|
Name |
Accession |
Description |
Interval |
E-value |
| gldA |
PRK09423 |
glycerol dehydrogenase; Provisional |
2-367 |
0e+00 |
|
glycerol dehydrogenase; Provisional
Pssm-ID: 181843 Cd Length: 366 Bit Score: 594.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 2 SEKVFISPDKYVQGKNVIDKTGEYVKPLGHTALVIADKLVWEIAADRVVKSLEQADITAIKVEFQGEASKNEVNRIADEG 81
Cdd:PRK09423 1 MDRIFISPSKYVQGKGALARLGEYLKPLGKRALVIADEFVLGIVGDRVEASLKEAGLTVVFEVFNGECSDNEIDRLVAIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 82 RSGQVDIVIGVGGGKTLDTAKAVNELLGSSVVIVPTTASTDAPTSALSVLYTDEGAFDTYTFFSKNPSLILVDTKVISQA 161
Cdd:PRK09423 81 EENGCDVVIGIGGGKTLDTAKAVADYLGVPVVIVPTIASTDAPTSALSVIYTEEGEFERYLFLPKNPDLVLVDTAIIAKA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 162 PPLFLSSGIADAMATWIEARAVIEARATTMAGGLPTLAAEAIASKCEEVLFDYGLQAYESVKRKVVTPALEAVVEANTLL 241
Cdd:PRK09423 161 PARFLAAGIGDALATWFEARACSRSGGTTMAGGKPTLAALALAELCYETLLEDGLKAKLAVEAKVVTPALENVIEANTLL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 242 SGLGFESGGLAGAHAIHNGFTVLEgDIHHLTHGQKVAFGTLVQLALEKRPLTEVERYIDFYLKLDLPVTLEDIKLQDASR 321
Cdd:PRK09423 241 SGLGFESGGLAAAHAIHNGLTALE-DTHHLTHGEKVAFGTLTQLVLENRPKEEIEEVIDFCHAVGLPTTLADLGLKEDSD 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 515237560 322 EDLYRVAQAATKEGETAHNLPFAVTADDVLDAILAADQYSVAYKTK 367
Cdd:PRK09423 320 EELRKVAEAACAEGETIHNMPFKVTPEDVAAAILAADAYGQRYKQE 365
|
|
| GlyDH |
cd08170 |
Glycerol dehydrogenases (GlyDH) catalyzes oxidation of glycerol to dihydroxyacetone in ... |
9-360 |
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: 551.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 9 PDKYVQGKNVIDKTGEYVKPLGHTALVIADKLVWEIAADRVVKSLEQADITAIKVEFQGEASKNEVNRIADEGRSGQVDI 88
Cdd:cd08170 1 PSRYVQGPGALDRLGEYLAPLGKKALVIADPFVLDLVGERLEESLEKAGLEVVFEVFGGECSREEIERLAAIARANGADV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 89 VIGVGGGKTLDTAKAVNELLGSSVVIVPTTASTDAPTSALSVLYTDEGAFDTYTFFSKNPSLILVDTKVISQAPPLFLSS 168
Cdd:cd08170 81 VIGIGGGKTIDTAKAVADYLGLPVVIVPTIASTDAPCSALSVIYTEDGEFDEYLFLPRNPDLVLVDTEIIAKAPVRFLVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 169 GIADAMATWIEARAVIEARATTMAGGLPTLAAEAIASKCEEVLFDYGLQAYESVKRKVVTPALEAVVEANTLLSGLGFES 248
Cdd:cd08170 161 GMGDALATYFEARACARSGAPNMAGGRPTLAALALAELCYDTLLEYGVAAKAAVEAGVVTPALEAVIEANTLLSGLGFES 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 249 GGLAGAHAIHNGFTVLEGDiHHLTHGQKVAFGTLVQLALEKRPLTEVERYIDFYLKLDLPVTLEDIKLQDASREDLYRVA 328
Cdd:cd08170 241 GGLAAAHAIHNGLTALPET-HHLLHGEKVAFGTLVQLVLEGRPDEEIEEVIRFCRSVGLPVTLADLGLEDVTDEELRKVA 319
|
330 340 350
....*....|....*....|....*....|..
gi 515237560 329 QAATKEGETAHNLPFAVTADDVLDAILAADQY 360
Cdd:cd08170 320 EAACAPGETIHNMPFPVTPEDVVDAILAADAL 351
|
|
| GldA |
COG0371 |
Glycerol dehydrogenase or related enzyme, iron-containing ADH family [Energy production and ... |
4-357 |
5.80e-164 |
|
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: 462.71 E-value: 5.80e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 4 KVFISPDKYVQGKNVIDKTGEYVKPLGHTALVIADKLVWEIAADRVVKSLEQADITAIKVEFQGEASKNEVNRIADEGRS 83
Cdd:COG0371 1 RVIILPRRYVQGEGALDELGEYLADLGKRALIITGPTALKAAGDRLEESLEDAGIEVEVEVFGGECSEEEIERLAEEAKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 84 GQVDIVIGVGGGKTLDTAKAVNELLGSSVVIVPTTASTDAPTSALSVLYTDEGAFDTYTFFSKNPSLILVDTKVISQAPP 163
Cdd:COG0371 81 QGADVIIGVGGGKALDTAKAVAYRLGLPVVSVPTIASTDAPASPLSVIYTEDGAFDGYSFLAKNPDLVLVDTDIIAKAPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 164 LFLSSGIADAMATWIEARAVIEARAtTMAGGLPTLAAEAIASKCEEVLFDYGLQAYESVKRKVVTPALEAVVEANTLLSG 243
Cdd:COG0371 161 RLLAAGIGDALAKWYEARDWSLAHR-DLAGEYYTEAAVALARLCAETLLEYGEAAIKAVEAGVVTPALERVVEANLLLSG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 244 LGF----ESGGLAGAHAIHNGFTVLEgDIHHLTHGQKVAFGTLVQLALEKRPlTEVERYIDFYLKLDLPVTLEDIKLQDA 319
Cdd:COG0371 240 LAMgigsSRPGSGAAHAIHNGLTALP-ETHHALHGEKVAFGTLVQLVLEGRP-EEIEELLDFLRSVGLPTTLADLGLDDE 317
|
330 340 350
....*....|....*....|....*....|....*...
gi 515237560 320 SREDLYRVAQAATKEGETAHNLPFAVTADDVLDAILAA 357
Cdd:COG0371 318 TEEELLTVAEAARPERYTILNLPFEVTPEAVEAAILAT 355
|
|
| GlyDH-like |
cd08550 |
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins. ... |
9-357 |
3.18e-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: 410.00 E-value: 3.18e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 9 PDKYVQGKNVIDKTGEYVKPLGHTALVIADKLVWEIAADRVVKSLEQADITAIKVEFQGEASKNEVNRIADEGRSGQVDI 88
Cdd:cd08550 1 PGRYIQEPGILAKAGEYIAPLGKKALIIGGKTALEAVGEKLEKSLEEAGIDYEVEVFGGECTEENIERLAEKAKEEGADV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 89 VIGVGGGKTLDTAKAVNELLGSSVVIVPTTASTDAPTSALSVLYTDEGAFDTYTFFSKNPSLILVDTKVISQAPPLFLSS 168
Cdd:cd08550 81 IIGIGGGKVLDTAKAVADRLGLPVVTVPTIAATCAAWSALSVLYDEEGEFLGYSLLKRSPDLVLVDTDIIAAAPVRYLAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 169 GIADAMATWIEARAVIEArattMAGGLPTLAAEAIASKCEEVLFDYGLQAYESVKRKVVTPALEAVVEANTLLSGLGFES 248
Cdd:cd08550 161 GIGDTLAKWYEARPSSRG----GPDDLALQAAVQLAKLAYDLLLEYGVQAVEDVRQGKVTPALEDVVDAIILLAGLVGSL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 249 GG----LAGAHAIHNGFTVLEgDIHHLTHGQKVAFGTLVQLALEKRPLTEVERYIDFYLKLDLPVTLEDIKLqDASREDL 324
Cdd:cd08550 237 GGggcrTAAAHAIHNGLTKLP-ETHGTLHGEKVAFGLLVQLALEGRSEEEIEELIEFLRRLGLPVTLEDLGL-ELTEEEL 314
|
330 340 350
....*....|....*....|....*....|...
gi 515237560 325 YRVAQAATKEGETAHNLPFAVTADDVLDAILAA 357
Cdd:cd08550 315 RKIAEYACDPPDMAHMLPFPVTPEMLAEAILAA 347
|
|
| GlyDH-like |
cd08172 |
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins ... |
9-356 |
1.47e-107 |
|
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: 319.08 E-value: 1.47e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 9 PDKYVQGKNVIDKTGEYVKPLG-HTALVIADKLVWEIAADrVVKSLEQADITAIKveFQGEASKNEVNRIADEGRSGQVD 87
Cdd:cd08172 1 PQEYICEEGALKELPELLSEFGiKRPLIIHGEKSWQAAKP-YLPKLFEIEYPVLR--YDGECSYEEIDRLAEEAKEHQAD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 88 IVIGVGGGKTLDTAKAVNELLGSSVVIVPTTASTDAPTSALSVLYTDEGAFDTYTFFSKNPSLILVDTKVISQAPPLFLS 167
Cdd:cd08172 78 VIIGIGGGKVLDTAKAVADKLNIPLILIPTLASNCAAWTPLSVIYDEDGEFIGYDYFPRSAYLVLVDPRLLLDSPKDYFV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 168 SGIADAMATWIEARAVIEArattMAGGLPTLA-AEAIASKCEEVLFDYGLQAYESVKRKVVTPALEAVVEANTLLSGL-- 244
Cdd:cd08172 158 AGIGDTLAKWYEADAILRQ----LEELPAFLQlARQAAKLCRDILLKDSEQALADLEAGKLTPAFIKVVETIIALAGMvg 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 245 GF--ESGGLAGAHAIHNGFTVLEGdIHHLTHGQKVAFGTLVQLALEKRpLTEVERYIDFYLKLDLPVTLEDIKLQDASRE 322
Cdd:cd08172 234 GFgdEYGRSAGAHAIHNGLTKLPE-THHFLHGEKVAYGILVQLALEGK-WDEIKKLLPFYRRLGLPTSLADLGLTDDTEE 311
|
330 340 350
....*....|....*....|....*....|....
gi 515237560 323 DLYRVAQAATKEGETAHNLPFAVTADDVLDAILA 356
Cdd:cd08172 312 ALQKIAAFAASPEESIHLLPPDVTAEEVLQAIEK 345
|
|
| GlyDH-like |
cd08171 |
Glycerol dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins ... |
15-357 |
5.19e-74 |
|
Glycerol dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins that have yet to be characterized, but show sequence homology with glycerol dehydrogenase. Glycerol dehydrogenases (GlyDH) is a key enzyme in the glycerol dissimilation pathway. In anaerobic conditions, many microorganisms utilize glycerol as a source of carbon through coupled oxidative and reductive pathways. One of the pathways involves the oxidation of glycerol to dihydroxyacetone with the reduction of NAD+ to NADH catalyzed by glycerol dehydrogenases. Dihydroxyacetone is then phosphorylated by dihydroxyacetone kinase and enters the glycolytic pathway for further degradation. The activity of GlyDH is zinc-dependent; the zinc ion plays a role in stabilizing an alkoxide intermediate at the active site.
Pssm-ID: 341450 Cd Length: 345 Bit Score: 233.18 E-value: 5.19e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 15 GKNVIDKTGEYVKPLGHTALVIADKLVWEIAADRVVKSLEQADITAIKVE-FQGEASKNEVNRIADEGRSGQVDIVIGVG 93
Cdd:cd08171 7 GEDAYDAIPKICSPYGKKVVVIGGKKALAAAKPKLRAALEGSGLEITDFIwYGGEATYENVEKLKANPEVQEADMIFAVG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 94 GGKTLDTAKAVNELLGSSVVIVPTTASTDAPTSALSVLYTDEGAFDTYTFFSKNPSLILVDTKVISQAPPLFLSSGIADA 173
Cdd:cd08171 87 GGKAIDTVKVLADRLNKPVFTFPTIASNCAAVTAVSVMYNPDGSFKEYYFLKRPPVHTFIDTEIIAEAPEKYLWAGIGDT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 174 MATWIEARavIEARATTMAggLPTLAAEAIASKCEEVLFDYGLQAYESVKRKVVTPALEAVVEA---NTllsglGFES-- 248
Cdd:cd08171 167 LAKYYEVE--FSARGDELD--HTNALGVAISKMCSEPLLKYGVQALEDCRANKVSDALEQVVLDiivTT-----GLVSnl 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 249 ------GGLagAHAIHNGFTVLEGDIHHLTHGQKVAFGTLVQLALEKRpLTEVERYIDFYLKLDLPVTLEDIklqDASRE 322
Cdd:cd08171 238 vepdynSSL--AHALYYGLTTLPQIEEEHLHGEVVSYGVLVLLTVDGQ-FEELEKVYAFNKSIGLPTCLADL---GLTVE 311
|
330 340 350
....*....|....*....|....*....|....*
gi 515237560 323 DLYRVAQAATKEGETAHNlPFAVTADDVLDAILAA 357
Cdd:cd08171 312 DLEKVLDKALKTKDLRHS-PYPITKEMFEEAIKDL 345
|
|
| Fe-ADH |
pfam00465 |
Iron-containing alcohol dehydrogenase; |
9-350 |
1.61e-64 |
|
Iron-containing alcohol dehydrogenase;
Pssm-ID: 425696 [Multi-domain] Cd Length: 362 Bit Score: 209.38 E-value: 1.61e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 9 PDKYVQGKNVIDKTGEYVKPLGHTALVIADKLVWEI-AADRVVKSLEQADIT-AIKVEFQGEASKNEVNRIADEGRSGQV 86
Cdd:pfam00465 1 PTRIVFGAGALAELGEELKRLGARALIVTDPGSLKSgLLDKVLASLEEAGIEvVVFDGVEPEPTLEEVDEAAALAREAGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 87 DIVIGVGGGKTLDTAKAVNELLGSS------------------VVIVPTTASTDAPTSALSVLYTDEGAFDtYTFFSK-- 146
Cdd:pfam00465 81 DVIIAVGGGSVIDTAKAIALLLTNPgdvwdylggkpltkpalpLIAIPTTAGTGSEVTPLAVITDTETGEK-LGIFSPkl 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 147 NPSLILVDTKVISQAPPLFLSSGIADAMATWIEARAVIEARATTMAgglptLAAEAIaskceEVLFDYGLQAYESVKRkv 226
Cdd:pfam00465 160 LPDLAILDPELTLTLPPRLTAATGMDALAHAVEAYVSKGANPLTDA-----LALEAI-----RLIAENLPRAVADGED-- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 227 vTPALEAVVEANTlLSGLGFESGGLAGAHAIHNGFTVLEGDIHHLTHGQKVAFGT----------LVQLAL-------EK 289
Cdd:pfam00465 228 -LEARENMLLAST-LAGLAFSNAGLGAAHALAHALGGRYGIPHGLANAILLPYVLrfnapaapekLAQLARalgedsdEE 305
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515237560 290 RPLTEVERYIDFYLKLDLPVTLEDIKLqdaSREDLYRVAQAATKEGETAHNlPFAVTADDV 350
Cdd:pfam00465 306 AAEEAIEALRELLRELGLPTTLSELGV---TEEDLDALAEAALRDRSLANN-PRPLTAEDI 362
|
|
| DHQ_Fe-ADH |
cd07766 |
Dehydroquinate synthase-like (DHQ-like) and iron-containing alcohol dehydrogenases (Fe-ADH); ... |
9-332 |
4.51e-58 |
|
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: 189.88 E-value: 4.51e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 9 PDKYVQGKNVIDKTGEYVKPLGHTALVIADKLVWEIAADRVVKSLEQADITAIKVEFQGEASKNEVNRIADEGRSGQVDI 88
Cdd:cd07766 1 PTRIVFGEGAIAKLGEIKRRGFDRALVVSDEGVVKGVGEKVADSLKKGLAVAIFDFVGENPTFEEVKNAVERARAAEADA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 89 VIGVGGGKTLDTAKAVNELLGSSV--VIVPTTASTDAPTSALSVLYTDEGAFdTYTFFSKNPSLILVDTKVISQAPPLFL 166
Cdd:cd07766 81 VIAVGGGSTLDTAKAVAALLNRGIpfIIVPTTASTDSEVSPKSVITDKGGKN-KQVGPHYNPDVVFVDTDITKGLPPRQV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 167 SSGIADAMATWIEaraviearattmagglptlaaeaiaskceevlfdyglqayesvkrkvvtpaLEAVVEANTLLSGLGF 246
Cdd:cd07766 160 ASGGVDALAHAVE---------------------------------------------------LEKVVEAATLAGMGLF 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 247 ESGGLAGAHAIHNGFTVLegdiHHLTHGQKVAFGTLVQLALEKRPLTE----VERYIDFYLKLDLPVTLEDIklqDASRE 322
Cdd:cd07766 189 ESPGLGLAHAIGHALTAF----EGIPHGEAVAVGLPYVLKVANDMNPEpeaaIEAVFKFLEDLGLPTHLADL---GVSKE 261
|
330
....*....|
gi 515237560 323 DLYRVAQAAT 332
Cdd:cd07766 262 DIPKLAEKAL 271
|
|
| PRK10586 |
PRK10586 |
putative oxidoreductase; Provisional |
59-362 |
7.37e-43 |
|
putative oxidoreductase; Provisional
Pssm-ID: 182570 Cd Length: 362 Bit Score: 152.57 E-value: 7.37e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 59 TAIKVEFQGEASKNEVNRIADE-GRSGQVdiVIGVGGGKTLDTAKAVNELLGSSVVIVPTTASTDAPTSALSVLYTDEGA 137
Cdd:PRK10586 61 GAKHILFRGHCSESDVAQLAAAsGDDRQV--VIGVGGGALLDTAKALARRLGLPFVAIPTIAATCAAWTPLSVWYNDAGQ 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 138 FDTYTFFSKNPSLILVDTKVISQAPPLFLSSGIADAMATWIEArAVI----EARATTMAGGLPTlaAEAIaskcEEVLFD 213
Cdd:PRK10586 139 ALHFEIFDDANFLVLVEPRIILNAPQEYLLAGIGDTLAKWYEA-VVLapqpETLPLTVRLGINN--ALAI----RDVLLN 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 214 YGLQAYESVKRKVVTPALEAVVEA----NTLLSGLGFESGGLAGAHAIHNGFTVLEGDIHHLtHGQKVAFGTLVQLALEK 289
Cdd:PRK10586 212 SSEQALADQQNGQLTQDFCDVVDAiiagGGMVGGLGERYTRVAAAHAVHNGLTVLPQTEKFL-HGTKVAYGILVQSALLG 290
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515237560 290 RPLTeVERYIDFYLKLDLPVTLEDIKLQDASREDLYRVAQAATKEGETAHNLPFAVTADDVLDAILAADQYSV 362
Cdd:PRK10586 291 QDDV-LAQLIGAYQRFHLPTTLAELDVDINNQAEIDRVIAHTLRPVESIHYLPVTLTPDTLRAAFEKVESFKA 362
|
|
| Gro1PDH |
cd08173 |
Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) catalyzes the reversible conversion between ... |
15-175 |
7.91e-32 |
|
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: 122.66 E-value: 7.91e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 15 GKNVIDKTGEYVKPL--GHTALVIADKLVWEIAADRVVKSLEQADITAIKVEFQGEASKNEVNRIADEGRSGQVDIVIGV 92
Cdd:cd08173 8 GHGAINKIGEVLKKLllGKRALIITGPNTYKIAGKRVEDLLESSGVEVVIVDIATIEEAAEVEKVKKLIKESKADFIIGV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 93 GGGKTLDTAKAVNELLGSSVVIVPTTASTDAPTSALSVLYTDEGAfdtYTFFSKNPSLILVDTKVISQAPPLFLSSGIAD 172
Cdd:cd08173 88 GGGKVIDVAKYAAYKLNLPFISIPTSASHDGIASPFASIKGGDKP---YSIKAKAPIAIIADTEIISKAPKRLLAAGCGD 164
|
...
gi 515237560 173 AMA 175
Cdd:cd08173 165 LIS 167
|
|
| egsA |
PRK00843 |
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed |
9-172 |
6.51e-29 |
|
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed
Pssm-ID: 179139 Cd Length: 350 Bit Score: 114.99 E-value: 6.51e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 9 PDKYVQGKNVIDKTGEYVKPL--GHTALVIADKLVWEIAADRVVKSLEQA-DITAIKVEfqgEASKNEVNRIADEGRSGQ 85
Cdd:PRK00843 11 PRDVVVGHGVLDDIGDVCSDLklTGRALIVTGPTTKKIAGDRVEENLEDAgDVEVVIVD---EATMEEVEKVEEKAKDVN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 86 VDIVIGVGGGKTLDTAKAVNELLGSSVVIVPTTASTDAPTSALSVLYTDEGafdTYTFFSKNPSLILVDTKVISQAPPLF 165
Cdd:PRK00843 88 AGFLIGVGGGKVIDVAKLAAYRLGIPFISVPTAASHDGIASPRASIKGGGK---PVSVKAKPPLAVIADTEIIAKAPYRL 164
|
....*..
gi 515237560 166 LSSGIAD 172
Cdd:PRK00843 165 LAAGCGD 171
|
|
| Fe-ADH_2 |
pfam13685 |
Iron-containing alcohol dehydrogenase; |
15-278 |
3.69e-27 |
|
Iron-containing alcohol dehydrogenase;
Pssm-ID: 404557 [Multi-domain] Cd Length: 251 Bit Score: 107.77 E-value: 3.69e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 15 GKNVIDKTGEYVKPLG-HTALVIADKLVWEIAADRVVKSLEQADITA-IKVEFQGEASKNEVNRIADEGRSGQVDIVIGV 92
Cdd:pfam13685 3 GPGALGRLGEYLAELGfRRVALVADANTYAAAGRKVAESLKRAGIEVeTRLEVAGNADMETAEKLVGALRERDADAVVGV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 93 GGGKTLDTAKAVNELLGSSVVIVPTTASTDAPTSALSVLYTDeGAfdTYTFFSKNPSLILVDTKVISQAPPLFLSSGIAD 172
Cdd:pfam13685 83 GGGTVIDLAKYAAFKLGKPFISVPTAASNDGFASPGASLTVD-GK--KRSIPAAAPFGVIADTDVIAAAPRRLLASGVGD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 173 AMATWI----EARAVIEARATTMAGglptLAAEAIASKCEEVLFDYGLqayesvkrkvvTPALEAVVEANTlLSGLGFES 248
Cdd:pfam13685 160 LLAKITavadWELAHAEEVAAPLAL----LSAAMVMNFADRPLRDPGD-----------IEALAELLSALA-MGGAGSSR 223
|
250 260 270
....*....|....*....|....*....|...
gi 515237560 249 GGLAGAHAI-HngftVLEgDIH--HLTHGQKVA 278
Cdd:pfam13685 224 PASGSEHLIsH----ALD-MIApkQALHGEQVG 251
|
|
| G1PDH-like |
cd08174 |
Glycerol-1-phosphate dehydrogenase-like; These glycerol-1-phosphate dehydrogenase-like ... |
15-333 |
1.07e-25 |
|
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: 105.68 E-value: 1.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 15 GKNVIDKTGEYVKPLGHT---ALVIADKLVWEIAADRVVKSLEQADITAIKVEfqgeASKNEVNRIADEGRSG-QVDIVI 90
Cdd:cd08174 7 EEGALEHLGKYLADRNQGfgkVAIVTGEGIDELLGEDILESLEEAGEIVTVEE----NTDNSAEELAEKAFSLpKVDAIV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 91 GVGGGKTLDTAKAVNELLGSSVVIVPTTASTDAPTSALSVLYTDEGafdTYTFFSKNPSLILVDTKVISQAPPLFLSSGI 170
Cdd:cd08174 83 GIGGGKVLDVAKYAAFLSKLPFISVPTSLSNDGIASPVAVLKVDGK---RKSLGAKMPYGVIVDLDVIKSAPRRLILAGI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 171 AD------AMATWIEARaviEARATTMAGglptlAAEAIASKCEEVLFDYGLQAYESvkrkvvTPALEAVVEAnTLLSGL 244
Cdd:cd08174 160 GDlisnitALYDWKLAE---EKGGEPVDD-----FAYLLSRTAADSLLNTPGKDIKD------DEFLKELAES-LVLSGI 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 245 GFEsggLAG------------AHAIhngftvlegDIHHLT---HGQKVAFGTLVQLALEKRPLTEVeryIDFYLKLDLPV 309
Cdd:cd08174 225 AME---IAGssrpasgsehliSHAL---------DKLFPGpalHGIQVGLGTYFMSFLQGQRYEEI---RDVLKRTGFPL 289
|
330 340
....*....|....*....|....
gi 515237560 310 TLEDIKLqdaSREDLYRVAQAATK 333
Cdd:cd08174 290 NPSDLGL---TKEEFIEAVKLAPS 310
|
|
| Fe-ADH-like |
cd14863 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
15-357 |
1.30e-23 |
|
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: 100.69 E-value: 1.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 15 GKNVIDKTGEYVKPLGHT-ALVIADKLVWEIA-ADRVVKSLEQADI-TAIKVEFQGEASKNEVNRIADEGRSGQVDIVIG 91
Cdd:cd14863 11 GAGAVEQIGELLKELGCKkVLLVTDKGLKKAGiVDKIIDLLEEAGIeVVVFDDVEPDPPDEIVDEAAEIAREEGADGVIG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 92 VGGGKTLDTAKAVNELLGSS-------------------VVIVPTTASTDAPTSALSVLYTDE-----GAFDTYTffskN 147
Cdd:cd14863 91 IGGGSVLDTAKAIAVLLTNPgpiidyalagppvpkpgipLIAIPTTAGTGSEVTPIAVITDEEngvkkSLLGPFL----V 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 148 PSLILVDTKV-ISQAPPLFLSSGIaDAMATWIEAraviearattMAGGLPTLAAEAIASKCEEVLFDYGLQAYESVKRkv 226
Cdd:cd14863 167 PDLAILDPELtVGLPPSLTAATGM-DALSHAIEA----------YTSKLANPMTDALALQAIRLIVKNLPRAVKDGDN-- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 227 vtpaLEA---VVEANTlLSGLGFESGGLAGAHAIHNGFtvleGDIHHLTHGQKVAFGTLV------------------QL 285
Cdd:cd14863 234 ----LEArenMLLASN-LAGIAFNNAGTHIGHAIAHAL----GALYHIPHGLACALALPVvlefnaeaypekvkkiakAL 304
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515237560 286 ALEKRPLTEVE-------RYIDFYLKLDLPVTLEDiklQDASREDLYRVAQAATKEgETAHNLPFAVTADDVLdAILAA 357
Cdd:cd14863 305 GVSFPGESDEElgeavadAIREFMKELGIPSLFED---YGIDKEDLDKIAEAVLKD-PFAMFNPRPITEEEVA-EILEA 378
|
|
| EutG |
COG1454 |
Alcohol dehydrogenase, class IV [Energy production and conversion]; |
6-357 |
6.39e-23 |
|
Alcohol dehydrogenase, class IV [Energy production and conversion];
Pssm-ID: 441063 [Multi-domain] Cd Length: 381 Bit Score: 98.65 E-value: 6.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 6 FISPDKYVQGKNVIDKTGEYVKPLGHT-ALVIADKLVWEI-AADRVVKSLEQADI-TAIKVEFQGEASKNEVNRIADEGR 82
Cdd:COG1454 5 FRLPTRIVFGAGALAELGEELKRLGAKrALIVTDPGLAKLgLLDRVLDALEAAGIeVVVFDDVEPNPTVETVEAGAAAAR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 83 SGQVDIVIGVGGGKTLDTAKAVN----------ELLGSS--------VVIVPTTASTDAPTSALSVLyTDEGAFDTYTFF 144
Cdd:COG1454 85 EFGADVVIALGGGSAIDAAKAIAllatnpgdleDYLGIKkvpgpplpLIAIPTTAGTGSEVTPFAVI-TDPETGVKKGIA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 145 SKN--PSLILVDTKVISQAPP-LFLSSGIaDAMAtwiearAVIEA----RATTMAGGlptLAAEAIaskceEVLFDYGLQ 217
Cdd:COG1454 164 DPEllPDVAILDPELTLTLPPsLTAATGM-DALT------HAIEAyvskGANPLTDA---LALEAI-----RLIARNLPR 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 218 AYESVKRKvvtPALEAVVEANTlLSGLGFESGGLAGAHAI-HngftVLeGDIHHLTHG---------------------- 274
Cdd:COG1454 229 AVADGDDL---EAREKMALASL-LAGMAFANAGLGAVHALaH----PL-GGLFHVPHGlanaillphvlrfnapaapery 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 275 QKVA--FGTLVQLALEKRPLTEVERYIDFYLKLDLPVTLEDIKLqdaSREDLYRVAQAATKEGETAHNlPFAVTADDVLD 352
Cdd:COG1454 300 AEIAraLGLDVGLSDEEAAEALIEAIRELLRDLGIPTRLSELGV---TEEDLPELAELALADRCLANN-PRPLTEEDIEA 375
|
....*
gi 515237560 353 AILAA 357
Cdd:COG1454 376 ILRAA 380
|
|
| Fe-ADH |
cd08551 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains large ... |
9-352 |
9.73e-23 |
|
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: 97.90 E-value: 9.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 9 PDKYVQGKNVIDKTGEYVKPLGHT-ALVIADKLVWEI-AADRVVKSLEQADItAIKV--EFQGEASKNEVNRIADEGRSG 84
Cdd:cd08551 1 PTRIVFGAGALARLGEELKALGGKkVLLVTDPGLVKAgLLDKVLESLKAAGI-EVEVfdDVEPNPTVETVEAAAELAREE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 85 QVDIVIGVGGGKTLDTAKAVNELLGSS------------------VVIVPTTASTDAPTSALSVLyTDEGAFDTYTFFSK 146
Cdd:cd08551 80 GADLVIAVGGGSVLDTAKAIAVLATNGgsirdyegigkvpkpglpLIAIPTTAGTGSEVTPNAVI-TDPETGRKMGIVSP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 147 N--PSLILVDTK-VISQAPPLFLSSGIaDAMATWIEARAVIEARATTMAgglptLAAEAIaskceEVLFDYGLQAYESVK 223
Cdd:cd08551 159 YllPDVAILDPElTLSLPPSVTAATGM-DALTHAIEAYTSKKANPISDA-----LALEAI-----RLIGKNLRRAVADGS 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 224 RKvvtPALEAVVEAnTLLSGLGFESGGLAGAHAIhnGFTVleGDIHHLTHGQKVAF--------------GTLVQLALEK 289
Cdd:cd08551 228 DL---EAREAMLLA-SLLAGIAFGNAGLGAVHAL--AYPL--GGRYHIPHGVANAIllpyvmefnlpacpEKYAEIAEAL 299
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515237560 290 RPLTE-----------VERYIDFYLKLDLPVTLEDIKLqdaSREDLYRVAQAATKEGETAHNLPFAVTADDVLD 352
Cdd:cd08551 300 GEDVEglsdeeaaeaaVEAVRELLRDLGIPTSLSELGV---TEEDIPELAEDAMKSGRLLSNNPRPLTEEDIRE 370
|
|
| Fe-ADH-like |
cd14864 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
6-357 |
1.74e-22 |
|
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: 97.37 E-value: 1.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 6 FISPDKYVQGKNVIDKTGEYVKPLGHTALVIADKLVWEI-AADRVVKSLEQADITAIKV-EFQGEASKNEVNRIADEGRS 83
Cdd:cd14864 1 FKIPPNIVFGADSLERIGEEVKEYGSRFLLITDPVLKESgLADKIVSSLEKAGISVIVFdEIPASATSDTIDEAAELARK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 84 GQVDIVIGVGGGKTLDTAKAVNELLGSSV------------------VIVPTTASTDAPTSAlSVLYTDEGAFDTYTFFS 145
Cdd:cd14864 81 AGADGIIAVGGGKVLDTAKAVAILANNDGgaydflegakpkkkplplIAVPTTPRSGFEFSD-RFPVVDSRSREVKLLKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 146 KN--PSLILVDTKVISQAPPLFLSSGIADAMATWIEarAVIEARATTMAGglpTLAAEAIAskceevLFDYGLQAyeSVK 223
Cdd:cd14864 160 QPglPKAVIVDPNLMASLTGNQTAAMALAALALAVE--AYLSKKSNFFSD---ALALKAIE------LVSENLDG--ALA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 224 RKVVTPALEAVVEANtLLSGLGFESG--GLAGA--HAIHNGFTVLEGDI------HHLTHGQKVAFGTLVQLAL------ 287
Cdd:cd14864 227 DPKNTPAEELLAQAG-CLAGLAASSSspGLATAlaLAVNSRYKVSKSLVasillpHVIEYAATSAPDKYAKIARalgedv 305
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515237560 288 --------EKRPLTEVERyidFYLKLDLPVTLEDIKLqDASREDLYRVAQAATKEgetaHNLPFAVTADDVLDAILAA 357
Cdd:cd14864 306 egaspeeaAIAAVEGVRR---LIAQLNLPTRLKDLDL-ASSLEQLAAIAEDAPKL----NGLPRSMSSDDIFDILKAA 375
|
|
| G1PDH |
cd08175 |
Glycerol-1-phosphate dehydrogenase (G1PDH) catalyzes the reversible reduction of ... |
15-329 |
5.51e-20 |
|
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: 89.49 E-value: 5.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 15 GKNVIDKTGEYVKPL--GHTALVIADKLVWEIAADRVVKSLEQADITAIKVEFqgeasKNEVNRIADEGRSGQV------ 86
Cdd:cd08175 7 GEGALKKLPEYLKELfgGKKVLVVADENTYAAAGEEVEAALEEAGVTVCLLIF-----PGEGDLIADEAAVGKVllelek 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 87 --DIVIGVGGGkTL-DTAKAVNELLGSSVVIVPTTASTDAPTSALSVLyTDEGaFDTyTFFSKNPSLILVDTKVISQAPP 163
Cdd:cd08175 82 dtDLIIAVGSG-TInDLTKYAAYKLGIPYISVPTAPSMDGYTSSGAPI-IVDG-VKK-TFPAHAPKAIFADLDVLANAPQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 164 LFLSSGIAD------AMATWIEARAV-IEARATTMAGglptLAAEAIAsKCeevlfdygLQAYESVKRKVVTpALEAVVE 236
Cdd:cd08175 158 RMIAAGFGDllgkytALADWKLSHLLgGEYYCPEVAD----LVQEALE-KC--------LDNAEGIAARDPE-AIEALME 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 237 ANtLLSGLGFE--------SGglaGAHAI-HngftVLEGDIH-----HLTHGQKVAFGTLVQLAL-EKRPLTEVERYIDF 301
Cdd:cd08175 224 AL-ILSGLAMQlvgnsrpaSG---AEHHLsH----YWEMEFLrlgkpPVLHGEKVGVGTLLIAALyILEQLPPPEELREL 295
|
330 340
....*....|....*....|....*...
gi 515237560 302 YLKLDLPVTLEDIKLQDASREDLYRVAQ 329
Cdd:cd08175 296 LRKAGAPTTPEDLGIDRDLLRDSLRLAK 323
|
|
| Fe-ADH-like |
cd08196 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
6-352 |
1.70e-17 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341475 [Multi-domain] Cd Length: 367 Bit Score: 82.63 E-value: 1.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 6 FISPDKYVQGKNVIDKTGEYVKPLGHT-ALVIADK-LVWEIAADRVVKSLEQADItAIKVEFQGEASKNEVNRIADEGRS 83
Cdd:cd08196 3 YYQPVKIIFGEGILKELPDIIKELGGKrGLLVTDPsFIKSGLAKRIVESLKGRIV-AVFSDVEPNPTVENVDKCARLARE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 84 GQVDIVIGVGGGKTLDTAKAV----------NELLGS---------SVVIVPTTASTDAPTSALSVlYTDEGAFDTYTFF 144
Cdd:cd08196 82 NGADFVIAIGGGSVLDTAKAAaclaktdgsiEDYLEGkkkipkkglPLIAIPTTAGTGSEVTPVAV-LTDKEKGKKAPLV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 145 SKN--PSLILVDTKV-ISQAPPLFLSSGIaDAMATWIEARAVIEARATTMAgglptLAAEAIAskceeVLFDYGLQAYES 221
Cdd:cd08196 161 SPGfyPDIAIVDPELtYSMPPKVTASTGI-DALCHAIEAYWSINHQPISDA-----LALEAAK-----LVLENLEKAYNN 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 222 VKRKVvtpALEAVVEAnTLLSGLGFESGGLAGAHAIHNGFTvlegDIHHLTHGQKVAFgTLVQL------ALEKRpLTEV 295
Cdd:cd08196 230 PNDKE---AREKMALA-SLLAGLAFSQTRTTASHACSYPLT----SHFGIPHGEACAL-TLPSFirlnaeALPGR-LDEL 299
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 296 ERYIDFY-----------LK--LDLPVTLEDIklqDASREDLYRVAQAATkEGETAHNLPFAVTADDVLD 352
Cdd:cd08196 300 AKQLGFKdaeeladkieeLKkrIGLRTRLSEL---GITEEDLEEIVEESF-HPNRANNNPVEVTKEDLEK 365
|
|
| G1PDH_related |
cd08549 |
Glycerol-1-phosphate dehydrogenase and related proteins; This family contains bacterial and ... |
9-321 |
2.60e-17 |
|
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: 81.84 E-value: 2.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 9 PDKYVQGKNVIDKTGEYVKPLGH-TALVIADKLVWEIAADRVVKSLEQadITAIKvefqgeaSKNEVNRIADE-GRSGQV 86
Cdd:cd08549 1 PRYTIVGDGAINKIEEILKKLNLkRVLIITGKNTKAKYCRFFYDQLKT--VCDIV-------YYDNIDNLEDElKKYTFY 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 87 DIVIGVGGGKTLDTAKAVNELLGSSVVIVPTTASTDAPTSALSVLYTDeGAFdtYTFFSKNPSLILVDTKVISQAPPLFL 166
Cdd:cd08549 72 DCVIGIGGGRSIDTGKYLAYKLKIPFISVPTSASNDGIASPIVSLRIP-GVK--KTFMADAPIAIIADTEIIKKSPRRLL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 167 SSGIADAMATWIearAVIEAR-ATTMAGGLPTLAAEAIASKCEEVLFDYglqAYESVKRKVVTPALEAVVEANTLLSGLG 245
Cdd:cd08549 149 SAGIGDLVSNIT---AVLDWKlAHKEKGEKYSEFAAILSKTSAKELVSY---VLKASDLEEYHRVLVKALVGSGIAMAIA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 246 FESGGLAGA-----HAIHNGFtvLEGDIHHLTHGQKVAFGTLVQLALEKRPLTEV----ERYIDFYLKLDLPVTLE--DI 314
Cdd:cd08549 223 GSSRPASGSehlfsHALDKLK--EEYLNINVLHGEQVGVGTIIMSYLHEKENKKLsglhERIKMILKKVGAPTTAKqlGI 300
|
....*..
gi 515237560 315 KLQDASR 321
Cdd:cd08549 301 DEDLIIE 307
|
|
| Fe-ADH-like |
cd08185 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
9-355 |
5.20e-15 |
|
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: 75.61 E-value: 5.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 9 PDKYVQGKNVIDKTGEYVKPLGHTALVIADKLVWEIAA--DRVVKSLEQADITAI---KVEfqgeasKNEVNRIADEG-- 81
Cdd:cd08185 4 PTRILFGAGKLNELGEEALRPGKKALIVTGKGSSKKTGllDRVKKLLEKAGVEVVvfdKVE------PNPLTTTVMEGaa 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 82 --RSGQVDIVIGVGGGKTLDTAKAV-----NE------LLGSS-----------VVIVPTTASTDAPTSALSVLyTDEGA 137
Cdd:cd08185 78 laKEEGCDFVIGLGGGSSMDAAKAIafmatNPgdiwdyIFGGTgkgpppekalpIIAIPTTAGTGSEVDPWAVI-TNPET 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 138 FDTYTFFSKN--PSLILVDTKVISQAPPLFLSSGIADAMATWIEarAVIEARATTMAGglpTLAAEAIaskceEVLFDYG 215
Cdd:cd08185 157 KEKKGIGHPAlfPKVSIVDPELMLTVPPRVTAYTGFDALFHAFE--SYISKNANPFSD---MLALEAI-----RLVAKYL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 216 LQAYESVKRKvvtPALEAVVEANTlLSGLGFESGGLAGAHAI-HngftVLEGDIHHLTHGQ------------------- 275
Cdd:cd08185 227 PRAVKDGSDL---EAREKMAWAST-LAGIVIANSGTTLPHGLeH----PLSGYHPNIPHGAglaalypayfeftiekape 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 276 ---KVAFGTLVQLALEKRPLTEVERYIDFYLKLDLPVTLEDIKLqdaSREDLYRVAQAATKE-GETAHNLPFAVTADDVL 351
Cdd:cd08185 299 kfaFVARAEASGLSDAKAAEDFIEALRKLLKDIGLDDLLSDLGV---TEEDIPWLAENAMETmGGLFANNPVELTEEDIV 375
|
....
gi 515237560 352 dAIL 355
Cdd:cd08185 376 -EIY 378
|
|
| Fe-ADH-like |
cd08183 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
15-104 |
4.71e-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: 69.45 E-value: 4.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 15 GKNVIDKTGEYVKPLGHTALVIADK-LVWEIAADRVVKSLEQADITAIKVEFQGEASKNEVNRIADEGRSGQVDIVIGVG 93
Cdd:cd08183 7 GRGSLQELGELAAELGKRALLVTGRsSLRSGRLARLLEALEAAGIEVALFSVSGEPTVETVDAAVALAREAGCDVVIAIG 86
|
90
....*....|.
gi 515237560 94 GGKTLDTAKAV 104
Cdd:cd08183 87 GGSVIDAAKAI 97
|
|
| Fe-ADH-like |
cd08191 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
6-357 |
6.90e-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: 69.18 E-value: 6.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 6 FISPDKYVQGKNVIDKTGEYVKPLGHTALVIADK-LVWEIAADRVVKSLEQADITAIkVEFQGEA--SKNEVNRIADEGR 82
Cdd:cd08191 1 LRSPSRLLFGPGARRALGRVAARLGSRVLIVTDPrLASTPLVAELLAALTAAGVAVE-VFDGGQPelPVSTVADAAAAAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 83 SGQVDIVIGVGGGKTLDTAKAVNELLGSS------------------VVIVPTTASTDAPTSALSVLYTDE-----GAFD 139
Cdd:cd08191 80 AFDPDVVIGLGGGSNMDLAKVVALLLAHGgdprdyygedrvpgpvlpLIAVPTTAGTGSEVTPVAVLTDPArgmkvGVSS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 140 TYTffskNPSLILVDTKVISQAPP-LFLSSGIaDAMATWIEARAVIEARATTMAGGLP----------TLAAEAIAskce 208
Cdd:cd08191 160 PYL----RPAVAIVDPELTLTCPPgVTADSGI-DALTHAIESYTARDFPPFPRLDPDPvyvgknpltdLLALEAIR---- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 209 evLFDYGLQAyeSVKRKVVTPALEAVVEAnTLLSGLGFESGGLAGAHAIHngFTVleGDIHHLTHGQKV----------- 277
Cdd:cd08191 231 --LIGRHLPR--AVRDGDDLEARSGMALA-ALLAGLAFGTAGTAAAHALQ--YPI--GALTHTSHGVGNglllpyvmrfn 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 278 -------------AFGTLVQLALEKRPLTEVERYIDFYLKLDLPVTLEDIKLQdasREDLYRVAQAATKEGETAHNLPFA 344
Cdd:cd08191 302 rparaaelaeiarALGVTTAGTSEEAADRAIERVEELLARIGIPTTLADLGVT---EADLPGLAEKALSVTRLIANNPRP 378
|
410
....*....|...
gi 515237560 345 VTADDVLDAILAA 357
Cdd:cd08191 379 PTEEDLLRILRAA 391
|
|
| Fe-ADH-like |
cd14862 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
6-350 |
3.00e-12 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341484 [Multi-domain] Cd Length: 375 Bit Score: 67.25 E-value: 3.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 6 FISPdKYVQGKNVIDKTGEYvkpLGHTALVIADK-LVWEIAADRVVKSLEQADI-TAIKVEFQGEASKNEVNRIADEGRS 83
Cdd:cd14862 4 FSSP-KIVFGEDALSHLEQL---SGKRALIVTDKvLVKLGLLKKVLKRLLQAGFeVEVFDEVEPEPPLETVLKGAEAMRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 84 GQVDIVIGVGGGKTLDTAKA-----------------VNELLGSSVVI---VPTTASTDAPTSALSVLyTDEGAFDTYTF 143
Cdd:cd14862 80 FEPDLIIALGGGSVMDAAKAawvlyerpdldpedispLDLLGLRKKAKliaIPTTSGTGSEATWAIVL-TDTEEPRKIAV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 144 FSKN--PSLILVDTKVISQAPP-LFLSSGIaDAMATwiearaVIEARATTMAGGLptlaAEAIASKCEEVLFDYGLQAYE 220
Cdd:cd14862 159 ANPElvPDVAILDPEFVLGMPPkLTAGTGL-DALAH------AVEAYLSTWSNDF----SDALALKAIELIFKYLPRAYK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 221 SVKRKvvtPALEAVVEANTlLSGLGFESGGLAGAHAIHNGFtvleGDIHHLTHGQKVA-----------------FGTLV 283
Cdd:cd14862 228 DGDDL---EAREKMHNAAT-IAGLAFGNSQAGLAHALGHSL----GAVFHVPHGIAVGlflpyviefyakvtderYDLLK 299
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515237560 284 QLALEKRPLTE-----VERYIDFYLKLDLPVTLEDIKL-QDASREDLYRVAQAATKEGETAHNlPFAVTADDV 350
Cdd:cd14862 300 LLGIEARDEEEalkklVEAIRELYKEVGQPLSIKDLGIsEEEFEEKLDELVEYAMEDSCTITS-PRPPSEEDL 371
|
|
| BDH |
cd08187 |
Butanol dehydrogenase catalyzes the conversion of butyraldehyde to butanol with the cofactor ... |
5-104 |
4.85e-12 |
|
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: 66.69 E-value: 4.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 5 VFISPDKYVQGKNVIDKTGEYVKPLGHTALVIADK-------LVweiaaDRVVKSLEQADITAikVEFQG-----EASKn 72
Cdd:cd08187 3 TFYNPTKIIFGKGAIEELGEEIKKYGKKVLLVYGGgsikkngLY-----DRVVASLKEAGIEV--VEFGGvepnpRLET- 74
|
90 100 110
....*....|....*....|....*....|..
gi 515237560 73 eVNRIADEGRSGQVDIVIGVGGGKTLDTAKAV 104
Cdd:cd08187 75 -VREGIELAREENVDFILAVGGGSVIDAAKAI 105
|
|
| Fe-ADH-like |
cd08194 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
9-121 |
1.27e-11 |
|
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) most of which have not been characterized. Their specific function is unknown. The protein structure represents a dehydroquinate synthase-like fold and belongs to the alcohol dehydrogenase-like superfamily. It is distinct from other alcohol dehydrogenases which contain different protein domains. Alcohol dehydrogenase catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions.
Pssm-ID: 341473 [Multi-domain] Cd Length: 378 Bit Score: 65.25 E-value: 1.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 9 PDKYVQGKNVIDKTGEYVKPL-GHTALVIADK-LVWEIAADRVVKSLEQADIT-AIKVEFQGEASKNEVNRIADEGRSGQ 85
Cdd:cd08194 1 PRTIIIGGGALEELGEEAASLgGKRALIVTDKvMVKLGLVDKVTQLLAEAGIAyAVFDDVVSEPTDEMVEEGLALYKEGG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 515237560 86 VDIVIGVGGGKTLDTAKAVNELLGSS------------------VVIVPTTAST 121
Cdd:cd08194 81 CDFIVALGGGSPIDTAKAIAVLATNGgpirdymgprkvdkpglpLIAIPTTAGT 134
|
|
| HEPD |
cd08182 |
Hydroxyethylphosphoate dehydrogenase (HEPD) catalyzes the reduction of phosphonoacetaldehyde ... |
9-354 |
7.53e-11 |
|
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: 63.01 E-value: 7.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 9 PDKYVQGKNVIDKTGEYVKPLG-HTALVIADKL-VWEIAADRVVKSLEQADITAIKVEFQGEASKNEVNRIADEGRSGQV 86
Cdd:cd08182 1 PVKIIFGPGALAELKDLLGGLGaRRVLLVTGPSaVRESGAADILDALGGRIPVVVFSDFSPNPDLEDLERGIELFRESGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 87 DIVIGVGGGKTLDTAKAVNELLGSS--------------------VVIVPTTASTDAPTSALSVLYtDEGAFDTYTFFSK 146
Cdd:cd08182 81 DVIIAVGGGSVIDTAKAIAALLGSPgenllllrtgekapeenalpLIAIPTTAGTGSEVTPFATIW-DEAEGKKYSLAHP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 147 N--PSLILVDTKVISQAPP-LFLSSGIaDAMATWIEA----RAVIEARAttmagglptLAAEAIAskceevlfdYGLQAY 219
Cdd:cd08182 160 SlyPDAAILDPELTLSLPLyLTASTGL-DALSHAIESiwsvNANPESRA---------YALRAIR---------LILENL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 220 ESVKRKVVTPAL-EAVVEAnTLLSGLGFESGGLAGAHAIHNGFTVLegdiHHLTHGQKVAF------------------- 279
Cdd:cd08182 221 PLLLENLPNLEArEAMAEA-SLLAGLAISITKTTAAHAISYPLTSR----YGVPHGHACALtlpavlrynagaddecddd 295
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515237560 280 --GTLVQLALEKRPLTEV-ERYIDFYLKLDLPVTLEDIKLQDASREDLyrVAQAATKegETAHNLPFAVTADDVLDAI 354
Cdd:cd08182 296 prGREILLALGASDPAEAaERLRALLESLGLPTRLSEYGVTAEDLEAL--AASVNTP--ERLKNNPVRLSEEDLLRLL 369
|
|
| PPD-like |
cd08181 |
1,3-propanediol dehydrogenase-like (PPD); This family contains proteins similar to 1, ... |
6-352 |
8.41e-10 |
|
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: 59.52 E-value: 8.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 6 FISPDKYVQGKNVIDKTGEYVKPLGHTALVI-----ADKLVweiAADRVVKSLEQADITAI---KVEfqgE-ASKNEVNR 76
Cdd:cd08181 1 FYMPTKVYFGKNCVEKHADELAALGKKALIVtgkhsAKKNG---SLDDVTEALEENGIEYFifdEVE---EnPSIETVEK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 77 IADEGRSGQVDIVIGVGGGKTLDTAKAV-----NELLGSS------------VVIVPTTASTDAPTSALSVLyTDEGAFD 139
Cdd:cd08181 75 GAELARKEGADFVIGIGGGSPLDAAKAIallaaNKDGDEDlfqngkynpplpIVAIPTTAGTGSEVTPYSIL-TDHEKGT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 140 TYTFFSKN--PSLILVDTKVISQAPPLFLSSGIADAMATWIEarAVIEARATTMAGglpTLAAEAIASKCEevlfdyglq 217
Cdd:cd08181 154 KKSFGNPLifPKLALLDPKYTLSLPEELTIDTAVDALSHAIE--GYLSVKATPLSD---ALALEALRLIGE--------- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 218 AYESVKRKVVTPAL-EAVVEANTLlsglgfesGGLAGAHAihnGFTVLEG---DI---HHLTHGQkvAFGTLVQLALEKR 290
Cdd:cd08181 220 CLPNLLGDELDEEDrEKLMYASTL--------AGMVIAQT---GTTLPHGlgyPLtyfKGIPHGR--ANGILLPAYLKLC 286
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515237560 291 PLTEVERyIDFYLKLDLPVTLEDI---------KLQDASREDLYRVAQAATKEGETaHNLPFAVTADDVLD 352
Cdd:cd08181 287 EKQEPEK-VDKILKLLGFGSIEEFqkflnrllgKKEELSEEELEKYADEAMKAKNK-KNTPGNVTKEDILR 355
|
|
| HVD |
cd08193 |
5-hydroxyvalerate dehydrogenase (HVD) catalyzes the oxidation of 5-hydroxyvalerate to ... |
19-136 |
8.64e-10 |
|
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: 59.83 E-value: 8.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 19 IDKTGEYVKPLGHT-ALVIADKLVWEIA-ADRVVKSLEQADItAIKVEFQGEASKNE--VNRIADEGRSGQVDIVIGVGG 94
Cdd:cd08193 14 AARLGELLRELGARrVLLVTDPGLVKAGlADPALAALEAAGI-AVTVFDDVVADPPEavVEAAVEQAREAGADGVIGFGG 92
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 95 GKTLDTAKAVNELLGSS------------------VVIVPTTASTDAPTSALSVLYTDEG 136
Cdd:cd08193 93 GSSMDVAKLVALLAGSDqplddiygvgkatgprlpLILVPTTAGTGSEVTPISIVTTGET 152
|
|
| LPO |
cd08176 |
Lactadehyde:propanediol oxidoreductase (LPO) catalyzes the interconversion between ... |
15-270 |
4.45e-08 |
|
Lactadehyde:propanediol oxidoreductase (LPO) catalyzes the interconversion between L-lactaldehyde and L-1,2-propanediol in Escherichia coli and other enterobacteria; Lactadehyde:propanediol oxidoreductase (LPO) is a member of the group III iron-activated dehydrogenases which catalyze the interconversion between L-lactaldehyde and L-1,2-propanediol in Escherichia coli and other enterobacteria. L-fucose and L-rhamnose are used by Escherichia coli through an inducible pathway mediated by the fucose regulon comprising four linked operons fucO, fucA, fucPIK, and fucR. The fucA-encoded aldolase catalyzes the formation of dihydroxyacetone phosphate and L-lactaldehyde. Under anaerobic conditions, with NADH as a cofactor, lactaldehyde is converted by a fucO-encoded lactadehyde:propanediol oxidoreductase (LPO) to L-1,2-propanediol, which is excreted as a fermentation product. In mutant strains, E. coli adapted to grow on L-1,2-propanediol, FucO catalyzes the oxidation of the polyol to L-lactaldehyde. FucO is induced regardless of the respiratory conditions of the culture, remains fully active in the absence of oxygen. In the presence of oxygen, this enzyme becomes oxidatively inactivated by a metal-catalyzed oxidation mechanism. FucO is an iron-dependent metalloenzyme that is inactivated by other metals, such as zinc, copper, or cadmium. This enzyme can also reduce glycol aldehyde with similar efficiency. Beside L-1,2-propanediol, the enzyme is also able to oxidize methanol as an alternative substrate.
Pssm-ID: 341455 [Multi-domain] Cd Length: 378 Bit Score: 54.47 E-value: 4.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 15 GKNVIDKTGEYVKPLGHT-ALVIADKLVWEIA-ADRVVKSLEQADItaiKVEFQGEASKN----EVNRIADEGRSGQVDI 88
Cdd:cd08176 12 GWGAIEEIGEEAKKRGFKkALIVTDKGLVKFGiVDKVTDVLKEAGI---AYTVFDEVKPNptieNVMAGVAAYKESGADG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 89 VIGVGGGKTLDTAKA-----------VNELLGSS--------VVIVPTTASTDAPTSALSVLyTDEGAFDTYTFFSKN-- 147
Cdd:cd08176 89 IIAVGGGSSIDTAKAigiivanpgadVRSLEGVAptknpavpIIAVPTTAGTGSEVTINYVI-TDTEKKRKFVCVDPHdi 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 148 PSLILVDTKVISQAPP-LFLSSGIaDAMATWIEarAVIEARATTMAGGlptLAAEAIaskceEVLFDYGLQAYESVKRKv 226
Cdd:cd08176 168 PTVAIVDPDLMSSMPKgLTAATGM-DALTHAIE--GYITKGAWELSDM---LALKAI-----ELIAKNLRKAVANPNNV- 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 515237560 227 vtPALEAVVEANTlLSGLGFESGGLAGAHAI-H--NGFTvlegDIHH 270
Cdd:cd08176 236 --EARENMALAQY-IAGMAFSNVGLGIVHSMaHplSAFY----DTPH 275
|
|
| HOT |
cd08190 |
Hydroxyacid-oxoacid transhydrogenase (HOT) involved in gamma-hydroxybutyrate metabolism; This ... |
15-131 |
4.96e-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: 54.47 E-value: 4.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 15 GKNVIDKTGEYVKPLG-HTALVIADKLVWEI-AADRVVKSLEQADITA-----IKVEfqgeASKNEVNRIADEGRSGQVD 87
Cdd:cd08190 7 GPGATRELGMDLKRLGaKKVLVVTDPGLAKLgLVERVLESLEKAGIEVvvydgVRVE----PTDESFEEAIEFAKEGDFD 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515237560 88 IVIGVGGGKTLDTAKAVNELL----------------GSSV-------VIVPTTASTDAPTSALSVL 131
Cdd:cd08190 83 AFVAVGGGSVIDTAKAANLYAthpgdfldyvnapigkGKPVpgplkplIAIPTTAGTGSETTGVAIF 149
|
|
| PDDH |
cd08188 |
1,3-Propanediol (1,3-PD) dehydrogenase; This family includes 1,3-propanediol (1,3-PD) ... |
4-274 |
5.00e-08 |
|
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: 54.06 E-value: 5.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 4 KVFISPDKYVQGKNVIDKTGEYVKPLG-HTALVIADK-LVWEIAADRVVKSLEQADI-TAIKVEFQGEASKNEVNRIADE 80
Cdd:cd08188 1 FRFYIPPVNLFGPGCLKEIGDELKKLGgKKALIVTDKgLVKLGLVKKVTDVLEEAGIeYVIFDGVQPNPTVTNVNEGLEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 81 GRSGQVDIVIGVGGGKTLDTAKAVNELLG-------------SSVVIVP-----TTASTDAPTSALSVLyTDEgafdtyt 142
Cdd:cd08188 81 FKENGCDFIISVGGGSAHDCAKAIGILATnggeiedyegvdkSKKPGLPliainTTAGTASEVTRFAVI-TDE------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 143 ffSKNPSLILVDTKVI------------SQAPPLFLSSGIaDAMATWIEARAVIEARATTMAgglptLAAEAIaskceEV 210
Cdd:cd08188 153 --ERHVKMVIVDWNVTptiavndpelmlGMPPSLTAATGM-DALTHAIEAYVSTGATPLTDA-----LALEAI-----RL 219
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515237560 211 LFDYGLQAYE---SVKrkvvtpALEAVVEAnTLLSGLGFESGGL----AGAHAIhngftvleGDIHHLTHG 274
Cdd:cd08188 220 IAENLPKAVAngkDLE------ARENMAYA-QFLAGMAFNNAGLgyvhAMAHQL--------GGFYNLPHG 275
|
|
| Fe-ADH-like |
cd14861 |
Iron-containing alcohol dehydrogenases-like; This family contains proteins similar to ... |
18-357 |
1.21e-07 |
|
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: 52.90 E-value: 1.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 18 VIDKTGEYVKPLGHTA-LVIADKLVWEI-AADRVVKSLEQADI-TAIKVEFQGEASKNEVNRIADEGRSGQVDIVIGVGG 94
Cdd:cd14861 12 AIAELPEELKALGIRRpLLVTDPGLAALgIVDRVLEALGAAGLsPAVFSDVPPNPTEADVEAGVAAYREGGCDGIIALGG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 95 GKTLDTAKAVNELLG----------------------SSVVIVPTTASTDAPTSALSVLYTDE-----GAFDTYTFfskn 147
Cdd:cd14861 92 GSAIDAAKAIALMAThpgplwdyedgeggpaaitpavPPLIAIPTTAGTGSEVGRAAVITDDDtgrkkIIFSPKLL---- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 148 PSLILVDTKVISQAPPL----------------FLSSG---IADAMA--------TWIEaRAV-----IEARATTMAGgl 195
Cdd:cd14861 168 PKVAICDPELTLGLPPRltaatgmdalthcieaYLSPGfhpMADGIAleglrlisEWLP-RAVadgsdLEARGEMMMA-- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 196 ptlaaeaiaskceevlfdyglqayesvkrkvvtpALEAvveantllsGLGFESgGLAGAHAIHNGFtvleGDIHHLTHGQ 275
Cdd:cd14861 245 ----------------------------------ALMG---------AVAFQK-GLGAVHALAHAL----GALYGLHHGL 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 276 KVA-----------------FGTLVQ-LALEKRPLTEVERYI-DFYLKLDLPVTLEDIklqDASREDLYRVAQAATKEGE 336
Cdd:cd14861 277 LNAillpyvlrfnrpavedkLARLARaLGLGLGGFDDFIAWVeDLNERLGLPATLSEL---GVTEDDLDELAELALADPC 353
|
410 420
....*....|....*....|.
gi 515237560 337 TAHNlPFAVTADDVLDAILAA 357
Cdd:cd14861 354 HATN-PRPVTAEDYRALLREA 373
|
|
| NADPH_BDH |
cd08179 |
NADPH-dependent butanol dehydrogenase involved in the butanol and ethanol formation pathway in ... |
6-350 |
1.58e-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: 1.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 6 FISPDKYVQGKNVIdktgEYVKPL-GHTALVIADKLVWEIAA--DRVVKSLEQADITaIKV--EFQGEASKNEVNRIADE 80
Cdd:cd08179 2 FFVPRDIYFGEGAL----EYLKTLkGKRAFIVTGGGSMKRNGflDKVEDYLKEAGME-VKVfeGVEPDPSVETVEKGAEA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 81 GRSGQVDIVIGVGGGKTLDTAKA--------------------VNELLGSSVVI-VPTTASTDAPTSALSVLyTDEGAFD 139
Cdd:cd08179 77 MREFEPDWIIAIGGGSVIDAAKAmwvfyeypeltfedalvpfpLPELRKKARFIaIPSTSGTGSEVTRASVI-TDTEKGI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 140 TYTFFSKN--PSLILVDTKVISQAPP-LFLSSGIaDAMATWIEarAVIEARATTMAgglPTLAAEAIaskceEVLFDYGL 216
Cdd:cd08179 156 KYPLASFEitPDVAILDPELTMTMPPhVTANTGM-DALTHAIE--AYVSTLANDFT---DALALGAI-----LDIFENLP 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 217 QAYESVKRKVvtpALEAVVEANTlLSGLGFESGGLAGAHAI-HNGftvleGDIHHLTHG--------------QKVAFGT 281
Cdd:cd08179 225 KSYNGGKDLE---AREKMHNASC-LAGMAFSNSGLGIVHSMaHKG-----GAFFGIPHGlanaillpyviefnSKDPEAR 295
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515237560 282 LVQLALEKRPLTE------VERYIDFYLKLDLPVTLEDIKL-QDASREDLYRVAQAATKEGETAHNlPFAVTADDV 350
Cdd:cd08179 296 ARYAALLIGLTDEelvedlIEAIEELNKKLGIPLSFKEAGIdEDEFFAKLDEMAENAMNDACTGTN-PRKPTVEEM 370
|
|
| Fe-ADH-like |
cd14865 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
6-357 |
2.06e-07 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341487 [Multi-domain] Cd Length: 383 Bit Score: 52.16 E-value: 2.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 6 FISPDKYVQGKNVIDKTGEYVKPLGHT-ALVIADKLVWEIA-ADRVVKSLEQAD-ITAIKVEFQGEASKNEVNRIADEGR 82
Cdd:cd14865 3 FFNPTKIVSGAGALENLPAELARLGARrPLIVTDKGLAAAGlLKKVEDALGDAIeIVGVFDDVPPDSSVAVVNEAAARAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 83 SGQVDIVIGVGGGKTLDTAKAVNELL-----------GSSV--------VIVPTTASTDAPTSALSVLYtDEGAFDTYTF 143
Cdd:cd14865 83 EAGADGIIAVGGGSVIDTAKGVNILLseggddlddygGANRltrplkplIAIPTTAGTGSEVTLVAVIK-DEEKKVKLLF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 144 FSKN--PSLILVDTKVISQAPPLFLSSGIADAMATWIEARAVIEARATTMAgglptLAAEAIaskceEVLFDYGLQAYES 221
Cdd:cd14865 162 VSPFllPDVAILDPRLTLSLPPKLTAATGMDALTHAIEAYTSLQKNPISDA-----LALQAI-----RLISENLPKAVKN 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 222 VKRKVvtpALEAVVEANTlLSGLGFESGGLAGAHAIhnGFTVleGDIHHLTHGQ--------------KVAFGTLVQLAL 287
Cdd:cd14865 232 GKDLE---ARLALAIAAT-MAGIAFSNSMVGLVHAI--AHAV--GAVAGVPHGLansillphvmrynlDAAAERYAELAL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 288 ---------EKRPLTEVERYIDFYLKL----DLPVTLEDIKLQdasREDLYRVAQAATKEGETAHNlPFAVTADDVLDAI 354
Cdd:cd14865 304 alaygvtpaGRRAEEAIEAAIDLVRRLhelcGLPTRLRDVGVP---EEQLEAIAELALNDGAILFN-PREVDPEDILAIL 379
|
...
gi 515237560 355 LAA 357
Cdd:cd14865 380 EAA 382
|
|
| Fe-ADH-like |
cd17814 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
6-180 |
3.01e-07 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341489 [Multi-domain] Cd Length: 374 Bit Score: 51.78 E-value: 3.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 6 FISPDkYVQGKNVIDKTGEYVKPLGHT-ALVIADKLVWEIA-ADRVVKSLEQADITAikVEFQGEaSKN----EVNRIAD 79
Cdd:cd17814 2 FVAPE-FIFGVGARKLAGRYAKNLGARkVLVVTDPGVIKAGwVDEVLDSLEAEGLEY--VVFSDV-TPNprdfEVMEGAE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 80 EGRSGQVDIVIGVGGGKTLDTAKA----------VNELLGSSVV--------IVPTTASTDAPTSALSVLyTDEGAFDTY 141
Cdd:cd17814 78 LYREEGCDGIVAVGGGSPIDCAKGigivvsngghILDYEGVDKVrrplppliCIPTTAGSSADVSQFAII-TDTERRVKM 156
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 515237560 142 TFFSKN--PSLILVDTKVISQAPP-LFLSSGIaDAMATWIEA 180
Cdd:cd17814 157 AIISKTlvPDVSLIDPETLTTMDPeLTACTGM-DALTHAIEA 197
|
|
| MAR-like |
cd08192 |
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic ... |
73-355 |
6.70e-07 |
|
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic microbes; Maleylacetate reductase (MAR) plays an important role in the degradation of aromatic compounds in aerobic microbes. In fungi and yeasts, the enzyme is involved in the catabolism of compounds such as phenol, tyrosine, benzoate, 4-hydroxybenzoate and resorcinol. In bacteria, the enzyme contributes to the degradation of resorcinol, 2,4-dihydroxybenzoate ([beta]-resorcylate) and 2,6-dihydroxybenzoate ([gamma]-resorcylate) via hydroxyquinol and maleylacetate. Maleylacetate reductase (MAR) catalyzes NADH- or NADPH-dependent reduction, at the carbon-carbon double bond, of maleylacetate or 2-chloromaleylacetate to 3-oxoadipate. In the case of 2-chloromaleylacetate, MAR initially catalyzes the NAD(P)H-dependent dechlorination to maleylacetate, which is then reduced to 3-oxoadipate. This enzyme is a homodimer. It is inhibited by thiol-blocking reagents such as p-chloromercuribenzoate and Hg++, indicating that the cysteine residue is probably necessary for the catalytic activity of maleylacetate reductase.
Pssm-ID: 341471 [Multi-domain] Cd Length: 380 Bit Score: 50.71 E-value: 6.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 73 EVNRIADEGRSGQVDIVIGVGGGKTLDTAKAVNELLGSSV--------------------------VIVPTTASTdAPTS 126
Cdd:cd08192 67 DVLEAARAVREAGADLLVSLGGGSPIDAAKAVALALAEDVtdvdqldaledgkridpnvtgptlphIAIPTTLSG-AEFT 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 127 ALSvLYTDE--GAFDTYTFFSKNPSLILVDTKVISQAPP-LFLSSGIadamatwieaRAV---IEaratTMAGGLPTLAA 200
Cdd:cd08192 146 AGA-GATDDdtGHKQGFAHPELGPDAVILDPELTLHTPErLWLSTGI----------RAVdhaVE----TLCSPQATPFV 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 201 EAIASKCEEVLFDYGLQayesvkrkvvTPALEAVVEANTLL------SGLGFESGGLAGA-HAI-----------HnGFT 262
Cdd:cd08192 211 DALALKALRLLFEGLPR----------SKADPEDLEARLKCqlaawlSLFGLGSGVPMGAsHAIghqlgplygvpH-GIT 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 263 -------VLEGDIHHLTHGQ----KVAFGTLVQLALEKRPLTEVeryID-FYLKLDLPVTLEDIKLqdaSREDLYRVAQA 330
Cdd:cd08192 280 scimlpaVLRFNAPVNAERQrliaRALGLVTGGLGREAADAADA---IDaLIRELGLPRTLRDVGV---GRDQLEKIAEN 353
|
330 340
....*....|....*....|....*
gi 515237560 331 ATKEGETAHNLPFAVTADDVLdAIL 355
Cdd:cd08192 354 ALTDVWCRTNPRPITDKDDVL-EIL 377
|
|
| AAD_C |
cd08178 |
C-terminal alcohol dehydrogenase domain of the acetaldehyde dehydrogenase-alcohol ... |
31-275 |
2.05e-06 |
|
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: 49.11 E-value: 2.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 31 HTALVIADK-LVWEIAADRVVKSLEQADI-TAIKVEFQGEASKNEVNRIADEGRSGQVDIVIGVGGGKTLDTAKAV---- 104
Cdd:cd08178 24 KRAFIVTDRvLYKLGYVDKVLDVLEARGVeTEVFSDVEPDPTLSTVRKGLEAMNAFKPDVIIALGGGSAMDAAKIMwlfy 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 105 -------NEL----------------LG--SSVVIVPTTASTDAPTSALSVLyTDEGAFDTYTFFSKN--PSLILVDTKV 157
Cdd:cd08178 104 ehpetkfEDLaqrfmdirkrvykfpkLGkkAKLVAIPTTSGTGSEVTPFAVI-TDDKTGKKYPLADYAltPDMAIVDPEL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 158 ISQAPP-LFLSSGIaDAMATWIEARAVIEARATTMAgglptLAAEAIaskceEVLFDYGLQAYESVKRKVvtpALEAVVE 236
Cdd:cd08178 183 VMTMPKrLTADTGI-DALTHAIEAYVSVMASDYTDG-----LALQAI-----KLIFEYLPRSYNNGNDIE---AREKMHN 248
|
250 260 270
....*....|....*....|....*....|....*....
gi 515237560 237 ANTlLSGLGFESGGLAGAHAIHNGFtvleGDIHHLTHGQ 275
Cdd:cd08178 249 AAT-IAGMAFANAFLGICHSLAHKL----GAAFHIPHGR 282
|
|
| PRK15454 |
PRK15454 |
ethanolamine utilization ethanol dehydrogenase EutG; |
67-275 |
2.95e-06 |
|
ethanolamine utilization ethanol dehydrogenase EutG;
Pssm-ID: 185351 [Multi-domain] Cd Length: 395 Bit Score: 48.87 E-value: 2.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 67 GEASKNEVNRIADEGRSGQVDIVIGVGGGKTLDTAKAVNELLGS------------------SVVIVPTTASTDAPTSAL 128
Cdd:PRK15454 88 GEPCITDVCAAVAQLRESGCDGVIAFGGGSVLDAAKAVALLVTNpdstlaemsetsvlqprlPLIAIPTTAGTGSETTNV 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 129 SVLYTD-EGAFDTYTFFSKNPSLILVDTKVISQAPPLFLSSGIADAMATWIEARAVIEARATTmagglPTLAAEAIA--- 204
Cdd:PRK15454 168 TVIIDAvSGRKQVLAHASLMPDVAILDAALTEGVPSHVTAMTGIDALTHAIEAYSALNATPFT-----DSLAIGAIAmig 242
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515237560 205 -SKCEEVLFDYGLQAYESVkrkvvtpaLEAvveanTLLSGLGFESGGLAGAHAIHNGftvlEGDIHHLTHGQ 275
Cdd:PRK15454 243 kSLPKAVGYGHDLAARESM--------LLA-----SCMAGMAFSSAGLGLCHAMAHQ----PGAALHIPHGL 297
|
|
| PDD |
cd08180 |
1,3-propanediol dehydrogenase (PPD) catalyzes the reduction of 3-hydroxypropionaldehyde (3-HPA) ... |
87-350 |
2.09e-04 |
|
1,3-propanediol dehydrogenase (PPD) catalyzes the reduction of 3-hydroxypropionaldehyde (3-HPA) to 1,3-propanediol in glycerol metabolism; 1,3-propanediol dehydrogenase (PPD) plays a role in glycerol metabolism of some bacteria in anaerobic conditions. In this degradation pathway, glycerol is converted in a two-step process to 1,3-propanediol (1,3-PD) which is then excreted into the extracellular medium. The first reaction involves the transformation of glycerol into 3-hydroxypropionaldehyde (3-HPA) by a coenzyme B-12-dependent dehydratase. The second reaction involves the dismutation of the 3-hydroxypropionaldehyde (3-HPA) to 1,3-propanediol by the NADH-linked 1,3-propanediol dehydrogenase (PPD). The enzyme requires iron ion for its function. Because many genes in this pathway are present in the propanediol utilization (pdu) operon, they are also named pdu genes. PPD is a member of the iron-containing alcohol dehydrogenase superfamily. The PPD structure has a dehydroquinate synthase-like fold.
Pssm-ID: 341459 [Multi-domain] Cd Length: 333 Bit Score: 42.87 E-value: 2.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 87 DIVIGVGGGKTLDTAKAVNELLGSSVVI--------VPTTASTDAPTSALSVLyTDEGAFDTYTFFSKN--PSLILVDTK 156
Cdd:cd08180 80 DTIIALGGGSAIDAAKAIIYFALKQKGNikkplfiaIPTTSGTGSEVTSFAVI-TDPEKGIKYPLVDDSmlPDIAILDPE 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 157 VISQAPPLFLS-SGIaDAMATWIEARAVIEARATTMAgglptLAAEAIaskceEVLFDYGLQAYESVKRKVvtpALEAVV 235
Cdd:cd08180 159 LVKSVPPKVTAdTGM-DVLTHALEAYVSTNANDFTDA-----LAEKAI-----KLVFENLPRAYRDGDDLE---AREKMH 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 236 EANTlLSGLGFESGGL----AGAHAIhngftvleGDIHHLTHGQkvAFGTLvqlalekrpLTEVERY----IDFYLK-LD 306
Cdd:cd08180 225 NASC-MAGIAFNNAGLginhSLAHAL--------GGRFHIPHGR--ANAIL---------LPYVIEFliaaIRRLNKkLG 284
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 515237560 307 LPVTLEDIKL-QDASREDLYRVAQAATKEGETAHNlPFAVTADDV 350
Cdd:cd08180 285 IPSTLKELGIdEEEFEKAIDEMAEAALADRCTATN-PRKPTAEDL 328
|
|
| Fe-ADH-like |
cd08186 |
Iron-containing alcohol dehydrogenase; This family contains iron-containing alcohol ... |
15-108 |
7.76e-04 |
|
Iron-containing alcohol dehydrogenase; This family contains iron-containing alcohol dehydrogenase (ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. The ADH of hyperthermophilic archaeon Thermococcus hydrothermalis oxidizes a series of primary aliphatic and aromatic alcohols, preferentially from C2 to C8, but is also active towards methanol and glycerol, and is stereospecific for monoterpenes. It has been suggested that the type III ADHs in microorganisms are involved in acetaldehyde detoxication rather than in alcohol turnover.
Pssm-ID: 341465 [Multi-domain] Cd Length: 380 Bit Score: 41.10 E-value: 7.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 15 GKNVIDKTGEYVKPLGHT-ALVIADKLVWEI--AADRVVKSLEQADITAI---KVefqgeaSKNEVNRIADE----GRSG 84
Cdd:cd08186 7 GVGAIAKIKDILKDLGIDkVIIVTGRSSYKKsgAWDDVEKALEENGIEYVvydKV------TPNPTVDQADEaaklARDF 80
|
90 100
....*....|....*....|....
gi 515237560 85 QVDIVIGVGGGKTLDTAKAVNELL 108
Cdd:cd08186 81 GADAVIAIGGGSPIDTAKSVAVLL 104
|
|
| Fe-ADH_KdnB-like |
cd08184 |
Iron-containing alcohol dehydrogenase similar to Shewanella oneidensis KdnB required for Kdo8N ... |
11-131 |
2.17e-03 |
|
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: 39.56 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 11 KYVQGKNVIDKTGEYVKPLGHTAlviADKLVWEIaaDRVVKSLEQADITAIK-------VEFQGEASKNEVNRIADEGR- 82
Cdd:cd08184 3 KYLFGRGSFDQLGELLAERRKSN---NDYVVFFI--DDVFKGKPLLDRLPLQngdllifVDTTDEPKTDQIDALRAQIRa 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515237560 83 --SGQVDIVIGVGGGKTLDTAKAVNELL---GSS---------------VVIVPTTASTDAPTSALSVL 131
Cdd:cd08184 78 enDKLPAAVVGIGGGSTMDIAKAVSNMLtnpGSAadyqgwdlvknpgiyKIGVPTLSGTGAEASRTAVL 146
|
|
| DOIS |
cd08197 |
2-deoxy-scyllo-inosose synthase (DOIS) catalyzes carbocycle formation from ... |
15-173 |
3.69e-03 |
|
2-deoxy-scyllo-inosose synthase (DOIS) catalyzes carbocycle formation from D-glucose-6-phosphate to 2-deoxy-scyllo-inosose; 2-deoxy-scyllo-inosose synthase (DOIS) catalyzes carbocycle formation from D-glucose-6-phosphate to 2-deoxy-scyllo-inosose through a multistep reaction in the biosynthesis of aminoglycoside antibiotics. 2-deoxystreptamine (DOS)-containing aminoglycoside antibiotics includes neomycin, kanamycin, gentamicin, and ribostamycin. They are important antibacterial agents. DOIS is a homolog of the dehydroquinate synthase which catalyzes the cyclization of 3-deoxy-D-arabino-heputulosonate-7-phosphate to dehydroquinate (DHQ) in the shikimate pathway.
Pssm-ID: 341476 Cd Length: 355 Bit Score: 39.10 E-value: 3.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 15 GKNVIDKTGEYVKPLGHTAL-VIADKLVWEIAADRVVKSLEQADITAIKVEFQ-GEASKN--EVNRIADE----G---RS 83
Cdd:cd08197 7 GRGILESLLSILEELKADRHfLVTDSNVNDLYGDRLLEGLKKAGIPVELLVVPaGESNKTlsTLTELAERliaaGitrRS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515237560 84 gqvdIVIGVGGGKTLDTAKAVNELL--GSSVVIVPTT--ASTDAPTSALSVLYTDEGafdtytffsKN-------PSLIL 152
Cdd:cd08197 87 ----VIIALGGGVVGNIAGLLAGLLyrGIRLVHVPTTllAQSDSVLSLKQAVNGKSG---------KNlvgsyyaPLFVF 153
|
170 180
....*....|....*....|.
gi 515237560 153 VDTKVISQAPPLFLSSGIADA 173
Cdd:cd08197 154 VDTEFLKTLPPRQIRSGLCEA 174
|
|
| |
