|
Name |
Accession |
Description |
Interval |
E-value |
| GlyDH |
cd08170 |
Glycerol dehydrogenases (GlyDH) catalyzes oxidation of glycerol to dihydroxyacetone in ... |
10-350 |
2.61e-174 |
|
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: 488.07 E-value: 2.61e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 10 PGRYVQGPGELSRQGRYLSWLGCAAYVLFDQGTEDRLCRQIVDGFLDDDLsEPFFKIYNGPCTEEAVAEMAKEAQAEYCD 89
Cdd:cd08170 1 PSRYVQGPGALDRLGEYLAPLGKKALVIADPFVLDLVGERLEESLEKAGL-EVVFEVFGGECSREEIERLAAIARANGAD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 90 MVVGIGGGKMLDIAKAVAFYAELPLCVCPTAASMDGPCSAISVLYHEDGSFDRYLMLEKNPDLVVVDTNVVAAAPLRMTV 169
Cdd:cd08170 80 VVIGIGGGKTIDTAKAVADYLGLPVVIVPTIASTDAPCSALSVIYTEDGEFDEYLFLPRNPDLVLVDTEIIAKAPVRFLV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 170 AGMGDALATYFEARSCAAAHGANEHGGAPGHLALVAARACYDTLMECGVAAKRDLKKGRTSPAVERLIECNILLSGVGFE 249
Cdd:cd08170 160 AGMGDALATYFEARACARSGAPNMAGGRPTLAALALAELCYDTLLEYGVAAKAAVEAGVVTPALEAVIEANTLLSGLGFE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 250 SGGLALAHAIANGLTILPEC-KAMHGEAVAFGLVVQLRLERAP--ELDQVLEFCQRVGLPTTLEELGLDEITDADLLSVA 326
Cdd:cd08170 240 SGGLAAAHAIHNGLTALPEThHLLHGEKVAFGTLVQLVLEGRPdeEIEEVIRFCRSVGLPVTLADLGLEDVTDEELRKVA 319
|
330 340
....*....|....*....|....
gi 1469304371 327 DATFKNERNMANEQTKVTRQKLVQ 350
Cdd:cd08170 320 EAACAPGETIHNMPFPVTPEDVVD 343
|
|
| gldA |
PRK09423 |
glycerol dehydrogenase; Provisional |
6-350 |
1.44e-149 |
|
glycerol dehydrogenase; Provisional
Pssm-ID: 181843 Cd Length: 366 Bit Score: 425.77 E-value: 1.44e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 6 VYGGPGRYVQGPGELSRQGRYLSWLGCAAYVLFDQGTEDRLCRQIVDGFLDDDLsEPFFKIYNGPCTEEAVAEMAKEAQA 85
Cdd:PRK09423 4 IFISPSKYVQGKGALARLGEYLKPLGKRALVIADEFVLGIVGDRVEASLKEAGL-TVVFEVFNGECSDNEIDRLVAIAEE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 86 EYCDMVVGIGGGKMLDIAKAVAFYAELPLCVCPTAASMDGPCSAISVLYHEDGSFDRYLMLEKNPDLVVVDTNVVAAAPL 165
Cdd:PRK09423 83 NGCDVVIGIGGGKTLDTAKAVADYLGVPVVIVPTIASTDAPTSALSVIYTEEGEFERYLFLPKNPDLVLVDTAIIAKAPA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 166 RMTVAGMGDALATYFEARSCAAAHGANEHGGAPGHLALVAARACYDTLMECGVAAKRDLKKGRTSPAVERLIECNILLSG 245
Cdd:PRK09423 163 RFLAAGIGDALATWFEARACSRSGGTTMAGGKPTLAALALAELCYETLLEDGLKAKLAVEAKVVTPALENVIEANTLLSG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 246 VGFESGGLALAHAIANGLTILPEC-KAMHGEAVAFGLVVQLRLERAP--ELDQVLEFCQRVGLPTTLEELGLDEITDADL 322
Cdd:PRK09423 243 LGFESGGLAAAHAIHNGLTALEDThHLTHGEKVAFGTLTQLVLENRPkeEIEEVIDFCHAVGLPTTLADLGLKEDSDEEL 322
|
330 340
....*....|....*....|....*...
gi 1469304371 323 LSVADATFKNERNMANEQTKVTRQKLVQ 350
Cdd:PRK09423 323 RKVAEAACAEGETIHNMPFKVTPEDVAA 350
|
|
| GldA |
COG0371 |
Glycerol dehydrogenase or related enzyme, iron-containing ADH family [Energy production and ... |
6-352 |
2.33e-141 |
|
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: 404.55 E-value: 2.33e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 6 VYGGPGRYVQGPGELSRQGRYLSWLGCAAYVLFDQGTEDRLCRQIVDGFLDDDLsEPFFKIYNGPCTEEAVAEMAKEAQA 85
Cdd:COG0371 2 VIILPRRYVQGEGALDELGEYLADLGKRALIITGPTALKAAGDRLEESLEDAGI-EVEVEVFGGECSEEEIERLAEEAKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 86 EYCDMVVGIGGGKMLDIAKAVAFYAELPLCVCPTAASMDGPCSAISVLYHEDGSFDRYLMLEKNPDLVVVDTNVVAAAPL 165
Cdd:COG0371 81 QGADVIIGVGGGKALDTAKAVAYRLGLPVVSVPTIASTDAPASPLSVIYTEDGAFDGYSFLAKNPDLVLVDTDIIAKAPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 166 RMTVAGMGDALATYFEARSCAAAHgANEHGGAPGHLALVAARACYDTLMECGVAAKRDLKKGRTSPAVERLIECNILLSG 245
Cdd:COG0371 161 RLLAAGIGDALAKWYEARDWSLAH-RDLAGEYYTEAAVALARLCAETLLEYGEAAIKAVEAGVVTPALERVVEANLLLSG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 246 VGF----ESGGLALAHAIANGLTILPEC-KAMHGEAVAFGLVVQLRLERAP-ELDQVLEFCQRVGLPTTLEELGLDEITD 319
Cdd:COG0371 240 LAMgigsSRPGSGAAHAIHNGLTALPEThHALHGEKVAFGTLVQLVLEGRPeEIEELLDFLRSVGLPTTLADLGLDDETE 319
|
330 340 350
....*....|....*....|....*....|...
gi 1469304371 320 ADLLSVADATFKNERNMANEQTKVTRQKLVQLM 352
Cdd:COG0371 320 EELLTVAEAARPERYTILNLPFEVTPEAVEAAI 352
|
|
| GlyDH-like |
cd08550 |
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins. ... |
10-350 |
6.57e-100 |
|
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: 299.07 E-value: 6.57e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 10 PGRYVQGPGELSRQGRYLSWLGCAAYVLfdqGTEDRLcrQIVDGFLDDDLSE----PFFKIYNGPCTEEAVAEMAKEAQA 85
Cdd:cd08550 1 PGRYIQEPGILAKAGEYIAPLGKKALII---GGKTAL--EAVGEKLEKSLEEagidYEVEVFGGECTEENIERLAEKAKE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 86 EYCDMVVGIGGGKMLDIAKAVAFYAELPLCVCPTAASMDGPCSAISVLYHEDGSFDRYLMLEKNPDLVVVDTNVVAAAPL 165
Cdd:cd08550 76 EGADVIIGIGGGKVLDTAKAVADRLGLPVVTVPTIAATCAAWSALSVLYDEEGEFLGYSLLKRSPDLVLVDTDIIAAAPV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 166 RMTVAGMGDALATYFEARSCAaahgANEHGGAPGHLALVAARACYDTLMECGVAAKRDLKKGRTSPAVERLIECNILLSG 245
Cdd:cd08550 156 RYLAAGIGDTLAKWYEARPSS----RGGPDDLALQAAVQLAKLAYDLLLEYGVQAVEDVRQGKVTPALEDVVDAIILLAG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 246 VGFESGG----LALAHAIANGLTILPEC-KAMHGEAVAFGLVVQLRLERAP--ELDQVLEFCQRVGLPTTLEELGLdEIT 318
Cdd:cd08550 232 LVGSLGGggcrTAAAHAIHNGLTKLPEThGTLHGEKVAFGLLVQLALEGRSeeEIEELIEFLRRLGLPVTLEDLGL-ELT 310
|
330 340 350
....*....|....*....|....*....|..
gi 1469304371 319 DADLLSVADATFKNERNMANEQTKVTRQKLVQ 350
Cdd:cd08550 311 EEELRKIAEYACDPPDMAHMLPFPVTPEMLAE 342
|
|
| GlyDH-like |
cd08172 |
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins ... |
54-354 |
4.59e-80 |
|
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: 248.20 E-value: 4.59e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 54 FLDDDLSEPF-FKIYNGPCTEEAVAEMAKEAQAEYCDMVVGIGGGKMLDIAKAVAFYAELPLCVCPTAASMDGPCSAISV 132
Cdd:cd08172 41 YLPKLFEIEYpVLRYDGECSYEEIDRLAEEAKEHQADVIIGIGGGKVLDTAKAVADKLNIPLILIPTLASNCAAWTPLSV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 133 LYHEDGSFDRYLMLEKNPDLVVVDTNVVAAAPLRMTVAGMGDALATYFEARSCAAAHganEHGGAPGHLALVAARACYDT 212
Cdd:cd08172 121 IYDEDGEFIGYDYFPRSAYLVLVDPRLLLDSPKDYFVAGIGDTLAKWYEADAILRQL---EELPAFLQLARQAAKLCRDI 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 213 LMECGVAAKRDLKKGRTSPAVERLIECNILLSGV--GF--ESGGLALAHAIANGLTILPECKA-MHGEAVAFGLVVQLRL 287
Cdd:cd08172 198 LLKDSEQALADLEAGKLTPAFIKVVETIIALAGMvgGFgdEYGRSAGAHAIHNGLTKLPETHHfLHGEKVAYGILVQLAL 277
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1469304371 288 E-RAPELDQVLEFCQRVGLPTTLEELGLDEITDADLLSVADATFKNERNMANEQTKVTRQKLVQLMCE 354
Cdd:cd08172 278 EgKWDEIKKLLPFYRRLGLPTSLADLGLTDDTEEALQKIAAFAASPEESIHLLPPDVTAEEVLQAIEK 345
|
|
| GlyDH-like |
cd08171 |
Glycerol dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins ... |
67-355 |
2.21e-62 |
|
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: 202.75 E-value: 2.21e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 67 YNGPCTEEAVAEMAKEAQAEYCDMVVGIGGGKMLDIAKAVAFYAELPLCVCPTAASMDGPCSAISVLYHEDGSFDRYLML 146
Cdd:cd08171 58 YGGEATYENVEKLKANPEVQEADMIFAVGGGKAIDTVKVLADRLNKPVFTFPTIASNCAAVTAVSVMYNPDGSFKEYYFL 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 147 EKNPDLVVVDTNVVAAAPLRMTVAGMGDALATYFEARSCAaahganeHGGAPGH---LALVAARACYDTLMECGVAAKRD 223
Cdd:cd08171 138 KRPPVHTFIDTEIIAEAPEKYLWAGIGDTLAKYYEVEFSA-------RGDELDHtnaLGVAISKMCSEPLLKYGVQALED 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 224 LKKGRTSPAVERLIeCNILLSgVGFESGGL------ALAHAIANGLTILPEC--KAMHGEAVAFGLVVQLRLERA-PELD 294
Cdd:cd08171 211 CRANKVSDALEQVV-LDIIVT-TGLVSNLVepdynsSLAHALYYGLTTLPQIeeEHLHGEVVSYGVLVLLTVDGQfEELE 288
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1469304371 295 QVLEFCQRVGLPTTLEELGldeITDADLLSVADATFKNERnMANEQTKVTRQKLVQLMCEA 355
Cdd:cd08171 289 KVYAFNKSIGLPTCLADLG---LTVEDLEKVLDKALKTKD-LRHSPYPITKEMFEEAIKDL 345
|
|
| Fe-ADH |
pfam00465 |
Iron-containing alcohol dehydrogenase; |
10-348 |
1.78e-53 |
|
Iron-containing alcohol dehydrogenase;
Pssm-ID: 425696 [Multi-domain] Cd Length: 362 Bit Score: 180.11 E-value: 1.78e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 10 PGRYVQGPGELSRQGRYLSWLGCAAYVLFDQGTEDR-LCRQIVDGFLDDDLSepfFKIYNGP---CTEEAVAEMAKEAQA 85
Cdd:pfam00465 1 PTRIVFGAGALAELGEELKRLGARALIVTDPGSLKSgLLDKVLASLEEAGIE---VVVFDGVepePTLEEVDEAAALARE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 86 EYCDMVVGIGGGKMLDIAKAVAFYAE------------------LPLCVCPTAASMDGPCSAISVLYHEDGSFDRYLM-L 146
Cdd:pfam00465 78 AGADVIIAVGGGSVIDTAKAIALLLTnpgdvwdylggkpltkpaLPLIAIPTTAGTGSEVTPLAVITDTETGEKLGIFsP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 147 EKNPDLVVVDTNVVAAAPLRMTVAGMGDALATYFEARSCAAAHganehggapgHLALVAARACYDTLMECGVAAKRDlkk 226
Cdd:pfam00465 158 KLLPDLAILDPELTLTLPPRLTAATGMDALAHAVEAYVSKGAN----------PLTDALALEAIRLIAENLPRAVAD--- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 227 GRTSPAVERLIECNiLLSGVGFESGGLALAHAIANGLTilPECKAMHGEAVAFGL--VVQLRLERAPE------------ 292
Cdd:pfam00465 225 GEDLEARENMLLAS-TLAGLAFSNAGLGAAHALAHALG--GRYGIPHGLANAILLpyVLRFNAPAAPEklaqlaralged 301
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1469304371 293 ---------LDQVLEFCQRVGLPTTLEELGLDEitdADLLSVADATFKNeRNMANEQTKVTRQKL 348
Cdd:pfam00465 302 sdeeaaeeaIEALRELLRELGLPTTLSELGVTE---EDLDALAEAALRD-RSLANNPRPLTAEDI 362
|
|
| DHQ_Fe-ADH |
cd07766 |
Dehydroquinate synthase-like (DHQ-like) and iron-containing alcohol dehydrogenases (Fe-ADH); ... |
10-328 |
1.35e-41 |
|
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: 146.35 E-value: 1.35e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 10 PGRYVQGPGELSRQGRYLSWLGCAAYVLFDQGTEDRLCRQIVDgFLDDDLSEPFFKIYNGPCTEEAVAEMAKEAQAEYCD 89
Cdd:cd07766 1 PTRIVFGEGAIAKLGEIKRRGFDRALVVSDEGVVKGVGEKVAD-SLKKGLAVAIFDFVGENPTFEEVKNAVERARAAEAD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 90 MVVGIGGGKMLDIAKAVAFYAE--LPLCVCPTAASMDGPCSAISVLYHEDGSFdRYLMLEKNPDLVVVDTNVVAAAPLRM 167
Cdd:cd07766 80 AVIAVGGGSTLDTAKAVAALLNrgIPFIIVPTTASTDSEVSPKSVITDKGGKN-KQVGPHYNPDVVFVDTDITKGLPPRQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 168 TVAGMGDALATYFEarscaaahganehggapghlalvaaracydtlmecgvaakrdlkkgrtspaVERLIECNILLSGVG 247
Cdd:cd07766 159 VASGGVDALAHAVE---------------------------------------------------LEKVVEAATLAGMGL 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 248 FESGGLALAHAIANGLTILPecKAMHGEAVAFGLVVQLRLERAP------ELDQVLEFCQRVGLPTTLEELGldeITDAD 321
Cdd:cd07766 188 FESPGLGLAHAIGHALTAFE--GIPHGEAVAVGLPYVLKVANDMnpepeaAIEAVFKFLEDLGLPTHLADLG---VSKED 262
|
....*..
gi 1469304371 322 LLSVADA 328
Cdd:cd07766 263 IPKLAEK 269
|
|
| PRK10586 |
PRK10586 |
putative oxidoreductase; Provisional |
67-331 |
4.61e-33 |
|
putative oxidoreductase; Provisional
Pssm-ID: 182570 Cd Length: 362 Bit Score: 125.99 E-value: 4.61e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 67 YNGPCTEEAVAEMAKEAQAEyCDMVVGIGGGKMLDIAKAVAFYAELPLCVCPTAASMDGPCSAISVLYHEDGSFDRYLML 146
Cdd:PRK10586 67 FRGHCSESDVAQLAAASGDD-RQVVIGVGGGALLDTAKALARRLGLPFVAIPTIAATCAAWTPLSVWYNDAGQALHFEIF 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 147 EKNPDLVVVDTNVVAAAPLRMTVAGMGDALATYFEARSCAAAhgaNEHGGAPGHLALVAARACYDTLMECGVAAKRDLKK 226
Cdd:PRK10586 146 DDANFLVLVEPRIILNAPQEYLLAGIGDTLAKWYEAVVLAPQ---PETLPLTVRLGINNALAIRDVLLNSSEQALADQQN 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 227 GRTSPA----VERLIECNILLSGVGFESGGLALAHAIANGLTILPEC-KAMHGEAVAFGLVVQLRLERAPE-LDQVLEFC 300
Cdd:PRK10586 223 GQLTQDfcdvVDAIIAGGGMVGGLGERYTRVAAAHAVHNGLTVLPQTeKFLHGTKVAYGILVQSALLGQDDvLAQLIGAY 302
|
250 260 270
....*....|....*....|....*....|.
gi 1469304371 301 QRVGLPTTLEELGLDEITDADLLSVADATFK 331
Cdd:PRK10586 303 QRFHLPTTLAELDVDINNQAEIDRVIAHTLR 333
|
|
| Gro1PDH |
cd08173 |
Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) catalyzes the reversible conversion between ... |
74-316 |
4.90e-30 |
|
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: 117.27 E-value: 4.90e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 74 EAVAEMAKEAQAeycDMVVGIGGGKMLDIAKAVAFYAELPLCVCPTAASMDGPCSAISVLYHEDGSfdrYLMLEKNPDLV 153
Cdd:cd08173 70 EKVKKLIKESKA---DFIIGVGGGKVIDVAKYAAYKLNLPFISIPTSASHDGIASPFASIKGGDKP---YSIKAKAPIAI 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 154 VVDTNVVAAAPLRMTVAGMGDALATYFEARSCAAAHG-ANEH-GGAPGHLALVAARAcydtLMECGVAAKRDLKKG-RTs 230
Cdd:cd08173 144 IADTEIISKAPKRLLAAGCGDLISNITAVKDWRLAHRlKGEYySEYAASLALMSAKL----IIENADLIKPGLEEGvRT- 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 231 pAVERLIecnilLSGVGFE--------SGGlalAHAIANGLTILPECKAMHGEAVAFGLVVQLRLERApELDQVLEFCQR 302
Cdd:cd08173 219 -VVKALI-----SSGVAMSiagssrpaSGS---EHLFSHALDKLAPGPALHGEQCGVGTIMMAYLHGG-DWKEIREALKK 288
|
250
....*....|....
gi 1469304371 303 VGLPTTLEELGLDE 316
Cdd:cd08173 289 IGAPTTAKELGLDK 302
|
|
| G1PDH-like |
cd08174 |
Glycerol-1-phosphate dehydrogenase-like; These glycerol-1-phosphate dehydrogenase-like ... |
16-316 |
2.06e-29 |
|
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: 115.31 E-value: 2.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 16 GPGELSRQGRYLSWLGCA---AYVLFDQGTEDRLCRQIVDGFLDDDLsepfFKIYNGPCTEEAVAEMAKEAQAEYCDMVV 92
Cdd:cd08174 7 EEGALEHLGKYLADRNQGfgkVAIVTGEGIDELLGEDILESLEEAGE----IVTVEENTDNSAEELAEKAFSLPKVDAIV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 93 GIGGGKMLDIAKAVAFYAELPLCVCPTAASMDGPCSAISVLYHED--GSFDrylmlEKNPDLVVVDTNVVAAAPLRMTVA 170
Cdd:cd08174 83 GIGGGKVLDVAKYAAFLSKLPFISVPTSLSNDGIASPVAVLKVDGkrKSLG-----AKMPYGVIVDLDVIKSAPRRLILA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 171 GMGDALATY-------FearscaaahgANEHGGAPGH-LALVAARACYDTLMECGVAAKRDLkkgrtsPAVERLIECnIL 242
Cdd:cd08174 158 GIGDLISNItalydwkL----------AEEKGGEPVDdFAYLLSRTAADSLLNTPGKDIKDD------EFLKELAES-LV 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 243 LSGVGFE--------SGGlalAHAIANGLTILPECKAMHGEAVAFGLVVQLRLeRAPELDQVLEFCQRVGLPTTLEELGL 314
Cdd:cd08174 221 LSGIAMEiagssrpaSGS---EHLISHALDKLFPGPALHGIQVGLGTYFMSFL-QGQRYEEIRDVLKRTGFPLNPSDLGL 296
|
..
gi 1469304371 315 DE 316
Cdd:cd08174 297 TK 298
|
|
| Fe-ADH_2 |
pfam13685 |
Iron-containing alcohol dehydrogenase; |
16-278 |
8.33e-28 |
|
Iron-containing alcohol dehydrogenase;
Pssm-ID: 404557 [Multi-domain] Cd Length: 251 Bit Score: 109.31 E-value: 8.33e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 16 GPGELSRQGRYLSWLG-CAAYVLFDQGTEDRLCRQIVDGFLDDDLSEPFFKIYNGPCTEEAVAEMAKEAQAEYCDMVVGI 94
Cdd:pfam13685 3 GPGALGRLGEYLAELGfRRVALVADANTYAAAGRKVAESLKRAGIEVETRLEVAGNADMETAEKLVGALRERDADAVVGV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 95 GGGKMLDIAKAVAFYAELPLCVCPTAASMDGPCSAISVLYHeDGSfdRYLMLEKNPDLVVVDTNVVAAAPLRMTVAGMGD 174
Cdd:pfam13685 83 GGGTVIDLAKYAAFKLGKPFISVPTAASNDGFASPGASLTV-DGK--KRSIPAAAPFGVIADTDVIAAAPRRLLASGVGD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 175 ALATYFEARSCAAAHganeHGGAPGHLALVAAracyDTLMECGVAAKRDLKKGRtspAVERLIEcNILLSGVGFESGGLA 254
Cdd:pfam13685 160 LLAKITAVADWELAH----AEEVAAPLALLSA----AMVMNFADRPLRDPGDIE---ALAELLS-ALAMGGAGSSRPASG 227
|
250 260
....*....|....*....|....
gi 1469304371 255 LAHAIANGLTILPECKAMHGEAVA 278
Cdd:pfam13685 228 SEHLISHALDMIAPKQALHGEQVG 251
|
|
| egsA |
PRK00843 |
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed |
74-316 |
3.45e-22 |
|
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed
Pssm-ID: 179139 Cd Length: 350 Bit Score: 95.73 E-value: 3.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 74 EAVAEMAKEAQAEYcdmVVGIGGGKMLDIAKAVAFYAELPLCVCPTAASMDGPCSAISVLYHEDGsfdRYLMLEKNPDLV 153
Cdd:PRK00843 77 EKVEEKAKDVNAGF---LIGVGGGKVIDVAKLAAYRLGIPFISVPTAASHDGIASPRASIKGGGK---PVSVKAKPPLAV 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 154 VVDTNVVAAAPLRMTVAGMGDALATYFEARSCAAAHG-ANEH-GGAPGHLALVAARacydTLMECGVAAKRDLKKGrtsp 231
Cdd:PRK00843 151 IADTEIIAKAPYRLLAAGCGDIISNYTAVKDWRLAHRlRGEYySEYAAALSLMTAK----MLIENADIIKPGLEES---- 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 232 avERLIECNILLSGVGFE--------SGGlalAHAIANGLTILPECKAMHGEAVAFGLVVQLRLErAPELDQVLEFCQRV 303
Cdd:PRK00843 223 --ARLVVKALISSGVAMSiagssrpaSGS---EHLFSHALDRLAPGPALHGEQCGVGTIIMMYLH-GGDWRKIRDALKKI 296
|
250
....*....|...
gi 1469304371 304 GLPTTLEELGLDE 316
Cdd:PRK00843 297 GAPTTAKELGIDD 309
|
|
| G1PDH |
cd08175 |
Glycerol-1-phosphate dehydrogenase (G1PDH) catalyzes the reversible reduction of ... |
16-316 |
1.04e-21 |
|
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: 94.11 E-value: 1.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 16 GPGELSRQGRYLS--WLGCAAYVLFDQGTEDRLCRQIVDGfLDDDLSEPFFKIYNGP----CTEEAVAEMAKEAQAEYcD 89
Cdd:cd08175 7 GEGALKKLPEYLKelFGGKKVLVVADENTYAAAGEEVEAA-LEEAGVTVCLLIFPGEgdliADEAAVGKVLLELEKDT-D 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 90 MVVGIGGGKMLDIAKAVAFYAELPLCVCPTAASMDGPCSAISVLYHeDG---SFDRylmleKNPDLVVVDTNVVAAAPLR 166
Cdd:cd08175 85 LIIAVGSGTINDLTKYAAYKLGIPYISVPTAPSMDGYTSSGAPIIV-DGvkkTFPA-----HAPKAIFADLDVLANAPQR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 167 MTVAGMGDALATYfearSCAA----AHGANEHGGAPGHLALVaaracYDTLMECgVAAKRDLKKgRTSPAVERLIECnIL 242
Cdd:cd08175 159 MIAAGFGDLLGKY----TALAdwklSHLLGGEYYCPEVADLV-----QEALEKC-LDNAEGIAA-RDPEAIEALMEA-LI 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 243 LSGVGFE--------SGG--LaLAH-----AIANGLTilpecKAMHGEAVAFGLVVQLRL---ERAPELDQVLEFCQRVG 304
Cdd:cd08175 227 LSGLAMQlvgnsrpaSGAehH-LSHywemeFLRLGKP-----PVLHGEKVGVGTLLIAALyilEQLPPPEELRELLRKAG 300
|
330
....*....|..
gi 1469304371 305 LPTTLEELGLDE 316
Cdd:cd08175 301 APTTPEDLGIDR 312
|
|
| G1PDH_related |
cd08549 |
Glycerol-1-phosphate dehydrogenase and related proteins; This family contains bacterial and ... |
16-316 |
6.73e-21 |
|
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: 91.86 E-value: 6.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 16 GPGELSRQGRYLSWLGCA-AYVLFDQGTEDRLCRQIVDGFLDDDLSEPFFKIYNgpcteeAVAEMAKEAqaeYCDMVVGI 94
Cdd:cd08549 7 GDGAINKIEEILKKLNLKrVLIITGKNTKAKYCRFFYDQLKTVCDIVYYDNIDN------LEDELKKYT---FYDCVIGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 95 GGGKMLDIAKAVAFYAELPLCVCPTAASMDGPCSAISVLYHEDgsfDRYLMLEKNPDLVVVDTNVVAAAPLRMTVAGMGD 174
Cdd:cd08549 78 GGGRSIDTGKYLAYKLKIPFISVPTSASNDGIASPIVSLRIPG---VKKTFMADAPIAIIADTEIIKKSPRRLLSAGIGD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 175 ALATYFEARSCAAAHganEHGGAP-----GHLALVAARACYDTLMEcgvAAKR--DLKKgrtspAVERLIECNI--LLSG 245
Cdd:cd08549 155 LVSNITAVLDWKLAH---KEKGEKysefaAILSKTSAKELVSYVLK---ASDLeeYHRV-----LVKALVGSGIamAIAG 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1469304371 246 VGFESGGLA--LAHAIANGLTILPECKAMHGEAVAFGLVVQLRL------ERAPELDQVLEFCQRVGLPTTLEELGLDE 316
Cdd:cd08549 224 SSRPASGSEhlFSHALDKLKEEYLNINVLHGEQVGVGTIIMSYLhekenkKLSGLHERIKMILKKVGAPTTAKQLGIDE 302
|
|
| EutG |
COG1454 |
Alcohol dehydrogenase, class IV [Energy production and conversion]; |
72-338 |
3.47e-19 |
|
Alcohol dehydrogenase, class IV [Energy production and conversion];
Pssm-ID: 441063 [Multi-domain] Cd Length: 381 Bit Score: 87.48 E-value: 3.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 72 TEEAVAEMAKEAQAEYCDMVVGIGGGKMLDIAKAVAFYAE------------------LPLCVCPT---AASMdgpCSAI 130
Cdd:COG1454 72 TVETVEAGAAAAREFGADVVIALGGGSAIDAAKAIALLATnpgdledylgikkvpgppLPLIAIPTtagTGSE---VTPF 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 131 SVLYHED-----GSFDRYLMleknPDLVVVDTNVVAAAPLRMTVA-GMgDALATYFEArscAAAHGANEHGGApghLALV 204
Cdd:COG1454 149 AVITDPEtgvkkGIADPELL----PDVAILDPELTLTLPPSLTAAtGM-DALTHAIEA---YVSKGANPLTDA---LALE 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 205 AARACYDTLMECgVAAKRDLKkgrtspAVERLIECNiLLSGVGFESGGLALAHAIANGLTilPECKAMHGEAVA------ 278
Cdd:COG1454 218 AIRLIARNLPRA-VADGDDLE------AREKMALAS-LLAGMAFANAGLGAVHALAHPLG--GLFHVPHGLANAillphv 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 279 ------------------FGLVVQLRLERAPE--LDQVLEFCQRVGLPTTLEELGLDEitdADLLSVADATFKNeRNMAN 338
Cdd:COG1454 288 lrfnapaaperyaeiaraLGLDVGLSDEEAAEalIEAIRELLRDLGIPTRLSELGVTE---EDLPELAELALAD-RCLAN 363
|
|
| Fe-ADH |
cd08551 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains large ... |
10-352 |
1.06e-18 |
|
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: 85.96 E-value: 1.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 10 PGRYVQGPGELSRQGRYLSWLGCA-AYVLFDQGTEDR-LCRQIVDGFLDDDLSepfFKIYNG----PcTEEAVAEMAKEA 83
Cdd:cd08551 1 PTRIVFGAGALARLGEELKALGGKkVLLVTDPGLVKAgLLDKVLESLKAAGIE---VEVFDDvepnP-TVETVEAAAELA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 84 QAEYCDMVVGIGGGKMLDIAKAVAFYAE------------------LPLCVCPTAAsmdGP---CSAISVLYHEDGSF-- 140
Cdd:cd08551 77 REEGADLVIAVGGGSVLDTAKAIAVLATnggsirdyegigkvpkpgLPLIAIPTTA---GTgseVTPNAVITDPETGRkm 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 141 ---DRYLMleknPDLVVVDTNVVAAAPLRMTVA-GMgDALATYFEArscAAAHGANEHGGApghLALVAARACYDTLmec 216
Cdd:cd08551 154 givSPYLL----PDVAILDPELTLSLPPSVTAAtGM-DALTHAIEA---YTSKKANPISDA---LALEAIRLIGKNL--- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 217 gvaaKRDLKKGRTSPAVERLIECNiLLSGVGFESGGLALAHAIANGLT---------------------ILPECKAMHGE 275
Cdd:cd08551 220 ----RRAVADGSDLEAREAMLLAS-LLAGIAFGNAGLGAVHALAYPLGgryhiphgvanaillpyvmefNLPACPEKYAE 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 276 -AVAFGLVVQ-LRLERAPEL--DQVLEFCQRVGLPTTLEELGldeITDADLLSVADATFKNERNMANEQTKVTRQKLVQL 351
Cdd:cd08551 295 iAEALGEDVEgLSDEEAAEAavEAVRELLRDLGIPTSLSELG---VTEEDIPELAEDAMKSGRLLSNNPRPLTEEDIREI 371
|
.
gi 1469304371 352 M 352
Cdd:cd08551 372 Y 372
|
|
| Fe-ADH-like |
cd14863 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
16-352 |
1.98e-18 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341485 [Multi-domain] Cd Length: 380 Bit Score: 85.28 E-value: 1.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 16 GPGELSRQGRYLSWLGCA-AYVLFDQGTEDRlcrQIVDGFLDD-DLSEPFFKIYNGP---CTEEAVAEMAKEAQAEYCDM 90
Cdd:cd14863 11 GAGAVEQIGELLKELGCKkVLLVTDKGLKKA---GIVDKIIDLlEEAGIEVVVFDDVepdPPDEIVDEAAEIAREEGADG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 91 VVGIGGGKMLDIAKAVA------------------FYAELPLCVC-PTAASMDGPCSAISVLYHEDGsfDRYLML---EK 148
Cdd:cd14863 88 VIGIGGGSVLDTAKAIAvlltnpgpiidyalagppVPKPGIPLIAiPTTAGTGSEVTPIAVITDEEN--GVKKSLlgpFL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 149 NPDLVVVDTNVVAAAPLRMTVA-GMgDALATYFEARSCAAahgANEHGGApghLALVAARACYDTLMECgVAAKRDLKkg 227
Cdd:cd14863 166 VPDLAILDPELTVGLPPSLTAAtGM-DALSHAIEAYTSKL---ANPMTDA---LALQAIRLIVKNLPRA-VKDGDNLE-- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 228 rtspAVER-LIECNilLSGVGFESGGLALAHAIANGLTIL---PeckamHGEAVAFGLVVQLRL--ERAPE--------- 292
Cdd:cd14863 236 ----ARENmLLASN--LAGIAFNNAGTHIGHAIAHALGALyhiP-----HGLACALALPVVLEFnaEAYPEkvkkiakal 304
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1469304371 293 ----------------LDQVLEFCQRVGLPTTLEELGLDEitdADLLSVADATFKNERNMANeQTKVTRQKLVQLM 352
Cdd:cd14863 305 gvsfpgesdeelgeavADAIREFMKELGIPSLFEDYGIDK---EDLDKIAEAVLKDPFAMFN-PRPITEEEVAEIL 376
|
|
| HEPD |
cd08182 |
Hydroxyethylphosphoate dehydrogenase (HEPD) catalyzes the reduction of phosphonoacetaldehyde ... |
10-351 |
2.68e-15 |
|
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: 76.11 E-value: 2.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 10 PGRYVQGPGELSRQGRYLSWLGCAAYVLF--DQGTEDRLCRQIVDGFLDDDLSEPFFKIYNGPcTEEAVAEMAKEAQAEY 87
Cdd:cd08182 1 PVKIIFGPGALAELKDLLGGLGARRVLLVtgPSAVRESGAADILDALGGRIPVVVFSDFSPNP-DLEDLERGIELFRESG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 88 CDMVVGIGGGKMLDIAKAVAFYAE--------------------LPLCVCPTAAsmdGPCSAI---SVLYHEDG----SF 140
Cdd:cd08182 80 PDVIIAVGGGSVIDTAKAIAALLGspgenllllrtgekapeenaLPLIAIPTTA---GTGSEVtpfATIWDEAEgkkySL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 141 DRYLMLeknPDLVVVDTNVVAAAPLRMTVAGMGDALATYFEArscAAAHGANEhggAPGHLALVAARacydTLMECGVAA 220
Cdd:cd08182 157 AHPSLY---PDAAILDPELTLSLPLYLTASTGLDALSHAIES---IWSVNANP---ESRAYALRAIR----LILENLPLL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 221 KRDLkkgRTSPAVERLIECNiLLSGVGFESGGLALAHAIANGLTI---LPeckamHGEAVAFGL-----------VVQLR 286
Cdd:cd08182 224 LENL---PNLEAREAMAEAS-LLAGLAISITKTTAAHAISYPLTSrygVP-----HGHACALTLpavlrynagadDECDD 294
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1469304371 287 LERAPEL-------------DQVLEFCQRVGLPTTLEELGldeITDADLLSVADATFKNERnMANEQTKVTRQKLVQL 351
Cdd:cd08182 295 DPRGREIllalgasdpaeaaERLRALLESLGLPTRLSEYG---VTAEDLEALAASVNTPER-LKNNPVRLSEEDLLRL 368
|
|
| Fe-ADH-like |
cd08191 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
10-338 |
1.65e-14 |
|
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: 73.80 E-value: 1.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 10 PGRYVQGPGELSRQGRYLSWLGCAAYVLFDQG-TEDRLCRQIVDGFLDDDLSepfFKIYNGPCTE---EAVAEMAKEAQA 85
Cdd:cd08191 4 PSRLLFGPGARRALGRVAARLGSRVLIVTDPRlASTPLVAELLAALTAAGVA---VEVFDGGQPElpvSTVADAAAAARA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 86 EYCDMVVGIGGGKMLDIAKAVA-----------FYAE-------LPLCVCPTAASMDGPCSAISVLYHED-----GSFDR 142
Cdd:cd08191 81 FDPDVVIGLGGGSNMDLAKVVAlllahggdprdYYGEdrvpgpvLPLIAVPTTAGTGSEVTPVAVLTDPArgmkvGVSSP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 143 YLMleknPDLVVVDTNVVAAAPLRMTVAGMGDALATYFEArSCAAAHGANEHGGAP----------GHLALVAARACYDT 212
Cdd:cd08191 161 YLR----PAVAIVDPELTLTCPPGVTADSGIDALTHAIES-YTARDFPPFPRLDPDpvyvgknpltDLLALEAIRLIGRH 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 213 LmecgVAAKRDlkkGRTSPAVERLIECNiLLSGVGFESGGLALAHAIANGLTILPECKamHGEAVAFGL--VVQ-LRLER 289
Cdd:cd08191 236 L----PRAVRD---GDDLEARSGMALAA-LLAGLAFGTAGTAAAHALQYPIGALTHTS--HGVGNGLLLpyVMRfNRPAR 305
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1469304371 290 APEL-----------------------DQVLEFCQRVGLPTTLEELGLDEitdADLLSVADATFKNERNMAN 338
Cdd:cd08191 306 AAELaeiaralgvttagtseeaadraiERVEELLARIGIPTTLADLGVTE---ADLPGLAEKALSVTRLIAN 374
|
|
| Fe-ADH-like |
cd14864 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
10-340 |
1.05e-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: 341486 [Multi-domain] Cd Length: 376 Bit Score: 71.56 E-value: 1.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 10 PGRYVQGPGELSRQGRYLSWLGCAAYVLFDQGT-EDRLCRQIVDGFLDDDLSepfFKIYN--GPCTEEAVAEMA-KEAQA 85
Cdd:cd14864 4 PPNIVFGADSLERIGEEVKEYGSRFLLITDPVLkESGLADKIVSSLEKAGIS---VIVFDeiPASATSDTIDEAaELARK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 86 EYCDMVVGIGGGKMLDIAKAVA-FYAE-----------------LPLCVCPTAASMDGPCSAISVLYHEDGSFDRYLMLE 147
Cdd:cd14864 81 AGADGIIAVGGGKVLDTAKAVAiLANNdggaydflegakpkkkpLPLIAVPTTPRSGFEFSDRFPVVDSRSREVKLLKAQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 148 KN-PDLVVVDTNVVAAAPLRMTVAGMGDALATYFEarscaaahganehggapghlALVAARACY--DTLMECGVAAKRD- 223
Cdd:cd14864 161 PGlPKAVIVDPNLMASLTGNQTAAMALAALALAVE--------------------AYLSKKSNFfsDALALKAIELVSEn 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 224 ----LKKGRTSPAVERLIECNiLLSGVGFESGGLALAHAIA---NGLTILPECKAM----------HGEAVAFGLVVQLR 286
Cdd:cd14864 221 ldgaLADPKNTPAEELLAQAG-CLAGLAASSSSPGLATALAlavNSRYKVSKSLVAsillphvieyAATSAPDKYAKIAR 299
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1469304371 287 LERAPELDQ------------VLEFCQRVGLPTTLEELGLDEITDaDLLSVADATFKNE---RNMANEQ 340
Cdd:cd14864 300 ALGEDVEGAspeeaaiaavegVRRLIAQLNLPTRLKDLDLASSLE-QLAAIAEDAPKLNglpRSMSSDD 367
|
|
| Fe-ADH-like |
cd14862 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
72-342 |
1.05e-11 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341484 [Multi-domain] Cd Length: 375 Bit Score: 65.32 E-value: 1.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 72 TEEAVAEMAKEAQAeycDMVVGIGGGKMLDIAKAVAFYAELP--------------------LCVCPTAASMDGPCSAIS 131
Cdd:cd14862 69 TVLKGAEAMREFEP---DLIIALGGGSVMDAAKAAWVLYERPdldpedispldllglrkkakLIAIPTTSGTGSEATWAI 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 132 VLyHEDGSFDRYLML--EKNPDLVVVDTNVVAAAPLRMTVA-GMgDALATYFEARSCAAahgANEHGGApghLALVAARA 208
Cdd:cd14862 146 VL-TDTEEPRKIAVAnpELVPDVAILDPEFVLGMPPKLTAGtGL-DALAHAVEAYLSTW---SNDFSDA---LALKAIEL 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 209 CYDTLMecgvaakRDLKKGRTSPAVERL-IECNIllSGVGFESGGLALAHAIANGL-TILpecKAMHGEAVA-------- 278
Cdd:cd14862 218 IFKYLP-------RAYKDGDDLEAREKMhNAATI--AGLAFGNSQAGLAHALGHSLgAVF---HVPHGIAVGlflpyvie 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 279 ---------------FGLVVQLRLERAPEL-DQVLEFCQRVGLPTTLEELGLDEIT-DADLLSVADATFK------NERN 335
Cdd:cd14862 286 fyakvtderydllklLGIEARDEEEALKKLvEAIRELYKEVGQPLSIKDLGISEEEfEEKLDELVEYAMEdsctitSPRP 365
|
....*..
gi 1469304371 336 MANEQTK 342
Cdd:cd14862 366 PSEEDLK 372
|
|
| Fe-ADH-like |
cd08196 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
55-351 |
1.50e-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: 341475 [Multi-domain] Cd Length: 367 Bit Score: 64.91 E-value: 1.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 55 LDDDLSEPFFKIYNG--P-CTEEAVAEMAKEAQAEYCDMVVGIGGGKMLDIAKAVAFYAE-------------------L 112
Cdd:cd08196 48 IVESLKGRIVAVFSDvePnPTVENVDKCARLARENGADFVIAIGGGSVLDTAKAAACLAKtdgsiedylegkkkipkkgL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 113 PLCVCPTAASMDGPCSAISVL-YHEDG---SFDRYLMLeknPDLVVVDTNVVAAAPLRMTVA-GMgDALATYFEA----- 182
Cdd:cd08196 128 PLIAIPTTAGTGSEVTPVAVLtDKEKGkkaPLVSPGFY---PDIAIVDPELTYSMPPKVTAStGI-DALCHAIEAywsin 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 183 --RSCAAahganehggapghLALVAARACYDTLmecgvaaKRDLKKGRTSPAVERLIECNiLLSGVGFESGGLALAHAIA 260
Cdd:cd08196 204 hqPISDA-------------LALEAAKLVLENL-------EKAYNNPNDKEAREKMALAS-LLAGLAFSQTRTTASHACS 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 261 NGLTI---LPeckamHGEAVAFGLVVQLRL---ERAPELDQVLEFC----------------QRVGLPTTLEELGldeIT 318
Cdd:cd08196 263 YPLTShfgIP-----HGEACALTLPSFIRLnaeALPGRLDELAKQLgfkdaeeladkieelkKRIGLRTRLSELG---IT 334
|
330 340 350
....*....|....*....|....*....|...
gi 1469304371 319 DADLLSVADATFKNERnMANEQTKVTRQKLVQL 351
Cdd:cd08196 335 EEDLEEIVEESFHPNR-ANNNPVEVTKEDLEKL 366
|
|
| NADPH_BDH |
cd08179 |
NADPH-dependent butanol dehydrogenase involved in the butanol and ethanol formation pathway in ... |
9-316 |
1.33e-10 |
|
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: 61.82 E-value: 1.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 9 GPGRYVQGPGELSrqgrYLS-WLGCAAYVLFDQGTEDRLcrqivdGFLD---DDLSEPFF--KIYNG----PCTEEaVAE 78
Cdd:cd08179 4 VPRDIYFGEGALE----YLKtLKGKRAFIVTGGGSMKRN------GFLDkveDYLKEAGMevKVFEGvepdPSVET-VEK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 79 MAKEAQAEYCDMVVGIGGGKMLDIAKAVAFYAELP---------------------LCVCPTAASMDGPCSAISVL-YHE 136
Cdd:cd08179 73 GAEAMREFEPDWIIAIGGGSVIDAAKAMWVFYEYPeltfedalvpfplpelrkkarFIAIPSTSGTGSEVTRASVItDTE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 137 DGSfdRYLMLEKN--PDLVVVDTNVVAAAPLRMTVA-GMgDALATYFEARSCAAAHGANEhggapgHLALVAARACYDTL 213
Cdd:cd08179 153 KGI--KYPLASFEitPDVAILDPELTMTMPPHVTANtGM-DALTHAIEAYVSTLANDFTD------ALALGAILDIFENL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 214 MECgVAAKRDLKkgrtspAVERL--IECnilLSGVGFESGGLALAHAIA---NGLTILPeckamHGEAVAFGL------- 281
Cdd:cd08179 224 PKS-YNGGKDLE------AREKMhnASC---LAGMAFSNSGLGIVHSMAhkgGAFFGIP-----HGLANAILLpyviefn 288
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1469304371 282 -----VVQLRLERAPELDQ----------VLEFCQRVGLPTTLEELGLDE 316
Cdd:cd08179 289 skdpeARARYAALLIGLTDeelvedlieaIEELNKKLGIPLSFKEAGIDE 338
|
|
| HOT |
cd08190 |
Hydroxyacid-oxoacid transhydrogenase (HOT) involved in gamma-hydroxybutyrate metabolism; This ... |
64-355 |
1.47e-10 |
|
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: 62.18 E-value: 1.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 64 FKIYNGPCTE---EAVAEMAKEAQAEYCDMVVGIGGGKMLDIAKAVAFYA-----------------------ELPLCVC 117
Cdd:cd08190 54 VVVYDGVRVEptdESFEEAIEFAKEGDFDAFVAVGGGSVIDTAKAANLYAthpgdfldyvnapigkgkpvpgpLKPLIAI 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 118 PTAASMDGPCSAISVLYHED-----GSFDRYLmlekNPDLVVVDTNVVAAAPLRMTVA-GMgDAL--------ATYFEAR 183
Cdd:cd08190 134 PTTAGTGSETTGVAIFDLEElkvktGISSRYL----RPTLAIVDPLLTLTLPPRVTASsGF-DVLchalesytARPYNAR 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 184 SCAAA-------HGAN-------EHGgapghLALVAA---RACYDTLmecGVAAKRDLKKGRTspaverliecnilLSGV 246
Cdd:cd08190 209 PRPANpderpayQGSNpisdvwaEKA-----IELIGKylrRAVNDGD---DLEARSNMLLAST-------------LAGI 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 247 GFESGGLALAHAIA----------------NGLTILPeckamHGEAVAFGL--VVQL-------RLERAPEL-------- 293
Cdd:cd08190 268 GFGNAGVHLPHAMAypiaglvkdyrppgypVDHPHVP-----HGLSVALTApaVFRFtapacpeRHLEAAELlgadtsga 342
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1469304371 294 ----------DQVLEFCQRVGLPTTLEELGldeITDADLLSVADATFKNERNMANEQTKVTRQKLVQLMCEA 355
Cdd:cd08190 343 sdrdagevlaDALIKLMRDIGIPNGLSALG---YSEDDIPALVEGTLPQQRLLKLNPRPVTEEDLEEIFEDA 411
|
|
| Fe-ADH-like |
cd14865 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
74-334 |
7.27e-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: 341487 [Multi-domain] Cd Length: 383 Bit Score: 59.86 E-value: 7.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 74 EAVAEMAKEAQaeyCDMVVGIGGGKMLDIAKAVAFYAEL-------------------PLCVCPTAASMDGPCSAISVLY 134
Cdd:cd14865 75 NEAAARAREAG---ADGIIAVGGGSVIDTAKGVNILLSEggddlddygganrltrplkPLIAIPTTAGTGSEVTLVAVIK 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 135 HEDG----SF-DRYLMleknPDLVVVDTNVVAAAPLRMTVA-GMgDALATYFEARSCAaahGANEHGGApghLALVAARA 208
Cdd:cd14865 152 DEEKkvklLFvSPFLL----PDVAILDPRLTLSLPPKLTAAtGM-DALTHAIEAYTSL---QKNPISDA---LALQAIRL 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 209 CYDTLMECgVAAKRDLkKGRTSPAVERliecniLLSGVGFESGGLALAHAIANGLTILpeCKAMHGEAVAFGL--VVQLR 286
Cdd:cd14865 221 ISENLPKA-VKNGKDL-EARLALAIAA------TMAGIAFSNSMVGLVHAIAHAVGAV--AGVPHGLANSILLphVMRYN 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 287 LERAPE----LDQVLEFC-----------------------QRVGLPTTLEELG-----LDEITDadlLSVAD-ATFKNE 333
Cdd:cd14865 291 LDAAAEryaeLALALAYGvtpagrraeeaieaaidlvrrlhELCGLPTRLRDVGvpeeqLEAIAE---LALNDgAILFNP 367
|
.
gi 1469304371 334 R 334
Cdd:cd14865 368 R 368
|
|
| Fe-ADH-like |
cd14861 |
Iron-containing alcohol dehydrogenases-like; This family contains proteins similar to ... |
72-331 |
5.15e-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: 57.14 E-value: 5.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 72 TEEAVAEMAKEAQAEYCDMVVGIGGGKMLDIAKAVAFYAE----------------------LPLCVCPTAAsmdGPCSA 129
Cdd:cd14861 67 TEADVEAGVAAYREGGCDGIIALGGGSAIDAAKAIALMAThpgplwdyedgeggpaaitpavPPLIAIPTTA---GTGSE 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 130 I---SVLYHEDGS-----FDRYLMleknPDLVVVDTNVVAAAPLRMTVA-GMgDALATYFEARSCaaahgANEHGGAPGh 200
Cdd:cd14861 144 VgraAVITDDDTGrkkiiFSPKLL----PKVAICDPELTLGLPPRLTAAtGM-DALTHCIEAYLS-----PGFHPMADG- 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 201 LALVAARACYDTLMECgVAAKRDLkKGRTSPAVERliecniLLSGVGFESgGLALAHAIANGLTILpeCKAMHGEAVAFG 280
Cdd:cd14861 213 IALEGLRLISEWLPRA-VADGSDL-EARGEMMMAA------LMGAVAFQK-GLGAVHALAHALGAL--YGLHHGLLNAIL 281
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1469304371 281 LVVQLRL------ERAPELDQ---------------VLEFCQRVGLPTTLEELGldeITDADLLSVADATFK 331
Cdd:cd14861 282 LPYVLRFnrpaveDKLARLARalglglggfddfiawVEDLNERLGLPATLSELG---VTEDDLDELAELALA 350
|
|
| PRK15454 |
PRK15454 |
ethanolamine utilization ethanol dehydrogenase EutG; |
70-261 |
7.49e-08 |
|
ethanolamine utilization ethanol dehydrogenase EutG;
Pssm-ID: 185351 [Multi-domain] Cd Length: 395 Bit Score: 53.49 E-value: 7.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 70 PCTEEAVAEMAKEAQAEyCDMVVGIGGGKMLDIAKAVAFYA------------------ELPLCVCPTAASMDGPCSAIS 131
Cdd:PRK15454 90 PCITDVCAAVAQLRESG-CDGVIAFGGGSVLDAAKAVALLVtnpdstlaemsetsvlqpRLPLIAIPTTAGTGSETTNVT 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 132 VLYheDGSFDRYLMLEKN---PDLVVVDTNVVAAAPLRMTVAGMGDALATYFEARSCAAAHGANEhGGAPGHLALVaara 208
Cdd:PRK15454 169 VII--DAVSGRKQVLAHAslmPDVAILDAALTEGVPSHVTAMTGIDALTHAIEAYSALNATPFTD-SLAIGAIAMI---- 241
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1469304371 209 cydtlmecGVAAKRDLKKGRTSPAVERLIECNIlLSGVGFESGGLALAHAIAN 261
Cdd:PRK15454 242 --------GKSLPKAVGYGHDLAARESMLLASC-MAGMAFSSAGLGLCHAMAH 285
|
|
| LPO |
cd08176 |
Lactadehyde:propanediol oxidoreductase (LPO) catalyzes the interconversion between ... |
72-316 |
1.07e-06 |
|
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: 49.85 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 72 TEEAVAEMAKEAQAEYCDMVVGIGGGKMLDIAKAVAFYA-------------------ELPLCVCPTAASMDGPCSAISV 132
Cdd:cd08176 70 TIENVMAGVAAYKESGADGIIAVGGGSSIDTAKAIGIIVanpgadvrslegvaptknpAVPIIAVPTTAGTGSEVTINYV 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 133 LYHEDGSFdRYLMLEKN--PDLVVVDTNVVAAAPLRMTVA-GMgDALATYFEArscAAAHGANEHGGApghLALVAARAC 209
Cdd:cd08176 150 ITDTEKKR-KFVCVDPHdiPTVAIVDPDLMSSMPKGLTAAtGM-DALTHAIEG---YITKGAWELSDM---LALKAIELI 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 210 YDTLMEcgVAAKRDLKKGRTSPAVERLIecnillSGVGFESGGLALAHAIANGLT-------------ILPEC----KAM 272
Cdd:cd08176 222 AKNLRK--AVANPNNVEARENMALAQYI------AGMAFSNVGLGIVHSMAHPLSafydtphgvanaiLLPYVmefnAPA 293
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1469304371 273 HGE-----AVAFGL-VVQLRLERAPE--LDQVLEFCQRVGLPTTLEELGLDE 316
Cdd:cd08176 294 TGEkyrdiARAMGVdTTGMSDEEAAEaaVDAVKKLSKDVGIPQKLSELGVKE 345
|
|
| Fe-ADH-like |
cd08185 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
74-110 |
2.01e-06 |
|
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: 49.03 E-value: 2.01e-06
10 20 30
....*....|....*....|....*....|....*..
gi 1469304371 74 EAVAEMAKEaqaEYCDMVVGIGGGKMLDIAKAVAFYA 110
Cdd:cd08185 73 MEGAALAKE---EGCDFVIGLGGGSSMDAAKAIAFMA 106
|
|
| PPD-like |
cd08181 |
1,3-propanediol dehydrogenase-like (PPD); This family contains proteins similar to 1, ... |
53-351 |
2.61e-06 |
|
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: 48.74 E-value: 2.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 53 GFLDD------DLSEPFFkIYNG----PCTE--EAVAEMAKEaqaEYCDMVVGIGGGKMLDIAKAVAFYAE--------- 111
Cdd:cd08181 41 GSLDDvtealeENGIEYF-IFDEveenPSIEtvEKGAELARK---EGADFVIGIGGGSPLDAAKAIALLAAnkdgdedlf 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 112 --------LPLCVCPTAASMDGPCSAISVL-YHEDGSfdrylmlEKN-------PDLVVVDTNVVAAAPLRMTVAGMGDA 175
Cdd:cd08181 117 qngkynppLPIVAIPTTAGTGSEVTPYSILtDHEKGT-------KKSfgnplifPKLALLDPKYTLSLPEELTIDTAVDA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 176 LATYFEarscaaahganehggapGHLAlVAARACYDTLMECGV----AAKRDLKKGRTSPAV-ERLIECNILlsgvgfes 250
Cdd:cd08181 190 LSHAIE-----------------GYLS-VKATPLSDALALEALrligECLPNLLGDELDEEDrEKLMYASTL-------- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 251 GGLALAHA---IANG----LTI---LPeckamHGEAVAFGLVVQLRL--ERAPE-LDQVLEFcqrVGLPTTlEELGL--- 314
Cdd:cd08181 244 AGMVIAQTgttLPHGlgypLTYfkgIP-----HGRANGILLPAYLKLceKQEPEkVDKILKL---LGFGSI-EEFQKfln 314
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1469304371 315 ------DEITDADLLSVADATFKNeRNMANEQTKVTRQKLVQL 351
Cdd:cd08181 315 rllgkkEELSEEELEKYADEAMKA-KNKKNTPGNVTKEDILRI 356
|
|
| PDDH |
cd08188 |
1,3-Propanediol (1,3-PD) dehydrogenase; This family includes 1,3-propanediol (1,3-PD) ... |
16-351 |
2.82e-06 |
|
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: 48.66 E-value: 2.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 16 GPGELSRQGRYLSWLGCA-AYVLFDQG-TEDRLCRQIVDGFLDDDLsepFFKIYNG----PcTEEAVAEMAKEAQAEYCD 89
Cdd:cd08188 12 GPGCLKEIGDELKKLGGKkALIVTDKGlVKLGLVKKVTDVLEEAGI---EYVIFDGvqpnP-TVTNVNEGLELFKENGCD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 90 MVVGIGGGKMLDIAKAVAFYAE------------------LPL-CVCPTAasmdGPCSAISVLY-------HEdgsfdRY 143
Cdd:cd08188 88 FIISVGGGSAHDCAKAIGILATnggeiedyegvdkskkpgLPLiAINTTA----GTASEVTRFAvitdeerHV-----KM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 144 LMLEKN--PDLVVVDTNVVAAAPLRMTVA-GMgDALATYFEARSCAAAHGANEhggapgHLALVAARACYDTLMECgVAA 220
Cdd:cd08188 159 VIVDWNvtPTIAVNDPELMLGMPPSLTAAtGM-DALTHAIEAYVSTGATPLTD------ALALEAIRLIAENLPKA-VAN 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 221 KRDLKkgrtspAVERLIECnILLSGVGFESGGLALAHAIAN---GLTILPE--CKAM---HGE--------------AVA 278
Cdd:cd08188 231 GKDLE------ARENMAYA-QFLAGMAFNNAGLGYVHAMAHqlgGFYNLPHgvCNAIllpHVMefnlpacperfadiARA 303
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1469304371 279 FGL-VVQLRLERAPE--LDQVLEFCQRVGLPTTLEELGldeITDADLLSVADATFKnERNMANEQTKVTRQKLVQL 351
Cdd:cd08188 304 LGEnTEGLSDEEAAEaaIEAIRKLSRRVGIPSGLKELG---VKEEDFPLLAENALK-DACGPTNPRQATKEDVIAI 375
|
|
| DHQ_synthase |
pfam01761 |
3-dehydroquinate synthase; The 3-dehydroquinate synthase EC:4.6.1.3 domain is present in ... |
149-320 |
2.99e-06 |
|
3-dehydroquinate synthase; The 3-dehydroquinate synthase EC:4.6.1.3 domain is present in isolation in various bacterial 3-dehydroquinate synthases and also present as a domain in the pentafunctional AROM polypeptide. 3-dehydroquinate (DHQ) synthase catalyzes the formation of dehydroquinate (DHQ) and orthophosphate from 3-deoxy-D-arabino heptulosonic 7 phosphate. This reaction is part of the shikimate pathway which is involved in the biosynthesis of aromatic amino acids.
Pssm-ID: 426414 Cd Length: 260 Bit Score: 47.88 E-value: 2.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 149 NPDLVVVDTNVVAAAPLRMTVAGMGDALATyfearscaaahganehggapghlALVAARACYDTLMECGVAAKRdlkkgR 228
Cdd:pfam01761 94 QPKAVLIDLDFLKTLPDREFRAGLAEVIKY-----------------------GLIADAEFFEWLEENAEALLN-----L 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 229 TSPAVERLIE--CNILLSGVG---FESG-------GLALAHAI---ANGLTILpeckamHGEAVAFGLVVQLRLERA--- 290
Cdd:pfam01761 146 DPDALEEAIArsCEVKADVVAqdeKESGlrallnlGHTFGHAIealSGYGALL------HGEAVAIGMVLAARLSERlgl 219
|
170 180 190
....*....|....*....|....*....|...
gi 1469304371 291 ---PELDQVLEFCQRVGLPTTLEELGLDEITDA 320
Cdd:pfam01761 220 ldeADVERIRALLKKYGLPTSLPDLDVEQLLAA 252
|
|
| AroB |
COG0337 |
3-dehydroquinate synthetase [Amino acid transport and metabolism]; 3-dehydroquinate synthetase ... |
150-320 |
5.99e-06 |
|
3-dehydroquinate synthetase [Amino acid transport and metabolism]; 3-dehydroquinate synthetase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis
Pssm-ID: 440106 Cd Length: 355 Bit Score: 47.39 E-value: 5.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 150 PDLVVVDTNVVAAAPLRMTVAGMGDALATyfearscaaahganehggapghlALVAARACYDTLMECGVAAKRdlkkgRT 229
Cdd:COG0337 161 PRAVLIDLDFLKTLPERELRAGLAEVIKY-----------------------GLIADAEFFEWLEENADALLA-----RD 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 230 SPAVERLIE--CNILLSGVG---FESGGLAL-------AHAI--ANGLTILpeckamHGEAVAFGLVVQLRL-ER----- 289
Cdd:COG0337 213 PEALEEAIArsCEIKAEVVAadeRESGLRALlnfghtfGHAIeaATGYRLL------HGEAVAIGMVFAARLsARlglls 286
|
170 180 190
....*....|....*....|....*....|.
gi 1469304371 290 APELDQVLEFCQRVGLPTTLEELGLDEITDA 320
Cdd:COG0337 287 EEDVERIRALLEALGLPTRLPALDPEALLAA 317
|
|
| DHQS |
cd08195 |
Dehydroquinate synthase (DHQS) catalyzes the conversion of DAHP to DHQ in shikimate pathway ... |
255-320 |
6.78e-06 |
|
Dehydroquinate synthase (DHQS) catalyzes the conversion of DAHP to DHQ in shikimate pathway for aromatic compounds synthesis; 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, which involves seven sequential enzymatic steps in the conversion of erythrose 4-phosphate and phosphoenolpyruvate into chorismate for subsequent synthesis of aromatic compounds, is found in bacteria, microbial eukaryotes, and plants, but not in mammals. Therefore, enzymes of this pathway are attractive targets for the development of non-toxic antimicrobial compounds, herbicides and anti-parasitic agents. The activity of DHQS requires nicotinamide adenine dinucleotide (NAD) as cofactor. A single active site in DHQS catalyzes five sequential reactions involving alcohol oxidation, phosphate elimination, carbonyl reduction, ring opening, and intramolecular aldol condensation. The binding of substrates and ligands induces domain conformational changes. In some fungi and protozoa, this domain is fused with the other four domains in shikimate pathway and forms a penta-domain AROM protein, which catalyzes steps 2-6 in the shikimate pathway.
Pssm-ID: 341474 Cd Length: 343 Bit Score: 47.44 E-value: 6.78e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1469304371 255 LAHAI--ANGLTILpeckamHGEAVAFGLVVQLRLER------APELDQVLEFCQRVGLPTTLEELGLDEITDA 320
Cdd:cd08195 238 FGHAIesASGYKLL------HGEAVAIGMVAAARLSVklgllsEEDLERIRALLKKLGLPTSIKDLDPEELLEA 305
|
|
| 4HBD_NAD |
cd14860 |
4-hydroxybutyrate dehydrogenase, also called gamma-hydroxybutyrate dehydrogenase, catalyzes ... |
61-157 |
8.20e-06 |
|
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: 47.21 E-value: 8.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 61 EPFFKIYNGPC-------------TEEAVAEMAKEAQAEYCDMVVGIGGGKMLDIAKAVAFyaelplcvcptaasmdGPC 127
Cdd:cd14860 39 EPYFEPLNLDCavifqekygtgepSDEMVEAIYKDIKKYGYKRVIAIGGGTVIDIAKLLAL----------------KGI 102
|
90 100 110
....*....|....*....|....*....|
gi 1469304371 128 SAISVLyhedgsFDRYLMLEKNPDLVVVDT 157
Cdd:cd14860 103 SPVLDL------FDGKIPLIKEKELIIVPT 126
|
|
| MAR-like |
cd08192 |
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic ... |
74-351 |
3.48e-05 |
|
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic microbes; Maleylacetate reductase (MAR) plays an important role in the degradation of aromatic compounds in aerobic microbes. In fungi and yeasts, the enzyme is involved in the catabolism of compounds such as phenol, tyrosine, benzoate, 4-hydroxybenzoate and resorcinol. In bacteria, the enzyme contributes to the degradation of resorcinol, 2,4-dihydroxybenzoate ([beta]-resorcylate) and 2,6-dihydroxybenzoate ([gamma]-resorcylate) via hydroxyquinol and maleylacetate. Maleylacetate reductase (MAR) catalyzes NADH- or NADPH-dependent reduction, at the carbon-carbon double bond, of maleylacetate or 2-chloromaleylacetate to 3-oxoadipate. In the case of 2-chloromaleylacetate, MAR initially catalyzes the NAD(P)H-dependent dechlorination to maleylacetate, which is then reduced to 3-oxoadipate. This enzyme is a homodimer. It is inhibited by thiol-blocking reagents such as p-chloromercuribenzoate and Hg++, indicating that the cysteine residue is probably necessary for the catalytic activity of maleylacetate reductase.
Pssm-ID: 341471 [Multi-domain] Cd Length: 380 Bit Score: 45.32 E-value: 3.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 74 EAVAEMAKEAQAEYCDMVVGIGGGKMLDIAKAVAF-YAELPLCVCPTAASMDGPCSAISV----LYH------------- 135
Cdd:cd08192 66 EDVLEAARAVREAGADLLVSLGGGSPIDAAKAVALaLAEDVTDVDQLDALEDGKRIDPNVtgptLPHiaipttlsgaeft 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 136 --------EDGSFDRYLMLEKNPDLVVVDTNVVAAAPLRMTVA-GMgDALATYFEArscAAAHGANEHGGApghLALVAA 206
Cdd:cd08192 146 agagatddDTGHKQGFAHPELGPDAVILDPELTLHTPERLWLStGI-RAVDHAVET---LCSPQATPFVDA---LALKAL 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 207 RacydTLMECGVAAKRDLKkgrtspAVERLIECNI---LLSGVGFESGGLALAHAIanGLTILPECKAMHGEA--VAFGL 281
Cdd:cd08192 219 R----LLFEGLPRSKADPE------DLEARLKCQLaawLSLFGLGSGVPMGASHAI--GHQLGPLYGVPHGITscIMLPA 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 282 VVQLRLERAPEL-----------------------DQVLEFCQRVGLPTTLEELGldeITDADLLSVADATFKNERNMAN 338
Cdd:cd08192 287 VLRFNAPVNAERqrliaralglvtgglgreaadaaDAIDALIRELGLPRTLRDVG---VGRDQLEKIAENALTDVWCRTN 363
|
330
....*....|...
gi 1469304371 339 EQTKVTRQKLVQL 351
Cdd:cd08192 364 PRPITDKDDVLEI 376
|
|
| Fe-ADH-like |
cd08183 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
10-329 |
8.65e-05 |
|
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and 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: 44.03 E-value: 8.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 10 PGRYVQGPGELSRQGRYLSWLGCAAYVLFDQGTED-RLCRQIVDGFLDDDLSEPFFKIYNGPcTEEAVAEMAKEAQAEYC 88
Cdd:cd08183 1 PPRIVFGRGSLQELGELAAELGKRALLVTGRSSLRsGRLARLLEALEAAGIEVALFSVSGEP-TVETVDAAVALAREAGC 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 89 DMVVGIGGGKMLDIAKAVA---------------FYAELPLcvcpTAASMdgPCSAI-------------SVL-YHEDG- 138
Cdd:cd08183 80 DVVIAIGGGSVIDAAKAIAalltnegsvldylevVGKGRPL----TEPPL--PFIAIpttagtgsevtknAVLsSPEHGv 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 139 --SFDRYLMLeknPDLVVVDTNVVAAAPLRMTVA-GMgDALATYFEArscAAAHGANEHGGApghLALVAARACYDTLME 215
Cdd:cd08183 154 kvSLRSPSML---PDVALVDPELTLSLPPEVTAAsGL-DALTQLIEP---YVSRKANPLTDA---LAREGLRLAARSLRR 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 216 CgvaakrdLKKGRTSPAVERLIECNiLLSGVGFESGGLALAHAIANGL-------------TILPEC-----KAMHGE-- 275
Cdd:cd08183 224 A-------YEDGEDLEAREDMALAS-LLGGLALANAGLGAVHGLAGPLggmfgaphgaicaALLPPVleanlRALRERep 295
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1469304371 276 --------AVAFGLVVQLRLERAPEL-DQVLEFCQRVGLPtTLEELGLdeiTDADLLSVADAT 329
Cdd:cd08183 296 dspalaryRELAGILTGDPDAAAEDGvEWLEELCEELGIP-RLSEYGL---TEEDFPEIVEKA 354
|
|
| HVD |
cd08193 |
5-hydroxyvalerate dehydrogenase (HVD) catalyzes the oxidation of 5-hydroxyvalerate to ... |
74-346 |
1.03e-04 |
|
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: 43.66 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 74 EAVAEMAKEAQAeycDMVVGIGGGKMLDIAKAVAFYAE------------------LPLCVCPTAASMDGPCSAISVLYH 135
Cdd:cd08193 73 EAAVEQAREAGA---DGVIGFGGGSSMDVAKLVALLAGsdqplddiygvgkatgprLPLILVPTTAGTGSEVTPISIVTT 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 136 EDGsfdrylmlEKN--------PDLVVVDTNVVAAAPLRMTVAGMGDALATYFEARScaAAHGANEHGGApghLALVAAR 207
Cdd:cd08193 150 GET--------EKKgvvspqllPDVALLDAELTLGLPPHVTAATGIDAMVHAIEAYT--SRHKKNPISDA---LAREALR 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 208 ACYDTLMECgvaakrdLKKGRTSPAVERLIEcNILLSGVGFESGGLALAHAIA--------------NGLTI-------L 266
Cdd:cd08193 217 LLGANLRRA-------VEDGSDLEAREAMLL-GSMLAGQAFANAPVAAVHALAyplgghfhvphglsNALVLphvlrfnL 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 267 PECKAMHGE---AVAFGLVVQLRLERAPEL-DQVLEFCQRVGLPTTLEELGldeITDADLLSVADATFKNERNMANEQTK 342
Cdd:cd08193 289 PAAEALYAElarALLPGLAFGSDAAAAEAFiDALEELVEASGLPTRLRDVG---VTEEDLPMLAEDAMKQTRLLVNNPRE 365
|
....
gi 1469304371 343 VTRQ 346
Cdd:cd08193 366 VTEE 369
|
|
| Fe-ADH-like |
cd08194 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
72-107 |
1.12e-04 |
|
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: 43.67 E-value: 1.12e-04
10 20 30
....*....|....*....|....*....|....*.
gi 1469304371 72 TEEAVAEMAKEAQAEYCDMVVGIGGGKMLDIAKAVA 107
Cdd:cd08194 65 TDEMVEEGLALYKEGGCDFIVALGGGSPIDTAKAIA 100
|
|
| Fe-ADH-like |
cd08189 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
4-107 |
3.35e-04 |
|
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: 42.07 E-value: 3.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 4 PMVYGGPGRYVQGPGELSRQG--RYLswlgcaayVLFDQGTEDR-LCRQIVDGFLDDDLSepfFKIYNG----PcTEEAV 76
Cdd:cd08189 6 PELFEGAGSLLQLPEALKKLGikRVL--------IVTDKGLVKLgLLDPLLDALKKAGIE---YVVFDGvvpdP-TIDNV 73
|
90 100 110
....*....|....*....|....*....|.
gi 1469304371 77 AEMAKEAQAEYCDMVVGIGGGKMLDIAKAVA 107
Cdd:cd08189 74 EEGLALYKENGCDAIIAIGGGSVIDCAKVIA 104
|
|
| Fe-ADH-like |
cd14866 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
10-338 |
1.60e-03 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341488 [Multi-domain] Cd Length: 384 Bit Score: 39.91 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 10 PGRYVQGPGELSRQGRYLSWLGCAAYVLF---DQGTEDRLCRQIVDGfLDDDLSepffkiynGPCTE----------EAV 76
Cdd:cd14866 5 PLRLFSGRGALARLGRELDRLGARRALVVcgsSVGANPDLMDPVRAA-LGDRLA--------GVFDGvrphspletvEAA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 77 AEMAKEAQAeycDMVVGIGGGKMLDIAKAVA-FYAE--------------------------LPLCVCPTA---ASMDGP 126
Cdd:cd14866 76 AEALREADA---DAVVAVGGGSAIVTARAASiLLAEdrdvrelctrraedglmvsprldapkLPIFVVPTTpttADVKAG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 127 CSAI-SVLYHEDGSFDRYLMleknPDLVVVDTNVVAAAPLRMTVA----GMGDALATYFEARSCAAAHGANEHggapghl 201
Cdd:cd14866 153 SAVTdPPAGQRLALFDPKTR----PAAVFYDPELLATAPASLVAGaamnGFDMAVEGLYSRHADPLADATLMH------- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 202 alvAARACYDTLmecgvaakRDLKKGRTSPAVERLIEcNILLSGVGFESGGLALAHAIANGLTilpeckAMHG------E 275
Cdd:cd14866 222 ---ALRLLADGL--------PRLADDDDPAARADLVL-AAVLAGYGTDHTGGGVIHALGHAIG------ARYGvqngvvH 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 276 AVAFGLVVQLRLERAPE-------------------LDQVLEFCQRV----GLPTTLEELGLDEitdADLLSVADATFKN 332
Cdd:cd14866 284 AILLPHVLRFNAPATDGrldrlaealgvadagdeasAAAVVDAVEALldalGVPTRLRDLGVSR---EDLPAIAEAAMDD 360
|
....*.
gi 1469304371 333 eRNMAN 338
Cdd:cd14866 361 -WFMDN 365
|
|
| Fe-ADH_KdnB-like |
cd08184 |
Iron-containing alcohol dehydrogenase similar to Shewanella oneidensis KdnB required for Kdo8N ... |
10-107 |
3.69e-03 |
|
Iron-containing alcohol dehydrogenase similar to Shewanella oneidensis KdnB required for Kdo8N biosynthesis; This family contains iron-containing alcohol dehydrogenase-like proteins, many of which have not been characterized. Their specific function is unknown. The protein structure represents a dehydroquinate synthase-like fold and belongs to the iron-containing alcohol dehydrogenase-like superfamily. It is distinct from other alcohol dehydrogenases which contain different protein domains. Alcohol dehydrogenase catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron or zinc ions. This family also includes Shewanella oneidensis KdnB which is required for biosynthesis of 8-Amino-3,8-dideoxy-D-manno-octulosonic acid (Kdo8N), a unique amino sugar that has thus far only been observed on the lipopolysaccharides of marine bacteria belonging to the genus Shewanella, and thought to be important for the integrity of the bacterial cell outer membrane. KdnB requires NAD(P) and zinc ion for activity.
Pssm-ID: 341463 [Multi-domain] Cd Length: 348 Bit Score: 38.79 E-value: 3.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469304371 10 PGRYVQGPGELSRQGRYLSWLGCAA--YVLF-------DQGTEDRLCRQIVDGFLDDDLSEPffkiyngPCTEE--AVAE 78
Cdd:cd08184 1 VPKYLFGRGSFDQLGELLAERRKSNndYVVFfiddvfkGKPLLDRLPLQNGDLLIFVDTTDE-------PKTDQidALRA 73
|
90 100
....*....|....*....|....*....
gi 1469304371 79 MAKEAQAEYCDMVVGIGGGKMLDIAKAVA 107
Cdd:cd08184 74 QIRAENDKLPAAVVGIGGGSTMDIAKAVS 102
|
|
| |
