|
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: 634.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 1 MLKVIQSPAKYLQGPDASTLFGQYAKNLADSFFVIADDFVMKLAGEKVLEGLHSHNISCHAERFNGECSHVEINRLIAIL 80
Cdd:PRK09423 1 MDRIFISPSKYVQGKGALARLGEYLKPLGKRALVIADEFVLGIVGDRVEASLKEAGLTVVFEVFNGECSDNEIDRLVAIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 81 KQHGCRGVVGIGGGKTLDTAKAIGYYQKLPVVVIPTIASTDAPTSALSVIYTEAGEFEEYLIYPKNPDMVVMDTAIIAKA 160
Cdd:PRK09423 81 EENGCDVVIGIGGGKTLDTAKAVADYLGVPVVIVPTIASTDAPTSALSVIYTEEGEFERYLFLPKNPDLVLVDTAIIAKA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 161 PVRLLVAGMGDALSTWFEAKACYDARATSMAGGQSTAAALSLARLCYDTLLAEGEKARLAAQAGVVTDALERIVEANTYL 240
Cdd:PRK09423 161 PARFLAAGIGDALATWFEARACSRSGGTTMAGGKPTLAALALAELCYETLLEDGLKAKLAVEAKVVTPALENVIEANTLL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 241 SGIGFESSGLAAAHAIHNGFTILEECHHLYHGEKVAFGTLAQLVLQNSPMEEIETVLNFCHTVGLPVTLAQMGVKEGIDE 320
Cdd:PRK09423 241 SGLGFESGGLAAAHAIHNGLTALEDTHHLTHGEKVAFGTLTQLVLENRPKEEIEEVIDFCHAVGLPTTLADLGLKEDSDE 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1730616599 321 KIQAVAKATCAEGETIHNMPFPVSAQSVHAAILTADLLGQQWLAR 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: 599.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 8 PAKYLQGPDASTLFGQYAKNLADSFFVIADDFVMKLAGEKVLEGLHSHNISCHAERFNGECSHVEINRLIAILKQHGCRG 87
Cdd:cd08170 1 PSRYVQGPGALDRLGEYLAPLGKKALVIADPFVLDLVGERLEESLEKAGLEVVFEVFGGECSREEIERLAAIARANGADV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 88 VVGIGGGKTLDTAKAIGYYQKLPVVVIPTIASTDAPTSALSVIYTEAGEFEEYLIYPKNPDMVVMDTAIIAKAPVRLLVA 167
Cdd:cd08170 81 VIGIGGGKTIDTAKAVADYLGLPVVIVPTIASTDAPCSALSVIYTEDGEFDEYLFLPRNPDLVLVDTEIIAKAPVRFLVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 168 GMGDALSTWFEAKACYDARATSMAGGQSTAAALSLARLCYDTLLAEGEKARLAAQAGVVTDALERIVEANTYLSGIGFES 247
Cdd:cd08170 161 GMGDALATYFEARACARSGAPNMAGGRPTLAALALAELCYDTLLEYGVAAKAAVEAGVVTPALEAVIEANTLLSGLGFES 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 248 SGLAAAHAIHNGFTILEECHHLYHGEKVAFGTLAQLVLQNSPMEEIETVLNFCHTVGLPVTLAQMGVKEGIDEKIQAVAK 327
Cdd:cd08170 241 GGLAAAHAIHNGLTALPETHHLLHGEKVAFGTLVQLVLEGRPDEEIEEVIRFCRSVGLPVTLADLGLEDVTDEELRKVAE 320
|
330 340 350
....*....|....*....|....*....|.
gi 1730616599 328 ATCAEGETIHNMPFPVSAQSVHAAILTADLL 358
Cdd:cd08170 321 AACAPGETIHNMPFPVTPEDVVDAILAADAL 351
|
|
| GldA |
COG0371 |
Glycerol dehydrogenase or related enzyme, iron-containing ADH family [Energy production and ... |
3-355 |
8.78e-175 |
|
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: 489.68 E-value: 8.78e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 3 KVIQSPAKYLQGPDASTLFGQYAKNLADSFFVIADDFVMKLAGEKVLEGLHSHNISCHAERFNGECSHVEINRLIAILKQ 82
Cdd:COG0371 1 RVIILPRRYVQGEGALDELGEYLADLGKRALIITGPTALKAAGDRLEESLEDAGIEVEVEVFGGECSEEEIERLAEEAKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 83 HGCRGVVGIGGGKTLDTAKAIGYYQKLPVVVIPTIASTDAPTSALSVIYTEAGEFEEYLIYPKNPDMVVMDTAIIAKAPV 162
Cdd:COG0371 81 QGADVIIGVGGGKALDTAKAVAYRLGLPVVSVPTIASTDAPASPLSVIYTEDGAFDGYSFLAKNPDLVLVDTDIIAKAPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 163 RLLVAGMGDALSTWFEAKACYDARATsMAGGQSTAAALSLARLCYDTLLAEGEKARLAAQAGVVTDALERIVEANTYLSG 242
Cdd:COG0371 161 RLLAAGIGDALAKWYEARDWSLAHRD-LAGEYYTEAAVALARLCAETLLEYGEAAIKAVEAGVVTPALERVVEANLLLSG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 243 IGF----ESSGLAAAHAIHNGFTILEECHHLYHGEKVAFGTLAQLVLQNSPmEEIETVLNFCHTVGLPVTLAQMGVKEGI 318
Cdd:COG0371 240 LAMgigsSRPGSGAAHAIHNGLTALPETHHALHGEKVAFGTLVQLVLEGRP-EEIEELLDFLRSVGLPTTLADLGLDDET 318
|
330 340 350
....*....|....*....|....*....|....*..
gi 1730616599 319 DEKIQAVAKATCAEGETIHNMPFPVSAQSVHAAILTA 355
Cdd:COG0371 319 EEELLTVAEAARPERYTILNLPFEVTPEAVEAAILAT 355
|
|
| GlyDH-like |
cd08550 |
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins. ... |
8-355 |
7.80e-133 |
|
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: 383.04 E-value: 7.80e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 8 PAKYLQGPDASTLFGQYAKNLADSFFVIADDFVMKLAGEKVLEGLHSHNISCHAERFNGECSHVEINRLIAILKQHGCRG 87
Cdd:cd08550 1 PGRYIQEPGILAKAGEYIAPLGKKALIIGGKTALEAVGEKLEKSLEEAGIDYEVEVFGGECTEENIERLAEKAKEEGADV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 88 VVGIGGGKTLDTAKAIGYYQKLPVVVIPTIASTDAPTSALSVIYTEAGEFEEYLIYPKNPDMVVMDTAIIAKAPVRLLVA 167
Cdd:cd08550 81 IIGIGGGKVLDTAKAVADRLGLPVVTVPTIAATCAAWSALSVLYDEEGEFLGYSLLKRSPDLVLVDTDIIAAAPVRYLAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 168 GMGDALSTWFEAKACYDARATSMAggqsTAAALSLARLCYDTLLAEGEKARLAAQAGVVTDALERIVEANTYLSGIGFES 247
Cdd:cd08550 161 GIGDTLAKWYEARPSSRGGPDDLA----LQAAVQLAKLAYDLLLEYGVQAVEDVRQGKVTPALEDVVDAIILLAGLVGSL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 248 SG----LAAAHAIHNGFTILEECHHLYHGEKVAFGTLAQLVLQNSPMEEIETVLNFCHTVGLPVTLAQMGVKEgIDEKIQ 323
Cdd:cd08550 237 GGggcrTAAAHAIHNGLTKLPETHGTLHGEKVAFGLLVQLALEGRSEEEIEELIEFLRRLGLPVTLEDLGLEL-TEEELR 315
|
330 340 350
....*....|....*....|....*....|..
gi 1730616599 324 AVAKATCAEGETIHNMPFPVSAQSVHAAILTA 355
Cdd:cd08550 316 KIAEYACDPPDMAHMLPFPVTPEMLAEAILAA 347
|
|
| GlyDH-like |
cd08172 |
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins ... |
45-354 |
9.63e-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: 314.07 E-value: 9.63e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 45 GEKVLEGL-----HSHNISCHAERFNGECSHVEINRLIAILKQHGCRGVVGIGGGKTLDTAKAIGYYQKLPVVVIPTIAS 119
Cdd:cd08172 31 GEKSWQAAkpylpKLFEIEYPVLRYDGECSYEEIDRLAEEAKEHQADVIIGIGGGKVLDTAKAVADKLNIPLILIPTLAS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 120 TDAPTSALSVIYTEAGEFEEYLIYPKNPDMVVMDTAIIAKAPVRLLVAGMGDALSTWFEAkacyDARATSMAgGQSTAAA 199
Cdd:cd08172 111 NCAAWTPLSVIYDEDGEFIGYDYFPRSAYLVLVDPRLLLDSPKDYFVAGIGDTLAKWYEA----DAILRQLE-ELPAFLQ 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 200 LSL--ARLCYDTLLAEGEKARLAAQAGVVTDALERIVEANTYLSGI--GF--ESSGLAAAHAIHNGFTILEECHHLYHGE 273
Cdd:cd08172 186 LARqaAKLCRDILLKDSEQALADLEAGKLTPAFIKVVETIIALAGMvgGFgdEYGRSAGAHAIHNGLTKLPETHHFLHGE 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 274 KVAFGTLAQLVLQNSpMEEIETVLNFCHTVGLPVTLAQMGVKEGIDEKIQAVAKATCAEGETIHNMPFPVSAQSVHAAIL 353
Cdd:cd08172 266 KVAYGILVQLALEGK-WDEIKKLLPFYRRLGLPTSLADLGLTDDTEEALQKIAAFAASPEESIHLLPPDVTAEEVLQAIE 344
|
.
gi 1730616599 354 T 354
Cdd:cd08172 345 K 345
|
|
| Fe-ADH |
pfam00465 |
Iron-containing alcohol dehydrogenase; |
8-348 |
1.22e-70 |
|
Iron-containing alcohol dehydrogenase;
Pssm-ID: 425696 [Multi-domain] Cd Length: 362 Bit Score: 224.79 E-value: 1.22e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 8 PAKYLQGPDASTLFGQYAKNLADSFFVIADDFVMKL-AGEKVLEGLHSHNISC-HAERFNGECSHVEINRLIAILKQHGC 85
Cdd:pfam00465 1 PTRIVFGAGALAELGEELKRLGARALIVTDPGSLKSgLLDKVLASLEEAGIEVvVFDGVEPEPTLEEVDEAAALAREAGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 86 RGVVGIGGGKTLDTAKAIGYY------------------QKLPVVVIPTIASTDAPTSALSVIYTEAGEFEEYLIYPK-N 146
Cdd:pfam00465 81 DVIIAVGGGSVIDTAKAIALLltnpgdvwdylggkpltkPALPLIAIPTTAGTGSEVTPLAVITDTETGEKLGIFSPKlL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 147 PDMVVMDTAIIAKAPVRLLVAGMGDALSTWFEAkacYDARATSMAGGQSTAAALSLARLCYDTLLAEGEKArlaaqagvv 226
Cdd:pfam00465 161 PDLAILDPELTLTLPPRLTAATGMDALAHAVEA---YVSKGANPLTDALALEAIRLIAENLPRAVADGEDL--------- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 227 tDALERIVEANTyLSGIGFESSGLAAAHAIHNGFTILEECHH-LYHGEKVAFGT----------LAQLVL-------QNS 288
Cdd:pfam00465 229 -EARENMLLAST-LAGLAFSNAGLGAAHALAHALGGRYGIPHgLANAILLPYVLrfnapaapekLAQLARalgedsdEEA 306
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 289 PMEEIETVLNFCHTVGLPVTLAQMGVKEgidEKIQAVAKATCAEGeTIHNMPFPVSAQSV 348
Cdd:pfam00465 307 AEEAIEALRELLRELGLPTTLSELGVTE---EDLDALAEAALRDR-SLANNPRPLTAEDI 362
|
|
| GlyDH-like |
cd08171 |
Glycerol dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins ... |
14-353 |
8.46e-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: 214.31 E-value: 8.46e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 14 GPDASTLFGQYAKNLADSFFVIADDFVMKLAGEKVLEGLHSHNISCHAER-FNGECSHVEINRLIAILKQHGCRGVVGIG 92
Cdd:cd08171 7 GEDAYDAIPKICSPYGKKVVVIGGKKALAAAKPKLRAALEGSGLEITDFIwYGGEATYENVEKLKANPEVQEADMIFAVG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 93 GGKTLDTAKAIGYYQKLPVVVIPTIASTDAPTSALSVIYTEAGEFEEYLIYPKNPDMVVMDTAIIAKAPVRLLVAGMGDA 172
Cdd:cd08171 87 GGKAIDTVKVLADRLNKPVFTFPTIASNCAAVTAVSVMYNPDGSFKEYYFLKRPPVHTFIDTEIIAEAPEKYLWAGIGDT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 173 LSTWFEakACYDARATSMAggQSTAAALSLARLCYDTLLAEGEKARLAAQAGVVTDALERIVEANTYLSGIgfeSSGLAA 252
Cdd:cd08171 167 LAKYYE--VEFSARGDELD--HTNALGVAISKMCSEPLLKYGVQALEDCRANKVSDALEQVVLDIIVTTGL---VSNLVE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 253 -------AHAIHNGFTILEEC--HHLyHGEKVAFGTLAQLVLQNSpMEEIETVLNFCHTVGLPVTLAQMGVKEgidEKIQ 323
Cdd:cd08171 240 pdynsslAHALYYGLTTLPQIeeEHL-HGEVVSYGVLVLLTVDGQ-FEELEKVYAFNKSIGLPTCLADLGLTV---EDLE 314
|
330 340 350
....*....|....*....|....*....|
gi 1730616599 324 AVAKATcAEGETIHNMPFPVSAQSVHAAIL 353
Cdd:cd08171 315 KVLDKA-LKTKDLRHSPYPITKEMFEEAIK 343
|
|
| DHQ_Fe-ADH |
cd07766 |
Dehydroquinate synthase-like (DHQ-like) and iron-containing alcohol dehydrogenases (Fe-ADH); ... |
8-330 |
6.38e-50 |
|
Dehydroquinate synthase-like (DHQ-like) and iron-containing alcohol dehydrogenases (Fe-ADH); This superfamily consists of two subgroups: the dehydroquinate synthase (DHQS)-like, and a large metal-containing alcohol dehydrogenases (ADH), known as iron-containing alcohol dehydrogenases. Dehydroquinate synthase (DHQS) catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate-7-phosphate (DAHP) to dehydroquinate (DHQ) in the second step of the shikimate pathway. This pathway involves seven sequential enzymatic steps in the conversion of erythrose 4-phosphate and phosphoenolpyruvate into chorismate for subsequent synthesis of aromatic compounds. Dehydroquinate synthase-like group includes dehydroquinate synthase, 2-deoxy-scyllo-inosose synthase, and 2-epi-5-epi-valiolone synthase. The alcohol dehydrogenases (ADHs) in this superfamily contain a dehydroquinate synthase-like protein structural fold and mostly contain iron. They are distinct from other alcohol dehydrogenases which contains different protein domains. There are several distinct families of alcohol dehydrogenases: Zinc-containing long-chain alcohol dehydrogenases; insect-type, or short-chain alcohol dehydrogenases; iron-containing alcohol dehydrogenases, and others. The iron-containing family has a Rossmann fold-like topology that resembles the fold of the zinc-dependent alcohol dehydrogenases, but lacks sequence homology, and differs in strand arrangement. ADH catalyzes the reversible oxidation of alcohol to acetaldehyde with the simultaneous reduction of NAD(P)+ to NAD(P)H.
Pssm-ID: 341447 [Multi-domain] Cd Length: 271 Bit Score: 168.31 E-value: 6.38e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 8 PAKYLQGPDASTLFGQYAKNLADSFFVIADDFVMKLAGEKVLEGLhSHNISCHAERF-NGECSHVEINRLIAILKQHGCR 86
Cdd:cd07766 1 PTRIVFGEGAIAKLGEIKRRGFDRALVVSDEGVVKGVGEKVADSL-KKGLAVAIFDFvGENPTFEEVKNAVERARAAEAD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 87 GVVGIGGGKTLDTAKAIGY--YQKLPVVVIPTIASTDAPTSALSVIYTEAGEFEEyLIYPKNPDMVVMDTAIIAKAPVRL 164
Cdd:cd07766 80 AVIAVGGGSTLDTAKAVAAllNRGIPFIIVPTTASTDSEVSPKSVITDKGGKNKQ-VGPHYNPDVVFVDTDITKGLPPRQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 165 LVAGMGDALSTWFEakacydaratsmaggqstaaalslarlcydtllaegekarlaaqagvvtdaLERIVEANTYLSGIG 244
Cdd:cd07766 159 VASGGVDALAHAVE---------------------------------------------------LEKVVEAATLAGMGL 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 245 FESSGLAAAHAIHNGFTILeecHHLYHGEKVAFGTLAQLVLQNSPMEE----IETVLNFCHTVGLPVTLAQMGVKegiDE 320
Cdd:cd07766 188 FESPGLGLAHAIGHALTAF---EGIPHGEAVAVGLPYVLKVANDMNPEpeaaIEAVFKFLEDLGLPTHLADLGVS---KE 261
|
330
....*....|
gi 1730616599 321 KIQAVAKATC 330
Cdd:cd07766 262 DIPKLAEKAL 271
|
|
| PRK10586 |
PRK10586 |
putative oxidoreductase; Provisional |
63-360 |
3.35e-47 |
|
putative oxidoreductase; Provisional
Pssm-ID: 182570 Cd Length: 362 Bit Score: 164.13 E-value: 3.35e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 63 RFNGECSHVEINRLIAilkQHG--CRGVVGIGGGKTLDTAKAIGYYQKLPVVVIPTIASTDAPTSALSVIYTEAGEFEEY 140
Cdd:PRK10586 66 LFRGHCSESDVAQLAA---ASGddRQVVIGVGGGALLDTAKALARRLGLPFVAIPTIAATCAAWTPLSVWYNDAGQALHF 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 141 LIYPKNPDMVVMDTAIIAKAPVRLLVAGMGDALSTWFEAKACYDARAT---SMAGGQSTAAALSlarlcyDTLLAEGEKA 217
Cdd:PRK10586 143 EIFDDANFLVLVEPRIILNAPQEYLLAGIGDTLAKWYEAVVLAPQPETlplTVRLGINNALAIR------DVLLNSSEQA 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 218 RLAAQAGVVT----DALERIVEANTYLSGIGFESSGLAAAHAIHNGFTILEECHHLYHGEKVAFGTLAQLVL--QNSPME 291
Cdd:PRK10586 217 LADQQNGQLTqdfcDVVDAIIAGGGMVGGLGERYTRVAAAHAVHNGLTVLPQTEKFLHGTKVAYGILVQSALlgQDDVLA 296
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1730616599 292 EIETVLnfcHTVGLPVTLAQMGVKEGIDEKIQAVAKATCAEGETIHNMPFPVSAQSVHAAILTADLLGQ 360
Cdd:PRK10586 297 QLIGAY---QRFHLPTTLAELDVDINNQAEIDRVIAHTLRPVESIHYLPVTLTPDTLRAAFEKVESFKA 362
|
|
| G1PDH-like |
cd08174 |
Glycerol-1-phosphate dehydrogenase-like; These glycerol-1-phosphate dehydrogenase-like ... |
34-328 |
5.02e-31 |
|
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: 119.93 E-value: 5.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 34 VIADDFVMKLAGEKVLEGLHSHNIScHAERFNGECSHVEINRLIAILKQHGCrgVVGIGGGKTLDTAKAIGYYQKLPVVV 113
Cdd:cd08174 30 IVTGEGIDELLGEDILESLEEAGEI-VTVEENTDNSAEELAEKAFSLPKVDA--IVGIGGGKVLDVAKYAAFLSKLPFIS 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 114 IPTIASTDAPTSALSVIYTEAGefeeYLIYP-KNPDMVVMDTAIIAKAPVRLLVAGMGDALS--TwfeakACYDARATSM 190
Cdd:cd08174 107 VPTSLSNDGIASPVAVLKVDGK----RKSLGaKMPYGVIVDLDVIKSAPRRLILAGIGDLISniT-----ALYDWKLAEE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 191 AGGQS--TAAALsLARLCYDTLLAEGEKArlaaqagvVTDA--LERIVEANTyLSGIGFE-------SSGlaAAHAIhng 259
Cdd:cd08174 178 KGGEPvdDFAYL-LSRTAADSLLNTPGKD--------IKDDefLKELAESLV-LSGIAMEiagssrpASG--SEHLI--- 242
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1730616599 260 ftileeCHHL--------YHGEKVAFGTLAQLVLQNSPMEEIETVLnfcHTVGLPVTLAQMGVKEgiDEKIQAVAKA 328
Cdd:cd08174 243 ------SHALdklfpgpaLHGIQVGLGTYFMSFLQGQRYEEIRDVL---KRTGFPLNPSDLGLTK--EEFIEAVKLA 308
|
|
| Gro1PDH |
cd08173 |
Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) catalyzes the reversible conversion between ... |
8-328 |
2.37e-27 |
|
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: 110.34 E-value: 2.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 8 PAKYLQGPDASTLFGQYAKNL--ADSFFVIADDFVMKLAGEKVLEGLHSHNISCHAERFNGECSHVEINRLIAILKQHGC 85
Cdd:cd08173 2 PRNVVVGHGAINKIGEVLKKLllGKRALIITGPNTYKIAGKRVEDLLESSGVEVVIVDIATIEEAAEVEKVKKLIKESKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 86 RGVVGIGGGKTLDTAKAIGYYQKLPVVVIPTIASTDAPTSALSVIYteaGEFEEYLIYPKNPDMVVMDTAIIAKAPVRLL 165
Cdd:cd08173 82 DFIIGVGGGKVIDVAKYAAYKLNLPFISIPTSASHDGIASPFASIK---GGDKPYSIKAKAPIAIIADTEIISKAPKRLL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 166 VAGMGDALS--TwfeakACYDAR-ATSMAG---GQStAAALSL--ARLcydtLLAEGEKARLAAQAGVVTdalerIVEAn 237
Cdd:cd08173 159 AAGCGDLISniT-----AVKDWRlAHRLKGeyySEY-AASLALmsAKL----IIENADLIKPGLEEGVRT-----VVKA- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 238 tylsgigFESSGLAAA----------------HAIHngftILEECHHLyHGEKVAFGTLAQLVLQNSPMEEIETVLnfcH 301
Cdd:cd08173 223 -------LISSGVAMSiagssrpasgsehlfsHALD----KLAPGPAL-HGEQCGVGTIMMAYLHGGDWKEIREAL---K 287
|
330 340
....*....|....*....|....*..
gi 1730616599 302 TVGLPVTLAQMGVKEgiDEKIQAVAKA 328
Cdd:cd08173 288 KIGAPTTAKELGLDK--EIIIEALTIA 312
|
|
| Fe-ADH |
cd08551 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains large ... |
8-350 |
6.74e-24 |
|
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: 100.98 E-value: 6.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 8 PAKYLQGPDASTLFGQYAKNL-ADSFFVIADDFVMKL-AGEKVLEGLHSHNISChaERFNG---ECSHVEINRLIAILKQ 82
Cdd:cd08551 1 PTRIVFGAGALARLGEELKALgGKKVLLVTDPGLVKAgLLDKVLESLKAAGIEV--EVFDDvepNPTVETVEAAAELARE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 83 HGCRGVVGIGGGKTLDTAKAIG-----------YY-------QKLPVVVIPTIASTDAPTSALSVIYTEAGEFEEYLIYP 144
Cdd:cd08551 79 EGADLVIAVGGGSVLDTAKAIAvlatnggsirdYEgigkvpkPGLPLIAIPTTAGTGSEVTPNAVITDPETGRKMGIVSP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 145 KN-PDMVVMDTAIIAKAPVRLLVA-GMgDALSTWFEAkacYDAR-ATSMaggqSTAAALSLARLCYDTLlaegekaRLAA 221
Cdd:cd08551 159 YLlPDVAILDPELTLSLPPSVTAAtGM-DALTHAIEA---YTSKkANPI----SDALALEAIRLIGKNL-------RRAV 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 222 QAGVVTDALERIVEAnTYLSGIGFESSGLAAAHAIhnGFTiLEECHHLYHGEKVA-----------------FGTLAQLV 284
Cdd:cd08551 224 ADGSDLEAREAMLLA-SLLAGIAFGNAGLGAVHAL--AYP-LGGRYHIPHGVANAillpyvmefnlpacpekYAEIAEAL 299
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1730616599 285 LQN----SPMEE----IETVLNFCHTVGLPVTLAQMGVKEgidEKIQAVAKATCAEGETIHNMPFPVSAQSVHA 350
Cdd:cd08551 300 GEDveglSDEEAaeaaVEAVRELLRDLGIPTSLSELGVTE---EDIPELAEDAMKSGRLLSNNPRPLTEEDIRE 370
|
|
| Fe-ADH_2 |
pfam13685 |
Iron-containing alcohol dehydrogenase; |
34-276 |
1.57e-23 |
|
Iron-containing alcohol dehydrogenase;
Pssm-ID: 404557 [Multi-domain] Cd Length: 251 Bit Score: 97.76 E-value: 1.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 34 VIADDFVMKLAGEKVLEGLHSHNISCHA-ERFNGECSHVEINRLIAILKQHGCRGVVGIGGGKTLDTAKAIGYYQKLPVV 112
Cdd:pfam13685 24 LVADANTYAAAGRKVAESLKRAGIEVETrLEVAGNADMETAEKLVGALRERDADAVVGVGGGTVIDLAKYAAFKLGKPFI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 113 VIPTIASTDAPTSALSVIYteaGEFEEYLIYPKNPDMVVMDTAIIAKAPVRLLVAGMGDALSTWfeaKACYDARAtSMAG 192
Cdd:pfam13685 104 SVPTAASNDGFASPGASLT---VDGKKRSIPAAAPFGVIADTDVIAAAPRRLLASGVGDLLAKI---TAVADWEL-AHAE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 193 GQSTAAALSLARLCYdtllaegEKARLAAQAGVVTDALERIVEANTyLSGIGFESSGLAAAHAI-HngftILEECH--HL 269
Cdd:pfam13685 177 EVAAPLALLSAAMVM-------NFADRPLRDPGDIEALAELLSALA-MGGAGSSRPASGSEHLIsH----ALDMIApkQA 244
|
....*..
gi 1730616599 270 YHGEKVA 276
Cdd:pfam13685 245 LHGEQVG 251
|
|
| egsA |
PRK00843 |
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed |
3-328 |
5.95e-22 |
|
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed
Pssm-ID: 179139 Cd Length: 350 Bit Score: 95.35 E-value: 5.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 3 KVIQSPAKYLQGPDASTLFGQYAKNLA--DSFFVIADDFVMKLAGEKVLEGLHShniSCHAERF-NGECSHVEINRLIAI 79
Cdd:PRK00843 6 HWIQLPRDVVVGHGVLDDIGDVCSDLKltGRALIVTGPTTKKIAGDRVEENLED---AGDVEVViVDEATMEEVEKVEEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 80 LKQHGCRGVVGIGGGKTLDTAKAIGYYQKLPVVVIPTIASTDAPTSALSVIYTEAGefeEYLIYPKNPDMVVMDTAIIAK 159
Cdd:PRK00843 83 AKDVNAGFLIGVGGGKVIDVAKLAAYRLGIPFISVPTAASHDGIASPRASIKGGGK---PVSVKAKPPLAVIADTEIIAK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 160 APVRLLVAGMGDALSTWfeaKACYDAR-ATSMAGGQ--STAAALSL--ARLCYDTllAEGEKARLAAQAGVVTDALeriv 234
Cdd:PRK00843 160 APYRLLAAGCGDIISNY---TAVKDWRlAHRLRGEYysEYAAALSLmtAKMLIEN--ADIIKPGLEESARLVVKAL---- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 235 eantylsgigfESSGLAA----------------AHA---IHNGFTIleechhlyHGEKVAFGTLAQLVLQNSPMEEIET 295
Cdd:PRK00843 231 -----------ISSGVAMsiagssrpasgsehlfSHAldrLAPGPAL--------HGEQCGVGTIIMMYLHGGDWRKIRD 291
|
330 340 350
....*....|....*....|....*....|...
gi 1730616599 296 VLNfchTVGLPVTLAQMGVKEgiDEKIQAVAKA 328
Cdd:PRK00843 292 ALK---KIGAPTTAKELGIDD--EYIIEALTIA 319
|
|
| EutG |
COG1454 |
Alcohol dehydrogenase, class IV [Energy production and conversion]; |
1-355 |
6.63e-22 |
|
Alcohol dehydrogenase, class IV [Energy production and conversion];
Pssm-ID: 441063 [Multi-domain] Cd Length: 381 Bit Score: 95.57 E-value: 6.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 1 MLKVIQSPAKYLQGPDASTLFGQYAKNL-ADSFFVIADDFVMKL-AGEKVLEGLHSHNISCHA-ERFNGECSHVEINRLI 77
Cdd:COG1454 1 MMFTFRLPTRIVFGAGALAELGEELKRLgAKRALIVTDPGLAKLgLLDRVLDALEAAGIEVVVfDDVEPNPTVETVEAGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 78 AILKQHGCRGVVGIGGGKTLDTAKAIG-----------YY-------QKLPVVVIPTIASTDAPTSALSVIYTEAGEFEE 139
Cdd:COG1454 81 AAAREFGADVVIALGGGSAIDAAKAIAllatnpgdledYLgikkvpgPPLPLIAIPTTAGTGSEVTPFAVITDPETGVKK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 140 YLIYPKN-PDMVVMDTAIIAKAPVRLLVA-GMgDALSTWFEakACYDARATSMaggqSTAAALSLARLCYDTLlaegeka 217
Cdd:COG1454 161 GIADPELlPDVAILDPELTLTLPPSLTAAtGM-DALTHAIE--AYVSKGANPL----TDALALEAIRLIARNL------- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 218 RLAAQAGVVTDALERIVEANTyLSGIGFESSGLAAAHAI-H--NGFtileecHHLYHGEKVA-----------------F 277
Cdd:COG1454 227 PRAVADGDDLEAREKMALASL-LAGMAFANAGLGAVHALaHplGGL------FHVPHGLANAillphvlrfnapaaperY 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 278 GTLAQLV---LQNSPMEE----IETVLNFCHTVGLPVTLAQMGVKEgidEKIQAVAKATCAEGETIHNmPFPVSAQSVhA 350
Cdd:COG1454 300 AEIARALgldVGLSDEEAaealIEAIRELLRDLGIPTRLSELGVTE---EDLPELAELALADRCLANN-PRPLTEEDI-E 374
|
....*
gi 1730616599 351 AILTA 355
Cdd:COG1454 375 AILRA 379
|
|
| Fe-ADH-like |
cd14863 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
14-350 |
3.35e-17 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341485 [Multi-domain] Cd Length: 380 Bit Score: 81.81 E-value: 3.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 14 GPDASTLFGQYAKNL-ADSFFVIADDFVMKlAG--EKVLEGLHSHNISchAERFNG---ECSHVEINRLIAILKQHGCRG 87
Cdd:cd14863 11 GAGAVEQIGELLKELgCKKVLLVTDKGLKK-AGivDKIIDLLEEAGIE--VVVFDDvepDPPDEIVDEAAEIAREEGADG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 88 VVGIGGGKTLDTAKAIGY-------------------YQKLPVVVIPTIASTDAPTSALSVIYTEAGEFEEYLIYPK-NP 147
Cdd:cd14863 88 VIGIGGGSVLDTAKAIAVlltnpgpiidyalagppvpKPGIPLIAIPTTAGTGSEVTPIAVITDEENGVKKSLLGPFlVP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 148 DMVVMDTAIIAKAPVRLLVA-GMgDALSTWFEAkacydaratsMAGGQSTAAALSLA----RLCYDTL---LAEGE--KA 217
Cdd:cd14863 168 DLAILDPELTVGLPPSLTAAtGM-DALSHAIEA----------YTSKLANPMTDALAlqaiRLIVKNLpraVKDGDnlEA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 218 R----LAAqagvvtdaleriveantYLSGIGFESSGLAAAHAI-HngftILEECHHLYHGEKVAFGT------------- 279
Cdd:cd14863 237 RenmlLAS-----------------NLAGIAFNNAGTHIGHAIaH----ALGALYHIPHGLACALALpvvlefnaeaype 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 280 ----LAQ---LVLQNSPMEEI-----ETVLNFCHTVGLPVTLAQMGVKEgidEKIQAVAKATCAEgETIHNMPFPVSAQS 347
Cdd:cd14863 296 kvkkIAKalgVSFPGESDEELgeavaDAIREFMKELGIPSLFEDYGIDK---EDLDKIAEAVLKD-PFAMFNPRPITEEE 371
|
...
gi 1730616599 348 VHA 350
Cdd:cd14863 372 VAE 374
|
|
| Fe-ADH-like |
cd08196 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
29-349 |
5.61e-17 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341475 [Multi-domain] Cd Length: 367 Bit Score: 81.09 E-value: 5.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 29 ADSFFVIADDFvmklagEKVLEGLHSHNISCHAErFNGECSHVEINRLIAILKQHGCRGVVGIGGGKTLDTAKAIG---- 104
Cdd:cd08196 35 TDPSFIKSGLA------KRIVESLKGRIVAVFSD-VEPNPTVENVDKCARLARENGADFVIAIGGGSVLDTAKAAAclak 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 105 -------YYQK--------LPVVVIPTIASTDAPTSALSVI-YTEAGE---FEEYLIYPknpdmvvmDTAIIAKA----- 160
Cdd:cd08196 108 tdgsiedYLEGkkkipkkgLPLIAIPTTAGTGSEVTPVAVLtDKEKGKkapLVSPGFYP--------DIAIVDPEltysm 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 161 PVRLLVA-GMgDALSTWFEAkacYDARaTSMAggQSTAAALSLARLCYDTLLA---EGEKArlaaqagvvtDALERIVEA 236
Cdd:cd08196 180 PPKVTAStGI-DALCHAIEA---YWSI-NHQP--ISDALALEAAKLVLENLEKaynNPNDK----------EAREKMALA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 237 NTyLSGIGFESSGLAAAHAIHNGFTILeecHHLYHGEKVAFgTLAQLVLQNSPMEE--IETVLNFC-------------- 300
Cdd:cd08196 243 SL-LAGLAFSQTRTTASHACSYPLTSH---FGIPHGEACAL-TLPSFIRLNAEALPgrLDELAKQLgfkdaeeladkiee 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1730616599 301 --HTVGLPVTLAQMGVKEgidEKIQAVAKATCAEgETIHNMPFPVSAQSVH 349
Cdd:cd08196 318 lkKRIGLRTRLSELGITE---EDLEEIVEESFHP-NRANNNPVEVTKEDLE 364
|
|
| G1PDH_related |
cd08549 |
Glycerol-1-phosphate dehydrogenase and related proteins; This family contains bacterial and ... |
88-318 |
5.65e-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: 5.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 88 VVGIGGGKTLDTAKAIGYYQKLPVVVIPTIASTDAPTS-ALSVIYTEagefEEYLIYPKNPDMVVMDTAIIAKAPVRLLV 166
Cdd:cd08549 74 VIGIGGGRSIDTGKYLAYKLKIPFISVPTSASNDGIASpIVSLRIPG----VKKTFMADAPIAIIADTEIIKKSPRRLLS 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 167 AGMGDALSTWfeaKACYDAR-ATSMAGGQSTAAALSLARLCYDTLLAEGEKARLAAQ-AGVVTDALERiveantylSGIG 244
Cdd:cd08549 150 AGIGDLVSNI---TAVLDWKlAHKEKGEKYSEFAAILSKTSAKELVSYVLKASDLEEyHRVLVKALVG--------SGIA 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 245 FESSGLAA---------AHAIHNGFTILEECHHLyHGEKVAFGT-----LAQLVLQNSPM--EEIETVLNfchTVGLPVT 308
Cdd:cd08549 219 MAIAGSSRpasgsehlfSHALDKLKEEYLNINVL-HGEQVGVGTiimsyLHEKENKKLSGlhERIKMILK---KVGAPTT 294
|
250
....*....|
gi 1730616599 309 LAQMGVKEGI 318
Cdd:cd08549 295 AKQLGIDEDL 304
|
|
| Fe-ADH-like |
cd08191 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
7-355 |
4.70e-13 |
|
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contain different protein domain. Proteins of this family have not been characterized.
Pssm-ID: 341470 [Multi-domain] Cd Length: 392 Bit Score: 69.56 E-value: 4.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 7 SPAKYLQGPDASTLFGQYAKNLADSFFVIADDFVMKLAG-EKVLEGLHSHNISchAERFNGEC---SHVEINRLIAILKQ 82
Cdd:cd08191 3 SPSRLLFGPGARRALGRVAARLGSRVLIVTDPRLASTPLvAELLAALTAAGVA--VEVFDGGQpelPVSTVADAAAAARA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 83 HGCRGVVGIGGGKTLDTAKAIG-----------YY-------QKLPVVVIPTIASTDAPTSALSVIYTEA-----GEFEE 139
Cdd:cd08191 81 FDPDVVIGLGGGSNMDLAKVVAlllahggdprdYYgedrvpgPVLPLIAVPTTAGTGSEVTPVAVLTDPArgmkvGVSSP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 140 YLIypknPDMVVMDTAIIAKAPVRLLVAGMGDALSTWFEAkacYDARATSMAGGQSTAAALSLARLCYDTLLAEGekARL 219
Cdd:cd08191 161 YLR----PAVAIVDPELTLTCPPGVTADSGIDALTHAIES---YTARDFPPFPRLDPDPVYVGKNPLTDLLALEA--IRL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 220 AAQAgvvtdaLERIV------EANT------YLSGIGFESSGLAAAHAIH---NGFTileechHLYHGEKVA-------- 276
Cdd:cd08191 232 IGRH------LPRAVrdgddlEARSgmalaaLLAGLAFGTAGTAAAHALQypiGALT------HTSHGVGNGlllpyvmr 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 277 ---------FGTLAQL--VLQNSPMEE-----IETVLNFCHTVGLPVTLAQMGVKEgidEKIQAVAKATCAEGETIHNMP 340
Cdd:cd08191 300 fnrparaaeLAEIARAlgVTTAGTSEEaadraIERVEELLARIGIPTTLADLGVTE---ADLPGLAEKALSVTRLIANNP 376
|
410
....*....|....*
gi 1730616599 341 FPVSAQSVHaAILTA 355
Cdd:cd08191 377 RPPTEEDLL-RILRA 390
|
|
| Fe-ADH-like |
cd14865 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
73-355 |
4.71e-13 |
|
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: 69.49 E-value: 4.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 73 INRLIAILKQHGCRGVVGIGGGKTLDTAKAIG-----------YYQ--------KLPVVVIPTIASTDAPTSALSVIY-T 132
Cdd:cd14865 74 VNEAAARAREAGADGIIAVGGGSVIDTAKGVNillseggddldDYGganrltrpLKPLIAIPTTAGTGSEVTLVAVIKdE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 133 EAGEFEEYLIYPKNPDMVVMDTAIIAKAPVRLLVA-GMgDALSTWFEAKACydaratSMAGGQSTAAALSLARLCYDTL- 210
Cdd:cd14865 154 EKKVKLLFVSPFLLPDVAILDPRLTLSLPPKLTAAtGM-DALTHAIEAYTS------LQKNPISDALALQAIRLISENLp 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 211 --LAEG--EKARLAAQagvvtdalerivEANTyLSGIGFESSGLAAAHAI-HNgftiLEECHHLYHG------------- 272
Cdd:cd14865 227 kaVKNGkdLEARLALA------------IAAT-MAGIAFSNSMVGLVHAIaHA----VGAVAGVPHGlansillphvmry 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 273 ------EKVAFGTLAQLVLQN----SPMEEIETVLNFCHT----VGLPVTLAQMGVKEgidEKIQAVAKATCAEGETIHN 338
Cdd:cd14865 290 nldaaaERYAELALALAYGVTpagrRAEEAIEAAIDLVRRlhelCGLPTRLRDVGVPE---EQLEAIAELALNDGAILFN 366
|
330
....*....|....*..
gi 1730616599 339 mPFPVSAQSVhAAILTA 355
Cdd:cd14865 367 -PREVDPEDI-LAILEA 381
|
|
| HEPD |
cd08182 |
Hydroxyethylphosphoate dehydrogenase (HEPD) catalyzes the reduction of phosphonoacetaldehyde ... |
8-352 |
6.26e-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: 6.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 8 PAKYLQGPDASTLFGQYAKNLADS--FFVIADDFVMKLAGEKVLEGLHSHNIschAERFNGECSHVEINRL---IAILKQ 82
Cdd:cd08182 1 PVKIIFGPGALAELKDLLGGLGARrvLLVTGPSAVRESGAADILDALGGRIP---VVVFSDFSPNPDLEDLergIELFRE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 83 HGCRGVVGIGGGKTLDTAKAI--------------------GYYQKLPVVVIPTIASTDAPTSALSVIY-TEAGE---FE 138
Cdd:cd08182 78 SGPDVIIAVGGGSVIDTAKAIaallgspgenllllrtgekaPEENALPLIAIPTTAGTGSEVTPFATIWdEAEGKkysLA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 139 EYLIYpknPDMVVMDTAIIAKAPVRLLVAGMGDALSTWFEAkacYDARATSMAggqSTAAALSLARLCYDTLlaegekaR 218
Cdd:cd08182 158 HPSLY---PDAAILDPELTLSLPLYLTASTGLDALSHAIES---IWSVNANPE---SRAYALRAIRLILENL-------P 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 219 LAAQAGVVTDALERIVEAnTYLSGIGFESSGLAAAHAIHNGFTILeecHHLYHGEKVAF--------------------- 277
Cdd:cd08182 222 LLLENLPNLEAREAMAEA-SLLAGLAISITKTTAAHAISYPLTSR---YGVPHGHACALtlpavlrynagaddecdddpr 297
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1730616599 278 -GTLAQLVLQNSPMEEIETVLNFCHTVGLPVTLAQMGVKEgidEKIQAVAKAtCAEGETIHNMPFPVSAQSVHAAI 352
Cdd:cd08182 298 gREILLALGASDPAEAAERLRALLESLGLPTRLSEYGVTA---EDLEALAAS-VNTPERLKNNPVRLSEEDLLRLL 369
|
|
| G1PDH |
cd08175 |
Glycerol-1-phosphate dehydrogenase (G1PDH) catalyzes the reversible reduction of ... |
25-314 |
3.86e-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: 66.38 E-value: 3.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 25 AKNLADSFFVIADDFVMKLAGEKVLEGLHSHNISCHAERFNGE----CSHVEINRLIAILKQHgCRGVVGIGGGkTL-DT 99
Cdd:cd08175 20 ELFGGKKVLVVADENTYAAAGEEVEAALEEAGVTVCLLIFPGEgdliADEAAVGKVLLELEKD-TDLIIAVGSG-TInDL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 100 AKAIGYYQKLPVVVIPTIASTDAPTSALSVIyTEAGEFEEY-LIYPKnpdMVVMDTAIIAKAPVRLLVAGMGDALstwfe 178
Cdd:cd08175 98 TKYAAYKLGIPYISVPTAPSMDGYTSSGAPI-IVDGVKKTFpAHAPK---AIFADLDVLANAPQRMIAAGFGDLL----- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 179 akacydARATSMAGGQstaaalsLARL---------CYDtLLAEGEKARLAAQAGVVT---DALERIVEANTyLSGIGFE 246
Cdd:cd08175 169 ------GKYTALADWK-------LSHLlggeyycpeVAD-LVQEALEKCLDNAEGIAArdpEAIEALMEALI-LSGLAMQ 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 247 -------SSGlaAAHAI-HngftILEECHH------LYHGEKVAFGTLA----QLVLQNSPMEEIETVLNfchTVGLPVT 308
Cdd:cd08175 234 lvgnsrpASG--AEHHLsH----YWEMEFLrlgkppVLHGEKVGVGTLLiaalYILEQLPPPEELRELLR---KAGAPTT 304
|
....*.
gi 1730616599 309 LAQMGV 314
Cdd:cd08175 305 PEDLGI 310
|
|
| Fe-ADH-like |
cd14864 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
8-256 |
1.43e-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: 341486 [Multi-domain] Cd Length: 376 Bit Score: 65.01 E-value: 1.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 8 PAKYLQGPDASTLFGQYAKNLADSFFVIADDfVMKLAGE--KVLEGLHSHNISCHA-ERFNGECSHVEINRLIAILKQHG 84
Cdd:cd14864 4 PPNIVFGADSLERIGEEVKEYGSRFLLITDP-VLKESGLadKIVSSLEKAGISVIVfDEIPASATSDTIDEAAELARKAG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 85 CRGVVGIGGGKTLDTAKAIG-----------YYQK-------LPVVVIPTIASTDAPTSAlSVIYTEAGEFEEYLIYPKN 146
Cdd:cd14864 83 ADGIIAVGGGKVLDTAKAVAilanndggaydFLEGakpkkkpLPLIAVPTTPRSGFEFSD-RFPVVDSRSREVKLLKAQP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 147 --PDMVVMDTAIIAKAPVRLLVAGMGDALSTWFEAKACYDAR-ATSMAGGQSTAaalslarlcydtLLAEGEKARLAAQA 223
Cdd:cd14864 162 glPKAVIVDPNLMASLTGNQTAAMALAALALAVEAYLSKKSNfFSDALALKAIE------------LVSENLDGALADPK 229
|
250 260 270
....*....|....*....|....*....|...
gi 1730616599 224 GvvTDALERIVEANtYLSGIGFESSGLAAAHAI 256
Cdd:cd14864 230 N--TPAEELLAQAG-CLAGLAASSSSPGLATAL 259
|
|
| Fe-ADH-like |
cd08194 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
8-225 |
1.43e-11 |
|
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) most of which have not been characterized. Their specific function is unknown. The protein structure represents a dehydroquinate synthase-like fold and belongs to the alcohol dehydrogenase-like superfamily. It is distinct from other alcohol dehydrogenases which contain different protein domains. Alcohol dehydrogenase catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions.
Pssm-ID: 341473 [Multi-domain] Cd Length: 378 Bit Score: 64.86 E-value: 1.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 8 PAKYLQGPDASTLFGQYAKNL-ADSFFVIADDFVMKL-AGEKVLEGLHSHNISC--HAErFNGECSHVEINRLIAILKQH 83
Cdd:cd08194 1 PRTIIIGGGALEELGEEAASLgGKRALIVTDKVMVKLgLVDKVTQLLAEAGIAYavFDD-VVSEPTDEMVEEGLALYKEG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 84 GCRGVVGIGGGKTLDTAKAIG-----------YYQK-------LPVVVIPTIASTDAPTSALSVIyTEAGEFEEYLIYPK 145
Cdd:cd08194 80 GCDFIVALGGGSPIDTAKAIAvlatnggpirdYMGPrkvdkpgLPLIAIPTTAGTGSEVTRFTVI-TDTETDVKMLLKGP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 146 N--PDMVVMDTAIIAKAPVRLLVA-GMgDALSTWFEAkacYdaraTSM-AGGQSTAAALSLARLCYDTLL---AEGE--K 216
Cdd:cd08194 159 AllPAVAIVDPELTLSMPPRVTAAtGI-DALTHAIEA---Y----VSRkAQPLTDTLALSAIKLIGRNLRrayADGDdlE 230
|
250
....*....|....
gi 1730616599 217 AR----LAA-QAGV 225
Cdd:cd08194 231 AReammLAAlEAGI 244
|
|
| BDH |
cd08187 |
Butanol dehydrogenase catalyzes the conversion of butyraldehyde to butanol with the cofactor ... |
46-337 |
1.04e-10 |
|
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: 62.45 E-value: 1.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 46 EKVLEGLHSHNISCHaerfngECSHVE-------INRLIAILKQHGCRGVVGIGGGKTLDTAKAIG------------YY 106
Cdd:cd08187 47 DRVVASLKEAGIEVV------EFGGVEpnprletVREGIELAREENVDFILAVGGGSVIDAAKAIAagakydgdvwdfFT 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 107 QK------LPVVVIPTIASTDAPTSALSVI-YTEAGE---FEEYLIYPKnpdMVVMDTAIIAKAPVRLLVAGMGDALS-- 174
Cdd:cd08187 121 GKappekaLPVGTVLTLAATGSEMNGGAVItNEETKEklgFGSPLLRPK---FSILDPELTYTLPKYQTAAGIVDIFShv 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 175 --TWF-------------EA--KAC-------------YDARATSMaggqsTAAALSLARLCydtllaegekarlaaQAG 224
Cdd:cd08187 198 leQYFtgtedaplqdrlaEGllRTViengpkalkdpddYEARANLM-----WAATLALNGLL---------------GAG 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 225 VVTDaleriveantylsgigfessglAAAHAI-HngftILEECHHLYHGEKVA--FGTLAQLVLQNSPM----------- 290
Cdd:cd08187 258 RGGD----------------------WATHAIeH----ELSALYDITHGAGLAivFPAWMRYVLKKKPErfaqfarrvfg 311
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1730616599 291 -----EEIETVL-------NFCHTVGLPVTLAQMGVKEgidEKIQAVAKATCAEGETIH 337
Cdd:cd08187 312 idpggDDEETALegiealeEFFKSIGLPTTLSELGIDE---EDIEEMAEKAVRGGGLGG 367
|
|
| Fe-ADH-like |
cd14862 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
14-345 |
1.50e-10 |
|
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: 61.86 E-value: 1.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 14 GPDASTLFGQYAKNLAdsfFVIADDFVMKLAG-EKVLEGLHSHNISChaERFNG---ECSHVEINRLIAILKQHGCRGVV 89
Cdd:cd14862 12 GEDALSHLEQLSGKRA---LIVTDKVLVKLGLlKKVLKRLLQAGFEV--EVFDEvepEPPLETVLKGAEAMREFEPDLII 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 90 GIGGGKTLDTAKAI--------------------GYYQKLPVVVIPTIASTDAPTSALSVIyTEAGEFEEY-LIYPKN-P 147
Cdd:cd14862 87 ALGGGSVMDAAKAAwvlyerpdldpedispldllGLRKKAKLIAIPTTSGTGSEATWAIVL-TDTEEPRKIaVANPELvP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 148 DMVVMDTAIIAKAPVRlLVAGMG-DALSTWFEAKACydARATSMaggqSTAAALSLARLCYDTLlaegekaRLAAQAGVV 226
Cdd:cd14862 166 DVAILDPEFVLGMPPK-LTAGTGlDALAHAVEAYLS--TWSNDF----SDALALKAIELIFKYL-------PRAYKDGDD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 227 TDALERIVEANTyLSGIGFESSGLAAAHAI-HNGFTILeechHLYHGEKVA----------------FGTLAQLVLQNSP 289
Cdd:cd14862 232 LEAREKMHNAAT-IAGLAFGNSQAGLAHALgHSLGAVF----HVPHGIAVGlflpyviefyakvtdeRYDLLKLLGIEAR 306
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1730616599 290 MEE------IETVLNFCHTVGLPVTLAQMGV-KEGIDEKIQAVAKATCAEGETIHNmPFPVSA 345
Cdd:cd14862 307 DEEealkklVEAIRELYKEVGQPLSIKDLGIsEEEFEEKLDELVEYAMEDSCTITS-PRPPSE 368
|
|
| Fe-ADH-like |
cd08185 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
22-327 |
2.40e-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: 61.36 E-value: 2.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 22 GQYAKNLADSFFVIADDFVMKLAG--EKVLEGLHSHNISchAERFNGecshVEINRLI-------AILKQHGCRGVVGIG 92
Cdd:cd08185 18 GEEALRPGKKALIVTGKGSSKKTGllDRVKKLLEKAGVE--VVVFDK----VEPNPLTttvmegaALAKEEGCDFVIGLG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 93 GGKTLDTAKAI----------------GYYQK------LPVVVIPTIASTDAPTSALSVIY-TEAGE---FEEYLIYPK- 145
Cdd:cd08185 92 GGSSMDAAKAIafmatnpgdiwdyifgGTGKGpppekaLPIIAIPTTAGTGSEVDPWAVITnPETKEkkgIGHPALFPKv 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 146 ---NPD-MVVMdtaiiakaPVRLLVA-GMgDALSTWFEakaCYDA-RATSMaggqSTAAALSLARLCYDTLLAegekarl 219
Cdd:cd08185 172 sivDPElMLTV--------PPRVTAYtGF-DALFHAFE---SYISkNANPF----SDMLALEAIRLVAKYLPR------- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 220 aaqagVVTD-----ALERIVEANTyLSGIGFESSGLAAAHAihngftiLEE-----CHHLYHGE---------------- 273
Cdd:cd08185 229 -----AVKDgsdleAREKMAWAST-LAGIVIANSGTTLPHG-------LEHplsgyHPNIPHGAglaalypayfeftiek 295
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 274 ------KVAFGTLAQLVLQNSPMEEIETVLNFCHTVGLPVTLAQMGVKEgidEKIQAVAK 327
Cdd:cd08185 296 apekfaFVARAEASGLSDAKAAEDFIEALRKLLKDIGLDDLLSDLGVTE---EDIPWLAE 352
|
|
| PRK15454 |
PRK15454 |
ethanolamine utilization ethanol dehydrogenase EutG; |
2-256 |
3.09e-10 |
|
ethanolamine utilization ethanol dehydrogenase EutG;
Pssm-ID: 185351 [Multi-domain] Cd Length: 395 Bit Score: 61.20 E-value: 3.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 2 LKVIQSPAKYLQGPDASTLFGQYAKNLADS-FFVIADDFVMK------LAGEKVLEGLHSHNISCHAerfnGECSHVEIN 74
Cdd:PRK15454 21 VKTFSVPPVTLCGPGAVSSCGQQAQTRGLKhLFVMADSFLHQagmtagLTRSLAVKGIAMTLWPCPV----GEPCITDVC 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 75 RLIAILKQHGCRGVVGIGGGKTLDTAKAIGYY------------------QKLPVVVIPTIASTDAPTSALSVIYTEAGE 136
Cdd:PRK15454 97 AAVAQLRESGCDGVIAFGGGSVLDAAKAVALLvtnpdstlaemsetsvlqPRLPLIAIPTTAGTGSETTNVTVIIDAVSG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 137 FEEYLIYPK-NPDMVVMDTAIIAKAPVRLLVAGMGDALSTWFEAKACYDAR--ATSMAGGQSTAAALSLARlcydtllAE 213
Cdd:PRK15454 177 RKQVLAHASlMPDVAILDAALTEGVPSHVTAMTGIDALTHAIEAYSALNATpfTDSLAIGAIAMIGKSLPK-------AV 249
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1730616599 214 GEKARLAAQagvvtdalERIVEANTyLSGIGFESSGLAAAHAI 256
Cdd:PRK15454 250 GYGHDLAAR--------ESMLLASC-MAGMAFSSAGLGLCHAM 283
|
|
| PDDH |
cd08188 |
1,3-Propanediol (1,3-PD) dehydrogenase; This family includes 1,3-propanediol (1,3-PD) ... |
3-348 |
5.32e-10 |
|
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: 60.22 E-value: 5.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 3 KVIQSPAKYLQGPDASTLFGQYAKNL-ADSFFVIADDFVMKLA-GEKVLEGLHSHNISchAERFNGecshVE-------I 73
Cdd:cd08188 1 FRFYIPPVNLFGPGCLKEIGDELKKLgGKKALIVTDKGLVKLGlVKKVTDVLEEAGIE--YVIFDG----VQpnptvtnV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 74 NRLIAILKQHGCRGVVGIGGGKTLDTAKAIG-----------Y-------YQKLPVVVIPTIASTDAPTSALSVIyTEAG 135
Cdd:cd08188 75 NEGLELFKENGCDFIISVGGGSAHDCAKAIGilatnggeiedYegvdkskKPGLPLIAINTTAGTASEVTRFAVI-TDEE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 136 EFEEYLIYPKN--PDMVVMDTAIIAKAPVRLLVA-GMgDALSTWFEAkacYdarATSMAGGQSTAAALSLARLCYDTL-- 210
Cdd:cd08188 154 RHVKMVIVDWNvtPTIAVNDPELMLGMPPSLTAAtGM-DALTHAIEA---Y---VSTGATPLTDALALEAIRLIAENLpk 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 211 -LAEGE--KARlaaqagvvtdalERIVEAnTYLSGIGFESSGLAAAHAI-H--NGFtileecHHLYHG------------ 272
Cdd:cd08188 227 aVANGKdlEAR------------ENMAYA-QFLAGMAFNNAGLGYVHAMaHqlGGF------YNLPHGvcnaillphvme 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 273 -------EKvaFGTLAQL----VLQNSPMEE----IETVLNFCHTVGLPVTLAQMGVKEgidEKIQAVAKATCAEGETIH 337
Cdd:cd08188 288 fnlpacpER--FADIARAlgenTEGLSDEEAaeaaIEAIRKLSRRVGIPSGLKELGVKE---EDFPLLAENALKDACGPT 362
|
410
....*....|.
gi 1730616599 338 NmPFPVSAQSV 348
Cdd:cd08188 363 N-PRQATKEDV 372
|
|
| Fe-ADH-like |
cd08183 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
14-256 |
1.66e-09 |
|
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contain different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341462 [Multi-domain] Cd Length: 377 Bit Score: 58.67 E-value: 1.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 14 GPDASTLFGQYAKNLADSFFVIAD-DFVMKLAGEKVLEGLHSHNISCHAERFNGECSHVEINRLIAILKQHGCRGVVGIG 92
Cdd:cd08183 7 GRGSLQELGELAAELGKRALLVTGrSSLRSGRLARLLEALEAAGIEVALFSVSGEPTVETVDAAVALAREAGCDVVIAIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 93 GGKTLDTAKAI---------------GYYQ-------KLPVVVIPTIASTDAPTSALSVIYTEAGEFE-----EYLIypk 145
Cdd:cd08183 87 GGSVIDAAKAIaalltnegsvldyleVVGKgrpltepPLPFIAIPTTAGTGSEVTKNAVLSSPEHGVKvslrsPSML--- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 146 nPDMVVMDTAIIAKAPVRLLVA-GMgDALSTWFEAKACYDA----RATSMAGGQstAAALSLARLCYDTLLAEgekARLA 220
Cdd:cd08183 164 -PDVALVDPELTLSLPPEVTAAsGL-DALTQLIEPYVSRKAnpltDALAREGLR--LAARSLRRAYEDGEDLE---ARED 236
|
250 260 270
....*....|....*....|....*....|....*..
gi 1730616599 221 -AQAgvvtdaleriveanTYLSGIGFESSGLAAAHAI 256
Cdd:cd08183 237 mALA--------------SLLGGLALANAGLGAVHGL 259
|
|
| Fe-ADH-like |
cd08189 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
12-258 |
1.83e-09 |
|
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and belongs to the alcohol dehydrogenase-like superfamily. It is distinct from other alcohol dehydrogenases which contain different protein domain. Proteins of this family have not been characterized.
Pssm-ID: 341468 [Multi-domain] Cd Length: 378 Bit Score: 58.63 E-value: 1.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 12 LQGPDASTLFGQYAKNLA-DSFFVIADDFVMKLaG--EKVLEGLHSHNISCHAerFNG-----ECSHVEinRLIAILKQH 83
Cdd:cd08189 9 FEGAGSLLQLPEALKKLGiKRVLIVTDKGLVKL-GllDPLLDALKKAGIEYVV--FDGvvpdpTIDNVE--EGLALYKEN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 84 GCRGVVGIGGGKTLDTAKAIG----------YYQK---------LPVVVIPTIASTDAPTSALSVIyTEAGEFEEYLIYP 144
Cdd:cd08189 84 GCDAIIAIGGGSVIDCAKVIAaraanpkksvRKLKgllkvrkklPPLIAVPTTAGTGSEATIAAVI-TDPETHEKYAIND 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 145 KN--PDMVVMDTAIIAKAPVRLLVA-GMgDALSTWFEAkacYDARATSmagGQSTAAALSLARLCYDTLL---AEGE--K 216
Cdd:cd08189 163 PKliPDAAVLDPELTLGLPPAITAAtGM-DALTHAVEA---YISRSAT---KETDEYALEAVKLIFENLPkayEDGSdlE 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1730616599 217 ARLA-AQAgvvtdaleriveanTYLSGIGFESSGLAAAHAI-HN 258
Cdd:cd08189 236 ARENmLLA--------------SYYAGLAFTRAYVGYVHAIaHQ 265
|
|
| Fe-ADH-like |
cd14861 |
Iron-containing alcohol dehydrogenases-like; This family contains proteins similar to ... |
77-345 |
2.25e-09 |
|
Iron-containing alcohol dehydrogenases-like; This family contains proteins similar to iron-containing alcohol dehydrogenase (Fe-ADH), most of which have not been characterized. Their specific function is unknown. The protein structure represents a dehydroquinate synthase-like fold and belongs to the alcohol dehydrogenase-like superfamily. It is distinct from other alcohol dehydrogenases which contain different protein domains. Alcohol dehydrogenase catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions.
Pssm-ID: 341483 [Multi-domain] Cd Length: 374 Bit Score: 58.29 E-value: 2.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 77 IAILKQHGCRGVVGIGGGKTLDTAKAIG-----------YYQKL-----------PVVVIPTIASTDAPTSALSVIY-TE 133
Cdd:cd14861 75 VAAYREGGCDGIIALGGGSAIDAAKAIAlmathpgplwdYEDGEggpaaitpavpPLIAIPTTAGTGSEVGRAAVITdDD 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 134 AGE----FEEYLIypknPDMVVMDTAIIAKAPVRLLVA-GMgDALSTWFEAkacYdaratsMAGGQ---STAAALSLARL 205
Cdd:cd14861 155 TGRkkiiFSPKLL----PKVAICDPELTLGLPPRLTAAtGM-DALTHCIEA---Y------LSPGFhpmADGIALEGLRL 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 206 CYDTLL-AEGEKARLAAQAGVVTDALEriveantylSGIGFeSSGLAAAHAIHNGFTILeecHHLYHGEKVA-------- 276
Cdd:cd14861 221 ISEWLPrAVADGSDLEARGEMMMAALM---------GAVAF-QKGLGAVHALAHALGAL---YGLHHGLLNAillpyvlr 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 277 ---------FGTLAQLV--LQNSPMEEIETVLNFCHTVGLPVTLAQMGVKEG-IDEKIQAVAKATCAegetiHNMPFPVS 344
Cdd:cd14861 288 fnrpavedkLARLARALglGLGGFDDFIAWVEDLNERLGLPATLSELGVTEDdLDELAELALADPCH-----ATNPRPVT 362
|
.
gi 1730616599 345 A 345
Cdd:cd14861 363 A 363
|
|
| PPD-like |
cd08181 |
1,3-propanediol dehydrogenase-like (PPD); This family contains proteins similar to 1, ... |
46-178 |
6.03e-09 |
|
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: 56.83 E-value: 6.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 46 EKVLEGLHSHNISChaERFNGecshVEINRLI-------AILKQHGCRGVVGIGGGKTLDTAKAI--------------- 103
Cdd:cd08181 44 DDVTEALEENGIEY--FIFDE----VEENPSIetvekgaELARKEGADFVIGIGGGSPLDAAKAIallaankdgdedlfq 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 104 -GYYQK-LPVVVIPTIASTDAPTSALSVI-YTEAG---EFEEYLIYPKnpdMVVMDTAIIAKAPVRLLVAGMGDALSTWF 177
Cdd:cd08181 118 nGKYNPpLPIVAIPTTAGTGSEVTPYSILtDHEKGtkkSFGNPLIFPK---LALLDPKYTLSLPEELTIDTAVDALSHAI 194
|
.
gi 1730616599 178 E 178
Cdd:cd08181 195 E 195
|
|
| Fe-ADH-like |
cd17814 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
14-179 |
1.22e-08 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341489 [Multi-domain] Cd Length: 374 Bit Score: 56.01 E-value: 1.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 14 GPDASTLFGQYAKNL-ADSFFVIADDFVMKlAG--EKVLEGLHSHNIscHAERFNGECSH---VEINRLIAILKQHGCRG 87
Cdd:cd17814 10 GVGARKLAGRYAKNLgARKVLVVTDPGVIK-AGwvDEVLDSLEAEGL--EYVVFSDVTPNprdFEVMEGAELYREEGCDG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 88 VVGIGGGKTLDTAKAIGY----------YQKL--------PVVVIPTIASTDAPTSALSVIyTEAGEFEEYLIYPKN--P 147
Cdd:cd17814 87 IVAVGGGSPIDCAKGIGIvvsngghildYEGVdkvrrplpPLICIPTTAGSSADVSQFAII-TDTERRVKMAIISKTlvP 165
|
170 180 190
....*....|....*....|....*....|..
gi 1730616599 148 DMVVMDTAIIAKAPVRLLVAGMGDALSTWFEA 179
Cdd:cd17814 166 DVSLIDPETLTTMDPELTACTGMDALTHAIEA 197
|
|
| DOIS |
cd08197 |
2-deoxy-scyllo-inosose synthase (DOIS) catalyzes carbocycle formation from ... |
29-281 |
2.27e-08 |
|
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: 55.28 E-value: 2.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 29 ADSFFVIADDFVMKLAGEKVLEGLHSHNISCHAERFNGECSHVEINRLIAILKQ---HGC---RGVVGIGGGKTLDTAka 102
Cdd:cd08197 23 ADRHFLVTDSNVNDLYGDRLLEGLKKAGIPVELLVVPAGESNKTLSTLTELAERliaAGItrrSVIIALGGGVVGNIA-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 103 iGY-----YQKLPVVVIPT--IASTDAPTSALSVIYTEAGefeeyliypKN-------PDMVVMDTAIIAKAPVRLLVAG 168
Cdd:cd08197 101 -GLlagllYRGIRLVHVPTtlLAQSDSVLSLKQAVNGKSG---------KNlvgsyyaPLFVFVDTEFLKTLPPRQIRSG 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 169 MGDALSTWFEAKACYDARATSMAGGQSTAAALSLARLCYDTLLAegeKARLAAQagvvtDALERiveantyLSGIGFEsS 248
Cdd:cd08197 171 LCEAIKNALIQDPEFLDYLEDYLNSDLDYDPEFLEKVIDLSIEA---KLEVLSN-----DPYEK-------KEGLILE-Y 234
|
250 260 270
....*....|....*....|....*....|...
gi 1730616599 249 GLAAAHAIHngftiLEECHHLYHGEKVAFGTLA 281
Cdd:cd08197 235 GHTVGHAIE-----LLSGGELSHGEAVAIGMCV 262
|
|
| HOT |
cd08190 |
Hydroxyacid-oxoacid transhydrogenase (HOT) involved in gamma-hydroxybutyrate metabolism; This ... |
7-329 |
1.03e-07 |
|
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: 53.32 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 7 SPAKYlqGPDASTLFGQYAKNL-ADSFFVIADDFVMKLAG-EKVLEGLHSHNISchAERFNGecSHVE-----INRLIAI 79
Cdd:cd08190 2 SNIRF--GPGATRELGMDLKRLgAKKVLVVTDPGLAKLGLvERVLESLEKAGIE--VVVYDG--VRVEptdesFEEAIEF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 80 LKQHGCRGVVGIGGGKTLDTAKAIGYYQK-----------------------LPVVVIPTIASTDAPTSALSVI-YTEA- 134
Cdd:cd08190 76 AKEGDFDAFVAVGGGSVIDTAKAANLYAThpgdfldyvnapigkgkpvpgplKPLIAIPTTAGTGSETTGVAIFdLEELk 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 135 ---GEFEEYLiypkNPDMVVMDTAIIAKAPVRLLVA-GMgDALSTWFEAkacYDARAtsmaggqstaaalslarlcYDTL 210
Cdd:cd08190 156 vktGISSRYL----RPTLAIVDPLLTLTLPPRVTASsGF-DVLCHALES---YTARP-------------------YNAR 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 211 LA-EGEKARLAAQ-AGVVTD-----ALERI-------------VEANTYLS------GIGFESSGLAAAHAI-------- 256
Cdd:cd08190 209 PRpANPDERPAYQgSNPISDvwaekAIELIgkylrravndgddLEARSNMLlastlaGIGFGNAGVHLPHAMaypiaglv 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 257 ----HNGFTILEecHHLYHGEKVA-----------------FGTLAQLVLQN-SPMEEIE-------TVLNFCHTVGLPV 307
Cdd:cd08190 289 kdyrPPGYPVDH--PHVPHGLSVAltapavfrftapacperHLEAAELLGADtSGASDRDagevladALIKLMRDIGIPN 366
|
410 420
....*....|....*....|..
gi 1730616599 308 TLAQMGVKEgidEKIQAVAKAT 329
Cdd:cd08190 367 GLSALGYSE---DDIPALVEGT 385
|
|
| LPO |
cd08176 |
Lactadehyde:propanediol oxidoreductase (LPO) catalyzes the interconversion between ... |
77-331 |
2.40e-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: 2.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 77 IAILKQHGCRGVVGIGGGKTLDTAKAIG-----------YY--------QKLPVVVIPTIASTDAPTSALSVIY-TEAGE 136
Cdd:cd08176 78 VAAYKESGADGIIAVGGGSSIDTAKAIGiivanpgadvrSLegvaptknPAVPIIAVPTTAGTGSEVTINYVITdTEKKR 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 137 ----FEEYLIypknPDMVVMDTAIIAKAPVRLLVA-GMgDALSTWFEAkacYdarATSMAGGQSTAAALSLARLCYDTLl 211
Cdd:cd08176 158 kfvcVDPHDI----PTVAIVDPDLMSSMPKGLTAAtGM-DALTHAIEG---Y---ITKGAWELSDMLALKAIELIAKNL- 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 212 aegekaRLAAQAGVVTDALERIVEAnTYLSGIGFESSGLAAAHAIHNGFTILEECHH----------------LYHGEK- 274
Cdd:cd08176 226 ------RKAVANPNNVEARENMALA-QYIAGMAFSNVGLGIVHSMAHPLSAFYDTPHgvanaillpyvmefnaPATGEKy 298
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1730616599 275 ----VAFGtlaqlVLQNSPMEE------IETVLNFCHTVGLPVTLAQMGVKEgidEKIQAVAKATCA 331
Cdd:cd08176 299 rdiaRAMG-----VDTTGMSDEeaaeaaVDAVKKLSKDVGIPQKLSELGVKE---EDIEALAEDALN 357
|
|
| YqdH |
COG1979 |
Alcohol dehydrogenase YqhD, Fe-dependent ADH family [Energy production and conversion]; |
46-335 |
8.70e-07 |
|
Alcohol dehydrogenase YqhD, Fe-dependent ADH family [Energy production and conversion];
Pssm-ID: 441582 [Multi-domain] Cd Length: 387 Bit Score: 50.46 E-value: 8.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 46 EKVLEGLHSHNISCHaerfngECSHVEIN-------RLIAILKQHGCRGVVGIGGGKTLDTAKAIG-----------YYQ 107
Cdd:COG1979 49 DQVKAALKEAGIEVV------EFGGVEPNprletvrKGVELCKEEGIDFILAVGGGSVIDGAKAIAagakydgdpwdILT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 108 K-------LPVVVIPTIASTDAPTSALSVIYTEAGE----FEEYLIYPKnpdMVVMDTAIIAKAPVRLLVAGMGDALSTW 176
Cdd:COG1979 123 GkapvekaLPLGTVLTLPATGSEMNSGSVITNEETKeklgFGSPLVFPK---FSILDPELTYTLPKRQTANGIVDIFSHV 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 177 FEA-------------------KAC-------------YDARATSMAggqstAAALSLARLCydtllaegekarlaaQAG 224
Cdd:COG1979 200 MEQyftypvdaplqdrfaegllRTLieegpkalkdpedYDARANLMW-----AATLALNGLI---------------GAG 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 225 VVTDaleriveantylsgigfessglAAAHAIHNGFTILeecHHLYHG----------------EKVA-FGTLAQLVLQN 287
Cdd:COG1979 260 VPQD----------------------WATHMIEHELSAL---YDIDHGaglaivlpawmryvleEKPEkFAQYAERVWGI 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1730616599 288 SPMEEIETVL-------NFCHTVGLPVTLAQMGVKEgidEKIQAVAKATCAEGET 335
Cdd:COG1979 315 TEGDDEERALegieateEFFESLGLPTRLSEYGIDE---EDIEEMAEKATAHGMT 366
|
|
| Fe-ADH_KdnB-like |
cd08184 |
Iron-containing alcohol dehydrogenase similar to Shewanella oneidensis KdnB required for Kdo8N ... |
67-268 |
1.89e-06 |
|
Iron-containing alcohol dehydrogenase similar to Shewanella oneidensis KdnB required for Kdo8N biosynthesis; This family contains iron-containing alcohol dehydrogenase-like proteins, many of which have not been characterized. Their specific function is unknown. The protein structure represents a dehydroquinate synthase-like fold and belongs to the iron-containing alcohol dehydrogenase-like superfamily. It is distinct from other alcohol dehydrogenases which contain different protein domains. Alcohol dehydrogenase catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron or zinc ions. This family also includes Shewanella oneidensis KdnB which is required for biosynthesis of 8-Amino-3,8-dideoxy-D-manno-octulosonic acid (Kdo8N), a unique amino sugar that has thus far only been observed on the lipopolysaccharides of marine bacteria belonging to the genus Shewanella, and thought to be important for the integrity of the bacterial cell outer membrane. KdnB requires NAD(P) and zinc ion for activity.
Pssm-ID: 341463 [Multi-domain] Cd Length: 348 Bit Score: 49.19 E-value: 1.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 67 ECSHVEINRLIAILKQHGCR---GVVGIGGGKTLDTAKAIG----------YYQ-----KLP---VVVIPTIASTDA--- 122
Cdd:cd08184 62 EPKTDQIDALRAQIRAENDKlpaAVVGIGGGSTMDIAKAVSnmltnpgsaaDYQgwdlvKNPgiyKIGVPTLSGTGAeas 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 123 PTSALSVIYTEAGEFEEYLIYpknpDMVVMDTAIIAKAPVrllvagmgdalSTWF-EAKACYDARATSMAGGQSTAAALS 201
Cdd:cd08184 142 RTAVLTGPEKKLGINSDYTVF----DQVILDPELIATVPR-----------DQYFyTGMDCYIHCVESLNGTYRNAFGDA 206
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1730616599 202 LAR----LCYDTLLAEGEKArlaaqagvvTDALERIVEAnTYLSGIGFESSGLAAAHAIHNGFTILEECHH 268
Cdd:cd08184 207 YAEkaleLCRDVFLSDDMMS---------PENREKLMVA-SYLGGSSIANSQVGVCHALSYGLSVVLGTHH 267
|
|
| HVD |
cd08193 |
5-hydroxyvalerate dehydrogenase (HVD) catalyzes the oxidation of 5-hydroxyvalerate to ... |
77-136 |
2.33e-06 |
|
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: 49.05 E-value: 2.33e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1730616599 77 IAILKQHGCRGVVGIGGGKTLDTAKAIGYY------------------QKLPVVVIPTIASTDAPTSALSVIYTEAGE 136
Cdd:cd08193 76 VEQAREAGADGVIGFGGGSSMDVAKLVALLagsdqplddiygvgkatgPRLPLILVPTTAGTGSEVTPISIVTTGETE 153
|
|
| NADPH_BDH |
cd08179 |
NADPH-dependent butanol dehydrogenase involved in the butanol and ethanol formation pathway in ... |
88-316 |
3.48e-05 |
|
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: 45.26 E-value: 3.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 88 VVGIGGGKTLDTAKAIG-YY--------------------QKLPVVVIPTIASTDAPTSALSVIyTEAGEFEEYLIYPKN 146
Cdd:cd08179 85 IIAIGGGSVIDAAKAMWvFYeypeltfedalvpfplpelrKKARFIAIPSTSGTGSEVTRASVI-TDTEKGIKYPLASFE 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 147 --PDMVVMDTAIIAKAPvRLLVA--GMgDALSTWFEAKACydARATSMaggqSTAAALSLARLCYDTLLaegekarLAAQ 222
Cdd:cd08179 164 itPDVAILDPELTMTMP-PHVTAntGM-DALTHAIEAYVS--TLANDF----TDALALGAILDIFENLP-------KSYN 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 223 AGVVTDALERIVEANTyLSGIGFESSGLAAAHAI-HNGFTILeechHLYHGEKVAFgtLAQLVLQ-NSPMEE-------- 292
Cdd:cd08179 229 GGKDLEAREKMHNASC-LAGMAFSNSGLGIVHSMaHKGGAFF----GIPHGLANAI--LLPYVIEfNSKDPEararyaal 301
|
250 260 270
....*....|....*....|....*....|....*..
gi 1730616599 293 -------------IETVLNFCHTVGLPVTLAQMGVKE 316
Cdd:cd08179 302 ligltdeelvedlIEAIEELNKKLGIPLSFKEAGIDE 338
|
|
| DHQ-like |
cd08169 |
Dehydroquinate synthase-like which includes dehydroquinate synthase, 2-deoxy-scyllo-inosose ... |
27-307 |
4.19e-05 |
|
Dehydroquinate synthase-like which includes dehydroquinate synthase, 2-deoxy-scyllo-inosose synthase, and 2-epi-5-epi-valiolone synthase; This group contains dehydroquinate synthase, 2-deoxy-scyllo-inosose synthase, and 2-epi-5-epi-valiolone synthase. These proteins exhibit the dehydroquinate synthase structural fold. 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. 2-deoxy-scyllo-inosose synthase (DOIS) catalyzes carbocycle formation from D-glucose-6-phosphate to 2-deoxy-scyllo-inosose through a multi-step reaction in the biosynthesis of aminoglycoside antibiotics. 2-deoxystreptamine (DOS)-containing aminoglycoside antibiotics includes neomycin, kanamycin, gentamicin, and ribostamycin. 2-epi-5-epi-valiolone synthases catalyze the cyclization of sedoheptulose 7-phosphate to 2-epi-5-epi-valiolone in the biosynthesis of C(7)N-aminocyclitol-containing products. The cyclization product, 2-epi-5-epi-valiolone ((2S,3S,4S,5R)-5-(hydroxymethyl)cyclohexanon-2,3,4,5-tetrol), is a precursor of the valienamine moiety. The valienamine unit is responsible for their biological activities as various glycosidic hydrolases inhibitors. Two important microbial secondary metabolites, validamycin and acarbose, are used in agricultural and biomedical applications.
Pssm-ID: 341448 [Multi-domain] Cd Length: 328 Bit Score: 45.09 E-value: 4.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 27 NLADSFFVIADDFVMKLAGEKVLEGLHSHnISCHAERFNGECSHVEINRLIAILKQ----HGCR--GVVGIGGGKTLDTA 100
Cdd:cd08169 21 DAFDQCLIIVDSGVPDLIVNYLAEYFGYY-LEVHVFIIQGGEAYKTFQTVVEELERaaalHLNRhsAVVAVGGGATGDVV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 101 --KAIGYYQKLPVVVIPT--IASTDAPTSALSVIYTEAGEFEEYLIYPknPDMVVMDTAIIAKAPVRLLVAGMGDAlstw 176
Cdd:cd08169 100 gfAAATYFRGIAFIRVPTtlLAQSDSSVGIKVGINTRGGKNLLGAFYP--PRAVFADFSFLKTLPFRQVRAGMAEL---- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 177 FEAKACYDARATSMAGGQSTAAALSLARlCYDTLLAEGEKARLaaqagvvtdaleRIVEANTYLSGIG-FESSGLAAAHA 255
Cdd:cd08169 174 VKMALIADNDFFEFLEDKANSATVYSPE-QLEKLINKCISLKL------------DVVVADEDEQGKRrGLNYGHTFGHA 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1730616599 256 IHngftiLEECHHLYHGEKVAFGTLAQLVLQNS----PMEEIETVLNFCHTVGLPV 307
Cdd:cd08169 241 LE-----LASGYKIPHGEAVAVGMAYAAKIANRlgllPEHDVSRIIWLLNKLGLPL 291
|
|
| MAR |
cd08177 |
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic ... |
59-116 |
1.82e-04 |
|
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: 42.88 E-value: 1.82e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1730616599 59 CHAERFNGECSHVEI---NRLIAILKQHGCRGVVGIGGGKTLDTAKAIGYYQKLPVVVIPT 116
Cdd:cd08177 48 RVAGVFDGAVMHVPVevaERALAAAREAGADGLVAIGGGSAIGLAKAIALRTGLPIVAVPT 108
|
|
| 4HBD_NAD |
cd14860 |
4-hydroxybutyrate dehydrogenase, also called gamma-hydroxybutyrate dehydrogenase, catalyzes ... |
33-256 |
2.43e-04 |
|
4-hydroxybutyrate dehydrogenase, also called gamma-hydroxybutyrate dehydrogenase, catalyzes the reduction of succinic simialdehyde to 4-hydroxybutyrate in the succinic degradation pathway; 4-hydroxybutyrate dehydrogenase (4HBD) is an iron-containing (type III) NAD-dependent alcohol dehydrogenase. It plays a role in the succinate metabolism biochemical pathway. It catalyzes the reduction of succinic simialdehide to 4-hydroxybutyrate in the succinate degradation pathway This succinate degradation pathway is present in some bacteria which can use succinate as sole carbon source.
Pssm-ID: 341482 Cd Length: 371 Bit Score: 42.59 E-value: 2.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 33 FVIADDFVMklagEKVLEGLhshNISCHA---ERFN-GECSHVEINRLIAILKQHGCRGVVGIGGGKTLDTAKAIG---- 104
Cdd:cd14860 30 LVLTNEYIY----EPYFEPL---NLDCAVifqEKYGtGEPSDEMVEAIYKDIKKYGYKRVIAIGGGTVIDIAKLLAlkgi 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 105 ------YYQKLPV------VVIPTIASTDAPTSALSVIY-----TEAGEFEEYLIypknPDMVVMDTAIIAKAPVRLLVA 167
Cdd:cd14860 103 spvldlFDGKIPLikekelIIVPTTCGTGSEVTNISIVEltslgTKKGLAVDELY----ADKAVLIPELLKGLPYKVFAT 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 168 GMGDALSTWFEakACYDARATSMAGGQSTAA-ALSLARlcYDTLLAEGEKARLaaqagvvtDALERIVEANTYlSGIGFE 246
Cdd:cd14860 179 SSIDALIHAIE--SYLSPKATPYTEMFSYKAiEMILEG--YQEIAEKGEEARF--------PLLGDFLIASNY-AGIAFG 245
|
250
....*....|
gi 1730616599 247 SSGLAAAHAI 256
Cdd:cd14860 246 NAGCAAVHAL 255
|
|
| PFK |
pfam00365 |
Phosphofructokinase; |
75-134 |
2.64e-04 |
|
Phosphofructokinase;
Pssm-ID: 459783 [Multi-domain] Cd Length: 271 Bit Score: 42.33 E-value: 2.64e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1730616599 75 RLIAILKQHGCRGVVGIGGGKTLDTAKAIGYYQKLPVVVIP-TI----ASTDApT----SALSVIyTEA 134
Cdd:pfam00365 82 KIAENLKKLGIDALVVIGGDGSLTGANKLSEERGIPVVGIPkTIdndiPGTDY-TigfdTALNTI-VEA 148
|
|
| PRK09860 |
PRK09860 |
putative alcohol dehydrogenase; Provisional |
77-256 |
5.13e-04 |
|
putative alcohol dehydrogenase; Provisional
Pssm-ID: 182118 [Multi-domain] Cd Length: 383 Bit Score: 41.86 E-value: 5.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 77 IAILKQHGCRGVVGIGGGKTLDTAKAIGY----------YQ--------KLPVVVIPTIASTDAPTSALSVIYTEAGEFE 138
Cdd:PRK09860 81 LKLLKENNCDSVISLGGGSPHDCAKGIALvaanggdirdYEgvdrsakpQLPMIAINTTAGTASEMTRFCIITDEARHIK 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 139 EYLIYPK-NPDMVVMDTAIIAKAPVRLLVAGMGDALSTWFEAkacydarATSMAGGQST-AAALSLARLCYDTLLaegek 216
Cdd:PRK09860 161 MAIVDKHvTPLLSVNDSSLMIGMPKSLTAATGMDALTHAIEA-------YVSIAATPITdACALKAVTMIAENLP----- 228
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1730616599 217 arLAAQAGVVTDALERIVEANtYLSGIGFESSGLAAAHAI 256
Cdd:PRK09860 229 --LAVEDGSNAKAREAMAYAQ-FLAGMAFNNASLGYVHAM 265
|
|
| PDD |
cd08180 |
1,3-propanediol dehydrogenase (PPD) catalyzes the reduction of 3-hydroxypropionaldehyde (3-HPA) ... |
77-348 |
6.91e-04 |
|
1,3-propanediol dehydrogenase (PPD) catalyzes the reduction of 3-hydroxypropionaldehyde (3-HPA) to 1,3-propanediol in glycerol metabolism; 1,3-propanediol dehydrogenase (PPD) plays a role in glycerol metabolism of some bacteria in anaerobic conditions. In this degradation pathway, glycerol is converted in a two-step process to 1,3-propanediol (1,3-PD) which is then excreted into the extracellular medium. The first reaction involves the transformation of glycerol into 3-hydroxypropionaldehyde (3-HPA) by a coenzyme B-12-dependent dehydratase. The second reaction involves the dismutation of the 3-hydroxypropionaldehyde (3-HPA) to 1,3-propanediol by the NADH-linked 1,3-propanediol dehydrogenase (PPD). The enzyme requires iron ion for its function. Because many genes in this pathway are present in the propanediol utilization (pdu) operon, they are also named pdu genes. PPD is a member of the iron-containing alcohol dehydrogenase superfamily. The PPD structure has a dehydroquinate synthase-like fold.
Pssm-ID: 341459 [Multi-domain] Cd Length: 333 Bit Score: 41.32 E-value: 6.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 77 IAILKQHGCRGVVGIGGGKTLDTAKAIGYY--------QKLPVVVIPTIASTDAPTSALSVIY-TEAGE----FEEYLIy 143
Cdd:cd08180 71 LAKILEFKPDTIIALGGGSAIDAAKAIIYFalkqkgniKKPLFIAIPTTSGTGSEVTSFAVITdPEKGIkyplVDDSML- 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 144 pknPDMVVMDTAIIAKAPVRLLV-AGMgDALSTWFEAkacYDA-RATSMaggqSTAAALSLARLCYDTLLAegekarlAA 221
Cdd:cd08180 150 ---PDIAILDPELVKSVPPKVTAdTGM-DVLTHALEA---YVStNANDF----TDALAEKAIKLVFENLPR-------AY 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730616599 222 QAGVVTDALERIVEANTyLSGIGFESSGL----AAAHAIHNGFtileechHLYHGekvafgtLAQLVLQNSPMEE-IETV 296
Cdd:cd08180 212 RDGDDLEAREKMHNASC-MAGIAFNNAGLginhSLAHALGGRF-------HIPHG-------RANAILLPYVIEFlIAAI 276
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1730616599 297 LNFCHTVGLPVTLAQMGV-KEGIDEKIQAVAKATCAEGETIHNmPFPVSAQSV 348
Cdd:cd08180 277 RRLNKKLGIPSTLKELGIdEEEFEKAIDEMAEAALADRCTATN-PRKPTAEDL 328
|
|
| |
