|
Name |
Accession |
Description |
Interval |
E-value |
| gldA |
PRK09423 |
glycerol dehydrogenase; Provisional |
1-365 |
0e+00 |
|
glycerol dehydrogenase; Provisional
Pssm-ID: 181843 Cd Length: 366 Bit Score: 626.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 1 MLKVIQSPAKYLQGPDAAVLFGQYAKNLAESFFVIADDFVMKLAGEKVVNGLQSHDIRCHAERFNGECSHAEINRLMAIL 80
Cdd:PRK09423 1 MDRIFISPSKYVQGKGALARLGEYLKPLGKRALVIADEFVLGIVGDRVEASLKEAGLTVVFEVFNGECSDNEIDRLVAIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 81 QKQGCRGVVGIGGGKTLDTAKAIGYYQKLPVVVIPTIASTDAPTSALSVIYTEAGEFEEYLIYPKNPDMVVMDTAIIAKA 160
Cdd:PRK09423 81 EENGCDVVIGIGGGKTLDTAKAVADYLGVPVVIVPTIASTDAPTSALSVIYTEEGEFERYLFLPKNPDLVLVDTAIIAKA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 161 PVRLLVSGMGDALSTWFEAKACYDARATSMAGGQSTEAALSLARLCYDTLLAEGEKARLAAQAGVVTEALERIIEANTYL 240
Cdd:PRK09423 161 PARFLAAGIGDALATWFEARACSRSGGTTMAGGKPTLAALALAELCYETLLEDGLKAKLAVEAKVVTPALENVIEANTLL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 241 SGIGFESSGLAAAHAIHNGFTILEECHHLYHGEKVAFGTLAQLVLQNSPMDEIETVLGFCQRVGLPVTLAQMGVKEGIDA 320
Cdd:PRK09423 241 SGLGFESGGLAAAHAIHNGLTALEDTHHLTHGEKVAFGTLTQLVLENRPKEEIEEVIDFCHAVGLPTTLADLGLKEDSDE 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1709669016 321 KIAAVAKATCAEGETIHNMPFAVTPESVHAAILTADLLGQQWLAR 365
Cdd:PRK09423 321 ELRKVAEAACAEGETIHNMPFKVTPEDVAAAILAADAYGQRYKQE 365
|
|
| 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: 595.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 8 PAKYLQGPDAAVLFGQYAKNLAESFFVIADDFVMKLAGEKVVNGLQSHDIRCHAERFNGECSHAEINRLMAILQKQGCRG 87
Cdd:cd08170 1 PSRYVQGPGALDRLGEYLAPLGKKALVIADPFVLDLVGERLEESLEKAGLEVVFEVFGGECSREEIERLAAIARANGADV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 88 VVGIGGGKTLDTAKAIGYYQKLPVVVIPTIASTDAPTSALSVIYTEAGEFEEYLIYPKNPDMVVMDTAIIAKAPVRLLVS 167
Cdd:cd08170 81 VIGIGGGKTIDTAKAVADYLGLPVVIVPTIASTDAPCSALSVIYTEDGEFDEYLFLPRNPDLVLVDTEIIAKAPVRFLVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 168 GMGDALSTWFEAKACYDARATSMAGGQSTEAALSLARLCYDTLLAEGEKARLAAQAGVVTEALERIIEANTYLSGIGFES 247
Cdd:cd08170 161 GMGDALATYFEARACARSGAPNMAGGRPTLAALALAELCYDTLLEYGVAAKAAVEAGVVTPALEAVIEANTLLSGLGFES 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 248 SGLAAAHAIHNGFTILEECHHLYHGEKVAFGTLAQLVLQNSPMDEIETVLGFCQRVGLPVTLAQMGVKEGIDAKIAAVAK 327
Cdd:cd08170 241 GGLAAAHAIHNGLTALPETHHLLHGEKVAFGTLVQLVLEGRPDEEIEEVIRFCRSVGLPVTLADLGLEDVTDEELRKVAE 320
|
330 340 350
....*....|....*....|....*....|.
gi 1709669016 328 ATCAEGETIHNMPFAVTPESVHAAILTADLL 358
Cdd:cd08170 321 AACAPGETIHNMPFPVTPEDVVDAILAADAL 351
|
|
| GldA |
COG0371 |
Glycerol dehydrogenase or related enzyme, iron-containing ADH family [Energy production and ... |
3-355 |
6.87e-174 |
|
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: 487.75 E-value: 6.87e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 3 KVIQSPAKYLQGPDAAVLFGQYAKNLAESFFVIADDFVMKLAGEKVVNGLQSHDIRCHAERFNGECSHAEINRLMAILQK 82
Cdd:COG0371 1 RVIILPRRYVQGEGALDELGEYLADLGKRALIITGPTALKAAGDRLEESLEDAGIEVEVEVFGGECSEEEIERLAEEAKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 83 QGCRGVVGIGGGKTLDTAKAIGYYQKLPVVVIPTIASTDAPTSALSVIYTEAGEFEEYLIYPKNPDMVVMDTAIIAKAPV 162
Cdd:COG0371 81 QGADVIIGVGGGKALDTAKAVAYRLGLPVVSVPTIASTDAPASPLSVIYTEDGAFDGYSFLAKNPDLVLVDTDIIAKAPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 163 RLLVSGMGDALSTWFEAKACYDARATsMAGGQSTEAALSLARLCYDTLLAEGEKARLAAQAGVVTEALERIIEANTYLSG 242
Cdd:COG0371 161 RLLAAGIGDALAKWYEARDWSLAHRD-LAGEYYTEAAVALARLCAETLLEYGEAAIKAVEAGVVTPALERVVEANLLLSG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 243 IGF----ESSGLAAAHAIHNGFTILEECHHLYHGEKVAFGTLAQLVLQNSPmDEIETVLGFCQRVGLPVTLAQMGVKEGI 318
Cdd:COG0371 240 LAMgigsSRPGSGAAHAIHNGLTALPETHHALHGEKVAFGTLVQLVLEGRP-EEIEELLDFLRSVGLPTTLADLGLDDET 318
|
330 340 350
....*....|....*....|....*....|....*..
gi 1709669016 319 DAKIAAVAKATCAEGETIHNMPFAVTPESVHAAILTA 355
Cdd:COG0371 319 EEELLTVAEAARPERYTILNLPFEVTPEAVEAAILAT 355
|
|
| GlyDH-like |
cd08550 |
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins. ... |
8-355 |
2.20e-134 |
|
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: 387.28 E-value: 2.20e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 8 PAKYLQGPDAAVLFGQYAKNLAESFFVIADDFVMKLAGEKVVNGLQSHDIRCHAERFNGECSHAEINRLMAILQKQGCRG 87
Cdd:cd08550 1 PGRYIQEPGILAKAGEYIAPLGKKALIIGGKTALEAVGEKLEKSLEEAGIDYEVEVFGGECTEENIERLAEKAKEEGADV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 88 VVGIGGGKTLDTAKAIGYYQKLPVVVIPTIASTDAPTSALSVIYTEAGEFEEYLIYPKNPDMVVMDTAIIAKAPVRLLVS 167
Cdd:cd08550 81 IIGIGGGKVLDTAKAVADRLGLPVVTVPTIAATCAAWSALSVLYDEEGEFLGYSLLKRSPDLVLVDTDIIAAAPVRYLAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 168 GMGDALSTWFEAKACYDARATSMAggqsTEAALSLARLCYDTLLAEGEKARLAAQAGVVTEALERIIEANTYLSGIGFES 247
Cdd:cd08550 161 GIGDTLAKWYEARPSSRGGPDDLA----LQAAVQLAKLAYDLLLEYGVQAVEDVRQGKVTPALEDVVDAIILLAGLVGSL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 248 SG----LAAAHAIHNGFTILEECHHLYHGEKVAFGTLAQLVLQNSPMDEIETVLGFCQRVGLPVTLAQMGVKEgIDAKIA 323
Cdd:cd08550 237 GGggcrTAAAHAIHNGLTKLPETHGTLHGEKVAFGLLVQLALEGRSEEEIEELIEFLRRLGLPVTLEDLGLEL-TEEELR 315
|
330 340 350
....*....|....*....|....*....|..
gi 1709669016 324 AVAKATCAEGETIHNMPFAVTPESVHAAILTA 355
Cdd:cd08550 316 KIAEYACDPPDMAHMLPFPVTPEMLAEAILAA 347
|
|
| GlyDH-like |
cd08172 |
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins ... |
53-354 |
4.85e-106 |
|
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins that have yet to be characterized, but show sequence homology with glycerol dehydrogenase. Glycerol dehydrogenases (GlyDH) is a key enzyme in the glycerol dissimilation pathway. In anaerobic conditions, many microorganisms utilize glycerol as a source of carbon through coupled oxidative and reductive pathways. One of the pathways involves the oxidation of glycerol to dihydroxyacetone with the reduction of NAD+ to NADH catalyzed by glycerol dehydrogenases. Dihydroxyacetone is then phosphorylated by dihydroxyacetone kinase and enters the glycolytic pathway for further degradation. The activity of GlyDH is zinc-dependent; the zinc ion plays a role in stabilizing an alkoxide intermediate at the active site.
Pssm-ID: 341451 [Multi-domain] Cd Length: 346 Bit Score: 314.84 E-value: 4.85e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 53 QSHDIRCHAERFNGECSHAEINRLMAILQKQGCRGVVGIGGGKTLDTAKAIGYYQKLPVVVIPTIASTDAPTSALSVIYT 132
Cdd:cd08172 44 KLFEIEYPVLRYDGECSYEEIDRLAEEAKEHQADVIIGIGGGKVLDTAKAVADKLNIPLILIPTLASNCAAWTPLSVIYD 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 133 EAGEFEEYLIYPKNPDMVVMDTAIIAKAPVRLLVSGMGDALSTWFEAkacyDARATSMAGGQST-EAALSLARLCYDTLL 211
Cdd:cd08172 124 EDGEFIGYDYFPRSAYLVLVDPRLLLDSPKDYFVAGIGDTLAKWYEA----DAILRQLEELPAFlQLARQAAKLCRDILL 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 212 AEGEKARLAAQAGVVTEALERIIEANTYLSGI--GF--ESSGLAAAHAIHNGFTILEECHHLYHGEKVAFGTLAQLVLQN 287
Cdd:cd08172 200 KDSEQALADLEAGKLTPAFIKVVETIIALAGMvgGFgdEYGRSAGAHAIHNGLTKLPETHHFLHGEKVAYGILVQLALEG 279
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1709669016 288 SpMDEIETVLGFCQRVGLPVTLAQMGVKEGIDAKIAAVAKATCAEGETIHNMPFAVTPESVHAAILT 354
Cdd:cd08172 280 K-WDEIKKLLPFYRRLGLPTSLADLGLTDDTEEALQKIAAFAASPEESIHLLPPDVTAEEVLQAIEK 345
|
|
| Fe-ADH |
pfam00465 |
Iron-containing alcohol dehydrogenase; |
8-348 |
1.16e-68 |
|
Iron-containing alcohol dehydrogenase;
Pssm-ID: 425696 [Multi-domain] Cd Length: 362 Bit Score: 219.78 E-value: 1.16e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 8 PAKYLQGPDAAVLFGQYAKNLAESFFVIADDFVMKL-AGEKVVNGLQSHDIRC-HAERFNGECSHAEINRLMAILQKQGC 85
Cdd:pfam00465 1 PTRIVFGAGALAELGEELKRLGARALIVTDPGSLKSgLLDKVLASLEEAGIEVvVFDGVEPEPTLEEVDEAAALAREAGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 86 RGVVGIGGGKTLDTAKAIGYY------------------QKLPVVVIPTIASTDAPTSALSVIYTEAGEFEEYLIYPK-N 146
Cdd:pfam00465 81 DVIIAVGGGSVIDTAKAIALLltnpgdvwdylggkpltkPALPLIAIPTTAGTGSEVTPLAVITDTETGEKLGIFSPKlL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 147 PDMVVMDTAIIAKAPVRLLVSGMGDALSTWFEAkacYDARATSMAGGQSTEAALSLARLCYDTLLAEGEKArlaaqagvv 226
Cdd:pfam00465 161 PDLAILDPELTLTLPPRLTAATGMDALAHAVEA---YVSKGANPLTDALALEAIRLIAENLPRAVADGEDL--------- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 227 tEALERIIEANTyLSGIGFESSGLAAAHAIHNGFTILEECHH-LYHGEKVAFGT----------LAQLVL-------QNS 288
Cdd:pfam00465 229 -EARENMLLAST-LAGLAFSNAGLGAAHALAHALGGRYGIPHgLANAILLPYVLrfnapaapekLAQLARalgedsdEEA 306
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 289 PMDEIETVLGFCQRVGLPVTLAQMGVKEgidAKIAAVAKATCAEGeTIHNMPFAVTPESV 348
Cdd:pfam00465 307 AEEAIEALRELLRELGLPTTLSELGVTE---EDLDALAEAALRDR-SLANNPRPLTAEDI 362
|
|
| GlyDH-like |
cd08171 |
Glycerol dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins ... |
14-353 |
1.38e-67 |
|
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: 216.62 E-value: 1.38e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 14 GPDAAVLFGQYAKNLAESFFVIADDFVMKLAGEKVVNGLQSHDIRCHAER-FNGECSHAEINRLMAILQKQGCRGVVGIG 92
Cdd:cd08171 7 GEDAYDAIPKICSPYGKKVVVIGGKKALAAAKPKLRAALEGSGLEITDFIwYGGEATYENVEKLKANPEVQEADMIFAVG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 93 GGKTLDTAKAIGYYQKLPVVVIPTIASTDAPTSALSVIYTEAGEFEEYLIYPKNPDMVVMDTAIIAKAPVRLLVSGMGDA 172
Cdd:cd08171 87 GGKAIDTVKVLADRLNKPVFTFPTIASNCAAVTAVSVMYNPDGSFKEYYFLKRPPVHTFIDTEIIAEAPEKYLWAGIGDT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 173 LSTWFEakACYDARATSMAggQSTEAALSLARLCYDTLLAEGEKARLAAQAGVVTEALERIIEANTYLSGIgfeSSGLAA 252
Cdd:cd08171 167 LAKYYE--VEFSARGDELD--HTNALGVAISKMCSEPLLKYGVQALEDCRANKVSDALEQVVLDIIVTTGL---VSNLVE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 253 -------AHAIHNGFTILEEC--HHLyHGEKVAFGTLAQLVLQNSpMDEIETVLGFCQRVGLPVTLAQMGVKEgidAKIA 323
Cdd:cd08171 240 pdynsslAHALYYGLTTLPQIeeEHL-HGEVVSYGVLVLLTVDGQ-FEELEKVYAFNKSIGLPTCLADLGLTV---EDLE 314
|
330 340 350
....*....|....*....|....*....|
gi 1709669016 324 AVAKATcAEGETIHNMPFAVTPESVHAAIL 353
Cdd:cd08171 315 KVLDKA-LKTKDLRHSPYPITKEMFEEAIK 343
|
|
| DHQ_Fe-ADH |
cd07766 |
Dehydroquinate synthase-like (DHQ-like) and iron-containing alcohol dehydrogenases (Fe-ADH); ... |
8-320 |
1.60e-49 |
|
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: 167.54 E-value: 1.60e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 8 PAKYLQGPDAAVLFGQYAKNLAESFFVIADDFVMKLAGEKVVNGLQSHdIRCHAERF-NGECSHAEINRLMAILQKQGCR 86
Cdd:cd07766 1 PTRIVFGEGAIAKLGEIKRRGFDRALVVSDEGVVKGVGEKVADSLKKG-LAVAIFDFvGENPTFEEVKNAVERARAAEAD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 87 GVVGIGGGKTLDTAKAIGY--YQKLPVVVIPTIASTDAPTSALSVIYTEAGEFEEyLIYPKNPDMVVMDTAIIAKAPVRL 164
Cdd:cd07766 80 AVIAVGGGSTLDTAKAVAAllNRGIPFIIVPTTASTDSEVSPKSVITDKGGKNKQ-VGPHYNPDVVFVDTDITKGLPPRQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 165 LVSGMGDALSTWFEakacydaratsmaggqsteaalslarlcydtllaegekarlaaqagvvteaLERIIEANTYLSGIG 244
Cdd:cd07766 159 VASGGVDALAHAVE---------------------------------------------------LEKVVEAATLAGMGL 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 245 FESSGLAAAHAIHNGFTILeecHHLYHGEKVAFGTLAQLVLQNSPMDE----IETVLGFCQRVGLPVTLAQMGV-KEGID 319
Cdd:cd07766 188 FESPGLGLAHAIGHALTAF---EGIPHGEAVAVGLPYVLKVANDMNPEpeaaIEAVFKFLEDLGLPTHLADLGVsKEDIP 264
|
.
gi 1709669016 320 A 320
Cdd:cd07766 265 K 265
|
|
| PRK10586 |
PRK10586 |
putative oxidoreductase; Provisional |
63-360 |
5.97e-49 |
|
putative oxidoreductase; Provisional
Pssm-ID: 182570 Cd Length: 362 Bit Score: 168.75 E-value: 5.97e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 63 RFNGECSHAEINRLMAiLQKQGCRGVVGIGGGKTLDTAKAIGYYQKLPVVVIPTIASTDAPTSALSVIYTEAGEFEEYLI 142
Cdd:PRK10586 66 LFRGHCSESDVAQLAA-ASGDDRQVVIGVGGGALLDTAKALARRLGLPFVAIPTIAATCAAWTPLSVWYNDAGQALHFEI 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 143 YPKNPDMVVMDTAIIAKAPVRLLVSGMGDALSTWFEAKACYDARAT-SMAGGQSTEAALSLArlcyDTLLAEGEKARLAA 221
Cdd:PRK10586 145 FDDANFLVLVEPRIILNAPQEYLLAGIGDTLAKWYEAVVLAPQPETlPLTVRLGINNALAIR----DVLLNSSEQALADQ 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 222 QAGVVTEA----LERIIEANTYLSGIGFESSGLAAAHAIHNGFTILEECHHLYHGEKVAFGTLAQLVLQNSPmDEIETVL 297
Cdd:PRK10586 221 QNGQLTQDfcdvVDAIIAGGGMVGGLGERYTRVAAAHAVHNGLTVLPQTEKFLHGTKVAYGILVQSALLGQD-DVLAQLI 299
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1709669016 298 GFCQRVGLPVTLAQMGVKEGIDAKIAAVAKATCAEGETIHNMPFAVTPESVHAAILTADLLGQ 360
Cdd:PRK10586 300 GAYQRFHLPTTLAELDVDINNQAEIDRVIAHTLRPVESIHYLPVTLTPDTLRAAFEKVESFKA 362
|
|
| G1PDH-like |
cd08174 |
Glycerol-1-phosphate dehydrogenase-like; These glycerol-1-phosphate dehydrogenase-like ... |
34-328 |
4.96e-28 |
|
Glycerol-1-phosphate dehydrogenase-like; These glycerol-1-phosphate dehydrogenase-like proteins have not been characterized. The protein sequences have high similarity with that of glycerol-1-phosphate dehydrogenase (G1PDH) which plays a role in the synthesis of phosphoglycerolipids in Gram-positive bacterial species. It catalyzes the reversibly reduction of dihydroxyacetone phosphate (DHAP) to glycerol-1-phosphate (G1P) in a NADH-dependent manner. Its activity requires Ni++ ion.
Pssm-ID: 341453 [Multi-domain] Cd Length: 332 Bit Score: 111.84 E-value: 4.96e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 34 VIADDFVMKLAGEKVVNGLQSHDIRCHAErfngECSHAEINRLMAILQKQGC-RGVVGIGGGKTLDTAKAIGYYQKLPVV 112
Cdd:cd08174 30 IVTGEGIDELLGEDILESLEEAGEIVTVE----ENTDNSAEELAEKAFSLPKvDAIVGIGGGKVLDVAKYAAFLSKLPFI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 113 VIPTIASTDAPTSALSVIYTEAGefeeYLIYP-KNPDMVVMDTAIIAKAPVRLLVSGMGDALS--TwfeakACYD----- 184
Cdd:cd08174 106 SVPTSLSNDGIASPVAVLKVDGK----RKSLGaKMPYGVIVDLDVIKSAPRRLILAGIGDLISniT-----ALYDwklae 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 185 -ARATSMAGgqsteAALSLARLCYDTLLAEGEKARLAaqagvvTEALERIIEANTyLSGIGFE-------SSGlaAAHAI 256
Cdd:cd08174 177 eKGGEPVDD-----FAYLLSRTAADSLLNTPGKDIKD------DEFLKELAESLV-LSGIAMEiagssrpASG--SEHLI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 257 hngftileeCHHL--------YHGEKVAFGTLAQLVLQNSPMDEIETVLgfcQRVGLPVTLAQMGVKEgiDAKIAAVAKA 328
Cdd:cd08174 243 ---------SHALdklfpgpaLHGIQVGLGTYFMSFLQGQRYEEIRDVL---KRTGFPLNPSDLGLTK--EEFIEAVKLA 308
|
|
| Gro1PDH |
cd08173 |
Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) catalyzes the reversible conversion between ... |
8-316 |
2.75e-26 |
|
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: 107.25 E-value: 2.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 8 PAKYLQGPDAAVLFGQYAKNLAES--FFVIADDFVMKLAGEKVVNGLQSHDIRCHAERFNGECSHAEINRLMAILQKQGC 85
Cdd:cd08173 2 PRNVVVGHGAINKIGEVLKKLLLGkrALIITGPNTYKIAGKRVEDLLESSGVEVVIVDIATIEEAAEVEKVKKLIKESKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 86 RGVVGIGGGKTLDTAKAIGYYQKLPVVVIPTIASTDAPTSALSVIYteaGEFEEYLIYPKNPDMVVMDTAIIAKAPVRLL 165
Cdd:cd08173 82 DFIIGVGGGKVIDVAKYAAYKLNLPFISIPTSASHDGIASPFASIK---GGDKPYSIKAKAPIAIIADTEIISKAPKRLL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 166 VSGMGDALS--TwfeakACYDAR-ATSMAGGQSTEAALSLARLCYDTLLAEGEKARLAAQAGV--VTEALerIieantyl 240
Cdd:cd08173 159 AAGCGDLISniT-----AVKDWRlAHRLKGEYYSEYAASLALMSAKLIIENADLIKPGLEEGVrtVVKAL--I------- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 241 sgigfeSSGLAAA----------------HAIHngftILEECHHLyHGEKVAFGTLAQLVLQNSPMDEIETVLgfcQRVG 304
Cdd:cd08173 225 ------SSGVAMSiagssrpasgsehlfsHALD----KLAPGPAL-HGEQCGVGTIMMAYLHGGDWKEIREAL---KKIG 290
|
330
....*....|..
gi 1709669016 305 LPVTLAQMGVKE 316
Cdd:cd08173 291 APTTAKELGLDK 302
|
|
| Fe-ADH_2 |
pfam13685 |
Iron-containing alcohol dehydrogenase; |
34-276 |
3.67e-25 |
|
Iron-containing alcohol dehydrogenase;
Pssm-ID: 404557 [Multi-domain] Cd Length: 251 Bit Score: 102.38 E-value: 3.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 34 VIADDFVMKLAGEKVVNGLQSHDIRCHA-ERFNGECSHAEINRLMAILQKQGCRGVVGIGGGKTLDTAKAIGYYQKLPVV 112
Cdd:pfam13685 24 LVADANTYAAAGRKVAESLKRAGIEVETrLEVAGNADMETAEKLVGALRERDADAVVGVGGGTVIDLAKYAAFKLGKPFI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 113 VIPTIASTDAPTSALSVIYteaGEFEEYLIYPKNPDMVVMDTAIIAKAPVRLLVSGMGDALSTWfeaKACYDARAtSMAG 192
Cdd:pfam13685 104 SVPTAASNDGFASPGASLT---VDGKKRSIPAAAPFGVIADTDVIAAAPRRLLASGVGDLLAKI---TAVADWEL-AHAE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 193 GQSTEAALSLARLCYdtllaegEKARLAAQAGVVTEALERIIEANTyLSGIGFESSGLAAAHAI-HngftILEECH--HL 269
Cdd:pfam13685 177 EVAAPLALLSAAMVM-------NFADRPLRDPGDIEALAELLSALA-MGGAGSSRPASGSEHLIsH----ALDMIApkQA 244
|
....*..
gi 1709669016 270 YHGEKVA 276
Cdd:pfam13685 245 LHGEQVG 251
|
|
| Fe-ADH |
cd08551 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains large ... |
8-350 |
1.06e-22 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains large metal-containing alcohol dehydrogenases (ADH), known as iron-containing alcohol dehydrogenases. They contain a dehydroquinate synthase-like protein structural fold and mostly contain iron. They are distinct from other alcohol dehydrogenases which contains different protein domains. There are several distinct families of alcohol dehydrogenases: Zinc-containing long-chain alcohol dehydrogenases, insect-type, or short-chain alcohol dehydrogenases, iron-containing alcohol dehydrogenases, among others. The iron-containing family has a Rossmann fold-like topology that resembles the fold of the zinc-dependent alcohol dehydrogenases, but lacks sequence homology, and differs in strand arrangement. ADH catalyzes the reversible oxidation of alcohol to acetaldehyde with the simultaneous reduction of NAD(P)+ to NAD(P)H.
Pssm-ID: 341481 [Multi-domain] Cd Length: 372 Bit Score: 97.90 E-value: 1.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 8 PAKYLQGPDAAVLFGQYAKNL-AESFFVIADDFVMKL-AGEKVVNGLQSHDIRChaERFNG---ECSHAEINRLMAILQK 82
Cdd:cd08551 1 PTRIVFGAGALARLGEELKALgGKKVLLVTDPGLVKAgLLDKVLESLKAAGIEV--EVFDDvepNPTVETVEAAAELARE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 83 QGCRGVVGIGGGKTLDTAKAIG-----------YY-------QKLPVVVIPTIASTDAPTSALSVIYTEAGEFEEYLIYP 144
Cdd:cd08551 79 EGADLVIAVGGGSVLDTAKAIAvlatnggsirdYEgigkvpkPGLPLIAIPTTAGTGSEVTPNAVITDPETGRKMGIVSP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 145 KN-PDMVVMDTAIIAKAPVRLLVS-GMgDALSTWFEAkacYDAR-ATSMaggqsTEA-ALSLARLCYDTLlaegekaRLA 220
Cdd:cd08551 159 YLlPDVAILDPELTLSLPPSVTAAtGM-DALTHAIEA---YTSKkANPI-----SDAlALEAIRLIGKNL-------RRA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 221 AQAGVVTEALERIIEAnTYLSGIGFESSGLAAAHAIhnGFTiLEECHHLYHGEKVA-----------------FGTLAQL 283
Cdd:cd08551 223 VADGSDLEAREAMLLA-SLLAGIAFGNAGLGAVHAL--AYP-LGGRYHIPHGVANAillpyvmefnlpacpekYAEIAEA 298
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1709669016 284 VLQN----SPMDE----IETVLGFCQRVGLPVTLAQMGVKEgidAKIAAVAKATCAEGETIHNMPFAVTPESVHA 350
Cdd:cd08551 299 LGEDveglSDEEAaeaaVEAVRELLRDLGIPTSLSELGVTE---EDIPELAEDAMKSGRLLSNNPRPLTEEDIRE 370
|
|
| egsA |
PRK00843 |
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed |
3-318 |
2.10e-21 |
|
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed
Pssm-ID: 179139 Cd Length: 350 Bit Score: 93.80 E-value: 2.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 3 KVIQSPAKYLQGPDAAVLFGQYAKNLA--ESFFVIADDFVMKLAGEKVVNGLQShdiRCHAERF-NGECSHAEINRLMAI 79
Cdd:PRK00843 6 HWIQLPRDVVVGHGVLDDIGDVCSDLKltGRALIVTGPTTKKIAGDRVEENLED---AGDVEVViVDEATMEEVEKVEEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 80 LQKQGCRGVVGIGGGKTLDTAKAIGYYQKLPVVVIPTIASTDAPTSALSVIYTEAGefeEYLIYPKNPDMVVMDTAIIAK 159
Cdd:PRK00843 83 AKDVNAGFLIGVGGGKVIDVAKLAAYRLGIPFISVPTAASHDGIASPRASIKGGGK---PVSVKAKPPLAVIADTEIIAK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 160 APVRLLVSGMGDALSTWfeaKACYDAR-ATSMAGGQSTEAALSLARLCYDTLL--AEGEKARLAAQAGVVTEALeriiea 236
Cdd:PRK00843 160 APYRLLAAGCGDIISNY---TAVKDWRlAHRLRGEYYSEYAAALSLMTAKMLIenADIIKPGLEESARLVVKAL------ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 237 ntylsgigfESSGLAA----------------AHA---IHNGFTIleechhlyHGEKVAFGTLAQLVLQNSPMDEIETVL 297
Cdd:PRK00843 231 ---------ISSGVAMsiagssrpasgsehlfSHAldrLAPGPAL--------HGEQCGVGTIIMMYLHGGDWRKIRDAL 293
|
330 340
....*....|....*....|.
gi 1709669016 298 gfcQRVGLPVTLAQMGVKEGI 318
Cdd:PRK00843 294 ---KKIGAPTTAKELGIDDEY 311
|
|
| EutG |
COG1454 |
Alcohol dehydrogenase, class IV [Energy production and conversion]; |
1-355 |
1.69e-20 |
|
Alcohol dehydrogenase, class IV [Energy production and conversion];
Pssm-ID: 441063 [Multi-domain] Cd Length: 381 Bit Score: 91.72 E-value: 1.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 1 MLKVIQSPAKYLQGPDAAVLFGQYAKNL-AESFFVIADDFVMKL-AGEKVVNGLQSHDIrcHAERFNG---ECSHAEINR 75
Cdd:COG1454 1 MMFTFRLPTRIVFGAGALAELGEELKRLgAKRALIVTDPGLAKLgLLDRVLDALEAAGI--EVVVFDDvepNPTVETVEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 76 LMAILQKQGCRGVVGIGGGKTLDTAKAIG-----------YY-------QKLPVVVIPTIASTDAPTSALSVIYTEAGEF 137
Cdd:COG1454 79 GAAAAREFGADVVIALGGGSAIDAAKAIAllatnpgdledYLgikkvpgPPLPLIAIPTTAGTGSEVTPFAVITDPETGV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 138 EEYLIYPKN-PDMVVMDTAIIAKAPVRLLV-SGMgDALSTWFEakACYDARATSMAGGQSTEAalslARLCYDTLlaege 215
Cdd:COG1454 159 KKGIADPELlPDVAILDPELTLTLPPSLTAaTGM-DALTHAIE--AYVSKGANPLTDALALEA----IRLIARNL----- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 216 kaRLAAQAGVVTEALERIIEANTyLSGIGFESSGLAAAHAI-H--NGFtileecHHLYHGEKVA---------------- 276
Cdd:COG1454 227 --PRAVADGDDLEAREKMALASL-LAGMAFANAGLGAVHALaHplGGL------FHVPHGLANAillphvlrfnapaape 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 277 -FGTLAQLVLQNSPMDE-------IETVLGFCQRVGLPVTLAQMGVKEgidAKIAAVAKATCAEGETIHNmPFAVTPESV 348
Cdd:COG1454 298 rYAEIARALGLDVGLSDeeaaealIEAIRELLRDLGIPTRLSELGVTE---EDLPELAELALADRCLANN-PRPLTEEDI 373
|
....*..
gi 1709669016 349 hAAILTA 355
Cdd:COG1454 374 -EAILRA 379
|
|
| Fe-ADH-like |
cd08196 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
33-349 |
2.53e-18 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341475 [Multi-domain] Cd Length: 367 Bit Score: 84.94 E-value: 2.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 33 FVIADDFVMK-LAGEKVVNGLQSHDIRCHAErFNGECSHAEINRLMAILQKQGCRGVVGIGGGKTLDTAKAIG------- 104
Cdd:cd08196 32 LLVTDPSFIKsGLAKRIVESLKGRIVAVFSD-VEPNPTVENVDKCARLARENGADFVIAIGGGSVLDTAKAAAclaktdg 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 105 ----YYQK--------LPVVVIPTIASTDAPTSALSVI-YTEAGE---FEEYLIYPknpdmvvmDTAIIAKA-----PVR 163
Cdd:cd08196 111 siedYLEGkkkipkkgLPLIAIPTTAGTGSEVTPVAVLtDKEKGKkapLVSPGFYP--------DIAIVDPEltysmPPK 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 164 LLVS-GMgDALSTWFEAkacYDARaTSMAggQSTEAALSLARLCYDTLLA---EGEKArlaaqagvvtEALERIIEANTy 239
Cdd:cd08196 183 VTAStGI-DALCHAIEA---YWSI-NHQP--ISDALALEAAKLVLENLEKaynNPNDK----------EAREKMALASL- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 240 LSGIGFESSGLAAAHAIHNGFTILeecHHLYHGEKVAFgTLAQLVLQNSP-----MDEIETVLGF------CQRV----- 303
Cdd:cd08196 245 LAGLAFSQTRTTASHACSYPLTSH---FGIPHGEACAL-TLPSFIRLNAEalpgrLDELAKQLGFkdaeelADKIeelkk 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1709669016 304 --GLPVTLAQMGVKEgidAKIAAVAKATCAEgETIHNMPFAVTPESVH 349
Cdd:cd08196 321 riGLRTRLSELGITE---EDLEEIVEESFHP-NRANNNPVEVTKEDLE 364
|
|
| G1PDH_related |
cd08549 |
Glycerol-1-phosphate dehydrogenase and related proteins; This family contains bacterial and ... |
88-318 |
5.92e-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: 80.69 E-value: 5.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 88 VVGIGGGKTLDTAKAIGYYQKLPVVVIPTIASTDAPTS-ALSVIYTEagefEEYLIYPKNPDMVVMDTAIIAKAPVRLLV 166
Cdd:cd08549 74 VIGIGGGRSIDTGKYLAYKLKIPFISVPTSASNDGIASpIVSLRIPG----VKKTFMADAPIAIIADTEIIKKSPRRLLS 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 167 SGMGDALSTWfeaKACYDAR-ATSMAGGQSTEAALSLARLCYDTLLaegekaRLAAQAGVVTEALERIIEANTYlSGIGF 245
Cdd:cd08549 150 AGIGDLVSNI---TAVLDWKlAHKEKGEKYSEFAAILSKTSAKELV------SYVLKASDLEEYHRVLVKALVG-SGIAM 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 246 ESSGLAA---------AHAIHNGFTILEECHHLyHGEKVAFGT-----LAQLVLQNSPMDE--IETVLgfcQRVGLPVTL 309
Cdd:cd08549 220 AIAGSSRpasgsehlfSHALDKLKEEYLNINVL-HGEQVGVGTiimsyLHEKENKKLSGLHerIKMIL---KKVGAPTTA 295
|
....*....
gi 1709669016 310 AQMGVKEGI 318
Cdd:cd08549 296 KQLGIDEDL 304
|
|
| Fe-ADH-like |
cd14863 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
14-355 |
1.70e-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: 341485 [Multi-domain] Cd Length: 380 Bit Score: 79.89 E-value: 1.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 14 GPDAAVLFGQYAKNL-AESFFVIADDFVMKlAG--EKVVNGLQSHDIRchAERFNG---ECSHAEINRLMAILQKQGCRG 87
Cdd:cd14863 11 GAGAVEQIGELLKELgCKKVLLVTDKGLKK-AGivDKIIDLLEEAGIE--VVVFDDvepDPPDEIVDEAAEIAREEGADG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 88 VVGIGGGKTLDTAKAIGY-------------------YQKLPVVVIPTIASTDAPTSALSVIYTEAGEFEEYLIYPK-NP 147
Cdd:cd14863 88 VIGIGGGSVLDTAKAIAVlltnpgpiidyalagppvpKPGIPLIAIPTTAGTGSEVTPIAVITDEENGVKKSLLGPFlVP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 148 DMVVMDTAIIAKAPVRLLVS-GMgDALSTWFEAkacydarATSMAGGQSTEA-ALSLARLCYDTLlaegekaRLAAQAGV 225
Cdd:cd14863 168 DLAILDPELTVGLPPSLTAAtGM-DALSHAIEA-------YTSKLANPMTDAlALQAIRLIVKNL-------PRAVKDGD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 226 VTEALERIIEAnTYLSGIGFESSGLAAAHAI-HngftILEECHHLYHGEKVAFGT-----------------LAQ-LVLQ 286
Cdd:cd14863 233 NLEARENMLLA-SNLAGIAFNNAGTHIGHAIaH----ALGALYHIPHGLACALALpvvlefnaeaypekvkkIAKaLGVS 307
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1709669016 287 NSPMDE-------IETVLGFCQRVGLPVTLAQMGVKEgidAKIAAVAKAtcAEGETIHNMPFAVTPESVHAAILTA 355
Cdd:cd14863 308 FPGESDeelgeavADAIREFMKELGIPSLFEDYGIDK---EDLDKIAEA--VLKDPFAMFNPRPITEEEVAEILEA 378
|
|
| HEPD |
cd08182 |
Hydroxyethylphosphoate dehydrogenase (HEPD) catalyzes the reduction of phosphonoacetaldehyde ... |
78-352 |
5.66e-13 |
|
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: 69.18 E-value: 5.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 78 AILQKQGCRGVVGIGGGKTLDTAKAI--------------------GYYQKLPVVVIPTIASTDAPTSALSVIY-TEAGE 136
Cdd:cd08182 73 ELFRESGPDVIIAVGGGSVIDTAKAIaallgspgenllllrtgekaPEENALPLIAIPTTAGTGSEVTPFATIWdEAEGK 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 137 ---FEEYLIYpknPDMVVMDTAIIAKAPVRLLVSGMGDALSTWFEAkacYDARATSMAggqSTEAALSLARLCYDTLlae 213
Cdd:cd08182 153 kysLAHPSLY---PDAAILDPELTLSLPLYLTASTGLDALSHAIES---IWSVNANPE---SRAYALRAIRLILENL--- 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 214 gekaRLAAQAGVVTEALERIIEAnTYLSGIGFESSGLAAAHAIHNGFTILeecHHLYHGEKVAF---------------- 277
Cdd:cd08182 221 ----PLLLENLPNLEAREAMAEA-SLLAGLAISITKTTAAHAISYPLTSR---YGVPHGHACALtlpavlrynagaddec 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 278 ------GTLAQLVLQNSPMDEIETVLGFCQRVGLPVTLAQMGVKEgidAKIAAVAKAtCAEGETIHNMPFAVTPESVHAA 351
Cdd:cd08182 293 dddprgREILLALGASDPAEAAERLRALLESLGLPTRLSEYGVTA---EDLEALAAS-VNTPERLKNNPVRLSEEDLLRL 368
|
.
gi 1709669016 352 I 352
Cdd:cd08182 369 L 369
|
|
| Fe-ADH-like |
cd08191 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
7-355 |
6.18e-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: 6.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 7 SPAKYLQGPDAAVLFGQYAKNLAESFFVIADDFVMKLAG-EKVVNGLQSHDIRchAERFNGEC---SHAEINRLMAILQK 82
Cdd:cd08191 3 SPSRLLFGPGARRALGRVAARLGSRVLIVTDPRLASTPLvAELLAALTAAGVA--VEVFDGGQpelPVSTVADAAAAARA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 83 QGCRGVVGIGGGKTLDTAKAIG-----------YY-------QKLPVVVIPTIASTDAPTSALSVIYTEA-----GEFEE 139
Cdd:cd08191 81 FDPDVVIGLGGGSNMDLAKVVAlllahggdprdYYgedrvpgPVLPLIAVPTTAGTGSEVTPVAVLTDPArgmkvGVSSP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 140 YLIypknPDMVVMDTAIIAKAPVRLLVSGMGDALSTWFEAkacYDARATSMAGGQSTEAALSLARLCYDTLLAEGekARL 219
Cdd:cd08191 161 YLR----PAVAIVDPELTLTCPPGVTADSGIDALTHAIES---YTARDFPPFPRLDPDPVYVGKNPLTDLLALEA--IRL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 220 -------AAQAGVVTEALERIIEANTyLSGIGFESSGLAAAHAIH---NGFTileechHLYHGEKVA------------- 276
Cdd:cd08191 232 igrhlprAVRDGDDLEARSGMALAAL-LAGLAFGTAGTAAAHALQypiGALT------HTSHGVGNGlllpyvmrfnrpa 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 277 ----FGTLAQL--VLQNSPMDE-----IETVLGFCQRVGLPVTLAQMGVKEgidAKIAAVAKATCAEGETIHNMPFAVTP 345
Cdd:cd08191 305 raaeLAEIARAlgVTTAGTSEEaadraIERVEELLARIGIPTTLADLGVTE---ADLPGLAEKALSVTRLIANNPRPPTE 381
|
410
....*....|
gi 1709669016 346 ESVHaAILTA 355
Cdd:cd08191 382 EDLL-RILRA 390
|
|
| G1PDH |
cd08175 |
Glycerol-1-phosphate dehydrogenase (G1PDH) catalyzes the reversible reduction of ... |
25-314 |
1.11e-12 |
|
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: 68.31 E-value: 1.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 25 AKNLAESFFVIADDFVMKLAGEKVVNGLQSHDIRCHAERFNGE-----CSHAEINRLMAIlqKQGCRGVVGIGGGkTL-D 98
Cdd:cd08175 20 ELFGGKKVLVVADENTYAAAGEEVEAALEEAGVTVCLLIFPGEgdliaDEAAVGKVLLEL--EKDTDLIIAVGSG-TInD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 99 TAKAIGYYQKLPVVVIPTIASTDAPTSALSVIyTEAGEFEEY-LIYPKnpdMVVMDTAIIAKAPVRLLVSGMGD------ 171
Cdd:cd08175 97 LTKYAAYKLGIPYISVPTAPSMDGYTSSGAPI-IVDGVKKTFpAHAPK---AIFADLDVLANAPQRMIAAGFGDllgkyt 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 172 ALSTWFEAKAC----YDARATSMaggqsTEAALslaRLCYDTL--LAEGEKarlaaqagvvtEALERIIEANTyLSGIGF 245
Cdd:cd08175 173 ALADWKLSHLLggeyYCPEVADL-----VQEAL---EKCLDNAegIAARDP-----------EAIEALMEALI-LSGLAM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 246 E-------SSGlaAAHAI-HngftILEECHH------LYHGEKVAFGTLA----QLVLQNSPMDEIETVLGfcqRVGLPV 307
Cdd:cd08175 233 QlvgnsrpASG--AEHHLsH----YWEMEFLrlgkppVLHGEKVGVGTLLiaalYILEQLPPPEELRELLR---KAGAPT 303
|
....*..
gi 1709669016 308 TLAQMGV 314
Cdd:cd08175 304 TPEDLGI 310
|
|
| Fe-ADH-like |
cd14864 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
8-326 |
4.82e-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: 341486 [Multi-domain] Cd Length: 376 Bit Score: 66.56 E-value: 4.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 8 PAKYLQGPDAAVLFGQYAKNLAESFFVIADDfVMKLAGE--KVVNGLQSHDIRCHA-ERFNGECSHAEINRLMAILQKQG 84
Cdd:cd14864 4 PPNIVFGADSLERIGEEVKEYGSRFLLITDP-VLKESGLadKIVSSLEKAGISVIVfDEIPASATSDTIDEAAELARKAG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 85 CRGVVGIGGGKTLDTAKAIG-----------YYQK-------LPVVVIPTIASTDAPTSAlSVIYTEAGEFEEYLIYPKN 146
Cdd:cd14864 83 ADGIIAVGGGKVLDTAKAVAilanndggaydFLEGakpkkkpLPLIAVPTTPRSGFEFSD-RFPVVDSRSREVKLLKAQP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 147 --PDMVVMDTAIIAKAPVRLLVSGMGDALSTWFEAKACYDAR-ATSMAGGQSTEA-ALSLARLCYDtllAEGEKAR-LAA 221
Cdd:cd14864 162 glPKAVIVDPNLMASLTGNQTAAMALAALALAVEAYLSKKSNfFSDALALKAIELvSENLDGALAD---PKNTPAEeLLA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 222 QAGVvtealeriieantyLSGIGFESSGL----AAAHAIHNGFTILE------------ECHHLYHGEKVA--FGTLAQL 283
Cdd:cd14864 239 QAGC--------------LAGLAASSSSPglatALALAVNSRYKVSKslvasillphviEYAATSAPDKYAkiARALGED 304
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1709669016 284 VLQNSP----MDEIETVLGFCQRVGLPVTLAQMGVKEGIDaKIAAVA 326
Cdd:cd14864 305 VEGASPeeaaIAAVEGVRRLIAQLNLPTRLKDLDLASSLE-QLAAIA 350
|
|
| Fe-ADH-like |
cd14865 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
73-355 |
5.46e-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: 63.33 E-value: 5.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 73 INRLMAILQKQGCRGVVGIGGGKTLDTAKAIG-----------YYQ--------KLPVVVIPTIASTDAPTSALSVIY-T 132
Cdd:cd14865 74 VNEAAARAREAGADGIIAVGGGSVIDTAKGVNillseggddldDYGganrltrpLKPLIAIPTTAGTGSEVTLVAVIKdE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 133 EAGEFEEYLIYPKNPDMVVMDTAIIAKAPVRLLVS-GMgDALSTWFEAKACydaratSMAGGQSTEAALSLARLCYDTL- 210
Cdd:cd14865 154 EKKVKLLFVSPFLLPDVAILDPRLTLSLPPKLTAAtGM-DALTHAIEAYTS------LQKNPISDALALQAIRLISENLp 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 211 --LAEG--EKARLAAQagvvtealeriIEANtyLSGIGFESSGLAAAHAI-HNgftiLEECHHLYHG------------- 272
Cdd:cd14865 227 kaVKNGkdLEARLALA-----------IAAT--MAGIAFSNSMVGLVHAIaHA----VGAVAGVPHGlansillphvmry 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 273 ------EKVAFGTLAQLVLQNSPMDE--------IETVLGFCQRVGLPVTLAQMGVKEgidAKIAAVAKATCAEGETIHN 338
Cdd:cd14865 290 nldaaaERYAELALALAYGVTPAGRRaeeaieaaIDLVRRLHELCGLPTRLRDVGVPE---EQLEAIAELALNDGAILFN 366
|
330
....*....|....*..
gi 1709669016 339 mPFAVTPESVhAAILTA 355
Cdd:cd14865 367 -PREVDPEDI-LAILEA 381
|
|
| Fe-ADH-like |
cd14861 |
Iron-containing alcohol dehydrogenases-like; This family contains proteins similar to ... |
71-329 |
2.34e-10 |
|
Iron-containing alcohol dehydrogenases-like; This family contains proteins similar to iron-containing alcohol dehydrogenase (Fe-ADH), most of which have not been characterized. Their specific function is unknown. The protein structure represents a dehydroquinate synthase-like fold and belongs to the alcohol dehydrogenase-like superfamily. It is distinct from other alcohol dehydrogenases which contain different protein domains. Alcohol dehydrogenase catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions.
Pssm-ID: 341483 [Multi-domain] Cd Length: 374 Bit Score: 61.37 E-value: 2.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 71 AEINRLMAILQKQGCRGVVGIGGGKTLDTAKAIG-----------YYQKL-----------PVVVIPTIASTDAPTSALS 128
Cdd:cd14861 69 ADVEAGVAAYREGGCDGIIALGGGSAIDAAKAIAlmathpgplwdYEDGEggpaaitpavpPLIAIPTTAGTGSEVGRAA 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 129 VIY-TEAGE----FEEYLIypknPDMVVMDTAIIAKAPVRLLV-SGMgDALSTWFEAkacYDA-RATSMAGGqsteAALS 201
Cdd:cd14861 149 VITdDDTGRkkiiFSPKLL----PKVAICDPELTLGLPPRLTAaTGM-DALTHCIEA---YLSpGFHPMADG----IALE 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 202 LARLCYDTLL-AEGEKARLAAQAGVVTEALEriieantylSGIGFeSSGLAAAHAIHNGFTILeecHHLYHGEKVA---- 276
Cdd:cd14861 217 GLRLISEWLPrAVADGSDLEARGEMMMAALM---------GAVAF-QKGLGAVHALAHALGAL---YGLHHGLLNAillp 283
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1709669016 277 -------------FGTLAQLV--LQNSPMDEIETVLGFCQRVGLPVTLAQMGVKEGIDAKIAAVAKAT 329
Cdd:cd14861 284 yvlrfnrpavedkLARLARALglGLGGFDDFIAWVEDLNERLGLPATLSELGVTEDDLDELAELALAD 351
|
|
| Fe-ADH-like |
cd08185 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
78-353 |
3.48e-10 |
|
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: 60.97 E-value: 3.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 78 AILQKQGCRGVVGIGGGKTLDTAKAI----------------GYYQK------LPVVVIPTIASTDAPTSALSVIY-TEA 134
Cdd:cd08185 77 ALAKEEGCDFVIGLGGGSSMDAAKAIafmatnpgdiwdyifgGTGKGpppekaLPIIAIPTTAGTGSEVDPWAVITnPET 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 135 GE---FEEYLIYPK----NPD-MVVMdtaiiakaPVRLLVS-GMgDALSTWFEakaCYDA-RATSMAGGQSTEA----AL 200
Cdd:cd08185 157 KEkkgIGHPALFPKvsivDPElMLTV--------PPRVTAYtGF-DALFHAFE---SYISkNANPFSDMLALEAirlvAK 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 201 SLARLCYDtllaeGEKArlaaqagvvtEALERIIEANTyLSGIGFESSGLAAAHAihngftiLEE-----CHHLYHGE-- 273
Cdd:cd08185 225 YLPRAVKD-----GSDL----------EAREKMAWAST-LAGIVIANSGTTLPHG-------LEHplsgyHPNIPHGAgl 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 274 --------------------KVAFGTLAQLVLQNSPMDEIETVLGFCQRVGLPVTLAQMGV-KEGIDaKIAAVAKATcaE 332
Cdd:cd08185 282 aalypayfeftiekapekfaFVARAEASGLSDAKAAEDFIEALRKLLKDIGLDDLLSDLGVtEEDIP-WLAENAMET--M 358
|
330 340
....*....|....*....|.
gi 1709669016 333 GETIHNMPFAVTPESVhAAIL 353
Cdd:cd08185 359 GGLFANNPVELTEEDI-VEIY 378
|
|
| Fe-ADH-like |
cd14862 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
14-346 |
1.05e-09 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341484 [Multi-domain] Cd Length: 375 Bit Score: 59.16 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 14 GPDAAVLFGQYaknLAESFFVIADDFVMKLAG-EKVVNGLQSHDIRChaERFNGECSHAEINRLMAILQKqgCRG----- 87
Cdd:cd14862 12 GEDALSHLEQL---SGKRALIVTDKVLVKLGLlKKVLKRLLQAGFEV--EVFDEVEPEPPLETVLKGAEA--MREfepdl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 88 VVGIGGGKTLDTAKAI--------------------GYYQKLPVVVIPTIASTDAPTSALSVIyTEAGEFEEY-LIYPKN 146
Cdd:cd14862 85 IIALGGGSVMDAAKAAwvlyerpdldpedispldllGLRKKAKLIAIPTTSGTGSEATWAIVL-TDTEEPRKIaVANPEL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 147 -PDMVVMDTAIIAKAPVRLLVS-GMgDALSTWFEAkacydarATSMAGGQSTEA-ALSLARLCYDTLlaegekaRLAAQA 223
Cdd:cd14862 164 vPDVAILDPEFVLGMPPKLTAGtGL-DALAHAVEA-------YLSTWSNDFSDAlALKAIELIFKYL-------PRAYKD 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 224 GVVTEALERIIEANTyLSGIGFESSGLAAAHAI-HNGFTILeechHLYHGEKVA----------------FGTLAQLVLQ 286
Cdd:cd14862 229 GDDLEAREKMHNAAT-IAGLAFGNSQAGLAHALgHSLGAVF----HVPHGIAVGlflpyviefyakvtdeRYDLLKLLGI 303
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1709669016 287 NSPMDE------IETVLGFCQRVGLPVTLAQMGV-KEGIDAKIAAVAKATCAEGETIHNmPFAVTPE 346
Cdd:cd14862 304 EARDEEealkklVEAIRELYKEVGQPLSIKDLGIsEEEFEEKLDELVEYAMEDSCTITS-PRPPSEE 369
|
|
| PRK15454 |
PRK15454 |
ethanolamine utilization ethanol dehydrogenase EutG; |
2-256 |
1.92e-09 |
|
ethanolamine utilization ethanol dehydrogenase EutG;
Pssm-ID: 185351 [Multi-domain] Cd Length: 395 Bit Score: 58.50 E-value: 1.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 2 LKVIQSPAKYLQGPDAAVLFGQYAKNLAES-FFVIADDFVMK------LAGEKVVNGLQSHDIRCHAerfnGECSHAEIN 74
Cdd:PRK15454 21 VKTFSVPPVTLCGPGAVSSCGQQAQTRGLKhLFVMADSFLHQagmtagLTRSLAVKGIAMTLWPCPV----GEPCITDVC 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 75 RLMAILQKQGCRGVVGIGGGKTLDTAKAIGYY------------------QKLPVVVIPTIASTDAPTSALSVIYTEAGE 136
Cdd:PRK15454 97 AAVAQLRESGCDGVIAFGGGSVLDAAKAVALLvtnpdstlaemsetsvlqPRLPLIAIPTTAGTGSETTNVTVIIDAVSG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 137 FEEYLIYPK-NPDMVVMDTAIIAKAPVRLLVSGMGDALSTWFEAKACYDAR--ATSMAGGQSTEAALSLARlcydtllAE 213
Cdd:PRK15454 177 RKQVLAHASlMPDVAILDAALTEGVPSHVTAMTGIDALTHAIEAYSALNATpfTDSLAIGAIAMIGKSLPK-------AV 249
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1709669016 214 GEKARLAAQagvvtealERIIEANTyLSGIGFESSGLAAAHAI 256
Cdd:PRK15454 250 GYGHDLAAR--------ESMLLASC-MAGMAFSSAGLGLCHAM 283
|
|
| Fe-ADH-like |
cd17814 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
14-316 |
3.58e-09 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341489 [Multi-domain] Cd Length: 374 Bit Score: 57.55 E-value: 3.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 14 GPDAAVLFGQYAKNL-AESFFVIADDFVMKlAG--EKVVNGLQSHDIrcHAERFNGECSH---AEINRLMAILQKQGCRG 87
Cdd:cd17814 10 GVGARKLAGRYAKNLgARKVLVVTDPGVIK-AGwvDEVLDSLEAEGL--EYVVFSDVTPNprdFEVMEGAELYREEGCDG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 88 VVGIGGGKTLDTAKAIGY----------YQKL--------PVVVIPTIASTDAPTSALSVIyTEAGEFEEYLIYPKN--P 147
Cdd:cd17814 87 IVAVGGGSPIDCAKGIGIvvsngghildYEGVdkvrrplpPLICIPTTAGSSADVSQFAII-TDTERRVKMAIISKTlvP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 148 DMVVMDTAIIAKAPVRLLVSGMGDALSTWFEAkacydarATSMAGGQSTEA-ALSLARLCYDTLlaegekaRLAAQAGVV 226
Cdd:cd17814 166 DVSLIDPETLTTMDPELTACTGMDALTHAIEA-------YVSNASSPLTDLhALEAIRLISENL-------PKAVADPDD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 227 TEALERIIEANTYlSGIGFESSGLAAAHAI-HN--GFtileecHHLYHGEKVA-----------------FGTLAQ-LVL 285
Cdd:cd17814 232 LEAREKMMLASLQ-AGLAFSNASLGAVHAMaHSlgGL------LDLPHGECNAlllphvirfnfpaaperYRKIAEaMGL 304
|
330 340 350
....*....|....*....|....*....|....*...
gi 1709669016 286 QNSPMDE-------IETVLGFCQRVGLPVTLAQMGVKE 316
Cdd:cd17814 305 DVDGLDDeevaerlIEAIRDLREDLGIPETLSELGVDE 342
|
|
| Fe-ADH-like |
cd08194 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
8-130 |
4.07e-09 |
|
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) most of which have not been characterized. Their specific function is unknown. The protein structure represents a dehydroquinate synthase-like fold and belongs to the alcohol dehydrogenase-like superfamily. It is distinct from other alcohol dehydrogenases which contain different protein domains. Alcohol dehydrogenase catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions.
Pssm-ID: 341473 [Multi-domain] Cd Length: 378 Bit Score: 57.54 E-value: 4.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 8 PAKYLQGPDAAVLFGQYAKNL-AESFFVIADDFVMKL-AGEKVVNGLQSHDIRC--HAErFNGECSHAEINRLMAILQKQ 83
Cdd:cd08194 1 PRTIIIGGGALEELGEEAASLgGKRALIVTDKVMVKLgLVDKVTQLLAEAGIAYavFDD-VVSEPTDEMVEEGLALYKEG 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1709669016 84 GCRGVVGIGGGKTLDTAKAIG-----------YYQK-------LPVVVIPTIASTDAPTSALSVI 130
Cdd:cd08194 80 GCDFIVALGGGSPIDTAKAIAvlatnggpirdYMGPrkvdkpgLPLIAIPTTAGTGSEVTRFTVI 144
|
|
| Fe-ADH-like |
cd08183 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
14-256 |
1.49e-08 |
|
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and 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: 55.97 E-value: 1.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 14 GPDAAVLFGQYAKNLAESFFVIAD-DFVMKLAGEKVVNGLQSHDIRCHAERFNGECSHAEINRLMAILQKQGCRGVVGIG 92
Cdd:cd08183 7 GRGSLQELGELAAELGKRALLVTGrSSLRSGRLARLLEALEAAGIEVALFSVSGEPTVETVDAAVALAREAGCDVVIAIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 93 GGKTLDTAKAI---------------GYYQ-------KLPVVVIPTIASTDAPTSALSVIYTEAGEFE-----EYLIypk 145
Cdd:cd08183 87 GGSVIDAAKAIaalltnegsvldyleVVGKgrpltepPLPFIAIPTTAGTGSEVTKNAVLSSPEHGVKvslrsPSML--- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 146 nPDMVVMDTAIIAKAPVRLLV-SGMgDALSTWFEAKACYDA----RATSMAGGQstEAALSLARLCYDtllaegeKARLA 220
Cdd:cd08183 164 -PDVALVDPELTLSLPPEVTAaSGL-DALTQLIEPYVSRKAnpltDALAREGLR--LAARSLRRAYED-------GEDLE 232
|
250 260 270
....*....|....*....|....*....|....*.
gi 1709669016 221 AQAGVVTEALeriieantyLSGIGFESSGLAAAHAI 256
Cdd:cd08183 233 AREDMALASL---------LGGLALANAGLGAVHGL 259
|
|
| BDH |
cd08187 |
Butanol dehydrogenase catalyzes the conversion of butyraldehyde to butanol with the cofactor ... |
73-174 |
8.43e-08 |
|
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: 53.59 E-value: 8.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 73 INRLMAILQKQGCRGVVGIGGGKTLDTAKAIG------------YYQK------LPVVVIPTIASTDAPTSALSVI-YTE 133
Cdd:cd08187 75 VREGIELAREENVDFILAVGGGSVIDAAKAIAagakydgdvwdfFTGKappekaLPVGTVLTLAATGSEMNGGAVItNEE 154
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1709669016 134 AGE---FEEYLIYPKnpdMVVMDTAIIAKAPVRLLVSGMGDALS 174
Cdd:cd08187 155 TKEklgFGSPLLRPK---FSILDPELTYTLPKYQTAAGIVDIFS 195
|
|
| PPD-like |
cd08181 |
1,3-propanediol dehydrogenase-like (PPD); This family contains proteins similar to 1, ... |
78-349 |
8.48e-08 |
|
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: 53.36 E-value: 8.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 78 AILQKQGCRGVVGIGGGKTLDTAKAI----------------GYYQK-LPVVVIPTIASTDAPTSALSVI-YTEAG---E 136
Cdd:cd08181 77 ELARKEGADFVIGIGGGSPLDAAKAIallaankdgdedlfqnGKYNPpLPIVAIPTTAGTGSEVTPYSILtDHEKGtkkS 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 137 FEEYLIYPKnpdMVVMDTAIIAKAPVRLLVSGMGDALSTWFEakACYDARATSMaggqSTEAAL-SLARL--CYDTLLAE 213
Cdd:cd08181 157 FGNPLIFPK---LALLDPKYTLSLPEELTIDTAVDALSHAIE--GYLSVKATPL----SDALALeALRLIgeCLPNLLGD 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 214 GEKarlaaqagvvTEALERIIEANTyLSGIGFESSGLAAAHAIhnGFTILEEcHHLYHG----------------EKVAF 277
Cdd:cd08181 228 ELD----------EEDREKLMYAST-LAGMVIAQTGTTLPHGL--GYPLTYF-KGIPHGrangillpaylklcekQEPEK 293
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1709669016 278 GTLAQLVLQNSPMDEIETVLGfcQRVGLPVTLaqmgVKEGIDAKIAAVAKATcaegeTIHNMPFAVTPESVH 349
Cdd:cd08181 294 VDKILKLLGFGSIEEFQKFLN--RLLGKKEEL----SEEELEKYADEAMKAK-----NKKNTPGNVTKEDIL 354
|
|
| PDDH |
cd08188 |
1,3-Propanediol (1,3-PD) dehydrogenase; This family includes 1,3-propanediol (1,3-PD) ... |
3-316 |
1.04e-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: 53.29 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 3 KVIQSPAKYLQGPDAAVLFGQYAKNL-AESFFVIADDFVMKLA-GEKVVNGLQSHDIRchAERFNGecshAE-------I 73
Cdd:cd08188 1 FRFYIPPVNLFGPGCLKEIGDELKKLgGKKALIVTDKGLVKLGlVKKVTDVLEEAGIE--YVIFDG----VQpnptvtnV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 74 NRLMAILQKQGCRGVVGIGGGKTLDTAKAIG-----------Y-------YQKLPVVVIPTIASTDAPTSALSVIYTEAg 135
Cdd:cd08188 75 NEGLELFKENGCDFIISVGGGSAHDCAKAIGilatnggeiedYegvdkskKPGLPLIAINTTAGTASEVTRFAVITDEE- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 136 efeeyliypKNPDMVVMDTAIIAKAPVR---LLVS---------GMgDALSTWFEAkacYdaraTSMAGGQSTEA-ALSL 202
Cdd:cd08188 154 ---------RHVKMVIVDWNVTPTIAVNdpeLMLGmppsltaatGM-DALTHAIEA---Y----VSTGATPLTDAlALEA 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 203 ARLCYDTLlaegekaRLAAQAGVVTEALERIIEAnTYLSGIGFESSGLAAAHAI-H--NGFtileecHHLYHG------- 272
Cdd:cd08188 217 IRLIAENL-------PKAVANGKDLEARENMAYA-QFLAGMAFNNAGLGYVHAMaHqlGGF------YNLPHGvcnaill 282
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1709669016 273 ------------EKvaFGTLAQLVLQNSP--MDE------IETVLGFCQRVGLPVTLAQMGVKE 316
Cdd:cd08188 283 phvmefnlpacpER--FADIARALGENTEglSDEeaaeaaIEAIRKLSRRVGIPSGLKELGVKE 344
|
|
| LPO |
cd08176 |
Lactadehyde:propanediol oxidoreductase (LPO) catalyzes the interconversion between ... |
78-348 |
1.94e-07 |
|
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: 52.16 E-value: 1.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 78 AILQKQGCRGVVGIGGGKTLDTAKAIG-----------YY--------QKLPVVVIPTIASTDAPTSALSVIY-TEAGE- 136
Cdd:cd08176 79 AAYKESGADGIIAVGGGSSIDTAKAIGiivanpgadvrSLegvaptknPAVPIIAVPTTAGTGSEVTINYVITdTEKKRk 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 137 ---FEEYLIypknPDMVVMDTAIIAKAPVRLLV-SGMgDALSTWFEAkacYdaraTSMAGGQSTEA-ALSLARLCYDTLl 211
Cdd:cd08176 159 fvcVDPHDI----PTVAIVDPDLMSSMPKGLTAaTGM-DALTHAIEG---Y----ITKGAWELSDMlALKAIELIAKNL- 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 212 aegekaRLAAQAGVVTEALERIIEAnTYLSGIGFESSGLAAAHAIHNGFTILEECHH----------------LYHGEK- 274
Cdd:cd08176 226 ------RKAVANPNNVEARENMALA-QYIAGMAFSNVGLGIVHSMAHPLSAFYDTPHgvanaillpyvmefnaPATGEKy 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 275 ----VAFGtlaqlVLQNSPMDE------IETVLGFCQRVGLPVTLAQMGVKEgidAKIAAVAKATCAEGETIHNmPFAVT 344
Cdd:cd08176 299 rdiaRAMG-----VDTTGMSDEeaaeaaVDAVKKLSKDVGIPQKLSELGVKE---EDIEALAEDALNDVCTPGN-PREAT 369
|
....
gi 1709669016 345 PESV 348
Cdd:cd08176 370 KEDI 373
|
|
| NADPH_BDH |
cd08179 |
NADPH-dependent butanol dehydrogenase involved in the butanol and ethanol formation pathway in ... |
88-348 |
1.03e-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: 50.27 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 88 VVGIGGGKTLDTAKAIG-YY--------------------QKLPVVVIPTIASTDAPTSALSVIyTEAGEFEEYLIYPKN 146
Cdd:cd08179 85 IIAIGGGSVIDAAKAMWvFYeypeltfedalvpfplpelrKKARFIAIPSTSGTGSEVTRASVI-TDTEKGIKYPLASFE 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 147 --PDMVVMDTAIIAKAPVRLLV-SGMgDALSTWFEAKACydARATSMAGGQSTEAALSLarlcYDTLLaegekarLAAQA 223
Cdd:cd08179 164 itPDVAILDPELTMTMPPHVTAnTGM-DALTHAIEAYVS--TLANDFTDALALGAILDI----FENLP-------KSYNG 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 224 GVVTEALERIIEANTyLSGIGFESSGLAAAHAI-HNGFTILeechHLYHGE-----------------------KVAFGT 279
Cdd:cd08179 230 GKDLEAREKMHNASC-LAGMAFSNSGLGIVHSMaHKGGAFF----GIPHGLanaillpyviefnskdpeararyAALLIG 304
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 280 LAQLVLQNspmDEIETVLGFCQRVGLPVTLAQMGVKEGI-DAKIAAVAKATCAEGETIHNmPFAVTPESV 348
Cdd:cd08179 305 LTDEELVE---DLIEAIEELNKKLGIPLSFKEAGIDEDEfFAKLDEMAENAMNDACTGTN-PRKPTVEEM 370
|
|
| DOIS |
cd08197 |
2-deoxy-scyllo-inosose synthase (DOIS) catalyzes carbocycle formation from ... |
29-173 |
2.84e-06 |
|
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: 48.73 E-value: 2.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 29 AESFFVIADDFVMKLAGEKVVNGLQSHDIRCHAERFNGECSHAEINRLMAILQ--------KQGCrgVVGIGGGKTLDTA 100
Cdd:cd08197 23 ADRHFLVTDSNVNDLYGDRLLEGLKKAGIPVELLVVPAGESNKTLSTLTELAErliaagitRRSV--IIALGGGVVGNIA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 101 kaiGY-----YQKLPVVVIPT--IASTDAPTSALSVIYTEAGefeeyliypKN-------PDMVVMDTAIIAKAPVRLLV 166
Cdd:cd08197 101 ---GLlagllYRGIRLVHVPTtlLAQSDSVLSLKQAVNGKSG---------KNlvgsyyaPLFVFVDTEFLKTLPPRQIR 168
|
....*..
gi 1709669016 167 SGMGDAL 173
Cdd:cd08197 169 SGLCEAI 175
|
|
| Fe-ADH-like |
cd08189 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
12-258 |
1.87e-05 |
|
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: 46.31 E-value: 1.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 12 LQGPDAAVLFGQYAKNLA-ESFFVIADDFVMKLaG--EKVVNGLQSHDIRCHAerFNG---ECSHAEINRLMAILQKQGC 85
Cdd:cd08189 9 FEGAGSLLQLPEALKKLGiKRVLIVTDKGLVKL-GllDPLLDALKKAGIEYVV--FDGvvpDPTIDNVEEGLALYKENGC 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 86 RGVVGIGGGKTLDTAKAIG----------YYQK---------LPVVVIPTIASTDAPTSALSVIyTEAGEFEEYLIYPKN 146
Cdd:cd08189 86 DAIIAIGGGSVIDCAKVIAaraanpkksvRKLKgllkvrkklPPLIAVPTTAGTGSEATIAAVI-TDPETHEKYAINDPK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 147 --PDMVVMDTAIIAKAPVRLLV-SGMgDALSTWFEAkacYDARATSmagGQSTEAALSLARLCYDTLL---AEGE--KAR 218
Cdd:cd08189 165 liPDAAVLDPELTLGLPPAITAaTGM-DALTHAVEA---YISRSAT---KETDEYALEAVKLIFENLPkayEDGSdlEAR 237
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1709669016 219 LA-AQAgvvtealeriieanTYLSGIGFESSGLAAAHAI-HN 258
Cdd:cd08189 238 ENmLLA--------------SYYAGLAFTRAYVGYVHAIaHQ 265
|
|
| Fe-ADH_KdnB-like |
cd08184 |
Iron-containing alcohol dehydrogenase similar to Shewanella oneidensis KdnB required for Kdo8N ... |
72-268 |
2.36e-05 |
|
Iron-containing alcohol dehydrogenase similar to Shewanella oneidensis KdnB required for Kdo8N biosynthesis; This family contains iron-containing alcohol dehydrogenase-like proteins, many of which have not been characterized. Their specific function is unknown. The protein structure represents a dehydroquinate synthase-like fold and belongs to the iron-containing alcohol dehydrogenase-like superfamily. It is distinct from other alcohol dehydrogenases which contain different protein domains. Alcohol dehydrogenase catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron or zinc ions. This family also includes Shewanella oneidensis KdnB which is required for biosynthesis of 8-Amino-3,8-dideoxy-D-manno-octulosonic acid (Kdo8N), a unique amino sugar that has thus far only been observed on the lipopolysaccharides of marine bacteria belonging to the genus Shewanella, and thought to be important for the integrity of the bacterial cell outer membrane. KdnB requires NAD(P) and zinc ion for activity.
Pssm-ID: 341463 [Multi-domain] Cd Length: 348 Bit Score: 45.72 E-value: 2.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 72 EINRLMAILQKQGCR---GVVGIGGGKTLDTAKAIG----------YYQ-----KLP---VVVIPTIASTDA---PTSAL 127
Cdd:cd08184 67 QIDALRAQIRAENDKlpaAVVGIGGGSTMDIAKAVSnmltnpgsaaDYQgwdlvKNPgiyKIGVPTLSGTGAeasRTAVL 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 128 SVIYTEAGEFEEYLIYpknpDMVVMDTAIIAKAPVRL-LVSGMGdalstwfeakaCYDARATSMAGGQSTEAALSLAR-- 204
Cdd:cd08184 147 TGPEKKLGINSDYTVF----DQVILDPELIATVPRDQyFYTGMD-----------CYIHCVESLNGTYRNAFGDAYAEka 211
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1709669016 205 --LCYDTLLAEGEKArlaaqagvvTEALERIIEAnTYLSGIGFESSGLAAAHAIHNGFTILEECHH 268
Cdd:cd08184 212 leLCRDVFLSDDMMS---------PENREKLMVA-SYLGGSSIANSQVGVCHALSYGLSVVLGTHH 267
|
|
| Fe-ADH-like |
cd14866 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
87-256 |
2.99e-05 |
|
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: 341488 [Multi-domain] Cd Length: 384 Bit Score: 45.68 E-value: 2.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 87 GVVGIGGGKTLDTAKAIG---------------YYQ------------KLPVVVIPTIASTDAPTSALSVIYTEAGEfEE 139
Cdd:cd14866 86 AVVAVGGGSAIVTARAASillaedrdvrelctrRAEdglmvsprldapKLPIFVVPTTPTTADVKAGSAVTDPPAGQ-RL 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 140 YLIYPK-NPDMVVMDTAIIAKAPVRLLVSGMGDALSTWFEakACYDARATSMAGGQSTEAalslARLCYDTLLA----EG 214
Cdd:cd14866 165 ALFDPKtRPAAVFYDPELLATAPASLVAGAAMNGFDMAVE--GLYSRHADPLADATLMHA----LRLLADGLPRladdDD 238
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1709669016 215 EKARLAAQAGVVtealeriieantyLSGIGFESSGLAAAHAI 256
Cdd:cd14866 239 PAARADLVLAAV-------------LAGYGTDHTGGGVIHAL 267
|
|
| HVD |
cd08193 |
5-hydroxyvalerate dehydrogenase (HVD) catalyzes the oxidation of 5-hydroxyvalerate to ... |
81-136 |
5.51e-05 |
|
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: 44.81 E-value: 5.51e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1709669016 81 QKQGCRGVVGIGGGKTLDTAKAIGYY------------------QKLPVVVIPTIASTDAPTSALSVIYTEAGE 136
Cdd:cd08193 80 REAGADGVIGFGGGSSMDVAKLVALLagsdqplddiygvgkatgPRLPLILVPTTAGTGSEVTPISIVTTGETE 153
|
|
| HOT |
cd08190 |
Hydroxyacid-oxoacid transhydrogenase (HOT) involved in gamma-hydroxybutyrate metabolism; This ... |
7-350 |
7.89e-05 |
|
Hydroxyacid-oxoacid transhydrogenase (HOT) involved in gamma-hydroxybutyrate metabolism; This family contains hydroxyacid-oxoacid transhydrogenase (HOT), also known as D-2-hydroxyglutarate transhydrogenase. It catalyzes the conversion of gamma-hydroxybutyrate (GHB) to succinic semialdehyde (SSA), coupled to the stoichiometric conversion of alpha-ketoglutarate to D-2-hydroxyglutarate in gamma-Hydroxybutyrate catabolism. Unlike many other alcohols, which are oxidized by NAD-linked dehydrogenases, gamma-hydroxybutyrate is metabolized to succinate semialdehyde by hydroxyacid-oxoacid transhydrogenase which does not require free NAD or NADP; instead, it uses alpha-ketoglutarate as an acceptor, converting it to d-2-hydroxyglutarate. Alpha-ketoglutarate serves as an intermediate acceptor to regenerate NAD(P) required for the oxidation of GHB. HOT also catalyzes the reversible oxidation of a hydroxyacid obligatorily coupled to the reduction of an oxoacid, and requires no cofactor. In mammals, the HOT enzyme is located in mitochondria, and is expressed with an N-terminal mitochondrial targeting sequence. HOT enzyme is member of the metal-containing alcohol dehydrogenase family. It typically contains an iron although other metal ions may be used.
Pssm-ID: 341469 [Multi-domain] Cd Length: 412 Bit Score: 44.46 E-value: 7.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 7 SPAKYlqGPDAAVLFGQYAKNL-AESFFVIADDFVMKLAG-EKVVNGLQSHDIRchAERFNG---ECSHAEINRLMAILQ 81
Cdd:cd08190 2 SNIRF--GPGATRELGMDLKRLgAKKVLVVTDPGLAKLGLvERVLESLEKAGIE--VVVYDGvrvEPTDESFEEAIEFAK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 82 KQGCRGVVGIGGGKTLDTAKAIGYYQK-----------------------LPVVVIPTIASTDAPTSALSVI-YTEA--- 134
Cdd:cd08190 78 EGDFDAFVAVGGGSVIDTAKAANLYAThpgdfldyvnapigkgkpvpgplKPLIAIPTTAGTGSETTGVAIFdLEELkvk 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 135 -GEFEEYLiypkNPDMVVMDTAIIAKAPVRLLV-SGMgDALSTWFEAkacYDARATSMAGGQSTEAalslARLCY----- 207
Cdd:cd08190 158 tGISSRYL----RPTLAIVDPLLTLTLPPRVTAsSGF-DVLCHALES---YTARPYNARPRPANPD----ERPAYqgsnp 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 208 --DTLlaeGEKA--------RLAAQAGVVTEALERIIEANTyLSGIGFESSGLAAAHAI------------HNGFTILEe 265
Cdd:cd08190 226 isDVW---AEKAieligkylRRAVNDGDDLEARSNMLLAST-LAGIGFGNAGVHLPHAMaypiaglvkdyrPPGYPVDH- 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 266 cHHLYHGEKVA-----------------FGTLAQL----VLQNSPMDE----IETVLGFCQRVGLPVTLAQMGVKEgidA 320
Cdd:cd08190 301 -PHVPHGLSVAltapavfrftapacperHLEAAELlgadTSGASDRDAgevlADALIKLMRDIGIPNGLSALGYSE---D 376
|
410 420 430
....*....|....*....|....*....|
gi 1709669016 321 KIAAVAKATCAEGETIHNMPFAVTPESVHA 350
Cdd:cd08190 377 DIPALVEGTLPQQRLLKLNPRPVTEEDLEE 406
|
|
| YqdH |
COG1979 |
Alcohol dehydrogenase YqhD, Fe-dependent ADH family [Energy production and conversion]; |
78-335 |
9.94e-04 |
|
Alcohol dehydrogenase YqhD, Fe-dependent ADH family [Energy production and conversion];
Pssm-ID: 441582 [Multi-domain] Cd Length: 387 Bit Score: 40.83 E-value: 9.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 78 AILQKQGCRGVVGIGGGKTLDTAKAIG-----------YYQK-------LPVVVIPTIASTDAPTSALSVIYTEAGE--- 136
Cdd:COG1979 82 ELCKEEGIDFILAVGGGSVIDGAKAIAagakydgdpwdILTGkapvekaLPLGTVLTLPATGSEMNSGSVITNEETKekl 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 137 -FEEYLIYPKnpdMVVMDTAIIAKAPVRLLVSGMGDALSTWFEAKACYDARAT---SMAggqstEAALSlarlcydTLLA 212
Cdd:COG1979 162 gFGSPLVFPK---FSILDPELTYTLPKRQTANGIVDIFSHVMEQYFTYPVDAPlqdRFA-----EGLLR-------TLIE 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 213 EGEKAR-----LAAQAGVV---TEALERIIeantylsGIGFESSglAAAHAIHNGFTILeecHHLYHG------------ 272
Cdd:COG1979 227 EGPKALkdpedYDARANLMwaaTLALNGLI-------GAGVPQD--WATHMIEHELSAL---YDIDHGaglaivlpawmr 294
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1709669016 273 ----EKVA-FGTLAQLVLQNSPMDEIETVLG-------FCQRVGLPVTLAQMGVKEgidAKIAAVAKATCAEGET 335
Cdd:COG1979 295 yvleEKPEkFAQYAERVWGITEGDDEERALEgieateeFFESLGLPTRLSEYGIDE---EDIEEMAEKATAHGMT 366
|
|
| PFK |
pfam00365 |
Phosphofructokinase; |
75-134 |
1.47e-03 |
|
Phosphofructokinase;
Pssm-ID: 459783 [Multi-domain] Cd Length: 271 Bit Score: 40.02 E-value: 1.47e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1709669016 75 RLMAILQKQGCRGVVGIGGGKTLDTAKAIGYYQKLPVVVIP-TI----ASTDApT----SALSVIyTEA 134
Cdd:pfam00365 82 KIAENLKKLGIDALVVIGGDGSLTGANKLSEERGIPVVGIPkTIdndiPGTDY-TigfdTALNTI-VEA 148
|
|
| MAR |
cd08177 |
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic ... |
59-116 |
1.68e-03 |
|
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 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 and 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: 341456 [Multi-domain] Cd Length: 337 Bit Score: 39.80 E-value: 1.68e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1709669016 59 CHAERFNGECSHAEI---NRLMAILQKQGCRGVVGIGGGKTLDTAKAIGYYQKLPVVVIPT 116
Cdd:cd08177 48 RVAGVFDGAVMHVPVevaERALAAAREAGADGLVAIGGGSAIGLAKAIALRTGLPIVAVPT 108
|
|
| PDD |
cd08180 |
1,3-propanediol dehydrogenase (PPD) catalyzes the reduction of 3-hydroxypropionaldehyde (3-HPA) ... |
77-348 |
3.29e-03 |
|
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: 39.01 E-value: 3.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 77 MAILQKQGCRGVVGIGGGKTLDTAKAIGYY--------QKLPVVVIPTIASTDAPTSALSVIY-TEAGE----FEEYLIy 143
Cdd:cd08180 71 LAKILEFKPDTIIALGGGSAIDAAKAIIYFalkqkgniKKPLFIAIPTTSGTGSEVTSFAVITdPEKGIkyplVDDSML- 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 144 pknPDMVVMDTAIIAKAPVRLLV-SGMgDALSTWFEAKACYDARATSMAggqsteAALSLARLCYDTLLAegekarlAAQ 222
Cdd:cd08180 150 ---PDIAILDPELVKSVPPKVTAdTGM-DVLTHALEAYVSTNANDFTDA------LAEKAIKLVFENLPR-------AYR 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 223 AGVVTEALERIIEANTyLSGIGFESSGL----AAAHAIHNGFtileechHLYHGekvafgtLAQLVLqnspMDE-----I 293
Cdd:cd08180 213 DGDDLEAREKMHNASC-MAGIAFNNAGLginhSLAHALGGRF-------HIPHG-------RANAIL----LPYvieflI 273
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1709669016 294 ETVLGFCQRVGLPVTLAQMGV-KEGIDAKIAAVAKATCAEGETIHNmPFAVTPESV 348
Cdd:cd08180 274 AAIRRLNKKLGIPSTLKELGIdEEEFEKAIDEMAEAALADRCTATN-PRKPTAEDL 328
|
|
| PRK09860 |
PRK09860 |
putative alcohol dehydrogenase; Provisional |
77-316 |
4.57e-03 |
|
putative alcohol dehydrogenase; Provisional
Pssm-ID: 182118 [Multi-domain] Cd Length: 383 Bit Score: 38.78 E-value: 4.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 77 MAILQKQGCRGVVGIGGGKTLDTAKAIGY----------YQ--------KLPVVVIPTIASTDAPTSALSVIYTEAGEFE 138
Cdd:PRK09860 81 LKLLKENNCDSVISLGGGSPHDCAKGIALvaanggdirdYEgvdrsakpQLPMIAINTTAGTASEMTRFCIITDEARHIK 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 139 EYLIYPK-NPDMVVMDTAIIAKAPVRLLVSGMGDALSTWFEAkacydarATSMAGGQSTEA-ALSLARLCYDTLLaegek 216
Cdd:PRK09860 161 MAIVDKHvTPLLSVNDSSLMIGMPKSLTAATGMDALTHAIEA-------YVSIAATPITDAcALKAVTMIAENLP----- 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669016 217 arLAAQAGVVTEALERIIEANtYLSGIGFESSGLAAAHAIHN---GFtileecHHLYHG--------------EKVAFGT 279
Cdd:PRK09860 229 --LAVEDGSNAKAREAMAYAQ-FLAGMAFNNASLGYVHAMAHqlgGF------YNLPHGvcnavllphvqvfnSKVAAAR 299
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1709669016 280 L----AQLVLQNSPMDE-------IETVLGFCQRVGLPVTLAQMGVKE 316
Cdd:PRK09860 300 LrdcaAAMGVNVTGKNDaegaeacINAIRELAKKVDIPAGLRDLNVKE 347
|
|
| |
