESLEDAGIEVEVEVFGGECSEEEIERLAEEAKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 83 AQCGAILGIGGGKTLDTAKALAHFMGVPVAIAPTIASTDAPCSALSVIYTDEGEFDRYLLLPNNPNMVIVDTKIVAGAPA 162
Cdd:COG0371 81 QGADVIIGVGGGKALDTAKAVAYRLGLPVVSVPTIASTDAPASPLSVIYTEDGAFDGYSFLAKNPDLVLVDTDIIAKAPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 163 RLLAAGIGDALATWFEARACSRSGAtTMAGGKCTQAALALAELCYNTLLEEGEKAMLAAEQHVVTPALERVIEANTYLSG 242
Cdd:COG0371 161 RLLAAGIGDALAKWYEARDWSLAHR-DLAGEYYTEAAVALARLCAETLLEYGEAAIKAVEAGVVTPALERVVEANLLLSG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 243 VGF----ESGGLAAAHAVHNGLTAIPDAHHYYHGEKVAFGTLTQLVLENAPvEEIETVAALSHAVGLPITLAQLDIKEDV 318
Cdd:COG0371 240 LAMgigsSRPGSGAAHAIHNGLTALPETHHALHGEKVAFGTLVQLVLEGRP-EEIEELLDFLRSVGLPTTLADLGLDDET 318
|
330 340 350
....*....|....*....|....*....|....*..
gi 446296152 319 PAKMRIVAEAACAEGETIHNMPSGATPDQVYAALLVA 355
Cdd:COG0371 319 EEELLTVAEAARPERYTILNLPFEVTPEAVEAAILAT 355
|
|
| GlyDH-like |
cd08550 |
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins. ... |
8-353 |
1.71e-143 |
|
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: 410.39 E-value: 1.71e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 8 PGKYIQGADVINRLGEYLKPLAERWLVVGDKFVLGFAQSTVEKSFKDAGLVVEIAPFGGECSQNEIDRLRGIAETAQCGA 87
Cdd:cd08550 1 PGRYIQEPGILAKAGEYIAPLGKKALIIGGKTALEAVGEKLEKSLEEAGIDYEVEVFGGECTEENIERLAEKAKEEGADV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 88 ILGIGGGKTLDTAKALAHFMGVPVAIAPTIASTDAPCSALSVIYTDEGEFDRYLLLPNNPNMVIVDTKIVAGAPARLLAA 167
Cdd:cd08550 81 IIGIGGGKVLDTAKAVADRLGLPVVTVPTIAATCAAWSALSVLYDEEGEFLGYSLLKRSPDLVLVDTDIIAAAPVRYLAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 168 GIGDALATWFEARACSRSGATTMAggkcTQAALALAELCYNTLLEEGEKAMLAAEQHVVTPALERVIEANTYLSGVGFES 247
Cdd:cd08550 161 GIGDTLAKWYEARPSSRGGPDDLA----LQAAVQLAKLAYDLLLEYGVQAVEDVRQGKVTPALEDVVDAIILLAGLVGSL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 248 GG----LAAAHAVHNGLTAIPDAHHYYHGEKVAFGTLTQLVLENAPVEEIETVAALSHAVGLPITLAQLDIKEDvPAKMR 323
Cdd:cd08550 237 GGggcrTAAAHAIHNGLTKLPETHGTLHGEKVAFGLLVQLALEGRSEEEIEELIEFLRRLGLPVTLEDLGLELT-EEELR 315
|
330 340 350
....*....|....*....|....*....|
gi 446296152 324 IVAEAACAEGETIHNMPSGATPDQVYAALL 353
Cdd:cd08550 316 KIAEYACDPPDMAHMLPFPVTPEMLAEAIL 345
|
|
| GlyDH-like |
cd08172 |
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins ... |
8-352 |
4.01e-109 |
|
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: 322.93 E-value: 4.01e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 8 PGKYIQGADVINRLGEYLKPL-AERWLVVGDKFVLGFAQSTVEKSFKDAglvVEIAPFGGECSQNEIDRLRGIAETAQCG 86
Cdd:cd08172 1 PQEYICEEGALKELPELLSEFgIKRPLIIHGEKSWQAAKPYLPKLFEIE---YPVLRYDGECSYEEIDRLAEEAKEHQAD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 87 AILGIGGGKTLDTAKALAHFMGVPVAIAPTIASTDAPCSALSVIYTDEGEFDRYLLLPNNPNMVIVDTKIVAGAPARLLA 166
Cdd:cd08172 78 VIIGIGGGKVLDTAKAVADKLNIPLILIPTLASNCAAWTPLSVIYDEDGEFIGYDYFPRSAYLVLVDPRLLLDSPKDYFV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 167 AGIGDALATWFEARACSRSGATTMAggkCTQAALALAELCYNTLLEEGEKAMLAAEQHVVTPALERVIEANTYLSGV--G 244
Cdd:cd08172 158 AGIGDTLAKWYEADAILRQLEELPA---FLQLARQAAKLCRDILLKDSEQALADLEAGKLTPAFIKVVETIIALAGMvgG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 245 F--ESGGLAAAHAVHNGLTAIPDAHHYYHGEKVAFGTLTQLVLENApVEEIETVAALSHAVGLPITLAQLDIKEDVPAKM 322
Cdd:cd08172 235 FgdEYGRSAGAHAIHNGLTKLPETHHFLHGEKVAYGILVQLALEGK-WDEIKKLLPFYRRLGLPTSLADLGLTDDTEEAL 313
|
330 340 350
....*....|....*....|....*....|
gi 446296152 323 RIVAEAACAEGETIHNMPSGATPDQVYAAL 352
Cdd:cd08172 314 QKIAAFAASPEESIHLLPPDVTAEEVLQAI 343
|
|
| GlyDH-like |
cd08171 |
Glycerol dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins ... |
14-353 |
3.30e-77 |
|
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: 241.27 E-value: 3.30e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 14 GADVINRLGEYLKPLAERWLVVGDKFVLGFAQSTVEKSFKDAGL-VVEIAPFGGECSQNEIDRLRGIAETAQCGAILGIG 92
Cdd:cd08171 7 GEDAYDAIPKICSPYGKKVVVIGGKKALAAAKPKLRAALEGSGLeITDFIWYGGEATYENVEKLKANPEVQEADMIFAVG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 93 GGKTLDTAKALAHFMGVPVAIAPTIASTDAPCSALSVIYTDEGEFDRYLLLPNNPNMVIVDTKIVAGAPARLLAAGIGDA 172
Cdd:cd08171 87 GGKAIDTVKVLADRLNKPVFTFPTIASNCAAVTAVSVMYNPDGSFKEYYFLKRPPVHTFIDTEIIAEAPEKYLWAGIGDT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 173 LATWFEARACSRSGATTMAggkcTQAALALAELCYNTLLEEGEKAMLAAEQHVVTPALERVIEANTYLSG-----VGFE- 246
Cdd:cd08171 167 LAKYYEVEFSARGDELDHT----NALGVAISKMCSEPLLKYGVQALEDCRANKVSDALEQVVLDIIVTTGlvsnlVEPDy 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 247 SGGLaaAHAVHNGLTAIPDA-HHYYHGEKVAFGTLTQLVLENApVEEIETVAALSHAVGLPITLAQLDIKEDvpaKMRIV 325
Cdd:cd08171 243 NSSL--AHALYYGLTTLPQIeEEHLHGEVVSYGVLVLLTVDGQ-FEELEKVYAFNKSIGLPTCLADLGLTVE---DLEKV 316
|
330 340
....*....|....*....|....*...
gi 446296152 326 AEAAcAEGETIHNMPSGATPDQVYAALL 353
Cdd:cd08171 317 LDKA-LKTKDLRHSPYPITKEMFEEAIK 343
|
|
| Fe-ADH |
pfam00465 |
Iron-containing alcohol dehydrogenase; |
8-348 |
4.74e-63 |
|
Iron-containing alcohol dehydrogenase;
Pssm-ID: 425696 [Multi-domain] Cd Length: 362 Bit Score: 205.14 E-value: 4.74e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 8 PGKYIQGADVINRLGEYLKPLAERWLVVGDKFVLGFAQ-STVEKSFKDAGLVVEIAP-FGGECSQNEIDRLRGIAETAQC 85
Cdd:pfam00465 1 PTRIVFGAGALAELGEELKRLGARALIVTDPGSLKSGLlDKVLASLEEAGIEVVVFDgVEPEPTLEEVDEAAALAREAGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 86 GAILGIGGGKTLDTAKALAHFMG------------------VPVAIAPTIASTDAPCSALSVIYTDEGEFDRYLLLPN-N 146
Cdd:pfam00465 81 DVIIAVGGGSVIDTAKAIALLLTnpgdvwdylggkpltkpaLPLIAIPTTAGTGSEVTPLAVITDTETGEKLGIFSPKlL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 147 PNMVIVDTKIVAGAPARLLAAGIGDALATWFEARACSRSGATTMAggkCTQAALALAELCYNTLLEEGEKAmlaaeqhvv 226
Cdd:pfam00465 161 PDLAILDPELTLTLPPRLTAATGMDALAHAVEAYVSKGANPLTDA---LALEAIRLIAENLPRAVADGEDL--------- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 227 tPALERVIEANTyLSGVGFESGGLAAAHAVHNGLTAIPDAHH-YYHGEKVAFGT----------LTQLVL-------ENA 288
Cdd:pfam00465 229 -EARENMLLAST-LAGLAFSNAGLGAAHALAHALGGRYGIPHgLANAILLPYVLrfnapaapekLAQLARalgedsdEEA 306
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 289 PVEEIETVAALSHAVGLPITLAQLDIKEDvpaKMRIVAEAACAEGeTIHNMPSGATPDQV 348
Cdd:pfam00465 307 AEEAIEALRELLRELGLPTTLSELGVTEE---DLDALAEAALRDR-SLANNPRPLTAEDI 362
|
|
| PRK10586 |
PRK10586 |
putative oxidoreductase; Provisional |
3-360 |
5.01e-53 |
|
putative oxidoreductase; Provisional
Pssm-ID: 182570 Cd Length: 362 Bit Score: 179.15 E-value: 5.01e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 3 RIIQSPGKYIQGADVINRLGEYLKPLA-ERWLVVGDKFVLGFAQSTVEKSFKDAGLVVeiAPFGGECSQNEIDRLrgiae 81
Cdd:PRK10586 7 RVVVGPANYFSHPGSIDHLHDFFTDEQlSRAVWIYGERAIAAAQPYLPPAFELPGAKH--ILFRGHCSESDVAQL----- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 82 TAQCG----AILGIGGGKTLDTAKALAHFMGVPVAIAPTIASTDAPCSALSVIYTDEGEFDRYLLLPNNPNMVIVDTKIV 157
Cdd:PRK10586 80 AAASGddrqVVIGVGGGALLDTAKALARRLGLPFVAIPTIAATCAAWTPLSVWYNDAGQALHFEIFDDANFLVLVEPRII 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 158 AGAPARLLAAGIGDALATWFEARACSRSGAT---TMAGGkcTQAALALAelcyNTLLEEGEKAMLAAEQHVVTPALERVI 234
Cdd:PRK10586 160 LNAPQEYLLAGIGDTLAKWYEAVVLAPQPETlplTVRLG--INNALAIR----DVLLNSSEQALADQQNGQLTQDFCDVV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 235 EAntYLSGVGFeSGGL-------AAAHAVHNGLTAIPDAHHYYHGEKVAFGTLTQLVLenapVEEIETVAALSHA---VG 304
Cdd:PRK10586 234 DA--IIAGGGM-VGGLgerytrvAAAHAVHNGLTVLPQTEKFLHGTKVAYGILVQSAL----LGQDDVLAQLIGAyqrFH 306
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 446296152 305 LPITLAQLDIKEDVPAKMRIVAEAACAEGETIHNMPSGATPDQVYAALLVADQYGQ 360
Cdd:PRK10586 307 LPTTLAELDVDINNQAEIDRVIAHTLRPVESIHYLPVTLTPDTLRAAFEKVESFKA 362
|
|
| DHQ_Fe-ADH |
cd07766 |
Dehydroquinate synthase-like (DHQ-like) and iron-containing alcohol dehydrogenases (Fe-ADH); ... |
8-330 |
8.41e-51 |
|
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: 170.62 E-value: 8.41e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 8 PGKYIQGADVINRLGEYLKPLAERWLVVGDKFVLGFAQSTVEKSFKdAGLVVEIAPF-GGECSQNEIDRLRGIAETAQCG 86
Cdd:cd07766 1 PTRIVFGEGAIAKLGEIKRRGFDRALVVSDEGVVKGVGEKVADSLK-KGLAVAIFDFvGENPTFEEVKNAVERARAAEAD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 87 AILGIGGGKTLDTAKALAH--FMGVPVAIAPTIASTDAPCSALSVIYTDEGEFdRYLLLPNNPNMVIVDTKIVAGAPARL 164
Cdd:cd07766 80 AVIAVGGGSTLDTAKAVAAllNRGIPFIIVPTTASTDSEVSPKSVITDKGGKN-KQVGPHYNPDVVFVDTDITKGLPPRQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 165 LAAGIGDALATWFEaracsrsgattmaggkctqaalalaelcyntlleegekamlaaeqhvvtpaLERVIEANTYLSGVG 244
Cdd:cd07766 159 VASGGVDALAHAVE---------------------------------------------------LEKVVEAATLAGMGL 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 245 FESGGLAAAHAVHNGLTAipdAHHYYHGEKVAFGTLTQLVLENAPVEE----IETVAALSHAVGLPITLAQLDI-KEDVP 319
Cdd:cd07766 188 FESPGLGLAHAIGHALTA---FEGIPHGEAVAVGLPYVLKVANDMNPEpeaaIEAVFKFLEDLGLPTHLADLGVsKEDIP 264
|
330
....*....|.
gi 446296152 320 AkmriVAEAAC 330
Cdd:cd07766 265 K----LAEKAL 271
|
|
| G1PDH-like |
cd08174 |
Glycerol-1-phosphate dehydrogenase-like; These glycerol-1-phosphate dehydrogenase-like ... |
14-317 |
3.61e-27 |
|
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: 109.53 E-value: 3.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 14 GADVINRLGEYLKPL---AERWLVVGDKFVLGFAQSTVEKSFKDAGLVVEIapfggecSQNEIDRLRGIAETAQCG---- 86
Cdd:cd08174 7 EEGALEHLGKYLADRnqgFGKVAIVTGEGIDELLGEDILESLEEAGEIVTV-------EENTDNSAEELAEKAFSLpkvd 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 87 AILGIGGGKTLDTAKALAHFMGVPVAIAPTIASTDAPCSALSVIYTDEGefdRYLLLPNNPNMVIVDTKIVAGAPARLLA 166
Cdd:cd08174 80 AIVGIGGGKVLDVAKYAAFLSKLPFISVPTSLSNDGIASPVAVLKVDGK---RKSLGAKMPYGVIVDLDVIKSAPRRLIL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 167 AGIGD------ALATW-FEARAcsrsGATTMAGgkctqAALALAELCYNTLLEEGEKAMLAAEqhvvtpALERVIEANTy 239
Cdd:cd08174 157 AGIGDlisnitALYDWkLAEEK----GGEPVDD-----FAYLLSRTAADSLLNTPGKDIKDDE------FLKELAESLV- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 240 LSGVGFE--------SGglaaahAVHNGLTAIpDAHH---YYHGEKVAFGTLTQLVLENAPVEEIETVAalsHAVGLPIT 308
Cdd:cd08174 221 LSGIAMEiagssrpaSG------SEHLISHAL-DKLFpgpALHGIQVGLGTYFMSFLQGQRYEEIRDVL---KRTGFPLN 290
|
....*....
gi 446296152 309 LAQLDIKED 317
Cdd:cd08174 291 PSDLGLTKE 299
|
|
| Gro1PDH |
cd08173 |
Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) catalyzes the reversible conversion between ... |
14-317 |
8.13e-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: 100.32 E-value: 8.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 14 GADVINRLGEYLKPLAE--RWLVVGDKFVLGFAQSTVEKSFKDAGLVVEIAPFGGECSQNEIDRLRGIAETAQCGAILGI 91
Cdd:cd08173 8 GHGAINKIGEVLKKLLLgkRALIITGPNTYKIAGKRVEDLLESSGVEVVIVDIATIEEAAEVEKVKKLIKESKADFIIGV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 92 GGGKTLDTAKALAHFMGVPVAIAPTIASTDAPCSALSVIYTDEGefdRYLLLPNNPNMVIVDTKIVAGAPARLLAAGIGD 171
Cdd:cd08173 88 GGGKVIDVAKYAAYKLNLPFISIPTSASHDGIASPFASIKGGDK---PYSIKAKAPIAIIADTEIISKAPKRLLAAGCGD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 172 ALAT------WFEARacsrsgatTMAGGKCTQAALALAELCYNTLLEEGEKAMLAAEQHVVTpalerVIEAnTYLSGVgf 245
Cdd:cd08173 165 LISNitavkdWRLAH--------RLKGEYYSEYAASLALMSAKLIIENADLIKPGLEEGVRT-----VVKA-LISSGV-- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 246 eSGGLAA------------AHAVH-----NGLtaipdahhyyHGEKVAFGTLTQLVLENAPVEEIetVAALsHAVGLPIT 308
Cdd:cd08173 229 -AMSIAGssrpasgsehlfSHALDklapgPAL----------HGEQCGVGTIMMAYLHGGDWKEI--REAL-KKIGAPTT 294
|
....*....
gi 446296152 309 LAQLDIKED 317
Cdd:cd08173 295 AKELGLDKE 303
|
|
| egsA |
PRK00843 |
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed |
3-171 |
2.44e-23 |
|
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed
Pssm-ID: 179139 Cd Length: 350 Bit Score: 99.20 E-value: 2.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 3 RIIQSPGKYIQGADVINRLGEYLKPLA--ERWLVVGDKFVLGFAQSTVEKSFKDAGLVVEIapFGGECSQNEIDRLRGIA 80
Cdd:PRK00843 6 HWIQLPRDVVVGHGVLDDIGDVCSDLKltGRALIVTGPTTKKIAGDRVEENLEDAGDVEVV--IVDEATMEEVEKVEEKA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 81 ETAQCGAILGIGGGKTLDTAKALAHFMGVPVAIAPTIASTDAPCSALSVIYTDEGefdRYLLLPNNPNMVIVDTKIVAGA 160
Cdd:PRK00843 84 KDVNAGFLIGVGGGKVIDVAKLAAYRLGIPFISVPTAASHDGIASPRASIKGGGK---PVSVKAKPPLAVIADTEIIAKA 160
|
170
....*....|.
gi 446296152 161 PARLLAAGIGD 171
Cdd:PRK00843 161 PYRLLAAGCGD 171
|
|
| Fe-ADH_2 |
pfam13685 |
Iron-containing alcohol dehydrogenase; |
14-276 |
7.20e-21 |
|
Iron-containing alcohol dehydrogenase;
Pssm-ID: 404557 [Multi-domain] Cd Length: 251 Bit Score: 90.44 E-value: 7.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 14 GADVINRLGEYLKPLA-ERWLVVGDKFVLGFAQSTVEKSFKDAGLVVEIAPF-GGECSQNEIDRLRGIAETAQCGAILGI 91
Cdd:pfam13685 3 GPGALGRLGEYLAELGfRRVALVADANTYAAAGRKVAESLKRAGIEVETRLEvAGNADMETAEKLVGALRERDADAVVGV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 92 GGGKTLDTAKALAHFMGVPVAIAPTIASTDAPCSALSVIYTDeGEFDRYLLLPnnPNMVIVDTKIVAGAPARLLAAGIGD 171
Cdd:pfam13685 83 GGGTVIDLAKYAAFKLGKPFISVPTAASNDGFASPGASLTVD-GKKRSIPAAA--PFGVIADTDVIAAAPRRLLASGVGD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 172 ALATWfEARACSRSGATTMAGGKCTQAALALAELCYNTLLEEGEKamlaaeqhvvTPALERVIEANTyLSGVGFESGGLA 251
Cdd:pfam13685 160 LLAKI-TAVADWELAHAEEVAAPLALLSAAMVMNFADRPLRDPGD----------IEALAELLSALA-MGGAGSSRPASG 227
|
250 260
....*....|....*....|....*
gi 446296152 252 AAHAVHNGLTAIPDAHHyYHGEKVA 276
Cdd:pfam13685 228 SEHLISHALDMIAPKQA-LHGEQVG 251
|
|
| Fe-ADH |
cd08551 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains large ... |
8-350 |
7.52e-21 |
|
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: 92.51 E-value: 7.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 8 PGKYIQGADVINRLGEYLKPL-AERWLVVGDKFV--LGFAQsTVEKSFKDAGLVVEIapFGG---ECSQNEIDRLRGIAE 81
Cdd:cd08551 1 PTRIVFGAGALARLGEELKALgGKKVLLVTDPGLvkAGLLD-KVLESLKAAGIEVEV--FDDvepNPTVETVEAAAELAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 82 TAQCGAILGIGGGKTLDTAKALAHFM------------------GVPVAIAPTIASTDAPCSALSVIyTDEGE------F 137
Cdd:cd08551 78 EEGADLVIAVGGGSVLDTAKAIAVLAtnggsirdyegigkvpkpGLPLIAIPTTAGTGSEVTPNAVI-TDPETgrkmgiV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 138 DRYLLlpnnPNMVIVDTKIVAGAPARLLAA-GIgDALATWFEArACSRsGATTMaggkcTQA-ALALAELCYNTL----- 210
Cdd:cd08551 157 SPYLL----PDVAILDPELTLSLPPSVTAAtGM-DALTHAIEA-YTSK-KANPI-----SDAlALEAIRLIGKNLrrava 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 211 ----LEEGEKAMLAAeqhvvtpalervieantYLSGVGFESGGLAAAHAVHNGLTAIPDAHH-------------YY--- 270
Cdd:cd08551 225 dgsdLEAREAMLLAS-----------------LLAGIAFGNAGLGAVHALAYPLGGRYHIPHgvanaillpyvmeFNlpa 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 271 HGEK-----VAFGTLTQLVLENAPVEE-IETVAALSHAVGLPITLAQLDIK-EDVPAkmriVAEAACAEGETIHNMPSGA 343
Cdd:cd08551 288 CPEKyaeiaEALGEDVEGLSDEEAAEAaVEAVRELLRDLGIPTSLSELGVTeEDIPE----LAEDAMKSGRLLSNNPRPL 363
|
....*..
gi 446296152 344 TPDQVYA 350
Cdd:cd08551 364 TEEDIRE 370
|
|
| EutG |
COG1454 |
Alcohol dehydrogenase, class IV [Energy production and conversion]; |
1-355 |
8.10e-21 |
|
Alcohol dehydrogenase, class IV [Energy production and conversion];
Pssm-ID: 441063 [Multi-domain] Cd Length: 381 Bit Score: 92.49 E-value: 8.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 1 MDRIIQSPGKYIQGADVINRLGEYLKPL-AERWLVVGDKFV--LGFAQsTVEKSFKDAGLVVEIapFGG---ECSQNEID 74
Cdd:COG1454 1 MMFTFRLPTRIVFGAGALAELGEELKRLgAKRALIVTDPGLakLGLLD-RVLDALEAAGIEVVV--FDDvepNPTVETVE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 75 RLRGIAETAQCGAILGIGGGKTLDTAKALA----------HFMGVP---------VAIaPTIASTDAPCSALSVIYTDEG 135
Cdd:COG1454 78 AGAAAAREFGADVVIALGGGSAIDAAKAIAllatnpgdleDYLGIKkvpgpplplIAI-PTTAGTGSEVTPFAVITDPET 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 136 E-----FDRYLLlpnnPNMVIVDTKIVAGAPARLLAA-GIgDALATWFEArACSRsGATTMAggkctqAALALA--ELCY 207
Cdd:COG1454 157 GvkkgiADPELL----PDVAILDPELTLTLPPSLTAAtGM-DALTHAIEA-YVSK-GANPLT------DALALEaiRLIA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 208 NTL---------LEEGEKAMLAAeqhvvtpalervieantYLSGVGFESGGLAAAHAVHNGLTAIPDAHH---------- 268
Cdd:COG1454 224 RNLpravadgddLEAREKMALAS-----------------LLAGMAFANAGLGAVHALAHPLGGLFHVPHglanaillph 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 269 ---YY---HGEKVA-----FGTLTQLVLENAPVEEIETVAALSHAVGLPITLAQLDIKE-DVPAkmriVAEAACAEGETI 336
Cdd:COG1454 287 vlrFNapaAPERYAeiaraLGLDVGLSDEEAAEALIEAIRELLRDLGIPTRLSELGVTEeDLPE----LAELALADRCLA 362
|
410
....*....|....*....
gi 446296152 337 HNmPSGATPDQVYAALLVA 355
Cdd:COG1454 363 NN-PRPLTEEDIEAILRAA 380
|
|
| G1PDH_related |
cd08549 |
Glycerol-1-phosphate dehydrogenase and related proteins; This family contains bacterial and ... |
8-318 |
4.73e-20 |
|
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: 89.55 E-value: 4.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 8 PGKYIQGADVINRLGEYLK-PLAERWLVVGDKFVLGFAQSTVEKSFKDAGLVVeiapfggecSQNEIDRLRGIAETAQ-C 85
Cdd:cd08549 1 PRYTIVGDGAINKIEEILKkLNLKRVLIITGKNTKAKYCRFFYDQLKTVCDIV---------YYDNIDNLEDELKKYTfY 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 86 GAILGIGGGKTLDTAKALAHFMGVPVAIAPTIASTDAPCS-ALSVIYTDEgefdRYLLLPNNPNMVIVDTKIVAGAPARL 164
Cdd:cd08549 72 DCVIGIGGGRSIDTGKYLAYKLKIPFISVPTSASNDGIASpIVSLRIPGV----KKTFMADAPIAIIADTEIIKKSPRRL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 165 LAAGIGD------ALATW-FEARacsrsgattMAGGKCTQAALALAELCYNTLLEEGEKAMLAAEQHvvtpaleRVIEAN 237
Cdd:cd08549 148 LSAGIGDlvsnitAVLDWkLAHK---------EKGEKYSEFAAILSKTSAKELVSYVLKASDLEEYH-------RVLVKA 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 238 TYLSGVGFESGGLA--AAHAVHNGLTAIPDAHHYY------HGEKVAFGTLTQLVL------ENAPVEE-IETVAALsha 302
Cdd:cd08549 212 LVGSGIAMAIAGSSrpASGSEHLFSHALDKLKEEYlninvlHGEQVGVGTIIMSYLhekenkKLSGLHErIKMILKK--- 288
|
330
....*....|....*.
gi 446296152 303 VGLPITLAQLDIKEDV 318
Cdd:cd08549 289 VGAPTTAKQLGIDEDL 304
|
|
| Fe-ADH-like |
cd14863 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
14-323 |
5.92e-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: 87.21 E-value: 5.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 14 GADVINRLGEYLKPL-AERWLVVGDKFV--LGFAQsTVEKSFKDAGLVV----EIAPfggECSQNEIDRLRGIAETAQCG 86
Cdd:cd14863 11 GAGAVEQIGELLKELgCKKVLLVTDKGLkkAGIVD-KIIDLLEEAGIEVvvfdDVEP---DPPDEIVDEAAEIAREEGAD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 87 AILGIGGGKTLDTAKALA-----------HFMGVPVAIA--------PTIASTDAPCSALSVIYTDEGEFDRYLLLPN-N 146
Cdd:cd14863 87 GVIGIGGGSVLDTAKAIAvlltnpgpiidYALAGPPVPKpgipliaiPTTAGTGSEVTPIAVITDEENGVKKSLLGPFlV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 147 PNMVIVDTKIVAGAPARLLAA-GIgDALATWFEARACSRSGATTMAggKCTQAalalAELCYNTL---------LEEGEK 216
Cdd:cd14863 167 PDLAILDPELTVGLPPSLTAAtGM-DALSHAIEAYTSKLANPMTDA--LALQA----IRLIVKNLpravkdgdnLEAREN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 217 AMLAAeqhvvtpalervieantYLSGVGFESGGLAAAHAVHNGLTAIpdaHHYYHGEKVAFGTLTqlVLENAPVEEIETV 296
Cdd:cd14863 240 MLLAS-----------------NLAGIAFNNAGTHIGHAIAHALGAL---YHIPHGLACALALPV--VLEFNAEAYPEKV 297
|
330 340
....*....|....*....|....*...
gi 446296152 297 AALSHAVGLPIT-LAQLDIKEDVPAKMR 323
Cdd:cd14863 298 KKIAKALGVSFPgESDEELGEAVADAIR 325
|
|
| Fe-ADH-like |
cd14864 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
8-329 |
1.28e-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: 341486 [Multi-domain] Cd Length: 376 Bit Score: 83.12 E-value: 1.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 8 PGKYIQGADVINRLGEYLKPLAERWLVVGDKFVLGF-AQSTVEKSFKDAGlvVEIAPF---GGECSQNEIDRLRGIAETA 83
Cdd:cd14864 4 PPNIVFGADSLERIGEEVKEYGSRFLLITDPVLKESgLADKIVSSLEKAG--ISVIVFdeiPASATSDTIDEAAELARKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 84 QCGAILGIGGGKTLDTAKALA----------HFMG--------VPVAIAPTIASTDAPCSAlSVIYTDEGEFDRYLL--L 143
Cdd:cd14864 82 GADGIIAVGGGKVLDTAKAVAilanndggayDFLEgakpkkkpLPLIAVPTTPRSGFEFSD-RFPVVDSRSREVKLLkaQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 144 PNNPNMVIVDTKIVAGAPARLLAAGIGDALATWFEARACSRSG-ATTMAGGKctqaALALAelcyntlleeGEKAMLAAE 222
Cdd:cd14864 161 PGLPKAVIVDPNLMASLTGNQTAAMALAALALAVEAYLSKKSNfFSDALALK----AIELV----------SENLDGALA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 223 QHVVTPALERVIEANtYLSGVGFESGGL----AAAHAVhNGLTAIPDAH-------HY--YHGEKVAFGTLTQLVLENAP 289
Cdd:cd14864 227 DPKNTPAEELLAQAG-CLAGLAASSSSPglatALALAV-NSRYKVSKSLvasillpHVieYAATSAPDKYAKIARALGED 304
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 446296152 290 VEEIETVAALSHAV----------GLPITLAQLDIKEDVPAKMRIVAEAA 329
Cdd:cd14864 305 VEGASPEEAAIAAVegvrrliaqlNLPTRLKDLDLASSLEQLAAIAEDAP 354
|
|
| Fe-ADH-like |
cd08196 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
5-352 |
3.65e-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: 341475 [Multi-domain] Cd Length: 367 Bit Score: 78.77 E-value: 3.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 5 IQSPGKYIQGADVINRLGEYLKPLA-ERWLVVGDKFvlgFAQSTVEKSFKDAGLVVEIAPFGG---ECSQNEIDRLRGIA 80
Cdd:cd08196 3 YYQPVKIIFGEGILKELPDIIKELGgKRGLLVTDPS---FIKSGLAKRIVESLKGRIVAVFSDvepNPTVENVDKCARLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 81 ETAQCGAILGIGGGKTLDTAKALA----------HFM---------GVPVAIAPTIASTDAPCSALSVIyTDEGEFDRYL 141
Cdd:cd08196 80 RENGADFVIAIGGGSVLDTAKAAAclaktdgsieDYLegkkkipkkGLPLIAIPTTAGTGSEVTPVAVL-TDKEKGKKAP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 142 LlpNNPNM----VIVDTKIVAGAPARLLAA-GIgDALATWFEArACSRSgattmAGGKCTQAALALAELCYNTLL---EE 213
Cdd:cd08196 159 L--VSPGFypdiAIVDPELTYSMPPKVTAStGI-DALCHAIEA-YWSIN-----HQPISDALALEAAKLVLENLEkayNN 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 214 GEKAmlaaeqhvvtPALERVIEANTyLSGVGFESGGLAAAHAVHNGLTAIpdaHHYYHGEKVAFgTLTQLVLENAPVEE- 292
Cdd:cd08196 230 PNDK----------EAREKMALASL-LAGLAFSQTRTTASHACSYPLTSH---FGIPHGEACAL-TLPSFIRLNAEALPg 294
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446296152 293 -----------------IETVAALSHAVGLPITLAQLDIKEDvpaKMRIVAEAACAEgETIHNMPSGATPDQVYAAL 352
Cdd:cd08196 295 rldelakqlgfkdaeelADKIEELKKRIGLRTRLSELGITEE---DLEEIVEESFHP-NRANNNPVEVTKEDLEKLL 367
|
|
| BDH |
cd08187 |
Butanol dehydrogenase catalyzes the conversion of butyraldehyde to butanol with the cofactor ... |
4-337 |
4.03e-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: 4.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 4 IIQSPGKYIQGADVINRLGEYLKPLAERWLVV-GDKFV--LG-FAQstVEKSFKDAGlvVEIAPFGGECSQNEIDRLRGI 79
Cdd:cd08187 3 TFYNPTKIIFGKGAIEELGEEIKKYGKKVLLVyGGGSIkkNGlYDR--VVASLKEAG--IEVVEFGGVEPNPRLETVREG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 80 AETA---QCGAILGIGGGKTLDTAKALA-----------HFMG-------VPVAIAPTIASTDAPCSALSVIYTDEGEFD 138
Cdd:cd08187 79 IELAreeNVDFILAVGGGSVIDAAKAIAagakydgdvwdFFTGkappekaLPVGTVLTLAATGSEMNGGAVITNEETKEK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 139 RYLLLP-NNPNMVIVDTKIVAGAPARLLAAGIGDALATWFEaracsrsgaTTMAGGKCTQAALALAELCYNTLLEEGEKA 217
Cdd:cd08187 159 LGFGSPlLRPKFSILDPELTYTLPKYQTAAGIVDIFSHVLE---------QYFTGTEDAPLQDRLAEGLLRTVIENGPKA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 218 -------------MLAAEQhvvtpalervieANTYLSGVGFESGglAAAHAVHNGLTAIPDAHH-------------YYH 271
Cdd:cd08187 230 lkdpddyearanlMWAATL------------ALNGLLGAGRGGD--WATHAIEHELSALYDITHgaglaivfpawmrYVL 295
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446296152 272 GEKVA----FGTLTQLVLENAPVEEI--ETVAALS---HAVGLPITLAQLDIKEDVPAKMrivAEAACAEGETIH 337
Cdd:cd08187 296 KKKPErfaqFARRVFGIDPGGDDEETalEGIEALEeffKSIGLPTTLSELGIDEEDIEEM---AEKAVRGGGLGG 367
|
|
| G1PDH |
cd08175 |
Glycerol-1-phosphate dehydrogenase (G1PDH) catalyzes the reversible reduction of ... |
14-317 |
1.65e-13 |
|
Glycerol-1-phosphate dehydrogenase (G1PDH) catalyzes the reversible reduction of dihydroxyacetone phosphate (DHAP) to glycerol-1-phosphate (G1P) in an NADH-dependent manner; Glycerol-1-phosphate dehydrogenase (G1PDH) plays a role in the synthesis of phosphoglycerolipids in Gram-positive bacterial species. It catalyzes the reversibly reduction of dihydroxyacetone phosphate (DHAP) to glycerol-1-phosphate (G1P) in a NADH-dependent manner. Its activity requires a Ni++ ion. In Bacillus subtilis, it has been described as AraM gene in L-arabinose (ara) operon. AraM protein forms homodimer.
Pssm-ID: 341454 Cd Length: 340 Bit Score: 70.62 E-value: 1.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 14 GADVINRLGEYLKPL--AERWLVVGDKFVLGFAQSTVEKSFKDAGLVVEIAPFGGE--------CSQNEIDRLRgiaetA 83
Cdd:cd08175 7 GEGALKKLPEYLKELfgGKKVLVVADENTYAAAGEEVEAALEEAGVTVCLLIFPGEgdliadeaAVGKVLLELE-----K 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 84 QCGAILGIGGGkTL-DTAKALAHFMGVPVAIAPTIASTDAPCSALSVIytdegefdryllLPNN---------PNMVIVD 153
Cdd:cd08175 82 DTDLIIAVGSG-TInDLTKYAAYKLGIPYISVPTAPSMDGYTSSGAPI------------IVDGvkktfpahaPKAIFAD 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 154 TKIVAGAPARLLAAGIGD------ALATWFEARAcsrsgattmAGGK--CTQAAlalaelcynTLLEEGEKAMLAAEQHV 225
Cdd:cd08175 149 LDVLANAPQRMIAAGFGDllgkytALADWKLSHL---------LGGEyyCPEVA---------DLVQEALEKCLDNAEGI 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 226 VT---PALERVIEANTyLSGVGFE--------SGglaAAH---------AVHNGLTAIpdahhyYHGEKVAFGTLTQL-- 283
Cdd:cd08175 211 AArdpEAIEALMEALI-LSGLAMQlvgnsrpaSG---AEHhlshywemeFLRLGKPPV------LHGEKVGVGTLLIAal 280
|
330 340 350
....*....|....*....|....*....|....*.
gi 446296152 284 -VLENAP-VEEIEtvaALSHAVGLPITLAQLDIKED 317
Cdd:cd08175 281 yILEQLPpPEELR---ELLRKAGAPTTPEDLGIDRD 313
|
|
| Fe-ADH-like |
cd14862 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
7-329 |
1.63e-12 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341484 [Multi-domain] Cd Length: 375 Bit Score: 68.02 E-value: 1.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 7 SPGKYIQGADVINRLGEYLKplaERWLVVGDKFV--LGFAQSTVEKsFKDAGLVVEIapFGG---ECSQNEIDRLRGIAE 81
Cdd:cd14862 5 SSPKIVFGEDALSHLEQLSG---KRALIVTDKVLvkLGLLKKVLKR-LLQAGFEVEV--FDEvepEPPLETVLKGAEAMR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 82 TAQCGAILGIGGGKTLDTAKALAHFMGVP---------------------VAIaPTIASTDAPCSALSVIyTDEGEFdRY 140
Cdd:cd14862 79 EFEPDLIIALGGGSVMDAAKAAWVLYERPdldpedispldllglrkkaklIAI-PTTSGTGSEATWAIVL-TDTEEP-RK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 141 LLLPNN---PNMVIVDTKIVAGAPARLLAA-GIgDALATWFEARACSRSgaTTMAGGKCTQAalalAELCYNTLleegek 216
Cdd:cd14862 156 IAVANPelvPDVAILDPEFVLGMPPKLTAGtGL-DALAHAVEAYLSTWS--NDFSDALALKA----IELIFKYL------ 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 217 aMLAAEQHVVTPALERVIEANTyLSGVGFESGGLAAAHAVHNGLTAIPDAHH--------------YYHGEKVAFGTLTQ 282
Cdd:cd14862 223 -PRAYKDGDDLEAREKMHNAAT-IAGLAFGNSQAGLAHALGHSLGAVFHVPHgiavglflpyviefYAKVTDERYDLLKL 300
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 446296152 283 LVLENAPVEE-----IETVAALSHAVGLPITLAQLDI-KEDVPAKMRIVAEAA 329
Cdd:cd14862 301 LGIEARDEEEalkklVEAIRELYKEVGQPLSIKDLGIsEEEFEEKLDELVEYA 353
|
|
| Fe-ADH-like |
cd08183 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
8-329 |
8.19e-12 |
|
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: 65.99 E-value: 8.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 8 PGKYIQGADVINRLGEYLKPLAERWLVV-GDKFVLGFAQSTVEKSFKDAGLVVEIAPFGGECSQNEIDRLRGIAETAQCG 86
Cdd:cd08183 1 PPRIVFGRGSLQELGELAAELGKRALLVtGRSSLRSGRLARLLEALEAAGIEVALFSVSGEPTVETVDAAVALAREAGCD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 87 AILGIGGGKTLDTAKALA----------------------HFMGVPVAIAPTIASTDAPCSALSVIYTDEGEF-----DR 139
Cdd:cd08183 81 VVIAIGGGSVIDAAKAIAalltnegsvldylevvgkgrplTEPPLPFIAIPTTAGTGSEVTKNAVLSSPEHGVkvslrSP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 140 YLLlpnnPNMVIVDTKIVAGAPARLLAAGIGDALATWFEARACSRSGATT----MAGgkCTQAALALAELCYN-TLLEEG 214
Cdd:cd08183 161 SML----PDVALVDPELTLSLPPEVTAASGLDALTQLIEPYVSRKANPLTdalaREG--LRLAARSLRRAYEDgEDLEAR 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 215 EKAMLAAeqhvvtpalervieantYLSGVGFESGGLAAAH---AVHNGLTAIP------------------------DAH 267
Cdd:cd08183 235 EDMALAS-----------------LLGGLALANAGLGAVHglaGPLGGMFGAPhgaicaallppvleanlralrerePDS 297
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446296152 268 HYYHGEKVAFGTLTQlvLENAPVEE-IETVAALSHAVGLPiTLAQLDIK-EDVPAkmrIVAEAA 329
Cdd:cd08183 298 PALARYRELAGILTG--DPDAAAEDgVEWLEELCEELGIP-RLSEYGLTeEDFPE---IVEKAR 355
|
|
| Fe-ADH-like |
cd14865 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
6-355 |
2.71e-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: 341487 [Multi-domain] Cd Length: 383 Bit Score: 64.10 E-value: 2.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 6 QSPGKYIQGADVINRLGEYLKPL-AERWLVVGDKFV--LGFAQsTVEKSFKDAGLVVEIapFGgECSQNE----IDRLRG 78
Cdd:cd14865 4 FNPTKIVSGAGALENLPAELARLgARRPLIVTDKGLaaAGLLK-KVEDALGDAIEIVGV--FD-DVPPDSsvavVNEAAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 79 IAETAQCGAILGIGGGKTLDTAKA-----------LAHFMG--------VPVAIAPTIASTDAPCSALSVIYTDEG---- 135
Cdd:cd14865 80 RAREAGADGIIAVGGGSVIDTAKGvnillseggddLDDYGGanrltrplKPLIAIPTTAGTGSEVTLVAVIKDEEKkvkl 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 136 EF-DRYLLlpnnPNMVIVDTKIVAGAPARLLAAGIGDALATWFEARACSRSGATTmaggkctqAALALA--ELCYNTLL- 211
Cdd:cd14865 160 LFvSPFLL----PDVAILDPRLTLSLPPKLTAATGMDALTHAIEAYTSLQKNPIS--------DALALQaiRLISENLPk 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 212 -------EEGEKAMLAAeqhvvtpalervieanTYLSGVGFESGGLAAAHAV-HngltAIPDAHHYYHGekVAFGTLTQL 283
Cdd:cd14865 228 avkngkdLEARLALAIA----------------ATMAGIAFSNSMVGLVHAIaH----AVGAVAGVPHG--LANSILLPH 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 284 VLE------------------------NAPVEE-----IETVAALSHAVGLPITLAQLDIKEDvpaKMRIVAEAACAEGE 334
Cdd:cd14865 286 VMRynldaaaeryaelalalaygvtpaGRRAEEaieaaIDLVRRLHELCGLPTRLRDVGVPEE---QLEAIAELALNDGA 362
|
410 420
....*....|....*....|.
gi 446296152 335 TIHNmPSGATPDQVYAALLVA 355
Cdd:cd14865 363 ILFN-PREVDPEDILAILEAA 382
|
|
| Fe-ADH-like |
cd08194 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
8-173 |
1.42e-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: 62.16 E-value: 1.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 8 PGKYIQGADVINRLGEYLKPL-AERWLVVGDKFV--LGFAQsTVEKSFKDAGLVVEI-APFGGECSQNEIDRLRGIAETA 83
Cdd:cd08194 1 PRTIIIGGGALEELGEEAASLgGKRALIVTDKVMvkLGLVD-KVTQLLAEAGIAYAVfDDVVSEPTDEMVEEGLALYKEG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 84 QCGAILGIGGGKTLDTAKA----------LAHFMG--------VPVAIAPTIASTDAPCSALSVIyTDEgEFDRYLLLPN 145
Cdd:cd08194 80 GCDFIVALGGGSPIDTAKAiavlatnggpIRDYMGprkvdkpgLPLIAIPTTAGTGSEVTRFTVI-TDT-ETDVKMLLKG 157
|
170 180 190
....*....|....*....|....*....|..
gi 446296152 146 ---NPNMVIVDTKIVAGAPARLLAA-GIgDAL 173
Cdd:cd08194 158 palLPAVAIVDPELTLSMPPRVTAAtGI-DAL 188
|
|
| LPO |
cd08176 |
Lactadehyde:propanediol oxidoreductase (LPO) catalyzes the interconversion between ... |
83-331 |
1.33e-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: 59.10 E-value: 1.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 83 AQCGAILGIGGGKTLDTAKAL----AH-------FMGV-------PVAIA-PTIASTDAPCSALSVIyTDEGEFDRYLLL 143
Cdd:cd08176 84 SGADGIIAVGGGSSIDTAKAIgiivANpgadvrsLEGVaptknpaVPIIAvPTTAGTGSEVTINYVI-TDTEKKRKFVCV 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 144 -PN-NPNMVIVDTKIVAGAPARLLAA-GIgDALATWFEARAcSRsGATTMAGGKCTQA----ALALAELCYNTLLEEGEK 216
Cdd:cd08176 163 dPHdIPTVAIVDPDLMSSMPKGLTAAtGM-DALTHAIEGYI-TK-GAWELSDMLALKAieliAKNLRKAVANPNNVEARE 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 217 AMLAAEqhvvtpalervieantYLSGVGFESGGLAAAHAVHNGLTAIPDAHH-------------Y---YHGEK-----V 275
Cdd:cd08176 240 NMALAQ----------------YIAGMAFSNVGLGIVHSMAHPLSAFYDTPHgvanaillpyvmeFnapATGEKyrdiaR 303
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 446296152 276 AFG-TLTQLVLENAPVEEIETVAALSHAVGLPITLAQLDIKE-DVPAkmriVAEAACA 331
Cdd:cd08176 304 AMGvDTTGMSDEEAAEAAVDAVKKLSKDVGIPQKLSELGVKEeDIEA----LAEDALN 357
|
|
| Fe-ADH-like |
cd14861 |
Iron-containing alcohol dehydrogenases-like; This family contains proteins similar to ... |
14-329 |
1.68e-09 |
|
Iron-containing alcohol dehydrogenases-like; This family contains proteins similar to iron-containing alcohol dehydrogenase (Fe-ADH), most of which have not been characterized. Their specific function is unknown. The protein structure represents a dehydroquinate synthase-like fold and belongs to the alcohol dehydrogenase-like superfamily. It is distinct from other alcohol dehydrogenases which contain different protein domains. Alcohol dehydrogenase catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions.
Pssm-ID: 341483 [Multi-domain] Cd Length: 374 Bit Score: 58.68 E-value: 1.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 14 GADVINRLGEYLKPL-AERWLVVGDKFV--LGFAQSTVEkSFKDAGLVVEIapFGGEcSQNEIDR--LRGIAE--TAQCG 86
Cdd:cd14861 9 GAGAIAELPEELKALgIRRPLLVTDPGLaaLGIVDRVLE-ALGAAGLSPAV--FSDV-PPNPTEAdvEAGVAAyrEGGCD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 87 AILGIGGGKTLDTAKA----------LAHF-----------MGVPVAIA-PTIASTDAPCSALSVIYTDEGE-----FDR 139
Cdd:cd14861 85 GIIALGGGSAIDAAKAialmathpgpLWDYedgeggpaaitPAVPPLIAiPTTAGTGSEVGRAAVITDDDTGrkkiiFSP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 140 YLLlpnnPNMVIVDTKIVAGAPARLLAA-GIgDALATWFEarACSRSGATTMAGGkctqAALALAELCYNTLleegEKAM 218
Cdd:cd14861 165 KLL----PKVAICDPELTLGLPPRLTAAtGM-DALTHCIE--AYLSPGFHPMADG----IALEGLRLISEWL----PRAV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 219 -----LAAEQHVVTPALErvieantylSGVGFESgGLAAAHAVHNGLTAIPDAHHyyhgekvafGTLTQLVLE-----NA 288
Cdd:cd14861 230 adgsdLEARGEMMMAALM---------GAVAFQK-GLGAVHALAHALGALYGLHH---------GLLNAILLPyvlrfNR 290
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446296152 289 PVEE--------------------IETVAALSHAVGLPITLAQLDIKEDVPAkmRIVAEAA 329
Cdd:cd14861 291 PAVEdklarlaralglglggfddfIAWVEDLNERLGLPATLSELGVTEDDLD--ELAELAL 349
|
|
| PRK10624 |
PRK10624 |
L-1,2-propanediol oxidoreductase; Provisional |
33-332 |
3.24e-09 |
|
L-1,2-propanediol oxidoreductase; Provisional
Pssm-ID: 182595 [Multi-domain] Cd Length: 382 Bit Score: 57.70 E-value: 3.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 33 LVVGDKFVLGF-AQSTVEKSFKDAGLVVEIapFGGECSQNEIDRLR-GIAETAQCGA--ILGIGGGKTLDTAKALA---- 104
Cdd:PRK10624 34 LIVTDKTLVKCgVVAKVTDVLDAAGLAYEI--YDGVKPNPTIEVVKeGVEVFKASGAdyLIAIGGGSPQDTCKAIGiisn 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 105 ----------------HFMGVPVAIAPTIASTDAPCSALSVIyTDEGEFDRYLLL-PNN-PNMVIVDTKIVAGAPARLLA 166
Cdd:PRK10624 112 npefadvrslegvaptKKPSVPIIAIPTTAGTAAEVTINYVI-TDEEKRRKFVCVdPHDiPQVAFVDADMMDSMPPGLKA 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 167 AGIGDALATWFEaracsrsgattmagGKCTQAALALAELCYNTLLE--------------EGEKAMLAAEqhvvtpaler 232
Cdd:PRK10624 191 ATGVDALTHAIE--------------GYITRGAWALTDMLHLKAIEiiagalrgavagdkEAGEGMALGQ---------- 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 233 vieantYLSGVGFESGGLAAAHAVHNGLTAIPDAHH-------------Y---YHGEK-----VAFGTLTQ-LVLENAPV 290
Cdd:PRK10624 247 ------YIAGMGFSNVGLGLVHGMAHPLGAFYNTPHgvanaillphvmeYnadFTGEKyrdiaRAMGVKVEgMSLEEARN 320
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 446296152 291 EEIETVAALSHAVGLPITLAQLDIK-EDVPAkmriVAEAACAE 332
Cdd:PRK10624 321 AAVEAVKALNRDVGIPPHLRDVGVKeEDIPA----LAQAAFDD 359
|
|
| Fe-ADH-like |
cd08191 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
7-340 |
5.31e-09 |
|
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contain different protein domain. Proteins of this family have not been characterized.
Pssm-ID: 341470 [Multi-domain] Cd Length: 392 Bit Score: 57.24 E-value: 5.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 7 SPGKYIQGADVINRLGEYLKPLAERWLVVGDKFVL---GFAQstVEKSFKDAGLVVEIapFGGECsqnEIDRLRGIAETA 83
Cdd:cd08191 3 SPSRLLFGPGARRALGRVAARLGSRVLIVTDPRLAstpLVAE--LLAALTAAGVAVEV--FDGGQ---PELPVSTVADAA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 84 QCGA------ILGIGGGKTLDTAKALA----------HFMG--------VPVAIAPTIASTDAPCSALSVIYTDE----- 134
Cdd:cd08191 76 AAARafdpdvVIGLGGGSNMDLAKVVAlllahggdprDYYGedrvpgpvLPLIAVPTTAGTGSEVTPVAVLTDPArgmkv 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 135 GEFDRYLLlpnnPNMVIVDTKIVAGAPARLLA-AGIgDALATWFEA------RACSRSGATTMAGGK---CTQAALALAE 204
Cdd:cd08191 156 GVSSPYLR----PAVAIVDPELTLTCPPGVTAdSGI-DALTHAIESytardfPPFPRLDPDPVYVGKnplTDLLALEAIR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 205 LCYNTLLEegekamlAAEQHVVTPALERVIEANTyLSGVGFESGGLAAAHAVHNGLTAipdAHHYYHGEKV--------- 275
Cdd:cd08191 231 LIGRHLPR-------AVRDGDDLEARSGMALAAL-LAGLAFGTAGTAAAHALQYPIGA---LTHTSHGVGNglllpyvmr 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 276 ---------------AFGTLTQLVLENAPVEEIETVAALSHAVGLPITLAQLDIKE-DVPAkmriVAEAACAEGETIHNM 339
Cdd:cd08191 300 fnrparaaelaeiarALGVTTAGTSEEAADRAIERVEELLARIGIPTTLADLGVTEaDLPG----LAEKALSVTRLIANN 375
|
.
gi 446296152 340 P 340
Cdd:cd08191 376 P 376
|
|
| HEPD |
cd08182 |
Hydroxyethylphosphoate dehydrogenase (HEPD) catalyzes the reduction of phosphonoacetaldehyde ... |
8-179 |
1.33e-08 |
|
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: 56.08 E-value: 1.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 8 PGKYIQGADVINRLGEYLKPL-AERWLVVGDKfvLGFAQSTVEKSFKDAGLVVEIAPFGGECSQNEIDRL-RGIAETAQC 85
Cdd:cd08182 1 PVKIIFGPGALAELKDLLGGLgARRVLLVTGP--SAVRESGAADILDALGGRIPVVVFSDFSPNPDLEDLeRGIELFRES 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 86 G--AILGIGGGKTLDTAKALAHFMGVP---------------------VAIaPTIASTDAPCSALSVIYtDEGEFDRY-L 141
Cdd:cd08182 79 GpdVIIAVGGGSVIDTAKAIAALLGSPgenllllrtgekapeenalplIAI-PTTAGTGSEVTPFATIW-DEAEGKKYsL 156
|
170 180 190
....*....|....*....|....*....|....*....
gi 446296152 142 LLPNN-PNMVIVDTKIVAGAPARLLAAGIGDALATWFEA 179
Cdd:cd08182 157 AHPSLyPDAAILDPELTLSLPLYLTASTGLDALSHAIES 195
|
|
| Fe-ADH-like |
cd08189 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
12-328 |
1.75e-07 |
|
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: 52.47 E-value: 1.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 12 IQGADVINRLGEYLKPLA-ERWLVVGDKFV--LGFAQSTVEkSFKDAGLVVEIapFGG-------ECSQNEIDRLRgiae 81
Cdd:cd08189 9 FEGAGSLLQLPEALKKLGiKRVLIVTDKGLvkLGLLDPLLD-ALKKAGIEYVV--FDGvvpdptiDNVEEGLALYK---- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 82 TAQCGAILGIGGGKTLDTAKALA-----------HFMGV-------PVAIA-PTIASTDAPCSALSVIyTDEGEFDRYLL 142
Cdd:cd08189 82 ENGCDAIIAIGGGSVIDCAKVIAaraanpkksvrKLKGLlkvrkklPPLIAvPTTAGTGSEATIAAVI-TDPETHEKYAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 143 LPNN--PNMVIVDTKIVAGAPARLLAA-GIgDALATWFEAR-ACSRSGATTMAGGKCTQAALALAELCYN--TLLEEGEK 216
Cdd:cd08189 161 NDPKliPDAAVLDPELTLGLPPAITAAtGM-DALTHAVEAYiSRSATKETDEYALEAVKLIFENLPKAYEdgSDLEAREN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 217 AMLAAeqhvvtpalervieantYLSGVGFESGGLAAAHAV-HN--GLTAIPdaHHY-----------YHGEKVA-----F 277
Cdd:cd08189 240 MLLAS-----------------YYAGLAFTRAYVGYVHAIaHQlgGLYGVP--HGLanavvlphvleFYGPAAEkrlaeL 300
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 446296152 278 GTLTQLVLENAPVEE-----IETVAALSHAVGLPITLAQLDiKEDVP--AKmRIVAEA 328
Cdd:cd08189 301 ADAAGLGDSGESDSEkaeafIAAIRELNRRMGIPTTLEELK-EEDIPeiAK-RALKEA 356
|
|
| HVD |
cd08193 |
5-hydroxyvalerate dehydrogenase (HVD) catalyzes the oxidation of 5-hydroxyvalerate to ... |
6-329 |
2.85e-07 |
|
5-hydroxyvalerate dehydrogenase (HVD) catalyzes the oxidation of 5-hydroxyvalerate to 5-oxovalerate with NAD+ as cofactor; 5-hydroxyvalerate dehydrogenase (HVD) is an iron-containing (type III) NAD-dependent alcohol dehydrogenase. It plays a role in the cyclopentanol metabolism biochemical pathway. It catalyzes the oxidation of 5-hydroxyvalerate to 5-oxovalerate with NAD+ as cofactor. This cyclopentanol (cpn) degradation pathway is present in some bacteria which can use cyclopentanol as sole carbon source. In Comamonas sp. strain NCIMB 9872, this enzyme is encoded by the CpnD gene.
Pssm-ID: 341472 [Multi-domain] Cd Length: 379 Bit Score: 51.74 E-value: 2.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 6 QSPGKYIQGADVINRLGEYLKPL-AERWLVVGDKFV--LGFAQsTVEKSFKDAGLVVEIapFGG---ECSQNEIDRLRGI 79
Cdd:cd08193 2 QTVPRIICGAGAAARLGELLRELgARRVLLVTDPGLvkAGLAD-PALAALEAAGIAVTV--FDDvvaDPPEAVVEAAVEQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 80 AETAQCGAILGIGGGKTLDTAK----------ALAHFMGV--------PVAIAPTIASTDAPCSALSVIYTDEGE----F 137
Cdd:cd08193 79 AREAGADGVIGFGGGSSMDVAKlvallagsdqPLDDIYGVgkatgprlPLILVPTTAGTGSEVTPISIVTTGETEkkgvV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 138 DRYLLlpnnPNMVIVDTKIVAGAPARLLAA-GIgDALATWFEARAcSRSGATTMAGGKCTQaalALAELCYN--TLLEEG 214
Cdd:cd08193 159 SPQLL----PDVALLDAELTLGLPPHVTAAtGI-DAMVHAIEAYT-SRHKKNPISDALARE---ALRLLGANlrRAVEDG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 215 EKamLAAEQHVVTPALervieantyLSGVGFESGGLAAAHAVhngltAIPDAHHYyhgeKVAFGTLTQLVLE-----NAP 289
Cdd:cd08193 230 SD--LEAREAMLLGSM---------LAGQAFANAPVAAVHAL-----AYPLGGHF----HVPHGLSNALVLPhvlrfNLP 289
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446296152 290 VEE--------------------------IETVAALSHAVGLPITLAQLDIKEDVPAKMrivAEAA 329
Cdd:cd08193 290 AAEalyaelarallpglafgsdaaaaeafIDALEELVEASGLPTRLRDVGVTEEDLPML---AEDA 352
|
|
| PDDH |
cd08188 |
1,3-Propanediol (1,3-PD) dehydrogenase; This family includes 1,3-propanediol (1,3-PD) ... |
3-348 |
5.68e-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: 50.98 E-value: 5.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 3 RIIQSPGKYIQGADVINRLGEYLKPL-AERWLVVGDKFV--LGFAQStVEKSFKDAGLVVEIapFGG-------ECSQNE 72
Cdd:cd08188 1 FRFYIPPVNLFGPGCLKEIGDELKKLgGKKALIVTDKGLvkLGLVKK-VTDVLEEAGIEYVI--FDGvqpnptvTNVNEG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 73 IDRLRGiaetAQCGAILGIGGGKTLDTAKALAHFM------------------GVP-VAIaPTIASTDAPCSALSVIyTD 133
Cdd:cd08188 78 LELFKE----NGCDFIISVGGGSAHDCAKAIGILAtnggeiedyegvdkskkpGLPlIAI-NTTAGTASEVTRFAVI-TD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 134 EGefdrylllpNNPNMVIVDTKIVA-----------GAPARLLAA-GIgDALATWFEARACsrSGATTMaggkcTQaALA 201
Cdd:cd08188 152 EE---------RHVKMVIVDWNVTPtiavndpelmlGMPPSLTAAtGM-DALTHAIEAYVS--TGATPL-----TD-ALA 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 202 LaelcyntlleegeKAMLAAEQHvvtpaLERV------IEANT------YLSGVGFESGGLAAAHAVHNGLTAIPDAHH- 268
Cdd:cd08188 214 L-------------EAIRLIAEN-----LPKAvangkdLEAREnmayaqFLAGMAFNNAGLGYVHAMAHQLGGFYNLPHg 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 269 ---------------YYHGEKVA------FGTLTQLVLENAPVEEIETVAALSHAVGLPITLAQLDIK-EDVPAkmriVA 326
Cdd:cd08188 276 vcnaillphvmefnlPACPERFAdiaralGENTEGLSDEEAAEAAIEAIRKLSRRVGIPSGLKELGVKeEDFPL----LA 351
|
410 420
....*....|....*....|..
gi 446296152 327 EAACAEGETIHNmPSGATPDQV 348
Cdd:cd08188 352 ENALKDACGPTN-PRQATKEDV 372
|
|
| NADPH_BDH |
cd08179 |
NADPH-dependent butanol dehydrogenase involved in the butanol and ethanol formation pathway in ... |
88-338 |
1.10e-06 |
|
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: 49.88 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 88 ILGIGGGKTLDTAKALAHF--------------MGVP--------VAIaPTIASTDAPCSALSVIyTDEGEFDRYLLLPN 145
Cdd:cd08179 85 IIAIGGGSVIDAAKAMWVFyeypeltfedalvpFPLPelrkkarfIAI-PSTSGTGSEVTRASVI-TDTEKGIKYPLASF 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 146 N--PNMVIVDTKIVAGAPARLLAAGIGDALATWFEARACSRsgATTMaggkcTQA-ALALAELCYNTLLE--EGEKAMLA 220
Cdd:cd08179 163 EitPDVAILDPELTMTMPPHVTANTGMDALTHAIEAYVSTL--ANDF-----TDAlALGAILDIFENLPKsyNGGKDLEA 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 221 AEQ-HVVtpalervieanTYLSGVGFESGGLAAAHAV-HngltAIPDAHHYYHGEKVAFgtLTQLVLE-NAPVEE----- 292
Cdd:cd08179 236 REKmHNA-----------SCLAGMAFSNSGLGIVHSMaH----KGGAFFGIPHGLANAI--LLPYVIEfNSKDPEarary 298
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446296152 293 ----------------IETVAALSHAVGLPITLAQLDIKEDV-PAKMRIVAEAACAEGETIHN 338
Cdd:cd08179 299 aalligltdeelvedlIEAIEELNKKLGIPLSFKEAGIDEDEfFAKLDEMAENAMNDACTGTN 361
|
|
| Fe-ADH_KdnB-like |
cd08184 |
Iron-containing alcohol dehydrogenase similar to Shewanella oneidensis KdnB required for Kdo8N ... |
8-268 |
1.65e-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: 46.11 E-value: 1.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 8 PGKYIQGADVINRLGEYLKPLAERwlvvGDKFVLGFaqstVEKSFKDAGLVVEIAPFGG----------ECSQNEIDRLR 77
Cdd:cd08184 1 VPKYLFGRGSFDQLGELLAERRKS----NNDYVVFF----IDDVFKGKPLLDRLPLQNGdllifvdttdEPKTDQIDALR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 78 GIAETAQCG---AILGIGGGKTLDTAKALAHFM------------------GVPVAIAPTIASTDAPCSALSV------- 129
Cdd:cd08184 73 AQIRAENDKlpaAVVGIGGGSTMDIAKAVSNMLtnpgsaadyqgwdlvknpGIYKIGVPTLSGTGAEASRTAVltgpekk 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 130 --IYTDEGEFDRylllpnnpnmVIVDTKIVAGAPARLLAAGIGDALATWFEARACSRSGATTMAGGkctQAALalaELCY 207
Cdd:cd08184 153 lgINSDYTVFDQ----------VILDPELIATVPRDQYFYTGMDCYIHCVESLNGTYRNAFGDAYA---EKAL---ELCR 216
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446296152 208 NTLLEEGEKAMLAAEQHVVTpalervieanTYLSGVGFESGGLAAAHAVHNGLTAIPDAHH 268
Cdd:cd08184 217 DVFLSDDMMSPENREKLMVA----------SYLGGSSIANSQVGVCHALSYGLSVVLGTHH 267
|
|
| PPD-like |
cd08181 |
1,3-propanediol dehydrogenase-like (PPD); This family contains proteins similar to 1, ... |
7-178 |
1.82e-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: 46.04 E-value: 1.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 7 SPGKYIQGADVINRLGEYLKPLAERWLVVGDK---FVLGfAQSTVEKSFKDAGLV------VEIAPfggecSQNEIDRLR 77
Cdd:cd08181 3 MPTKVYFGKNCVEKHADELAALGKKALIVTGKhsaKKNG-SLDDVTEALEENGIEyfifdeVEENP-----SIETVEKGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 78 GIAETAQCGAILGIGGGKTLDTAKALAHFM-----------------GVPVAIAPTIASTDAPCSALSVIYTDEGEFDRY 140
Cdd:cd08181 77 ELARKEGADFVIGIGGGSPLDAAKAIALLAankdgdedlfqngkynpPLPIVAIPTTAGTGSEVTPYSILTDHEKGTKKS 156
|
170 180 190
....*....|....*....|....*....|....*....
gi 446296152 141 LLLPNN-PNMVIVDTKIVAGAPARLLAAGIGDALATWFE 178
Cdd:cd08181 157 FGNPLIfPKLALLDPKYTLSLPEELTIDTAVDALSHAIE 195
|
|
| Fe-ADH-like |
cd08185 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
14-317 |
8.16e-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: 44.03 E-value: 8.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 14 GADVINRLGEYLKPLAERWLVV--GDKFVLGFAQSTVEKSFKDAGlvVEIAPFGgECSQN----EIDRLRGIAETAQCGA 87
Cdd:cd08185 10 GAGKLNELGEEALRPGKKALIVtgKGSSKKTGLLDRVKKLLEKAG--VEVVVFD-KVEPNplttTVMEGAALAKEEGCDF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 88 ILGIGGGKTLDTAKALAHFMGVP-----------------------VAIaPTIASTDAPCSALSVIyTDE------GEFD 138
Cdd:cd08185 87 VIGLGGGSSMDAAKAIAFMATNPgdiwdyifggtgkgpppekalpiIAI-PTTAGTGSEVDPWAVI-TNPetkekkGIGH 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 139 RYLLlpnnPNMVIVDTKIVAGAPARLLAA-GIgDALATWFEARACSRSGATTMaggkctqaALALaelcyntlleegeKA 217
Cdd:cd08185 165 PALF----PKVSIVDPELMLTVPPRVTAYtGF-DALFHAFESYISKNANPFSD--------MLAL-------------EA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 218 M-LAAEQ--HVVT-----PALERVIEANTyLSGVGFESGGLAAAHA------------VHN-GLTAI-PDAHHY---YHG 272
Cdd:cd08185 219 IrLVAKYlpRAVKdgsdlEAREKMAWAST-LAGIVIANSGTTLPHGlehplsgyhpniPHGaGLAALyPAYFEFtieKAP 297
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 446296152 273 EK---VAFGTLTQLVLENAPVEEIETVAALSHAVGLPITLAQLDIKED 317
Cdd:cd08185 298 EKfafVARAEASGLSDAKAAEDFIEALRKLLKDIGLDDLLSDLGVTEE 345
|
|
| Fe-ADH-like |
cd17814 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
11-179 |
1.22e-04 |
|
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: 43.69 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 11 YIQGADVINRLGEYLKPL-AERWLVVGDKFVL--GFAQStVEKSFKDAGLVVEIapFGGEcSQN----EIDRLRGIAETA 83
Cdd:cd17814 7 FIFGVGARKLAGRYAKNLgARKVLVVTDPGVIkaGWVDE-VLDSLEAEGLEYVV--FSDV-TPNprdfEVMEGAELYREE 82
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 84 QCGAILGIGGGKTLDTAKALA----------HFMGV--------PVAIAPTIASTDAPCSALSVIyTDEGEFDRYLLLPN 145
Cdd:cd17814 83 GCDGIVAVGGGSPIDCAKGIGivvsngghilDYEGVdkvrrplpPLICIPTTAGSSADVSQFAII-TDTERRVKMAIISK 161
|
170 180 190
....*....|....*....|....*....|....*.
gi 446296152 146 N--PNMVIVDTKIVAGAPARLLAAGIGDALATWFEA 179
Cdd:cd17814 162 TlvPDVSLIDPETLTTMDPELTACTGMDALTHAIEA 197
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| HOT |
cd08190 |
Hydroxyacid-oxoacid transhydrogenase (HOT) involved in gamma-hydroxybutyrate metabolism; This ... |
14-320 |
4.61e-04 |
|
Hydroxyacid-oxoacid transhydrogenase (HOT) involved in gamma-hydroxybutyrate metabolism; This family contains hydroxyacid-oxoacid transhydrogenase (HOT), also known as D-2-hydroxyglutarate transhydrogenase. It catalyzes the conversion of gamma-hydroxybutyrate (GHB) to succinic semialdehyde (SSA), coupled to the stoichiometric conversion of alpha-ketoglutarate to D-2-hydroxyglutarate in gamma-Hydroxybutyrate catabolism. Unlike many other alcohols, which are oxidized by NAD-linked dehydrogenases, gamma-hydroxybutyrate is metabolized to succinate semialdehyde by hydroxyacid-oxoacid transhydrogenase which does not require free NAD or NADP; instead, it uses alpha-ketoglutarate as an acceptor, converting it to d-2-hydroxyglutarate. Alpha-ketoglutarate serves as an intermediate acceptor to regenerate NAD(P) required for the oxidation of GHB. HOT also catalyzes the reversible oxidation of a hydroxyacid obligatorily coupled to the reduction of an oxoacid, and requires no cofactor. In mammals, the HOT enzyme is located in mitochondria, and is expressed with an N-terminal mitochondrial targeting sequence. HOT enzyme is member of the metal-containing alcohol dehydrogenase family. It typically contains an iron although other metal ions may be used.
Pssm-ID: 341469 [Multi-domain] Cd Length: 412 Bit Score: 41.76 E-value: 4.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 14 GADVINRLGEYLKPL-AERWLVVGDKFVLGFAQ-STVEKSFKDAGLVVEIapFGG---ECSQNEIDRLRGIAETAQCGAI 88
Cdd:cd08190 7 GPGATRELGMDLKRLgAKKVLVVTDPGLAKLGLvERVLESLEKAGIEVVV--YDGvrvEPTDESFEEAIEFAKEGDFDAF 84
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 89 LGIGGGKTLDTAKAL-------AHFM---------GVPVA------IA-PTIASTDAPCSALSVI-YTDE----GEFDRY 140
Cdd:cd08190 85 VAVGGGSVIDTAKAAnlyathpGDFLdyvnapigkGKPVPgplkplIAiPTTAGTGSETTGVAIFdLEELkvktGISSRY 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 141 LLlpnnPNMVIVDTKIVAGAPARLLAAGIGDAL--------ATWFEARACSRSGATTMAGGKCTQAALALA----ELCYN 208
Cdd:cd08190 165 LR----PTLAIVDPLLTLTLPPRVTASSGFDVLchalesytARPYNARPRPANPDERPAYQGSNPISDVWAekaiELIGK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446296152 209 TL---------LEEGEKAMLAAeqhvvtpalervieantYLSGVGFESGGLAAAHA--------VHNGLTA--IPDAHHY 269
Cdd:cd08190 241 YLrravndgddLEARSNMLLAS-----------------TLAGIGFGNAGVHLPHAmaypiaglVKDYRPPgyPVDHPHV 303
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446296152 270 YHGEKVA-----------------FGTLTQLV---LENAPVEEI-----ETVAALSHAVGLPITLAQLDIKE-DVPA 320
Cdd:cd08190 304 PHGLSVAltapavfrftapacperHLEAAELLgadTSGASDRDAgevlaDALIKLMRDIGIPNGLSALGYSEdDIPA 380
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