|
Name |
Accession |
Description |
Interval |
E-value |
| gldA |
PRK09423 |
glycerol dehydrogenase; Provisional |
1-364 |
0e+00 |
|
glycerol dehydrogenase; Provisional
Pssm-ID: 181843 Cd Length: 366 Bit Score: 582.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 1 MVTTAIFPSRYVQGKGALTtHLPQELAALGHKALILQDPVVHNTYRDTVATALHGV-IEFDIEVFSSECSDEEIARISAR 79
Cdd:PRK09423 1 MDRIFISPSKYVQGKGALA-RLGEYLKPLGKRALVIADEFVLGIVGDRVEASLKEAgLTVVFEVFNGECSDNEIDRLVAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 80 AQEIGADVIVGMGGGKTLNTAKATGASLRLPIAVVPTLASTDAPCSSLVVIYTPEGKFKRYLMIPRNPTLVLVDSSIIAA 159
Cdd:PRK09423 80 AEENGCDVVIGIGGGKTLDTAKAVADYLGVPVVIVPTIASTDAPTSALSVIYTEEGEFERYLFLPKNPDLVLVDTAIIAK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 160 APVRFLVSGIGDALATWFEAEDCRIKGAGNMTTRPGPMTAFELARFCYTTLMRYGRLAKLACEQHQVTPALEHVIEANTL 239
Cdd:PRK09423 160 APARFLAAGIGDALATWFEARACSRSGGTTMAGGKPTLAALALAELCYETLLEDGLKAKLAVEAKVVTPALENVIEANTL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 240 LSGLGFESGGLAAAHAIHNGLTVLPATHKYWHGEKVAFGTLAMLMLTDRAPELIEEVYQFCEDIGLPTTLADIGLAGVSD 319
Cdd:PRK09423 240 LSGLGFESGGLAAAHAIHNGLTALEDTHHLTHGEKVAFGTLTQLVLENRPKEEIEEVIDFCHAVGLPTTLADLGLKEDSD 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 446180989 320 DELLAVARASCQTGETMHNEPFTITPEAVQAALRAADAVGQARKK 364
Cdd:PRK09423 320 EELRKVAEAACAEGETIHNMPFKVTPEDVAAAILAADAYGQRYKQ 364
|
|
| GlyDH |
cd08170 |
Glycerol dehydrogenases (GlyDH) catalyzes oxidation of glycerol to dihydroxyacetone in ... |
8-357 |
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: 548.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 8 PSRYVQGKGALTtHLPQELAALGHKALILQDPVVHNTYRDTVATALHGV-IEFDIEVFSSECSDEEIARISARAQEIGAD 86
Cdd:cd08170 1 PSRYVQGPGALD-RLGEYLAPLGKKALVIADPFVLDLVGERLEESLEKAgLEVVFEVFGGECSREEIERLAAIARANGAD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 87 VIVGMGGGKTLNTAKATGASLRLPIAVVPTLASTDAPCSSLVVIYTPEGKFKRYLMIPRNPTLVLVDSSIIAAAPVRFLV 166
Cdd:cd08170 80 VVIGIGGGKTIDTAKAVADYLGLPVVIVPTIASTDAPCSALSVIYTEDGEFDEYLFLPRNPDLVLVDTEIIAKAPVRFLV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 167 SGIGDALATWFEAEDCRIKGAGNMTTRPGPMTAFELARFCYTTLMRYGRLAKLACEQHQVTPALEHVIEANTLLSGLGFE 246
Cdd:cd08170 160 AGMGDALATYFEARACARSGAPNMAGGRPTLAALALAELCYDTLLEYGVAAKAAVEAGVVTPALEAVIEANTLLSGLGFE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 247 SGGLAAAHAIHNGLTVLPATHKYWHGEKVAFGTLAMLMLTDRAPELIEEVYQFCEDIGLPTTLADIGLAGVSDDELLAVA 326
Cdd:cd08170 240 SGGLAAAHAIHNGLTALPETHHLLHGEKVAFGTLVQLVLEGRPDEEIEEVIRFCRSVGLPVTLADLGLEDVTDEELRKVA 319
|
330 340 350
....*....|....*....|....*....|.
gi 446180989 327 RASCQTGETMHNEPFTITPEAVQAALRAADA 357
Cdd:cd08170 320 EAACAPGETIHNMPFPVTPEDVVDAILAADA 350
|
|
| GldA |
COG0371 |
Glycerol dehydrogenase or related enzyme, iron-containing ADH family [Energy production and ... |
3-355 |
3.74e-161 |
|
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: 455.39 E-value: 3.74e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 3 TTAIFPSRYVQGKGALTtHLPQELAALGHKALILQDPVVHNTYRDTVATALHGV-IEFDIEVFSSECSDEEIARISARAQ 81
Cdd:COG0371 1 RVIILPRRYVQGEGALD-ELGEYLADLGKRALIITGPTALKAAGDRLEESLEDAgIEVEVEVFGGECSEEEIERLAEEAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 82 EIGADVIVGMGGGKTLNTAKATGASLRLPIAVVPTLASTDAPCSSLVVIYTPEGKFKRYLMIPRNPTLVLVDSSIIAAAP 161
Cdd:COG0371 80 EQGADVIIGVGGGKALDTAKAVAYRLGLPVVSVPTIASTDAPASPLSVIYTEDGAFDGYSFLAKNPDLVLVDTDIIAKAP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 162 VRFLVSGIGDALATWFEAEDCRiKGAGNMTTRPGPMTAFELARFCYTTLMRYGRLAKLACEQHQVTPALEHVIEANTLLS 241
Cdd:COG0371 160 VRLLAAGIGDALAKWYEARDWS-LAHRDLAGEYYTEAAVALARLCAETLLEYGEAAIKAVEAGVVTPALERVVEANLLLS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 242 GLGF----ESGGLAAAHAIHNGLTVLPATHKYWHGEKVAFGTLAMLMLTDRaPELIEEVYQFCEDIGLPTTLADIGLAGV 317
Cdd:COG0371 239 GLAMgigsSRPGSGAAHAIHNGLTALPETHHALHGEKVAFGTLVQLVLEGR-PEEIEELLDFLRSVGLPTTLADLGLDDE 317
|
330 340 350
....*....|....*....|....*....|....*...
gi 446180989 318 SDDELLAVARASCQTGETMHNEPFTITPEAVQAALRAA 355
Cdd:COG0371 318 TEEELLTVAEAARPERYTILNLPFEVTPEAVEAAILAT 355
|
|
| GlyDH-like |
cd08550 |
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins. ... |
8-355 |
3.71e-126 |
|
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: 366.48 E-value: 3.71e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 8 PSRYVQGKGALTtHLPQELAALGHKALILQDPVVHNTYRDTVATALH-GVIEFDIEVFSSECSDEEIARISARAQEIGAD 86
Cdd:cd08550 1 PGRYIQEPGILA-KAGEYIAPLGKKALIIGGKTALEAVGEKLEKSLEeAGIDYEVEVFGGECTEENIERLAEKAKEEGAD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 87 VIVGMGGGKTLNTAKATGASLRLPIAVVPTLASTDAPCSSLVVIYTPEGKFKRYLMIPRNPTLVLVDSSIIAAAPVRFLV 166
Cdd:cd08550 80 VIIGIGGGKVLDTAKAVADRLGLPVVTVPTIAATCAAWSALSVLYDEEGEFLGYSLLKRSPDLVLVDTDIIAAAPVRYLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 167 SGIGDALATWFEAEDCRIKGAGNMTTrpgpMTAFELARFCYTTLMRYGRLAKLACEQHQVTPALEHVIEANTLLSGLGFE 246
Cdd:cd08550 160 AGIGDTLAKWYEARPSSRGGPDDLAL----QAAVQLAKLAYDLLLEYGVQAVEDVRQGKVTPALEDVVDAIILLAGLVGS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 247 SGG----LAAAHAIHNGLTVLPATHKYWHGEKVAFGTLAMLMLTDRAPELIEEVYQFCEDIGLPTTLADIGLaGVSDDEL 322
Cdd:cd08550 236 LGGggcrTAAAHAIHNGLTKLPETHGTLHGEKVAFGLLVQLALEGRSEEEIEELIEFLRRLGLPVTLEDLGL-ELTEEEL 314
|
330 340 350
....*....|....*....|....*....|...
gi 446180989 323 LAVARASCQTGETMHNEPFTITPEAVQAALRAA 355
Cdd:cd08550 315 RKIAEYACDPPDMAHMLPFPVTPEMLAEAILAA 347
|
|
| GlyDH-like |
cd08172 |
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins ... |
8-354 |
1.91e-103 |
|
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: 308.68 E-value: 1.91e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 8 PSRYVQGKGALTtHLPQELAALG-HKALILQDPVVHNTYRDtVATALHgVIEFDIEVFSSECSDEEIARISARAQEIGAD 86
Cdd:cd08172 1 PQEYICEEGALK-ELPELLSEFGiKRPLIIHGEKSWQAAKP-YLPKLF-EIEYPVLRYDGECSYEEIDRLAEEAKEHQAD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 87 VIVGMGGGKTLNTAKATGASLRLPIAVVPTLASTDAPCSSLVVIYTPEGKFKRYLMIPRNPTLVLVDSSIIAAAPVRFLV 166
Cdd:cd08172 78 VIIGIGGGKVLDTAKAVADKLNIPLILIPTLASNCAAWTPLSVIYDEDGEFIGYDYFPRSAYLVLVDPRLLLDSPKDYFV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 167 SGIGDALATWFEAeDCRIKgagNMTTRPGPMT-AFELARFCYTTLMRYGRLAKLACEQHQVTPALEHVIEANTLLSGL-- 243
Cdd:cd08172 158 AGIGDTLAKWYEA-DAILR---QLEELPAFLQlARQAAKLCRDILLKDSEQALADLEAGKLTPAFIKVVETIIALAGMvg 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 244 GF--ESGGLAAAHAIHNGLTVLPATHKYWHGEKVAFGTLAMLMLTDRAPElIEEVYQFCEDIGLPTTLADIGLAGVSDDE 321
Cdd:cd08172 234 GFgdEYGRSAGAHAIHNGLTKLPETHHFLHGEKVAYGILVQLALEGKWDE-IKKLLPFYRRLGLPTSLADLGLTDDTEEA 312
|
330 340 350
....*....|....*....|....*....|...
gi 446180989 322 LLAVARASCQTGETMHNEPFTITPEAVQAALRA 354
Cdd:cd08172 313 LQKIAAFAASPEESIHLLPPDVTAEEVLQAIEK 345
|
|
| GlyDH-like |
cd08171 |
Glycerol dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins ... |
7-355 |
4.21e-70 |
|
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: 223.17 E-value: 4.21e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 7 FPSrYVQGKGALTtHLPQELAALGHKALILQDPVVHNTYRDTVATALHGV-IEF-DIEVFSSECSDEEIARISARAQEIG 84
Cdd:cd08171 1 LPS-YTIGEDAYD-AIPKICSPYGKKVVVIGGKKALAAAKPKLRAALEGSgLEItDFIWYGGEATYENVEKLKANPEVQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 85 ADVIVGMGGGKTLNTAKATGASLRLPIAVVPTLASTDAPCSSLVVIYTPEGKFKRYLMIPRNPTLVLVDSSIIAAAPVRF 164
Cdd:cd08171 79 ADMIFAVGGGKAIDTVKVLADRLNKPVFTFPTIASNCAAVTAVSVMYNPDGSFKEYYFLKRPPVHTFIDTEIIAEAPEKY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 165 LVSGIGDALATWFEAEdcrikgagnMTTRP-----GPMTAFELARFCYTTLMRYGRLAKLACEQHQVTPALEHVIEANTL 239
Cdd:cd08171 159 LWAGIGDTLAKYYEVE---------FSARGdeldhTNALGVAISKMCSEPLLKYGVQALEDCRANKVSDALEQVVLDIIV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 240 LSGL-------GFESGglaAAHAIHNGLTVLPAT-HKYWHGEKVAFGTLAMLMLtDRAPELIEEVYQFCEDIGLPTTLAD 311
Cdd:cd08171 230 TTGLvsnlvepDYNSS---LAHALYYGLTTLPQIeEEHLHGEVVSYGVLVLLTV-DGQFEELEKVYAFNKSIGLPTCLAD 305
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 446180989 312 IGLagvSDDELLAVARASCQTGETMHNePFTITPEAVQAALRAA 355
Cdd:cd08171 306 LGL---TVEDLEKVLDKALKTKDLRHS-PYPITKEMFEEAIKDL 345
|
|
| Fe-ADH |
pfam00465 |
Iron-containing alcohol dehydrogenase; |
8-348 |
2.49e-65 |
|
Iron-containing alcohol dehydrogenase;
Pssm-ID: 425696 [Multi-domain] Cd Length: 362 Bit Score: 211.31 E-value: 2.49e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 8 PSRYVQGKGALTtHLPQELAALGHKALILQDPVVHNT-YRDTVATALHGV-IEFDI-EVFSSECSDEEIARISARAQEIG 84
Cdd:pfam00465 1 PTRIVFGAGALA-ELGEELKRLGARALIVTDPGSLKSgLLDKVLASLEEAgIEVVVfDGVEPEPTLEEVDEAAALAREAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 85 ADVIVGMGGGKTLNTAKATGASL------------------RLPIAVVPTLASTDAPCSSLVVIYTPEGKFKRYLMIPR- 145
Cdd:pfam00465 80 ADVIIAVGGGSVIDTAKAIALLLtnpgdvwdylggkpltkpALPLIAIPTTAGTGSEVTPLAVITDTETGEKLGIFSPKl 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 146 NPTLVLVDSSIIAAAPVRFLVSGIGDALATWFEAEdcrikgagnMTTRPGPMTAfELARFCYTTLMRYGRlakLACEQHQ 225
Cdd:pfam00465 160 LPDLAILDPELTLTLPPRLTAATGMDALAHAVEAY---------VSKGANPLTD-ALALEAIRLIAENLP---RAVADGE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 226 VTPALEHVIEANTlLSGLGFESGGLAAAHAIHNGLT-VLPATHKYWHGEKVAFGT----------LAMLMLT-------D 287
Cdd:pfam00465 227 DLEARENMLLAST-LAGLAFSNAGLGAAHALAHALGgRYGIPHGLANAILLPYVLrfnapaapekLAQLARAlgedsdeE 305
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446180989 288 RAPELIEEVYQFCEDIGLPTTLADIglaGVSDDELLAVARASCQTGeTMHNEPFTITPEAV 348
Cdd:pfam00465 306 AAEEAIEALRELLRELGLPTTLSEL---GVTEEDLDALAEAALRDR-SLANNPRPLTAEDI 362
|
|
| DHQ_Fe-ADH |
cd07766 |
Dehydroquinate synthase-like (DHQ-like) and iron-containing alcohol dehydrogenases (Fe-ADH); ... |
8-330 |
7.34e-55 |
|
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: 181.41 E-value: 7.34e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 8 PSRYVQGKGALTThLPQELAALGHKALILQDPVVHNTYRDTVATALHGVIEFDIEVFSSE-CSDEEIARISARAQEIGAD 86
Cdd:cd07766 1 PTRIVFGEGAIAK-LGEIKRRGFDRALVVSDEGVVKGVGEKVADSLKKGLAVAIFDFVGEnPTFEEVKNAVERARAAEAD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 87 VIVGMGGGKTLNTAKATGASLR--LPIAVVPTLASTDAPCSSLVVIYTPEGKFKRyLMIPRNPTLVLVDSSIIAAAPVRF 164
Cdd:cd07766 80 AVIAVGGGSTLDTAKAVAALLNrgIPFIIVPTTASTDSEVSPKSVITDKGGKNKQ-VGPHYNPDVVFVDTDITKGLPPRQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 165 LVSGIGDALATWFEaedcrikgagnmttrpgpmtafelarfcyttlmrygrlaklaceqhqvtpaLEHVIEANTLLSGLG 244
Cdd:cd07766 159 VASGGVDALAHAVE---------------------------------------------------LEKVVEAATLAGMGL 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 245 FESGGLAAAHAIHNGLTVLpatHKYWHGEKVAFGTLAMLMLTDRAPEL----IEEVYQFCEDIGLPTTLADIglaGVSDD 320
Cdd:cd07766 188 FESPGLGLAHAIGHALTAF---EGIPHGEAVAVGLPYVLKVANDMNPEpeaaIEAVFKFLEDLGLPTHLADL---GVSKE 261
|
330
....*....|
gi 446180989 321 ELLAVARASC 330
Cdd:cd07766 262 DIPKLAEKAL 271
|
|
| PRK10586 |
PRK10586 |
putative oxidoreductase; Provisional |
64-360 |
9.76e-48 |
|
putative oxidoreductase; Provisional
Pssm-ID: 182570 Cd Length: 362 Bit Score: 165.67 E-value: 9.76e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 64 FSSECSDEEIARISARAqeiGAD--VIVGMGGGKTLNTAKATGASLRLPIAVVPTLASTDAPCSSLVVIYTPEGKFKRYL 141
Cdd:PRK10586 67 FRGHCSESDVAQLAAAS---GDDrqVVIGVGGGALLDTAKALARRLGLPFVAIPTIAATCAAWTPLSVWYNDAGQALHFE 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 142 MIPRNPTLVLVDSSIIAAAPVRFLVSGIGDALATWFEAEDCRIK-GAGNMTTRPGPMTAFELArfcyTTLMRYGRLAKLA 220
Cdd:PRK10586 144 IFDDANFLVLVEPRIILNAPQEYLLAGIGDTLAKWYEAVVLAPQpETLPLTVRLGINNALAIR----DVLLNSSEQALAD 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 221 CEQHQVTPALEHVIEA----NTLLSGLGFESGGLAAAHAIHNGLTVLPATHKYWHGEKVAFGTL---AMLMLTDRAPELI 293
Cdd:PRK10586 220 QQNGQLTQDFCDVVDAiiagGGMVGGLGERYTRVAAAHAVHNGLTVLPQTEKFLHGTKVAYGILvqsALLGQDDVLAQLI 299
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446180989 294 EEVYQFcediGLPTTLADIGLAGVSDDELLAVARASCQTGETMHNEPFTITPEAVQAALRAADAVGQ 360
Cdd:PRK10586 300 GAYQRF----HLPTTLAELDVDINNQAEIDRVIAHTLRPVESIHYLPVTLTPDTLRAAFEKVESFKA 362
|
|
| Gro1PDH |
cd08173 |
Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) catalyzes the reversible conversion between ... |
7-354 |
3.44e-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: 109.95 E-value: 3.44e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 7 FPSRYVQGKGALT---THLPQELaaLGHKALILQDPVVHNTYRDTVATAL--HGVIEFDIEVFSSECsDEEIARISARAQ 81
Cdd:cd08173 1 LPRNVVVGHGAINkigEVLKKLL--LGKRALIITGPNTYKIAGKRVEDLLesSGVEVVIVDIATIEE-AAEVEKVKKLIK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 82 EIGADVIVGMGGGKTLNTAKATGASLRLPIAVVPTLASTDAPCSSLVVIytpEGKFKRYLMIPRNPTLVLVDSSIIAAAP 161
Cdd:cd08173 78 ESKADFIIGVGGGKVIDVAKYAAYKLNLPFISIPTSASHDGIASPFASI---KGGDKPYSIKAKAPIAIIADTEIISKAP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 162 VRFLVSGIGDALAT------WFEAEdcRIKGA--GNmttrpgpmTAFELARFCYTTLMRYGRLAKlaceqhqvtPALEHV 233
Cdd:cd08173 155 KRLLAAGCGDLISNitavkdWRLAH--RLKGEyySE--------YAASLALMSAKLIIENADLIK---------PGLEEG 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 234 IEanTLLSGLGfeSGGLAAA----------------HAIHNgLTVLPAThkywHGEKVAFGTLAMLMLTDRAPELIEEVY 297
Cdd:cd08173 216 VR--TVVKALI--SSGVAMSiagssrpasgsehlfsHALDK-LAPGPAL----HGEQCGVGTIMMAYLHGGDWKEIREAL 286
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446180989 298 qfcEDIGLPTTLADIGLagvsDDELLAVARASCQtgeTMHNEPFTI------TPEAVQAALRA 354
Cdd:cd08173 287 ---KKIGAPTTAKELGL----DKEIIIEALTIAH---KIRPERYTIlgdnglTEEAAERLARI 339
|
|
| G1PDH-like |
cd08174 |
Glycerol-1-phosphate dehydrogenase-like; These glycerol-1-phosphate dehydrogenase-like ... |
14-314 |
8.49e-26 |
|
Glycerol-1-phosphate dehydrogenase-like; These glycerol-1-phosphate dehydrogenase-like proteins have not been characterized. The protein sequences have high similarity with that of glycerol-1-phosphate dehydrogenase (G1PDH) which plays a role in the synthesis of phosphoglycerolipids in Gram-positive bacterial species. It catalyzes the reversibly reduction of dihydroxyacetone phosphate (DHAP) to glycerol-1-phosphate (G1P) in a NADH-dependent manner. Its activity requires Ni++ ion.
Pssm-ID: 341453 [Multi-domain] Cd Length: 332 Bit Score: 105.68 E-value: 8.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 14 GKGALTtHLPQELAAL---GHKALILQDPVVHNTYRDTVATALHGVIEFDIEVFSSECSDEEIARISARAQEIgaDVIVG 90
Cdd:cd08174 7 EEGALE-HLGKYLADRnqgFGKVAIVTGEGIDELLGEDILESLEEAGEIVTVEENTDNSAEELAEKAFSLPKV--DAIVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 91 MGGGKTLNTAKATGASLRLPIAVVPTLASTDAPCSSLVVIYTpEGKFKRYlmiP-RNPTLVLVDSSIIAAAPVRFLVSGI 169
Cdd:cd08174 84 IGGGKVLDVAKYAAFLSKLPFISVPTSLSNDGIASPVAVLKV-DGKRKSL---GaKMPYGVIVDLDVIKSAPRRLILAGI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 170 GD------ALATWFEAedCRIKGAgnmttrpgPMTAFE--LARFCYTTLMRYgRLAKLACEQHqvtpaLEHVIEAnTLLS 241
Cdd:cd08174 160 GDlisnitALYDWKLA--EEKGGE--------PVDDFAylLSRTAADSLLNT-PGKDIKDDEF-----LKELAES-LVLS 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 242 GLGFE--------SGglaAAHAIHNGLTVLpATHKYWHGEKVAFGTLAMLMLTDRAPELIEEVYQfceDIGLPTTLADIG 313
Cdd:cd08174 223 GIAMEiagssrpaSG---SEHLISHALDKL-FPGPALHGIQVGLGTYFMSFLQGQRYEEIRDVLK---RTGFPLNPSDLG 295
|
.
gi 446180989 314 L 314
Cdd:cd08174 296 L 296
|
|
| EutG |
COG1454 |
Alcohol dehydrogenase, class IV [Energy production and conversion]; |
1-355 |
8.88e-26 |
|
Alcohol dehydrogenase, class IV [Energy production and conversion];
Pssm-ID: 441063 [Multi-domain] Cd Length: 381 Bit Score: 106.74 E-value: 8.88e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 1 MVTTAIFPSRYVQGKGALTtHLPQELAALG-HKALILQDPVVHNT-YRDTVATAL--HGViefDIEVFS---SECSDEEI 73
Cdd:COG1454 1 MMFTFRLPTRIVFGAGALA-ELGEELKRLGaKRALIVTDPGLAKLgLLDRVLDALeaAGI---EVVVFDdvePNPTVETV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 74 ARISARAQEIGADVIVGMGGGKTLNTAKATGASL------------------RLPIAVVPTLASTDAPCSSLVVIYTPEG 135
Cdd:COG1454 77 EAGAAAAREFGADVVIALGGGSAIDAAKAIALLAtnpgdledylgikkvpgpPLPLIAIPTTAGTGSEVTPFAVITDPET 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 136 KFKRYLMIPRN-PTLVLVDSSIIAAAPVRFLV-SGIgDALATWFEAEdcrikgagnMTTRPGPMT------AFELarfcy 207
Cdd:COG1454 157 GVKKGIADPELlPDVAILDPELTLTLPPSLTAaTGM-DALTHAIEAY---------VSKGANPLTdalaleAIRL----- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 208 ttLMRYgrLAKlACEQHQVTPALEHVIEANTlLSGLGFESGGLAAAHA----------IHNGLT---VLPATHKY---WH 271
Cdd:COG1454 222 --IARN--LPR-AVADGDDLEAREKMALASL-LAGMAFANAGLGAVHAlahplgglfhVPHGLAnaiLLPHVLRFnapAA 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 272 GEKVA-----FGTLAMLMLTDRAPELIEEVYQFCEDIGLPTTLADIglaGVSDDELLAVARASCQTGETMHNePFTITPE 346
Cdd:COG1454 296 PERYAeiaraLGLDVGLSDEEAAEALIEAIRELLRDLGIPTRLSEL---GVTEEDLPELAELALADRCLANN-PRPLTEE 371
|
....*....
gi 446180989 347 AVQAALRAA 355
Cdd:COG1454 372 DIEAILRAA 380
|
|
| Fe-ADH |
cd08551 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains large ... |
8-350 |
3.80e-25 |
|
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: 104.84 E-value: 3.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 8 PSRYVQGKGALTtHLPQELAALG-HKALILQDPVVHNT-YRDTVATALHGViEFDIEVFS---SECSDEEIARISARAQE 82
Cdd:cd08551 1 PTRIVFGAGALA-RLGEELKALGgKKVLLVTDPGLVKAgLLDKVLESLKAA-GIEVEVFDdvePNPTVETVEAAAELARE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 83 IGADVIVGMGGGKTLNTAKATGASL------------------RLPIAVVPTLASTDAPCSSLVVIYTPEGKFKRYLMIP 144
Cdd:cd08551 79 EGADLVIAVGGGSVLDTAKAIAVLAtnggsirdyegigkvpkpGLPLIAIPTTAGTGSEVTPNAVITDPETGRKMGIVSP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 145 RN-PTLVLVDSSIIAAAPVRFLVS-GIgDALATWFEAedcrikgagnMTTRPG-PMT---AFELARFCYTTLmrygrlaK 218
Cdd:cd08551 159 YLlPDVAILDPELTLSLPPSVTAAtGM-DALTHAIEA----------YTSKKAnPISdalALEAIRLIGKNL-------R 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 219 LACEQHQVTPALEHVIEAnTLLSGLGFESGGLAAAHAI-----------H---NGLtVLPATHKY---WHGEK-----VA 276
Cdd:cd08551 221 RAVADGSDLEAREAMLLA-SLLAGIAFGNAGLGAVHALayplggryhipHgvaNAI-LLPYVMEFnlpACPEKyaeiaEA 298
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446180989 277 FGTLAMLMLTDRAPE-LIEEVYQFCEDIGLPTTLADIglaGVSDDELLAVARASCQTGETMHNEPFTITPEAVQA 350
Cdd:cd08551 299 LGEDVEGLSDEEAAEaAVEAVRELLRDLGIPTSLSEL---GVTEEDIPELAEDAMKSGRLLSNNPRPLTEEDIRE 370
|
|
| Fe-ADH-like |
cd08191 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
8-355 |
5.77e-24 |
|
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: 101.54 E-value: 5.77e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 8 PSRYVQGKGALTtHLPQELAALGHKALILQDPVVHNTYRDTVATALHGVIEFDIEVFSSECSD---EEIARISARAQEIG 84
Cdd:cd08191 4 PSRLLFGPGARR-ALGRVAARLGSRVLIVTDPRLASTPLVAELLAALTAAGVAVEVFDGGQPElpvSTVADAAAAARAFD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 85 ADVIVGMGGGKTLNTAKATGASLR------------------LPIAVVPTLASTDAPCSSLVVIYTPEGKFKRYLMIPR- 145
Cdd:cd08191 83 PDVVIGLGGGSNMDLAKVVALLLAhggdprdyygedrvpgpvLPLIAVPTTAGTGSEVTPVAVLTDPARGMKVGVSSPYl 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 146 NPTLVLVDSSIIAAAPVRFLV-SGIgDALATWFEAEDCRIKgagNMTTRPGPMTAFE----LAR-FCYTTLMRYGRLAKL 219
Cdd:cd08191 163 RPAVAIVDPELTLTCPPGVTAdSGI-DALTHAIESYTARDF---PPFPRLDPDPVYVgknpLTDlLALEAIRLIGRHLPR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 220 ACEQHQVTPALEHVIEAnTLLSGLGFESGGLAAAHAI-----------H---NGLtVLPATHKYWHGEKVA-FGTLAMLM 284
Cdd:cd08191 239 AVRDGDDLEARSGMALA-ALLAGLAFGTAGTAAAHALqypigalthtsHgvgNGL-LLPYVMRFNRPARAAeLAEIARAL 316
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446180989 285 L-------TDRAPELIEEVYQFCEDIGLPTTLADIglaGVSDDELLAVARASCQTGETMHNEPFTITPEAVQAALRAA 355
Cdd:cd08191 317 GvttagtsEEAADRAIERVEELLARIGIPTTLADL---GVTEADLPGLAEKALSVTRLIANNPRPPTEEDLLRILRAA 391
|
|
| Fe-ADH_2 |
pfam13685 |
Iron-containing alcohol dehydrogenase; |
14-276 |
1.09e-19 |
|
Iron-containing alcohol dehydrogenase;
Pssm-ID: 404557 [Multi-domain] Cd Length: 251 Bit Score: 87.36 E-value: 1.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 14 GKGALTtHLPQELAALG-HKALILQDPVVHNTYRDTVATALHGvIEFDIEVFSSECSD---EEIARISARAQEIGADVIV 89
Cdd:pfam13685 3 GPGALG-RLGEYLAELGfRRVALVADANTYAAAGRKVAESLKR-AGIEVETRLEVAGNadmETAEKLVGALRERDADAVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 90 GMGGGKTLNTAKATGASLRLPIAVVPTLASTDAPCSSLVVIyTPEGKFKRylmIPRN-PTLVLVDSSIIAAAPVRFLVSG 168
Cdd:pfam13685 81 GVGGGTVIDLAKYAAFKLGKPFISVPTAASNDGFASPGASL-TVDGKKRS---IPAAaPFGVIADTDVIAAAPRRLLASG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 169 IGDALATWFEAEDCRIKGAGnmttrpgpMTAFELARFCYTTLMRYgrlAKLACEQHQVTPALEHVIEANTlLSGLGFESG 248
Cdd:pfam13685 157 VGDLLAKITAVADWELAHAE--------EVAAPLALLSAAMVMNF---ADRPLRDPGDIEALAELLSALA-MGGAGSSRP 224
|
250 260
....*....|....*....|....*...
gi 446180989 249 GLAAAHAIHNGLTVLPATHKYwHGEKVA 276
Cdd:pfam13685 225 ASGSEHLISHALDMIAPKQAL-HGEQVG 251
|
|
| egsA |
PRK00843 |
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed |
7-353 |
4.69e-17 |
|
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed
Pssm-ID: 179139 Cd Length: 350 Bit Score: 81.09 E-value: 4.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 7 FPSRYVQGKGAL--TTHLPQELAaLGHKALILQDPVVHNTYRDTVATALHGviEFDIEVF-SSECSDEEIARISARAQEI 83
Cdd:PRK00843 10 LPRDVVVGHGVLddIGDVCSDLK-LTGRALIVTGPTTKKIAGDRVEENLED--AGDVEVViVDEATMEEVEKVEEKAKDV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 84 GADVIVGMGGGKTLNTAKATGASLRLPIAVVPTLASTDAPCSSLVVIytPEGKfKRYLMIPRNPTLVLVDSSIIAAAPVR 163
Cdd:PRK00843 87 NAGFLIGVGGGKVIDVAKLAAYRLGIPFISVPTAASHDGIASPRASI--KGGG-KPVSVKAKPPLAVIADTEIIAKAPYR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 164 FLVSGIGD------ALATWFEAEdcRIKG------AGNMTTrpgpMTAFElarfcyttLMRYGRLAKLACEQhqvtpALE 231
Cdd:PRK00843 164 LLAAGCGDiisnytAVKDWRLAH--RLRGeyyseyAAALSL----MTAKM--------LIENADIIKPGLEE-----SAR 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 232 HVIEAntLLSglgfeSG---GLAA------------AHAIHngltvLPATHKYWHGEKVAFGTLAMLMLTDRAPELIEEV 296
Cdd:PRK00843 225 LVVKA--LIS-----SGvamSIAGssrpasgsehlfSHALD-----RLAPGPALHGEQCGVGTIIMMYLHGGDWRKIRDA 292
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446180989 297 YQfceDIGLPTTLADIGLagvsDDELLAVARASCQtgeTMHNEPFTI------TPEAVQAALR 353
Cdd:PRK00843 293 LK---KIGAPTTAKELGI----DDEYIIEALTIAH---TIRPERYTIlgdrglTREAAEKAAR 345
|
|
| BDH |
cd08187 |
Butanol dehydrogenase catalyzes the conversion of butyraldehyde to butanol with the cofactor ... |
8-353 |
7.55e-17 |
|
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: 80.94 E-value: 7.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 8 PSRYVQGKGALTtHLPQELAALGHKALIL--QDPVVHNTYRDTVATALHgviEFDIEVFssECS-------DEEIARISA 78
Cdd:cd08187 7 PTKIIFGKGAIE-ELGEEIKKYGKKVLLVygGGSIKKNGLYDRVVASLK---EAGIEVV--EFGgvepnprLETVREGIE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 79 RAQEIGADVIVGMGGGKTLNTAKATGASLR------------------LPIAVVPTLASTDAPCSSLVVIYTPEGKFKRY 140
Cdd:cd08187 81 LAREENVDFILAVGGGSVIDAAKAIAAGAKydgdvwdfftgkappekaLPVGTVLTLAATGSEMNGGAVITNEETKEKLG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 141 ----LMIPR----NPTLVLvdsSIiaaaPVRFLVSGIGDALATWFEaedcrikgaGNMTTRPG-PMTafelARFCYT--- 208
Cdd:cd08187 161 fgspLLRPKfsilDPELTY---TL----PKYQTAAGIVDIFSHVLE---------QYFTGTEDaPLQ----DRLAEGllr 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 209 TLMRYGRLAKL------ACEQHQVTPALEHvieaNTLLsGLGFESGglAAAHAI-HN-----------GLTVL-PATHKY 269
Cdd:cd08187 221 TVIENGPKALKdpddyeARANLMWAATLAL----NGLL-GAGRGGD--WATHAIeHElsalydithgaGLAIVfPAWMRY 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 270 WHGEKVA---------FGTLAMLMLTDRAPELIEEVYQFCEDIGLPTTLADIglaGVSDDELLAVARASCQTGETMHNEP 340
Cdd:cd08187 294 VLKKKPErfaqfarrvFGIDPGGDDEETALEGIEALEEFFKSIGLPTTLSEL---GIDEEDIEEMAEKAVRGGGLGGGFK 370
|
410
....*....|...
gi 446180989 341 fTITPEAVQAALR 353
Cdd:cd08187 371 -PLTREDIEEILK 382
|
|
| Fe-ADH-like |
cd08196 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
8-348 |
1.77e-16 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341475 [Multi-domain] Cd Length: 367 Bit Score: 79.93 E-value: 1.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 8 PSRYVQGKGALTThLPQELAALG-HKALILQDPVVH-NTYRDTVATALHGVIefdIEVFS---SECSDEEIARISARAQE 82
Cdd:cd08196 6 PVKIIFGEGILKE-LPDIIKELGgKRGLLVTDPSFIkSGLAKRIVESLKGRI---VAVFSdvePNPTVENVDKCARLARE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 83 IGADVIVGMGGGKTLNTAKA------TGASLR-------------LPIAVVPTLASTDAPCSSLVVIYTPEGKFKRYLMI 143
Cdd:cd08196 82 NGADFVIAIGGGSVLDTAKAaaclakTDGSIEdylegkkkipkkgLPLIAIPTTAGTGSEVTPVAVLTDKEKGKKAPLVS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 144 PR-NPTLVLVDSSI-------IAAApvrflvSGIgDALATWFEAedcrIKGAGNMttrpgPMT---AFELARFCYTTLMR 212
Cdd:cd08196 162 PGfYPDIAIVDPELtysmppkVTAS------TGI-DALCHAIEA----YWSINHQ-----PISdalALEAAKLVLENLEK 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 213 ygrlaklACEQHQVTPALEHVIEAnTLLSGLGFESGGLAAAHAIHNGLTvlpathKYW---HGEKVAFgTLAMLM----- 284
Cdd:cd08196 226 -------AYNNPNDKEAREKMALA-SLLAGLAFSQTRTTASHACSYPLT------SHFgipHGEACAL-TLPSFIrlnae 290
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446180989 285 -LTDR------------APELIEEVYQFCEDIGLPTTLADIglaGVSDDELLAVARASCQTgETMHNEPFTITPEAV 348
Cdd:cd08196 291 aLPGRldelakqlgfkdAEELADKIEELKKRIGLRTRLSEL---GITEEDLEEIVEESFHP-NRANNNPVEVTKEDL 363
|
|
| Fe-ADH-like |
cd14864 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
7-328 |
3.25e-16 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341486 [Multi-domain] Cd Length: 376 Bit Score: 78.88 E-value: 3.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 7 FPSRYVQGKGALTtHLPQELAALGHKALILQDPVVHNTYR-DTVATALH----GVIEFDieVFSSECSDEEIARISARAQ 81
Cdd:cd14864 3 IPPNIVFGADSLE-RIGEEVKEYGSRFLLITDPVLKESGLaDKIVSSLEkagiSVIVFD--EIPASATSDTIDEAAELAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 82 EIGADVIVGMGGGKTLNTAKATGASLR------------------LPIAVVPTLASTDAPCSSLVVIYTPEGKFKRYLMI 143
Cdd:cd14864 80 KAGADGIIAVGGGKVLDTAKAVAILANndggaydflegakpkkkpLPLIAVPTTPRSGFEFSDRFPVVDSRSREVKLLKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 144 PRN-PTLVLVDSSIIAAAPVRFLVSGIGDALATWFEAEDCRikgAGNMTTRPGPMTAFELARfcyttlmryGRLAKlACE 222
Cdd:cd14864 160 QPGlPKAVIVDPNLMASLTGNQTAAMALAALALAVEAYLSK---KSNFFSDALALKAIELVS---------ENLDG-ALA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 223 QHQVTPALEHVIEANtLLSGLGFESGGL----AAAHAIhNGLT----------VLPATHKYWHGEKVAF-GTLAMLMLTD 287
Cdd:cd14864 227 DPKNTPAEELLAQAG-CLAGLAASSSSPglatALALAV-NSRYkvskslvasiLLPHVIEYAATSAPDKyAKIARALGED 304
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 446180989 288 R--------APELIEEVYQFCEDIGLPTTLADIGLAgVSDDELLAVARA 328
Cdd:cd14864 305 VegaspeeaAIAAVEGVRRLIAQLNLPTRLKDLDLA-SSLEQLAAIAED 352
|
|
| G1PDH_related |
cd08549 |
Glycerol-1-phosphate dehydrogenase and related proteins; This family contains bacterial and ... |
69-314 |
4.49e-13 |
|
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: 69.52 E-value: 4.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 69 SDEEIARISARAQEIGA-DVIVGMGGGKTLNTAKATGASLRLPIAVVPTLASTDAPCSSLVVIYTPEgkfKRYLMIPRNP 147
Cdd:cd08549 54 YYDNIDNLEDELKKYTFyDCVIGIGGGRSIDTGKYLAYKLKIPFISVPTSASNDGIASPIVSLRIPG---VKKTFMADAP 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 148 TLVLVDSSIIAAAPVRFLVSGIGD------ALATWfeaedcriKGAGNMTTRPGPMTAFELARFCYTTLMRYGRLAKLAC 221
Cdd:cd08549 131 IAIIADTEIIKKSPRRLLSAGIGDlvsnitAVLDW--------KLAHKEKGEKYSEFAAILSKTSAKELVSYVLKASDLE 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 222 EQHQVTpaLEHVIEANTLLSGLGFESGGLAAAHAIHNGLTVLPATHKY---WHGEKVAFGTLAMLMLTDRAPELI----E 294
Cdd:cd08549 203 EYHRVL--VKALVGSGIAMAIAGSSRPASGSEHLFSHALDKLKEEYLNinvLHGEQVGVGTIIMSYLHEKENKKLsglhE 280
|
250 260
....*....|....*....|
gi 446180989 295 EVYQFCEDIGLPTTLADIGL 314
Cdd:cd08549 281 RIKMILKKVGAPTTAKQLGI 300
|
|
| Fe-ADH-like |
cd14862 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
3-324 |
8.80e-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: 341484 [Multi-domain] Cd Length: 375 Bit Score: 68.79 E-value: 8.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 3 TTAIFPSRYVQGKGALTtHLPQelaALGHKALILQDPVVHNT-YRDTVATALHGViEFDIEVFS---SECSDEEIARISA 78
Cdd:cd14862 1 MWYFSSPKIVFGEDALS-HLEQ---LSGKRALIVTDKVLVKLgLLKKVLKRLLQA-GFEVEVFDevePEPPLETVLKGAE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 79 RAQEIGADVIVGMGGGKTLNTAKATGASLRLP--------------------IAVVPTLASTDAPCSSLVVIyTPEGKFK 138
Cdd:cd14862 76 AMREFEPDLIIALGGGSVMDAAKAAWVLYERPdldpedispldllglrkkakLIAIPTTSGTGSEATWAIVL-TDTEEPR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 139 RYLMIPRN--PTLVLVDSSIIAAAPvRFLVSGIG-DALAtwfEAEDCRIKGAGNmttrpgPMT---AFELARFCYTTLMR 212
Cdd:cd14862 155 KIAVANPElvPDVAILDPEFVLGMP-PKLTAGTGlDALA---HAVEAYLSTWSN------DFSdalALKAIELIFKYLPR 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 213 ygrlaklACEQHQVTPALEHVIEANTlLSGLGFESGGLAAAHA----------IHNGLTV---LPATHKYWhgEKVAFGT 279
Cdd:cd14862 225 -------AYKDGDDLEAREKMHNAAT-IAGLAFGNSQAGLAHAlghslgavfhVPHGIAVglfLPYVIEFY--AKVTDER 294
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 446180989 280 LAMLMLTD--------RAPELIEEVYQFCEDIGLPTTLADiglAGVSDDELLA 324
Cdd:cd14862 295 YDLLKLLGieardeeeALKKLVEAIRELYKEVGQPLSIKD---LGISEEEFEE 344
|
|
| Fe-ADH-like |
cd14863 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
14-355 |
2.34e-12 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341485 [Multi-domain] Cd Length: 380 Bit Score: 67.56 E-value: 2.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 14 GKGALTThLPQELAALG-HKALILQDPVVHNT-YRDTVATAL----HGVIEFDieVFSSECSDEEIARISARAQEIGADV 87
Cdd:cd14863 11 GAGAVEQ-IGELLKELGcKKVLLVTDKGLKKAgIVDKIIDLLeeagIEVVVFD--DVEPDPPDEIVDEAAEIAREEGADG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 88 IVGMGGGKTLNTAKATGASL-------------------RLPIAVVPTLASTDAPCSSLVVIYTPEGKFKRYLMIPR-NP 147
Cdd:cd14863 88 VIGIGGGSVLDTAKAIAVLLtnpgpiidyalagppvpkpGIPLIAIPTTAGTGSEVTPIAVITDEENGVKKSLLGPFlVP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 148 TLVLVDSSIIAAAPVRFLVS-GIgDALATWFEAEdcrikgagnMTTRPGPMT---AFELARFCYTTLMRygrlaklACEQ 223
Cdd:cd14863 168 DLAILDPELTVGLPPSLTAAtGM-DALSHAIEAY---------TSKLANPMTdalALQAIRLIVKNLPR-------AVKD 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 224 HQVTPALEHVIEANTlLSGLGFESGGLAAAHAI-HngltVLPATHKYWHGEKVAFGTLAML------------------- 283
Cdd:cd14863 231 GDNLEARENMLLASN-LAGIAFNNAGTHIGHAIaH----ALGALYHIPHGLACALALPVVLefnaeaypekvkkiakalg 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 284 -MLTDRAPE-----LIEEVYQFCEDIGLPTTLADIGLagvSDDELLAVARAscqtgetMHNE------PFTITPEAVQAA 351
Cdd:cd14863 306 vSFPGESDEelgeaVADAIREFMKELGIPSLFEDYGI---DKEDLDKIAEA-------VLKDpfamfnPRPITEEEVAEI 375
|
....
gi 446180989 352 LRAA 355
Cdd:cd14863 376 LEAI 379
|
|
| LPO |
cd08176 |
Lactadehyde:propanediol oxidoreductase (LPO) catalyzes the interconversion between ... |
6-314 |
3.53e-12 |
|
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: 66.80 E-value: 3.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 6 IFPSRYVQGKGALTtHLPQELAALG-HKALILQDPVVHNTyrdTVATALHGVIE---FDIEVFS---SECSDEEIARISA 78
Cdd:cd08176 4 VLNPTSYFGWGAIE-EIGEEAKKRGfKKALIVTDKGLVKF---GIVDKVTDVLKeagIAYTVFDevkPNPTIENVMAGVA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 79 RAQEIGADVIVGMGGGKTLNTAKATGA----------SLR---------LPIAVVPTLASTDAPCSSLVVIYTPEGKFKR 139
Cdd:cd08176 80 AYKESGADGIIAVGGGSSIDTAKAIGIivanpgadvrSLEgvaptknpaVPIIAVPTTAGTGSEVTINYVITDTEKKRKF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 140 YLMIPR-NPTLVLVDSSIIAAAPvRFLVSGIG-DALATWFEaedcrikgaGNMTTRPGPMT-AFELarfcYTTLMRYGRL 216
Cdd:cd08176 160 VCVDPHdIPTVAIVDPDLMSSMP-KGLTAATGmDALTHAIE---------GYITKGAWELSdMLAL----KAIELIAKNL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 217 AKlACEQHQVTPALEHVIEANTlLSGLGFESGGL----AAAHA------IHNGLT---VLPATHKY---WHGEK-----V 275
Cdd:cd08176 226 RK-AVANPNNVEARENMALAQY-IAGMAFSNVGLgivhSMAHPlsafydTPHGVAnaiLLPYVMEFnapATGEKyrdiaR 303
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 446180989 276 AFG-TLAMLMLTDRAPELIEEVYQFCEDIGLPTTLADIGL 314
Cdd:cd08176 304 AMGvDTTGMSDEEAAEAAVDAVKKLSKDVGIPQKLSELGV 343
|
|
| Fe-ADH-like |
cd14865 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
8-355 |
1.44e-11 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341487 [Multi-domain] Cd Length: 383 Bit Score: 65.26 E-value: 1.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 8 PSRYVQGKGALTtHLPQELAALG-HKALILQDPVVHNT-YRDTVATALHGVIEfDIEVFS---SECSDEEIARISARAQE 82
Cdd:cd14865 6 PTKIVSGAGALE-NLPAELARLGaRRPLIVTDKGLAAAgLLKKVEDALGDAIE-IVGVFDdvpPDSSVAVVNEAAARARE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 83 IGADVIVGMGGGKTLNTAKATGASL-------------------RLPIAVVPTLASTDAPCSSLVVIYTPEGKFK----- 138
Cdd:cd14865 84 AGADGIIAVGGGSVIDTAKGVNILLseggddlddygganrltrpLKPLIAIPTTAGTGSEVTLVAVIKDEEKKVKllfvs 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 139 RYLMiprnPTLVLVDSSIIAAAPVRfLVSGIG-DALATWFEAEDCRIKgagnmttrpGPMT---AFELARFCYTTLMRyg 214
Cdd:cd14865 164 PFLL----PDVAILDPRLTLSLPPK-LTAATGmDALTHAIEAYTSLQK---------NPISdalALQAIRLISENLPK-- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 215 rlaklACEQHQVTPALEHVIEANTlLSGLGFESGGLAAAHAI----------HNGLT---VLPATHKYwHGEKVA--FGT 279
Cdd:cd14865 228 -----AVKNGKDLEARLALAIAAT-MAGIAFSNSMVGLVHAIahavgavagvPHGLAnsiLLPHVMRY-NLDAAAerYAE 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 280 LAMLMLT------DRAPELIEEVY----QFCEDIGLPTTLADiglAGVSDDELLAVARASCQTGETMHNePFTITPEAVQ 349
Cdd:cd14865 301 LALALAYgvtpagRRAEEAIEAAIdlvrRLHELCGLPTRLRD---VGVPEEQLEAIAELALNDGAILFN-PREVDPEDIL 376
|
....*.
gi 446180989 350 AALRAA 355
Cdd:cd14865 377 AILEAA 382
|
|
| Fe-ADH-like |
cd08183 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
8-353 |
2.99e-11 |
|
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: 64.06 E-value: 2.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 8 PSRYVQGKGALTThLPQELAALGHKALilqdpVVH-----NTYR-DTVATALHGV-IEFDIEVFSSECSDEEIARISARA 80
Cdd:cd08183 1 PPRIVFGRGSLQE-LGELAAELGKRAL-----LVTgrsslRSGRlARLLEALEAAgIEVALFSVSGEPTVETVDAAVALA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 81 QEIGADVIVGMGGGKTLNTAKATGASLR----------------------LPIAVVPTLASTDAPCSSLVVIYTPEGKFK 138
Cdd:cd08183 75 REAGCDVVIAIGGGSVIDAAKAIAALLTnegsvldylevvgkgrplteppLPFIAIPTTAGTGSEVTKNAVLSSPEHGVK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 139 RYL----MIPRnptLVLVDSSIIAAAPVRFLV-SGIgDALATWFEAEDCRikgagnmttRPGPMT---AFELARFCYTTL 210
Cdd:cd08183 155 VSLrspsMLPD---VALVDPELTLSLPPEVTAaSGL-DALTQLIEPYVSR---------KANPLTdalAREGLRLAARSL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 211 MRygrlaklACEQHQVTPALEHVIEAnTLLSGLGFESGGLAAAHA----------IHNGL---TVLPAT---------HK 268
Cdd:cd08183 222 RR-------AYEDGEDLEAREDMALA-SLLGGLALANAGLGAVHGlagplggmfgAPHGAicaALLPPVleanlralrER 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 269 YWHGEKVAFGTLAMLMLT----DRAPELIEEVYQFCEDIGLPtTLADIGLagvSDDELLAVARAScQTGETMHNEPFTIT 344
Cdd:cd08183 294 EPDSPALARYRELAGILTgdpdAAAEDGVEWLEELCEELGIP-RLSEYGL---TEEDFPEIVEKA-RGSSSMKGNPIELS 368
|
....*....
gi 446180989 345 PEAVQAALR 353
Cdd:cd08183 369 DEELLEILE 377
|
|
| NADPH_BDH |
cd08179 |
NADPH-dependent butanol dehydrogenase involved in the butanol and ethanol formation pathway in ... |
8-355 |
1.53e-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: 1.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 8 PSRYVQGKGALtthlpQELAAL-GHKALILQDPVV--HNTYRDTVATALHGViEFDIEVFS---SECSDEEIARISARAQ 81
Cdd:cd08179 5 PRDIYFGEGAL-----EYLKTLkGKRAFIVTGGGSmkRNGFLDKVEDYLKEA-GMEVKVFEgvePDPSVETVEKGAEAMR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 82 EIGADVIVGMGGGKTLNTAKA----------TGASLRLPIAV-----------VPTLASTDAPCSSLVVIYTPEGKFKRY 140
Cdd:cd08179 79 EFEPDWIIAIGGGSVIDAAKAmwvfyeypelTFEDALVPFPLpelrkkarfiaIPSTSGTGSEVTRASVITDTEKGIKYP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 141 LMIPRN-PTLVLVDSSIIAAAPvRFLVSGIG-DALATWFEAedcrikgagNMTTRPGPMTAFeLARFCYTTLMRYgrLAK 218
Cdd:cd08179 159 LASFEItPDVAILDPELTMTMP-PHVTANTGmDALTHAIEA---------YVSTLANDFTDA-LALGAILDIFEN--LPK 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 219 lACEQHQVTPALEHVIEANTlLSGLGFESGGLAAAHAI-----------HnGLT---VLPATHKYWHGEKVAFGTLAMLM 284
Cdd:cd08179 226 -SYNGGKDLEAREKMHNASC-LAGMAFSNSGLGIVHSMahkggaffgipH-GLAnaiLLPYVIEFNSKDPEARARYAALL 302
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446180989 285 --LTDR--APELIEEVYQFCEDIGLPTTLADiglAGVSDDELLA----VARASCQTGETMHNePFTITPEAVQAALRAA 355
Cdd:cd08179 303 igLTDEelVEDLIEAIEELNKKLGIPLSFKE---AGIDEDEFFAkldeMAENAMNDACTGTN-PRKPTVEEMKELLKAA 377
|
|
| HEPD |
cd08182 |
Hydroxyethylphosphoate dehydrogenase (HEPD) catalyzes the reduction of phosphonoacetaldehyde ... |
8-353 |
1.65e-09 |
|
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: 58.78 E-value: 1.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 8 PSRYVQGKGALTtHLPQELAALGHK--ALILQDPVVHNTYRDTVATALHGviEFDIEVFSSECSD---EEIARISARAQE 82
Cdd:cd08182 1 PVKIIFGPGALA-ELKDLLGGLGARrvLLVTGPSAVRESGAADILDALGG--RIPVVVFSDFSPNpdlEDLERGIELFRE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 83 IGADVIVGMGGGKTLNTAKATGASL--------------------RLPIAVVPTLASTDAPCSSLVVIYTPEGKFKRYLM 142
Cdd:cd08182 78 SGPDVIIAVGGGSVIDTAKAIAALLgspgenllllrtgekapeenALPLIAIPTTAGTGSEVTPFATIWDEAEGKKYSLA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 143 IPRN-PTLVLVDSSIIAAAPVRFLVSGIGDALATWFEAedcrI--KGAGNMTTRpgpmtafeLARFCYTTLMRYgrLAKL 219
Cdd:cd08182 158 HPSLyPDAAILDPELTLSLPLYLTASTGLDALSHAIES----IwsVNANPESRA--------YALRAIRLILEN--LPLL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 220 AcEQHQVTPALEHVIEAnTLLSGLGFESGGLAAAHAIHNGLTVLpatHKYWHGEKVAF---------------------- 277
Cdd:cd08182 224 L-ENLPNLEAREAMAEA-SLLAGLAISITKTTAAHAISYPLTSR---YGVPHGHACALtlpavlrynagaddecdddprg 298
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446180989 278 GTLAMLMLTDRAPELIEEVYQFCEDIGLPTTLADiglAGVSDDELLAVArASCQTGETMHNEPFTITPEAVQAALR 353
Cdd:cd08182 299 REILLALGASDPAEAAERLRALLESLGLPTRLSE---YGVTAEDLEALA-ASVNTPERLKNNPVRLSEEDLLRLLE 370
|
|
| G1PDH |
cd08175 |
Glycerol-1-phosphate dehydrogenase (G1PDH) catalyzes the reversible reduction of ... |
14-329 |
1.94e-09 |
|
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: 58.29 E-value: 1.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 14 GKGALTtHLPQELAAL--GHKALILQDPvvhNTYR---DTVATAL--HGVIEFDIEVFSSEC--SDEE-IARISARAQEi 83
Cdd:cd08175 7 GEGALK-KLPEYLKELfgGKKVLVVADE---NTYAaagEEVEAALeeAGVTVCLLIFPGEGDliADEAaVGKVLLELEK- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 84 GADVIVGMGGGkTLN--TAKATGAsLRLPIAVVPTLASTDAPCSSLVVIyTPEGKFKRYLMIPrnPTLVLVDSSIIAAAP 161
Cdd:cd08175 82 DTDLIIAVGSG-TINdlTKYAAYK-LGIPYISVPTAPSMDGYTSSGAPI-IVDGVKKTFPAHA--PKAIFADLDVLANAP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 162 VRFLVSGIGD------ALATWfeaedcriKGAGNMTTRPGPMTAFELARFCYTTLMRygRLAKLA-CEQHqvtpALEHVI 234
Cdd:cd08175 157 QRMIAAGFGDllgkytALADW--------KLSHLLGGEYYCPEVADLVQEALEKCLD--NAEGIAaRDPE----AIEALM 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 235 EANtLLSGLGFE--------SGG-------LAAAHAIHNGLTVLpathkywHGEKVAFGTLAMLMLTDRApELI--EEVY 297
Cdd:cd08175 223 EAL-ILSGLAMQlvgnsrpaSGAehhlshyWEMEFLRLGKPPVL-------HGEKVGVGTLLIAALYILE-QLPppEELR 293
|
330 340 350
....*....|....*....|....*....|..
gi 446180989 298 QFCEDIGLPTTLADIGLagvSDDELLAVARAS 329
Cdd:cd08175 294 ELLRKAGAPTTPEDLGI---DRDLLRDSLRLA 322
|
|
| Fe-ADH-like |
cd08194 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
8-173 |
6.20e-09 |
|
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) most of which have not been characterized. Their specific function is unknown. The protein structure represents a dehydroquinate synthase-like fold and belongs to the alcohol dehydrogenase-like superfamily. It is distinct from other alcohol dehydrogenases which contain different protein domains. Alcohol dehydrogenase catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions.
Pssm-ID: 341473 [Multi-domain] Cd Length: 378 Bit Score: 57.16 E-value: 6.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 8 PSRYVQGKGALTtHLPQELAAL-GHKALILQDPVVHNT-YRDTVATALHGViEFDIEVFS---SECSDEEIARISARAQE 82
Cdd:cd08194 1 PRTIIIGGGALE-ELGEEAASLgGKRALIVTDKVMVKLgLVDKVTQLLAEA-GIAYAVFDdvvSEPTDEMVEEGLALYKE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 83 IGADVIVGMGGGKTLNTAKATGA------SLR------------LPIAVVPTLASTDAPCSSLVVIYTPEGKFKrYLMIP 144
Cdd:cd08194 79 GGCDFIVALGGGSPIDTAKAIAVlatnggPIRdymgprkvdkpgLPLIAIPTTAGTGSEVTRFTVITDTETDVK-MLLKG 157
|
170 180 190
....*....|....*....|....*....|..
gi 446180989 145 RN--PTLVLVDSSIIAAAPVRFLV-SGIgDAL 173
Cdd:cd08194 158 PAllPAVAIVDPELTLSMPPRVTAaTGI-DAL 188
|
|
| MAR |
cd08177 |
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic ... |
8-116 |
2.14e-07 |
|
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic microbes; Maleylacetate reductase (MAR) plays an important role in the degradation of aromatic compounds in aerobic microbes. In fungi and yeasts, the enzyme is involved in the catabolism of compounds such as phenol, tyrosine, benzoate, 4-hydroxybenzoate and resorcinol. In bacteria, the enzyme contributes to the degradation of resorcinol, 2,4-dihydroxybenzoate ([beta]-resorcylate) and 2,6-dihydroxybenzoate ([gamma]-resorcylate) via hydroxyquinol and maleylacetate. Maleylacetate reductase 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: 52.12 E-value: 2.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 8 PSRYVQGKGALTThLPQELAALG-HKALILQDPVVHNTYrDTVATALHG--VIEFD-------IEVFssecsdeEIARis 77
Cdd:cd08177 1 PQRVVFGAGTLAE-LAEELERLGaRRALVLSTPRQRALA-ERVAALLGDrvAGVFDgavmhvpVEVA-------ERAL-- 69
|
90 100 110
....*....|....*....|....*....|....*....
gi 446180989 78 ARAQEIGADVIVGMGGGKTLNTAKATGASLRLPIAVVPT 116
Cdd:cd08177 70 AAAREAGADGLVAIGGGSAIGLAKAIALRTGLPIVAVPT 108
|
|
| Fe-ADH-like |
cd17814 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
32-314 |
2.15e-07 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341489 [Multi-domain] Cd Length: 374 Bit Score: 52.16 E-value: 2.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 32 KALILQDP-VVHNTYRDTVATALHGViEFDIEVFSSECS---DEEIARISARAQEIGADVIVGMGGGKTLNTAKATGA-- 105
Cdd:cd17814 28 KVLVVTDPgVIKAGWVDEVLDSLEAE-GLEYVVFSDVTPnprDFEVMEGAELYREEGCDGIVAVGGGSPIDCAKGIGIvv 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 106 ---------------SLRL-PIAVVPTLASTDAPCSSLVVIYTPEGKFKrYLMIPRN--PTLVLVDSSIIAAAPvRFLVS 167
Cdd:cd17814 107 sngghildyegvdkvRRPLpPLICIPTTAGSSADVSQFAIITDTERRVK-MAIISKTlvPDVSLIDPETLTTMD-PELTA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 168 GIG-DALATWFEAEdcrikgagnMTTRPGPMT---AFELARFCYTTLMRygrlaklACEQHQVTPALEHVIEAnTLLSGL 243
Cdd:cd17814 185 CTGmDALTHAIEAY---------VSNASSPLTdlhALEAIRLISENLPK-------AVADPDDLEAREKMMLA-SLQAGL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 244 GFESGGLAAAHAI-HN--GLTVLPathkywHGE------------------------KVAFGTLAMLMLT-DRAPELIEE 295
Cdd:cd17814 248 AFSNASLGAVHAMaHSlgGLLDLP------HGEcnalllphvirfnfpaaperyrkiAEAMGLDVDGLDDeEVAERLIEA 321
|
330
....*....|....*....
gi 446180989 296 VYQFCEDIGLPTTLADIGL 314
Cdd:cd17814 322 IRDLREDLGIPETLSELGV 340
|
|
| Fe-ADH-like |
cd14861 |
Iron-containing alcohol dehydrogenases-like; This family contains proteins similar to ... |
7-355 |
2.16e-07 |
|
Iron-containing alcohol dehydrogenases-like; This family contains proteins similar to iron-containing alcohol dehydrogenase (Fe-ADH), most of which have not been characterized. Their specific function is unknown. The protein structure represents a dehydroquinate synthase-like fold and belongs to the alcohol dehydrogenase-like superfamily. It is distinct from other alcohol dehydrogenases which contain different protein domains. Alcohol dehydrogenase catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions.
Pssm-ID: 341483 [Multi-domain] Cd Length: 374 Bit Score: 52.13 E-value: 2.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 7 FPSRYVQGKGALTThLPQELAALG-HKALILQDPVVHNT-YRDTVATALhGVIEFDIEVFS---SECSDEEIARISARAQ 81
Cdd:cd14861 2 YPTRIRFGAGAIAE-LPEELKALGiRRPLLVTDPGLAALgIVDRVLEAL-GAAGLSPAVFSdvpPNPTEADVEAGVAAYR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 82 EIGADVIVGMGGGKTLNTAKAT------GASLR----------------LPIAVVPTLASTDAPCSSLVVIYTPEGKFKR 139
Cdd:cd14861 80 EGGCDGIIALGGGSAIDAAKAIalmathPGPLWdyedgeggpaaitpavPPLIAIPTTAGTGSEVGRAAVITDDDTGRKK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 140 -----YLMiprnPTLVLVDSSIIAAAPvRFLVSGIG-DALATWFEAEdcrikgagnMTTRPGPM---TAFELARFCYTTL 210
Cdd:cd14861 160 iifspKLL----PKVAICDPELTLGLP-PRLTAATGmDALTHCIEAY---------LSPGFHPMadgIALEGLRLISEWL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 211 MRygrlaklACEQHQVTPALEHVIEAnTLLSGLGFESgGLAAAHAI----------HNGLTV---LPATHKYWH---GEK 274
Cdd:cd14861 226 PR-------AVADGSDLEARGEMMMA-ALMGAVAFQK-GLGAVHALahalgalyglHHGLLNailLPYVLRFNRpavEDK 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 275 VAfgTLAMLMLTDRAP--ELIEEVYQFCEDIGLPTTLADIGLAGVSDDEL--LAVARASCQTGetmhnePFTITPEAVQA 350
Cdd:cd14861 297 LA--RLARALGLGLGGfdDFIAWVEDLNERLGLPATLSELGVTEDDLDELaeLALADPCHATN------PRPVTAEDYRA 368
|
....*
gi 446180989 351 ALRAA 355
Cdd:cd14861 369 LLREA 373
|
|
| PRK10624 |
PRK10624 |
L-1,2-propanediol oxidoreductase; Provisional |
14-314 |
5.74e-06 |
|
L-1,2-propanediol oxidoreductase; Provisional
Pssm-ID: 182595 [Multi-domain] Cd Length: 382 Bit Score: 47.68 E-value: 5.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 14 GKGALTtHLPQELAALG-HKALILQDPVVHNTYRDTVATALHGVIEFDIEVFSSECSDEEIARIS---ARAQEIGADVIV 89
Cdd:PRK10624 14 GRGAIG-ALTDEVKRRGfKKALIVTDKTLVKCGVVAKVTDVLDAAGLAYEIYDGVKPNPTIEVVKegvEVFKASGADYLI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 90 GMGGGKTLNTAKATG--------ASLR------------LPIAVVPTLASTDAPCSSLVVIYTPEGKFKRYLMIPRN-PT 148
Cdd:PRK10624 93 AIGGGSPQDTCKAIGiisnnpefADVRslegvaptkkpsVPIIAIPTTAGTAAEVTINYVITDEEKRRKFVCVDPHDiPQ 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 149 LVLVDSSIIAAAPvRFLVSGIG-DALATWFEAedCRIKGAGNMTtrpgpmTAFELARFcyTTLMRYGRLAKLACEQHQVT 227
Cdd:PRK10624 173 VAFVDADMMDSMP-PGLKAATGvDALTHAIEG--YITRGAWALT------DMLHLKAI--EIIAGALRGAVAGDKEAGEG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 228 PALEHVIeantllSGLGFESGGLAAAHA--------------IHNGLtVLPATHKY---WHGEK-----VAFGTLAMLML 285
Cdd:PRK10624 242 MALGQYI------AGMGFSNVGLGLVHGmahplgafyntphgVANAI-LLPHVMEYnadFTGEKyrdiaRAMGVKVEGMS 314
|
330 340 350
....*....|....*....|....*....|
gi 446180989 286 TDRAPE-LIEEVYQFCEDIGLPTTLADIGL 314
Cdd:PRK10624 315 LEEARNaAVEAVKALNRDVGIPPHLRDVGV 344
|
|
| PPD-like |
cd08181 |
1,3-propanediol dehydrogenase-like (PPD); This family contains proteins similar to 1, ... |
8-178 |
1.16e-05 |
|
1,3-propanediol dehydrogenase-like (PPD); This family contains proteins similar to 1,3-propanediol dehydrogenase (PPD) which is a member of the iron-containing alcohol dehydrogenase superfamily, and exhibits a dehydroquinate synthase-like fold. Protein sequence similarity search and other biochemical evidences suggest that they are close to the iron-containing 1,3-propanediol dehydrogenase (EC 1.1.1.202). 1,3-propanediol dehydrogenase catalyzes the oxidation of propane-1,3-diol to 3-hydroxypropanal with the simultaneous reduction of NADP+ to NADPH. The protein structure of Thermotoga maritima TM0920 gene contains one NADP+ and one iron ion.
Pssm-ID: 341460 [Multi-domain] Cd Length: 358 Bit Score: 46.81 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 8 PSRYVQGKGALTTHlPQELAALGHKALIlqdpvV---HNTYR----DTVATAL--HGViefDIEVF---SSECSDEEIAR 75
Cdd:cd08181 4 PTKVYFGKNCVEKH-ADELAALGKKALI-----VtgkHSAKKngslDDVTEALeeNGI---EYFIFdevEENPSIETVEK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 76 ISARAQEIGADVIVGMGGGKTLNTAKA----------------TGASLR-LPIAVVPTLASTDAPCSSLVVIYTPEGKFK 138
Cdd:cd08181 75 GAELARKEGADFVIGIGGGSPLDAAKAiallaankdgdedlfqNGKYNPpLPIVAIPTTAGTGSEVTPYSILTDHEKGTK 154
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446180989 139 RYLMIPRN-PTLVLVDSSIIAAAPVRFLVSGIGDALATWFE 178
Cdd:cd08181 155 KSFGNPLIfPKLALLDPKYTLSLPEELTIDTAVDALSHAIE 195
|
|
| HOT |
cd08190 |
Hydroxyacid-oxoacid transhydrogenase (HOT) involved in gamma-hydroxybutyrate metabolism; This ... |
14-153 |
1.35e-05 |
|
Hydroxyacid-oxoacid transhydrogenase (HOT) involved in gamma-hydroxybutyrate metabolism; This family contains hydroxyacid-oxoacid transhydrogenase (HOT), also known as D-2-hydroxyglutarate transhydrogenase. It catalyzes the conversion of gamma-hydroxybutyrate (GHB) to succinic semialdehyde (SSA), coupled to the stoichiometric conversion of alpha-ketoglutarate to D-2-hydroxyglutarate in gamma-Hydroxybutyrate catabolism. Unlike many other alcohols, which are oxidized by NAD-linked dehydrogenases, gamma-hydroxybutyrate is metabolized to succinate semialdehyde by hydroxyacid-oxoacid transhydrogenase which does not require free NAD or NADP; instead, it uses alpha-ketoglutarate as an acceptor, converting it to d-2-hydroxyglutarate. Alpha-ketoglutarate serves as an intermediate acceptor to regenerate NAD(P) required for the oxidation of GHB. HOT also catalyzes the reversible oxidation of a hydroxyacid obligatorily coupled to the reduction of an oxoacid, and requires no cofactor. In mammals, the HOT enzyme is located in mitochondria, and is expressed with an N-terminal mitochondrial targeting sequence. HOT enzyme is member of the metal-containing alcohol dehydrogenase family. It typically contains an iron although other metal ions may be used.
Pssm-ID: 341469 [Multi-domain] Cd Length: 412 Bit Score: 46.77 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 14 GKGAlTTHLPQELAALG-HKALILQDPVVHNT-YRDTVATALHGViEFDIEVFSS---ECSDEEIARISARAQEIGADVI 88
Cdd:cd08190 7 GPGA-TRELGMDLKRLGaKKVLVVTDPGLAKLgLVERVLESLEKA-GIEVVVYDGvrvEPTDESFEEAIEFAKEGDFDAF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 89 VGMGGGKTLNTAKAT------------------GASLRLPIAV-----VPTLASTDAPCSSLVVIYTPEGKFK-----RY 140
Cdd:cd08190 85 VAVGGGSVIDTAKAAnlyathpgdfldyvnapiGKGKPVPGPLkpliaIPTTAGTGSETTGVAIFDLEELKVKtgissRY 164
|
170
....*....|...
gi 446180989 141 LmiprNPTLVLVD 153
Cdd:cd08190 165 L----RPTLAIVD 173
|
|
| DOIS |
cd08197 |
2-deoxy-scyllo-inosose synthase (DOIS) catalyzes carbocycle formation from ... |
21-328 |
2.64e-05 |
|
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: 45.65 E-value: 2.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 21 HLPQELAALGHKALIL-QDPVVHNTYRDTVATALHGViEFDIEVFSSECSD-----EEIARISARAQEIGAD---VIVGM 91
Cdd:cd08197 13 SLLSILEELKADRHFLvTDSNVNDLYGDRLLEGLKKA-GIPVELLVVPAGEsnktlSTLTELAERLIAAGITrrsVIIAL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 92 GGGKTLNTAkatG--ASL-----RLpiAVVPT--LASTDAPCSSLVVIYTPEGKfkrylmiprN-------PTLVLVDSS 155
Cdd:cd08197 92 GGGVVGNIA---GllAGLlyrgiRL--VHVPTtlLAQSDSVLSLKQAVNGKSGK---------NlvgsyyaPLFVFVDTE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 156 IIAAAPVRFLVSGIGDAlatwfeaedcrIKGAgnmttrpgpmTAFELARFCYttLMRYgrlakLACEQHQVTPALEHVIE 235
Cdd:cd08197 158 FLKTLPPRQIRSGLCEA-----------IKNA----------LIQDPEFLDY--LEDY-----LNSDLDYDPEFLEKVID 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 236 AN-----TLLSGLGFESG-------GLAAAHAIHngltvLPATHKYWHGEKVAFGTLAM------LMLTDraPELIEEVY 297
Cdd:cd08197 210 LSieaklEVLSNDPYEKKeglileyGHTVGHAIE-----LLSGGELSHGEAVAIGMCVAaeishlLGLLS--EEDVDKHY 282
|
330 340 350
....*....|....*....|....*....|.
gi 446180989 298 QFCEDIGLPTTLADiglaGVSDDELLAVARA 328
Cdd:cd08197 283 ELLEKIGLPTIIPD----GISVEAILEVIRY 309
|
|
| HVD |
cd08193 |
5-hydroxyvalerate dehydrogenase (HVD) catalyzes the oxidation of 5-hydroxyvalerate to ... |
8-136 |
7.80e-05 |
|
5-hydroxyvalerate dehydrogenase (HVD) catalyzes the oxidation of 5-hydroxyvalerate to 5-oxovalerate with NAD+ as cofactor; 5-hydroxyvalerate dehydrogenase (HVD) is an iron-containing (type III) NAD-dependent alcohol dehydrogenase. It plays a role in the cyclopentanol metabolism biochemical pathway. It catalyzes the oxidation of 5-hydroxyvalerate to 5-oxovalerate with NAD+ as cofactor. This cyclopentanol (cpn) degradation pathway is present in some bacteria which can use cyclopentanol as sole carbon source. In Comamonas sp. strain NCIMB 9872, this enzyme is encoded by the CpnD gene.
Pssm-ID: 341472 [Multi-domain] Cd Length: 379 Bit Score: 44.43 E-value: 7.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 8 PSRYVQGKGALTThLPQELAALG-HKALILQDPVVHNT-YRDTVATALhGVIEFDIEVFSSECSDEEIARISA---RAQE 82
Cdd:cd08193 4 VPRIICGAGAAAR-LGELLRELGaRRVLLVTDPGLVKAgLADPALAAL-EAAGIAVTVFDDVVADPPEAVVEAaveQARE 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446180989 83 IGADVIVGMGGGKTLNTAK------ATGASL------------RLPIAVVPTLASTDAPCSSLVVIYTPEGK 136
Cdd:cd08193 82 AGADGVIGFGGGSSMDVAKlvallaGSDQPLddiygvgkatgpRLPLILVPTTAGTGSEVTPISIVTTGETE 153
|
|
| Fe-ADH_KdnB-like |
cd08184 |
Iron-containing alcohol dehydrogenase similar to Shewanella oneidensis KdnB required for Kdo8N ... |
70-342 |
1.10e-04 |
|
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: 43.80 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 70 DEEIARIsaRAQEIG-ADVIVGMGGGKTLNTAKATGASLR------------------LPIAVVPTLASTDAPCSSLVVI 130
Cdd:cd08184 69 DALRAQI--RAENDKlPAAVVGIGGGSTMDIAKAVSNMLTnpgsaadyqgwdlvknpgIYKIGVPTLSGTGAEASRTAVL 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 131 YTPEGKF---KRYLMiprnPTLVLVDSSIIAAAPV--RFlvsgigdalatwFEAEDCRIKgagnmttrpgpmtafelarf 205
Cdd:cd08184 147 TGPEKKLginSDYTV----FDQVILDPELIATVPRdqYF------------YTGMDCYIH-------------------- 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 206 CYTTLM---------RYGRLAKLACEQ-----HQVTPALEHVIEANTLLSGLGFESGGLAAAHAIHNGLTVLPATHkywH 271
Cdd:cd08184 191 CVESLNgtyrnafgdAYAEKALELCRDvflsdDMMSPENREKLMVASYLGGSSIANSQVGVCHALSYGLSVVLGTH---H 267
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446180989 272 GekVAfGTLAMLMLTDRAPELIEEVYQFCE--DIGLPTTLAdiglAGVSDDELLAVARAScqtgeTMHNEPFT 342
Cdd:cd08184 268 G--VA-NCIVFNVLEEFYPEGVKEFREMLEkqNITLPKGIC----KDLTDEQYEKMVAVT-----LIHEKPLT 328
|
|
| Fe-ADH-like |
cd14866 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
8-355 |
1.49e-04 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341488 [Multi-domain] Cd Length: 384 Bit Score: 43.37 E-value: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 8 PSRYVQGKGALTtHLPQELAALGHK-ALIL------QDPVVHNTYRDTVATALHGVieFDiEVfSSECSDEEIARISARA 80
Cdd:cd14866 5 PLRLFSGRGALA-RLGRELDRLGARrALVVcgssvgANPDLMDPVRAALGDRLAGV--FD-GV-RPHSPLETVEAAAEAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 81 QEIGADVIVGMGGGKTLNTAKATGASL---------------------------RLPIAVVPTLASTDAPCSSLVVIYTP 133
Cdd:cd14866 80 READADAVVAVGGGSAIVTARAASILLaedrdvrelctrraedglmvsprldapKLPIFVVPTTPTTADVKAGSAVTDPP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 134 EGkfKRYLMI-PR-NPTLVLVDSSIIAAAPVRFLVSGigdALATWFEAEDCRIKGAGNMTTRPGPMTAFELARfcyTTLM 211
Cdd:cd14866 160 AG--QRLALFdPKtRPAAVFYDPELLATAPASLVAGA---AMNGFDMAVEGLYSRHADPLADATLMHALRLLA---DGLP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 212 RYGRLAKLAceqhqvtpALEHVIEAnTLLSGLGFESGGLAAAHAI----------HNGLT---VLPATHKYWHGE----- 273
Cdd:cd14866 232 RLADDDDPA--------ARADLVLA-AVLAGYGTDHTGGGVIHALghaigarygvQNGVVhaiLLPHVLRFNAPAtdgrl 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 274 -KVAfgtlAMLMLTDRAPE-----LIEEVYQFCEDIGLPTTLADIglaGVSDDELLAVARASCQTGeTMHNEP-FTITPE 346
Cdd:cd14866 303 dRLA----EALGVADAGDEasaaaVVDAVEALLDALGVPTRLRDL---GVSREDLPAIAEAAMDDW-FMDNNPrPVPTAE 374
|
....*....
gi 446180989 347 AVQAALRAA 355
Cdd:cd14866 375 ELEALLEAA 383
|
|
| PRK14021 |
PRK14021 |
bifunctional shikimate kinase/3-dehydroquinate synthase; Provisional |
5-177 |
5.30e-04 |
|
bifunctional shikimate kinase/3-dehydroquinate synthase; Provisional
Pssm-ID: 184458 [Multi-domain] Cd Length: 542 Bit Score: 41.77 E-value: 5.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 5 AIFPSRYVQGKGALTtHLPQELAALGHK-ALILQDPVVHNTYRDTVATALHGVIEFDIEVFSSECSDE-EIAR-ISARAQ 81
Cdd:PRK14021 185 GIEPYDVRIGEGAMN-HLPQVLGPKPVKvALIHTQPVQRHSDRARTLLRQGGYEVSDIVIPDAEAGKTiEVANgIWQRLG 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 82 EIG---ADVIVGMGGGKTLNTAKATGASLRLPIAVV--PT--LASTDAPCSSLVVIYTPEGkfKRYLMIPRNPTLVLVDS 154
Cdd:PRK14021 264 NEGftrSDAIVGLGGGAATDLAGFVAATWMRGIRYVncPTslLAMVDASTGGKTGINTPQG--KNLVGSFYTPAGVLADT 341
|
170 180
....*....|....*....|...
gi 446180989 155 SIIAAAPVRFLVSGIGDALATWF 177
Cdd:PRK14021 342 KTLATLPNDIFIEGLGEVAKSGF 364
|
|
| AAD_C |
cd08178 |
C-terminal alcohol dehydrogenase domain of the acetaldehyde dehydrogenase-alcohol ... |
31-102 |
4.28e-03 |
|
C-terminal alcohol dehydrogenase domain of the acetaldehyde dehydrogenase-alcohol dehydrogenase bifunctional two-domain protein (AAD); This alcohol dehydrogenase domain is located on the C-terminal of a bifunctional two-domain protein. The N-terminal of the protein contains an acetaldehyde-CoA dehydrogenase domain. This protein is involved in pyruvate metabolism whereby pyruvate is converted to acetyl-CoA and formate by pyruvate formate-lysase (PFL). Under anaerobic condition, acetyl-CoA is reduced to acetaldehyde and ethanol by this two-domain protein. Acetyl-CoA is first converted into an enzyme-bound thiohemiacetal by the N-terminal acetaldehyde dehydrogenase domain. The enzyme-bound thiohemiacetal is subsequently reduced by the C-terminal NAD+-dependent alcohol dehydrogenase domain. In E. coli, this protein is called AdhE and has been shown to have pyruvate formate-lyase (PFL) deactivase activity, which leads to the inactivation of PFL, a key enzyme in anaerobic metabolism. In Escherichia coli and Entamoeba histolytica, this enzyme forms homopolymeric peptides composed of more than 20 protomers associated in a helical rod-like structure.
Pssm-ID: 341457 [Multi-domain] Cd Length: 400 Bit Score: 38.71 E-value: 4.28e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446180989 31 HKALILQDPVVHNT-YRDTVATALHGvIEFDIEVFS---SECSDEEIARISARAQEIGADVIVGMGGGKTLNTAKA 102
Cdd:cd08178 24 KRAFIVTDRVLYKLgYVDKVLDVLEA-RGVETEVFSdvePDPTLSTVRKGLEAMNAFKPDVIIALGGGSAMDAAKI 98
|
|
| DHQS |
cd08195 |
Dehydroquinate synthase (DHQS) catalyzes the conversion of DAHP to DHQ in shikimate pathway ... |
14-170 |
7.17e-03 |
|
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: 38.19 E-value: 7.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 14 GKGALTTHLPQELAALGHKALILQDPVVHNTYRDTVATALHGViEFDIEVFSSECSD-----EEIARISARAQEIGAD-- 86
Cdd:cd08195 7 GSGLLDKLGELLELKKGSKVVIVTDENVAKLYGELLLKSLEAA-GFKVEVIVIPAGEkskslETVERIYDFLLEAGLDrd 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446180989 87 -VIVGMGGGktlntakATG------AS--LR-LPIAVVPT--LASTDapcSSL---VVIYTPEGK-----FKrylmiprN 146
Cdd:cd08195 86 sLLIALGGG-------VVGdlagfvAStyMRgIPFIQVPTtlLAQVD---SSIggkTGINLPGGKnligaFY-------Q 148
|
170 180
....*....|....*....|....
gi 446180989 147 PTLVLVDSSIIAAAPVRFLVSGIG 170
Cdd:cd08195 149 PKAVLIDPDFLKTLPEREFRSGLA 172
|
|
| |
