|
Name |
Accession |
Description |
Interval |
E-value |
| AroB |
COG0337 |
3-dehydroquinate synthetase [Amino acid transport and metabolism]; 3-dehydroquinate synthetase ... |
1-353 |
2.19e-151 |
|
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: 430.28 E-value: 2.19e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684960172 1 MGNIHIQTKSKEYDVHVGKEALSHLITIVQNMQPAvSNVMIISDEAVASLHLQTVVDALQIEQ-KVFSFVVPSGEKEKSF 79
Cdd:COG0337 1 MQTLTVNLGERSYDIRIGRGLLDELGELLAELLKG-RRVLVVTDENVAPLYGERLRAALEAAGfEVHLLVLPDGEASKTL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684960172 80 ENFYAAHTSALENKLDRNSLIVALGGGMIGDLAGFVAASFMRGIRFVQVPTTLLAH-DSAVGGKVAINHPLGKNMIGAFH 158
Cdd:COG0337 80 ETLERILDALLEAGLDRDDLVVALGGGVVGDLAGFAAATYLRGVPFIQVPTTLLAQvDSSVGGKTGVNHPGGKNLIGAFH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684960172 159 QPEAVVYHTPFLQSLSEKEWRSGYAEVIKHALIGNVKLYHWLKEEVQTLADLRDEKLIHILTKAIPVKANIVSQDETEKG 238
Cdd:COG0337 160 QPRAVLIDLDFLKTLPERELRAGLAEVIKYGLIADAEFFEWLEENADALLARDPEALEEAIARSCEIKAEVVAADERESG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684960172 239 VRAHLNFGHTLGHALEKELGYgNITHGDGVAVGMLFAIFLSEQVYKVDLA-YEDMKQWFLRYGYPKMPRDLNVERLVQLM 317
Cdd:COG0337 240 LRALLNFGHTFGHAIEAATGY-RLLHGEAVAIGMVFAARLSARLGLLSEEdVERIRALLEALGLPTRLPALDPEALLAAM 318
|
330 340 350
....*....|....*....|....*....|....*..
gi 1684960172 318 KQDKKANAGAIHMVLMQEYGVVNVVS-ISDETVHIAL 353
Cdd:COG0337 319 KRDKKVRGGKLRFVLLRGIGKAVIVDdVDEELLRAAL 355
|
|
| DHQS |
cd08195 |
Dehydroquinate synthase (DHQS) catalyzes the conversion of DAHP to DHQ in shikimate pathway ... |
12-353 |
9.54e-147 |
|
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: 418.00 E-value: 9.54e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684960172 12 EYDVHVGKEALSHLITIVQNMQPavSNVMIISDEAVASLHLQTVVDAL-QIEQKVFSFVVPSGEKEKSFENFYAAHTSAL 90
Cdd:cd08195 1 SYPILIGSGLLDKLGELLELKKG--SKVVIVTDENVAKLYGELLLKSLeAAGFKVEVIVIPAGEKSKSLETVERIYDFLL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684960172 91 ENKLDRNSLIVALGGGMIGDLAGFVAASFMRGIRFVQVPTTLLAH-DSAVGGKVAINHPLGKNMIGAFHQPEAVVYHTPF 169
Cdd:cd08195 79 EAGLDRDSLLIALGGGVVGDLAGFVASTYMRGIPFIQVPTTLLAQvDSSIGGKTGINLPGGKNLIGAFYQPKAVLIDPDF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684960172 170 LQSLSEKEWRSGYAEVIKHALIGNVKLYHWLKEEVQTLADLRDEKLIHILTKAIPVKANIVSQDETEKGVRAHLNFGHTL 249
Cdd:cd08195 159 LKTLPEREFRSGLAEVIKYGLIADKELFEFLEKNLDKILARDPEALEEIIARSVEIKADIVEEDEREKGLRAILNFGHTF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684960172 250 GHALEKELGYGnITHGDGVAVGMLFAIFLSEQVYKVDLA-YEDMKQWFLRYGYPKMPRDLNVERLVQLMKQDKKANAGAI 328
Cdd:cd08195 239 GHAIESASGYK-LLHGEAVAIGMVAAARLSVKLGLLSEEdLERIRALLKKLGLPTSIKDLDPEELLEAMKRDKKNRGGKI 317
|
330 340
....*....|....*....|....*.
gi 1684960172 329 HMVLMQEYGVVNVVS-ISDETVHIAL 353
Cdd:cd08195 318 RFVLLKGIGKAVIVDdVSEEEIREAL 343
|
|
| DHQ_synthase |
pfam01761 |
3-dehydroquinate synthase; The 3-dehydroquinate synthase EC:4.6.1.3 domain is present in ... |
67-323 |
1.08e-132 |
|
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: 379.15 E-value: 1.08e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684960172 67 SFVVPSGEKEKSFENFYAAHTSALENKLDRNSLIVALGGGMIGDLAGFVAASFMRGIRFVQVPTTLLAH-DSAVGGKVAI 145
Cdd:pfam01761 1 TIVIPDGEKSKTLETLERIYDALLEAGLDRSSLLIALGGGVIGDLAGFVAATYMRGIRFIQVPTTLLAQvDSSVGGKTGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684960172 146 NHPLGKNMIGAFHQPEAVVYHTPFLQSLSEKEWRSGYAEVIKHALIGNVKLYHWLKEEVQTLADLRDEKLIHILTKAIPV 225
Cdd:pfam01761 81 NHPLGKNLIGAFYQPKAVLIDLDFLKTLPDREFRAGLAEVIKYGLIADAEFFEWLEENAEALLNLDPDALEEAIARSCEV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684960172 226 KANIVSQDETEKGVRAHLNFGHTLGHALEKELGYGNITHGDGVAVGMLFAIFLSEQVYKVDLAY-EDMKQWFLRYGYPKM 304
Cdd:pfam01761 161 KADVVAQDEKESGLRALLNLGHTFGHAIEALSGYGALLHGEAVAIGMVLAARLSERLGLLDEADvERIRALLKKYGLPTS 240
|
250
....*....|....*....
gi 1684960172 305 PRDLNVERLVQLMKQDKKA 323
Cdd:pfam01761 241 LPDLDVEQLLAAMARDKKV 259
|
|
| aroB |
TIGR01357 |
3-dehydroquinate synthase; This model represents 3-dehydroquinate synthase, the enzyme ... |
13-337 |
2.50e-124 |
|
3-dehydroquinate synthase; This model represents 3-dehydroquinate synthase, the enzyme catalyzing the second of seven steps in the shikimate pathway of chorismate biosynthesis. Chorismate is the last common intermediate in the biosynthesis of all three aromatic amino acids. [Amino acid biosynthesis, Aromatic amino acid family]
Pssm-ID: 273575 Cd Length: 344 Bit Score: 361.18 E-value: 2.50e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684960172 13 YDVHVGKEALSHLITIVQNMQPavsnVMIISDEAVASLHLQTVVDALQI-EQKVFSFVVPSGEKEKSFENFYAAHTSALE 91
Cdd:TIGR01357 1 YPVHVGEGLLDQLVEELAEPSK----LVIITDETVADLYGDKLLEALQAlGYNVLKLTVPDGEESKSLETVQRLYDQLLE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684960172 92 NKLDRNSLIVALGGGMIGDLAGFVAASFMRGIRFVQVPTTLLAH-DSAVGGKVAINHPLGKNMIGAFHQPEAVVYHTPFL 170
Cdd:TIGR01357 77 AGLDRSSTIIALGGGVVGDLAGFVAATYMRGIRFIQVPTTLLAMvDSSVGGKTGINFPGGKNLIGTFYQPKAVLIDPDFL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684960172 171 QSLSEKEWRSGYAEVIKHALIGNVKLYHWLKEEVQTLADLRDEKLIH-ILTKAIPVKANIVSQDETEKGVRAHLNFGHTL 249
Cdd:TIGR01357 157 KTLPDRELRSGMAEVIKHGLIADAELFDELESNDKLRLNLQELEHLEeLIKRSIEVKASIVAEDEKESGLRAILNFGHTI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684960172 250 GHALEKELGYGNITHGDGVAVGMLFAIFLSEQVYKVDLA-YEDMKQWFLRYGYP-KMPRDLNVERLVQLMKQDKKANAGA 327
Cdd:TIGR01357 237 GHAIEAEAGYGKIPHGEAVAIGMVCEAKLSERLGLLPAElIERLVQLLKRYGLPtDLPKDLDVDELLNAMLNDKKNSGGK 316
|
330
....*....|
gi 1684960172 328 IHMVLMQEYG 337
Cdd:TIGR01357 317 IRFVLLEEIG 326
|
|
| PLN02834 |
PLN02834 |
3-dehydroquinate synthase |
37-358 |
1.84e-92 |
|
3-dehydroquinate synthase
Pssm-ID: 215448 Cd Length: 433 Bit Score: 283.20 E-value: 1.84e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684960172 37 SNVMIISDEAVASLHLQTVVDALQ---IEQKVFSFVVPSGEKEKSFENFYAAHTSALENKLDRNSLIVALGGGMIGDLAG 113
Cdd:PLN02834 101 KRVLVVTNETVAPLYLEKVVEALTakgPELTVESVILPDGEKYKDMETLMKVFDKALESRLDRRCTFVALGGGVIGDMCG 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684960172 114 FVAASFMRGIRFVQVPTTLLAH-DSAVGGKVAINHPLGKNMIGAFHQPEAVVYHTPFLQSLSEKEWRSGYAEVIKHALIG 192
Cdd:PLN02834 181 FAAASYQRGVNFVQIPTTVMAQvDSSVGGKTGVNHPLGKNMIGAFYQPQCVLIDTDTLATLPDRELASGIAEVVKYGLIR 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684960172 193 NVKLYHWLKEEVQTLADLRDEKLIHILTKAIPVKANIVSQDETEKGVRAHLNFGHTLGHALEKELGYGNITHGDGVAVGM 272
Cdd:PLN02834 261 DAEFFEWQEANMEKLLARDPGALAYAIKRSCENKAEVVSLDEKESGLRATLNLGHTFGHAIETGPGYGEWLHGEAVAAGT 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684960172 273 LFAIFLSEQVYKVDlayEDMKQWFL----RYGYP-KMPRDLNVERLVQLMKQDKKANAGAIHMVLMQ-EYGvvNVVSISD 346
Cdd:PLN02834 341 VMAADMSYRLGWID---MSLVNRIFallkRAKLPtNPPEKMTVEMFKSLMAVDKKVADGLLRLILLKgELG--NCVFTGD 415
|
330
....*....|....*
gi 1684960172 347 ---ETVHIALEAFQK 358
Cdd:PLN02834 416 fdrEALEETLRAFCK 430
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| AroB |
COG0337 |
3-dehydroquinate synthetase [Amino acid transport and metabolism]; 3-dehydroquinate synthetase ... |
1-353 |
2.19e-151 |
|
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: 430.28 E-value: 2.19e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684960172 1 MGNIHIQTKSKEYDVHVGKEALSHLITIVQNMQPAvSNVMIISDEAVASLHLQTVVDALQIEQ-KVFSFVVPSGEKEKSF 79
Cdd:COG0337 1 MQTLTVNLGERSYDIRIGRGLLDELGELLAELLKG-RRVLVVTDENVAPLYGERLRAALEAAGfEVHLLVLPDGEASKTL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684960172 80 ENFYAAHTSALENKLDRNSLIVALGGGMIGDLAGFVAASFMRGIRFVQVPTTLLAH-DSAVGGKVAINHPLGKNMIGAFH 158
Cdd:COG0337 80 ETLERILDALLEAGLDRDDLVVALGGGVVGDLAGFAAATYLRGVPFIQVPTTLLAQvDSSVGGKTGVNHPGGKNLIGAFH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684960172 159 QPEAVVYHTPFLQSLSEKEWRSGYAEVIKHALIGNVKLYHWLKEEVQTLADLRDEKLIHILTKAIPVKANIVSQDETEKG 238
Cdd:COG0337 160 QPRAVLIDLDFLKTLPERELRAGLAEVIKYGLIADAEFFEWLEENADALLARDPEALEEAIARSCEIKAEVVAADERESG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684960172 239 VRAHLNFGHTLGHALEKELGYgNITHGDGVAVGMLFAIFLSEQVYKVDLA-YEDMKQWFLRYGYPKMPRDLNVERLVQLM 317
Cdd:COG0337 240 LRALLNFGHTFGHAIEAATGY-RLLHGEAVAIGMVFAARLSARLGLLSEEdVERIRALLEALGLPTRLPALDPEALLAAM 318
|
330 340 350
....*....|....*....|....*....|....*..
gi 1684960172 318 KQDKKANAGAIHMVLMQEYGVVNVVS-ISDETVHIAL 353
Cdd:COG0337 319 KRDKKVRGGKLRFVLLRGIGKAVIVDdVDEELLRAAL 355
|
|
| DHQS |
cd08195 |
Dehydroquinate synthase (DHQS) catalyzes the conversion of DAHP to DHQ in shikimate pathway ... |
12-353 |
9.54e-147 |
|
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: 418.00 E-value: 9.54e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684960172 12 EYDVHVGKEALSHLITIVQNMQPavSNVMIISDEAVASLHLQTVVDAL-QIEQKVFSFVVPSGEKEKSFENFYAAHTSAL 90
Cdd:cd08195 1 SYPILIGSGLLDKLGELLELKKG--SKVVIVTDENVAKLYGELLLKSLeAAGFKVEVIVIPAGEKSKSLETVERIYDFLL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684960172 91 ENKLDRNSLIVALGGGMIGDLAGFVAASFMRGIRFVQVPTTLLAH-DSAVGGKVAINHPLGKNMIGAFHQPEAVVYHTPF 169
Cdd:cd08195 79 EAGLDRDSLLIALGGGVVGDLAGFVASTYMRGIPFIQVPTTLLAQvDSSIGGKTGINLPGGKNLIGAFYQPKAVLIDPDF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684960172 170 LQSLSEKEWRSGYAEVIKHALIGNVKLYHWLKEEVQTLADLRDEKLIHILTKAIPVKANIVSQDETEKGVRAHLNFGHTL 249
Cdd:cd08195 159 LKTLPEREFRSGLAEVIKYGLIADKELFEFLEKNLDKILARDPEALEEIIARSVEIKADIVEEDEREKGLRAILNFGHTF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684960172 250 GHALEKELGYGnITHGDGVAVGMLFAIFLSEQVYKVDLA-YEDMKQWFLRYGYPKMPRDLNVERLVQLMKQDKKANAGAI 328
Cdd:cd08195 239 GHAIESASGYK-LLHGEAVAIGMVAAARLSVKLGLLSEEdLERIRALLKKLGLPTSIKDLDPEELLEAMKRDKKNRGGKI 317
|
330 340
....*....|....*....|....*.
gi 1684960172 329 HMVLMQEYGVVNVVS-ISDETVHIAL 353
Cdd:cd08195 318 RFVLLKGIGKAVIVDdVSEEEIREAL 343
|
|
| DHQ_synthase |
pfam01761 |
3-dehydroquinate synthase; The 3-dehydroquinate synthase EC:4.6.1.3 domain is present in ... |
67-323 |
1.08e-132 |
|
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: 379.15 E-value: 1.08e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684960172 67 SFVVPSGEKEKSFENFYAAHTSALENKLDRNSLIVALGGGMIGDLAGFVAASFMRGIRFVQVPTTLLAH-DSAVGGKVAI 145
Cdd:pfam01761 1 TIVIPDGEKSKTLETLERIYDALLEAGLDRSSLLIALGGGVIGDLAGFVAATYMRGIRFIQVPTTLLAQvDSSVGGKTGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684960172 146 NHPLGKNMIGAFHQPEAVVYHTPFLQSLSEKEWRSGYAEVIKHALIGNVKLYHWLKEEVQTLADLRDEKLIHILTKAIPV 225
Cdd:pfam01761 81 NHPLGKNLIGAFYQPKAVLIDLDFLKTLPDREFRAGLAEVIKYGLIADAEFFEWLEENAEALLNLDPDALEEAIARSCEV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684960172 226 KANIVSQDETEKGVRAHLNFGHTLGHALEKELGYGNITHGDGVAVGMLFAIFLSEQVYKVDLAY-EDMKQWFLRYGYPKM 304
Cdd:pfam01761 161 KADVVAQDEKESGLRALLNLGHTFGHAIEALSGYGALLHGEAVAIGMVLAARLSERLGLLDEADvERIRALLKKYGLPTS 240
|
250
....*....|....*....
gi 1684960172 305 PRDLNVERLVQLMKQDKKA 323
Cdd:pfam01761 241 LPDLDVEQLLAAMARDKKV 259
|
|
| aroB |
TIGR01357 |
3-dehydroquinate synthase; This model represents 3-dehydroquinate synthase, the enzyme ... |
13-337 |
2.50e-124 |
|
3-dehydroquinate synthase; This model represents 3-dehydroquinate synthase, the enzyme catalyzing the second of seven steps in the shikimate pathway of chorismate biosynthesis. Chorismate is the last common intermediate in the biosynthesis of all three aromatic amino acids. [Amino acid biosynthesis, Aromatic amino acid family]
Pssm-ID: 273575 Cd Length: 344 Bit Score: 361.18 E-value: 2.50e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684960172 13 YDVHVGKEALSHLITIVQNMQPavsnVMIISDEAVASLHLQTVVDALQI-EQKVFSFVVPSGEKEKSFENFYAAHTSALE 91
Cdd:TIGR01357 1 YPVHVGEGLLDQLVEELAEPSK----LVIITDETVADLYGDKLLEALQAlGYNVLKLTVPDGEESKSLETVQRLYDQLLE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684960172 92 NKLDRNSLIVALGGGMIGDLAGFVAASFMRGIRFVQVPTTLLAH-DSAVGGKVAINHPLGKNMIGAFHQPEAVVYHTPFL 170
Cdd:TIGR01357 77 AGLDRSSTIIALGGGVVGDLAGFVAATYMRGIRFIQVPTTLLAMvDSSVGGKTGINFPGGKNLIGTFYQPKAVLIDPDFL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684960172 171 QSLSEKEWRSGYAEVIKHALIGNVKLYHWLKEEVQTLADLRDEKLIH-ILTKAIPVKANIVSQDETEKGVRAHLNFGHTL 249
Cdd:TIGR01357 157 KTLPDRELRSGMAEVIKHGLIADAELFDELESNDKLRLNLQELEHLEeLIKRSIEVKASIVAEDEKESGLRAILNFGHTI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684960172 250 GHALEKELGYGNITHGDGVAVGMLFAIFLSEQVYKVDLA-YEDMKQWFLRYGYP-KMPRDLNVERLVQLMKQDKKANAGA 327
Cdd:TIGR01357 237 GHAIEAEAGYGKIPHGEAVAIGMVCEAKLSERLGLLPAElIERLVQLLKRYGLPtDLPKDLDVDELLNAMLNDKKNSGGK 316
|
330
....*....|
gi 1684960172 328 IHMVLMQEYG 337
Cdd:TIGR01357 317 IRFVLLEEIG 326
|
|
| PLN02834 |
PLN02834 |
3-dehydroquinate synthase |
37-358 |
1.84e-92 |
|
3-dehydroquinate synthase
Pssm-ID: 215448 Cd Length: 433 Bit Score: 283.20 E-value: 1.84e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684960172 37 SNVMIISDEAVASLHLQTVVDALQ---IEQKVFSFVVPSGEKEKSFENFYAAHTSALENKLDRNSLIVALGGGMIGDLAG 113
Cdd:PLN02834 101 KRVLVVTNETVAPLYLEKVVEALTakgPELTVESVILPDGEKYKDMETLMKVFDKALESRLDRRCTFVALGGGVIGDMCG 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684960172 114 FVAASFMRGIRFVQVPTTLLAH-DSAVGGKVAINHPLGKNMIGAFHQPEAVVYHTPFLQSLSEKEWRSGYAEVIKHALIG 192
Cdd:PLN02834 181 FAAASYQRGVNFVQIPTTVMAQvDSSVGGKTGVNHPLGKNMIGAFYQPQCVLIDTDTLATLPDRELASGIAEVVKYGLIR 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684960172 193 NVKLYHWLKEEVQTLADLRDEKLIHILTKAIPVKANIVSQDETEKGVRAHLNFGHTLGHALEKELGYGNITHGDGVAVGM 272
Cdd:PLN02834 261 DAEFFEWQEANMEKLLARDPGALAYAIKRSCENKAEVVSLDEKESGLRATLNLGHTFGHAIETGPGYGEWLHGEAVAAGT 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684960172 273 LFAIFLSEQVYKVDlayEDMKQWFL----RYGYP-KMPRDLNVERLVQLMKQDKKANAGAIHMVLMQ-EYGvvNVVSISD 346
Cdd:PLN02834 341 VMAADMSYRLGWID---MSLVNRIFallkRAKLPtNPPEKMTVEMFKSLMAVDKKVADGLLRLILLKgELG--NCVFTGD 415
|
330
....*....|....*
gi 1684960172 347 ---ETVHIALEAFQK 358
Cdd:PLN02834 416 fdrEALEETLRAFCK 430
|
|
| DOIS |
cd08197 |
2-deoxy-scyllo-inosose synthase (DOIS) catalyzes carbocycle formation from ... |
12-354 |
6.16e-82 |
|
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: 253.66 E-value: 6.16e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684960172 12 EYDVHVGKEALSHLITIVQNMqpAVSNVMIISDEAVASLHLQTVVDAL-QIEQKVFSFVVPSGEKEKSFENFYAAHTSAL 90
Cdd:cd08197 1 LTDIYLGRGILESLLSILEEL--KADRHFLVTDSNVNDLYGDRLLEGLkKAGIPVELLVVPAGESNKTLSTLTELAERLI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684960172 91 ENKLDRNSLIVALGGGMIGDLAGFVAASFMRGIRFVQVPTTLLA-HDSAVGGKVAINHPLGKNMIGAFHQPEAVVYHTPF 169
Cdd:cd08197 79 AAGITRRSVIIALGGGVVGNIAGLLAGLLYRGIRLVHVPTTLLAqSDSVLSLKQAVNGKSGKNLVGSYYAPLFVFVDTEF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684960172 170 LQSLSEKEWRSGYAEVIKHALIGNVKLYHWLKEEVQTLADLRDEKLIHILTKAIPVKANIVSQDETEKGVRAHLNFGHTL 249
Cdd:cd08197 159 LKTLPPRQIRSGLCEAIKNALIQDPEFLDYLEDYLNSDLDYDPEFLEKVIDLSIEAKLEVLSNDPYEKKEGLILEYGHTV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684960172 250 GHALEKeLGYGNITHGDGVAVGMLFAI-------FLSEQVykVDLAYEDMKqwflRYGYPKM-PRDLNVERLVQLMKQDK 321
Cdd:cd08197 239 GHAIEL-LSGGELSHGEAVAIGMCVAAeishllgLLSEED--VDKHYELLE----KIGLPTIiPDGISVEAILEVIRYDN 311
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1684960172 322 K-----ANAGAIHMVLMQEYGVVN------VVSISDETVHIALE 354
Cdd:cd08197 312 KrgyikADADTIRMVLLEKLGKPAnpdgdyLTPVPEEIVKEALE 355
|
|
| DHQ-like |
cd08169 |
Dehydroquinate synthase-like which includes dehydroquinate synthase, 2-deoxy-scyllo-inosose ... |
12-337 |
1.77e-77 |
|
Dehydroquinate synthase-like which includes dehydroquinate synthase, 2-deoxy-scyllo-inosose synthase, and 2-epi-5-epi-valiolone synthase; This group contains dehydroquinate synthase, 2-deoxy-scyllo-inosose synthase, and 2-epi-5-epi-valiolone synthase. These proteins exhibit the dehydroquinate synthase structural fold. Dehydroquinate synthase (DHQS) catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate-7-phosphate (DAHP) to dehydroquinate (DHQ) in the second step of the shikimate pathway. This pathway involves seven sequential enzymatic steps in the conversion of erythrose 4-phosphate and phosphoenolpyruvate into chorismate for subsequent synthesis of aromatic compounds. 2-deoxy-scyllo-inosose synthase (DOIS) catalyzes carbocycle formation from D-glucose-6-phosphate to 2-deoxy-scyllo-inosose through a multi-step reaction in the biosynthesis of aminoglycoside antibiotics. 2-deoxystreptamine (DOS)-containing aminoglycoside antibiotics includes neomycin, kanamycin, gentamicin, and ribostamycin. 2-epi-5-epi-valiolone synthases catalyze the cyclization of sedoheptulose 7-phosphate to 2-epi-5-epi-valiolone in the biosynthesis of C(7)N-aminocyclitol-containing products. The cyclization product, 2-epi-5-epi-valiolone ((2S,3S,4S,5R)-5-(hydroxymethyl)cyclohexanon-2,3,4,5-tetrol), is a precursor of the valienamine moiety. The valienamine unit is responsible for their biological activities as various glycosidic hydrolases inhibitors. Two important microbial secondary metabolites, validamycin and acarbose, are used in agricultural and biomedical applications.
Pssm-ID: 341448 [Multi-domain] Cd Length: 328 Bit Score: 241.16 E-value: 1.77e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684960172 12 EYDVHVGKealsHLITIVQNMQP--AVSNVMIISDEAVASLHLQTVVDALQIEQKVFSFVVPSGEKEKSFENFYAAHTSA 89
Cdd:cd08169 1 EYPVFFGE----GVFESVNSYIPrdAFDQCLIIVDSGVPDLIVNYLAEYFGYYLEVHVFIIQGGEAYKTFQTVVEELERA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684960172 90 LENKLDRNSLIVALGGGMIGDLAGFVAASFMRGIRFVQVPTTLLAH-DSAVGGKVAINHPLGKNMIGAFHQPEAVVYHTP 168
Cdd:cd08169 77 AALHLNRHSAVVAVGGGATGDVVGFAAATYFRGIAFIRVPTTLLAQsDSSVGIKVGINTRGGKNLLGAFYPPRAVFADFS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684960172 169 FLQSLSEKEWRSGYAEVIKHALIGNVKLYHWLKEEVQTLA-DLRD--EKLIHiltKAIPVKANIVSQDETEKGVRAHLNF 245
Cdd:cd08169 157 FLKTLPFRQVRAGMAELVKMALIADNDFFEFLEDKANSATvYSPEqlEKLIN---KCISLKLDVVVADEDEQGKRRGLNY 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684960172 246 GHTLGHALEKELGYGnITHGDGVAVGMLFAIFLSEQVYKVDLAYEDMKQWFL-RYGYP-KMPRDLNVERLVQLMKQDKKA 323
Cdd:cd08169 234 GHTFGHALELASGYK-IPHGEAVAVGMAYAAKIANRLGLLPEHDVSRIIWLLnKLGLPlDHPLALDPDSLYEYLESDKKS 312
|
330
....*....|....
gi 1684960172 324 NAGAIHMVLMQEYG 337
Cdd:cd08169 313 LYGNLGMILLSGVG 326
|
|
| PRK14021 |
PRK14021 |
bifunctional shikimate kinase/3-dehydroquinate synthase; Provisional |
4-358 |
1.22e-49 |
|
bifunctional shikimate kinase/3-dehydroquinate synthase; Provisional
Pssm-ID: 184458 [Multi-domain] Cd Length: 542 Bit Score: 174.28 E-value: 1.22e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684960172 4 IHIQTKSKE-YDVHVGKEALSHLitiVQNMQPAVSNVMIISDEAVASLHLQTVVDALQIEQKVFSFVVPSGEKEKSFENF 82
Cdd:PRK14021 179 VHVTGAGIEpYDVRIGEGAMNHL---PQVLGPKPVKVALIHTQPVQRHSDRARTLLRQGGYEVSDIVIPDAEAGKTIEVA 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684960172 83 YAAHTSALENKLDRNSLIVALGGGMIGDLAGFVAASFMRGIRFVQVPTTLLAH-DSAVGGKVAINHPLGKNMIGAFHQPE 161
Cdd:PRK14021 256 NGIWQRLGNEGFTRSDAIVGLGGGAATDLAGFVAATWMRGIRYVNCPTSLLAMvDASTGGKTGINTPQGKNLVGSFYTPA 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684960172 162 AVVYHTPFLQSLSEKEWRSGYAEVIKHALIGNVKLYHWLKEEVQTL-----ADLRDEKL----IHILTKAIPVKANIVSQ 232
Cdd:PRK14021 336 GVLADTKTLATLPNDIFIEGLGEVAKSGFIRDPEILRILEDHAAELrafdgSTFLGSPLedvvAELIERTVKVKAYHVSS 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684960172 233 DETEKGVRAHLNFGHTLGHALEKeLGYGNITHGDGVAVGMLFAIFLSEQVYKVDLAYEDMKQWFL-RYGYPKMPRDLNVE 311
Cdd:PRK14021 416 DLKEAGLREFLNYGHTLGHAIEK-LEHFRWRHGNAVAVGMVYAAELAHLLGYIDQDLVDYHRSLLaSLGLPTSWNGGSFD 494
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1684960172 312 RLVQLMKQDKKANAGAIHMVLMQEYGvvNVVSISDETVHIALEAFQK 358
Cdd:PRK14021 495 DVLALMHRDKKARGNELRFVVLDEIG--HPVHLDNPPAEAVEEAFRR 539
|
|
| EEVS |
cd08199 |
2-epi-5-epi-valiolone synthase (EEVS); 2-epi-5-epi-valiolone synthase catalyzes the ... |
41-337 |
8.30e-45 |
|
2-epi-5-epi-valiolone synthase (EEVS); 2-epi-5-epi-valiolone synthase catalyzes the cyclization of sedoheptulose 7-phosphate to 2-epi-5-epi-valiolone in the biosynthesis of C(7)N-aminocyclitol-containing products. The cyclization product, 2-epi-5-epi-valiolone ((2S,3S,4S,5R)-5-(hydroxymethyl)cyclohexanon-2,3,4,5-tetrol), is a precursor of the valienamine moiety. The valienamine unit is responsible for their biological activities as various glycosidic hydrolases inhibitors. Two important microbial secondary metabolites, validamycin and acarbose, are used in agricultural and biomedical applications. Validamycin A is an antifungal antibiotic which has a strong trehalase inhibitory activity and has been used to control sheath blight disease in rice caused by Rhizoctonia solani. Acarbose is an alpha-glucosidase inhibitor used for the treatment of type II insulin-independent diabetes. Salbostatin produced by Streptomyces albus also belongs to this family. It exhibits strong trehalase inhibitory activity.
Pssm-ID: 341478 Cd Length: 349 Bit Score: 157.30 E-value: 8.30e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684960172 41 IISDEAVASLH---LQTVVDALQIEQKVFsfVVPSGEKEKSFENFYAAHTSALENKLDRNSLIVALGGGMIGDLAGFVAA 117
Cdd:cd08199 31 VVVDENVDRLYgarIRAYFAAHGIEATIL--VLPGGEANKTMETVLRIVDALDDFGLDRREPVIAIGGGVLLDVVGFAAS 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684960172 118 SFMRGIRFVQVPTTLLAH-DSAVGGKVAINHPLGKNMIGAFHQPEAVVYHTPFLQSLSEKEWRSGYAEVIKHALIGNVKL 196
Cdd:cd08199 109 LYRRGVPYIRVPTTLLGLvDAGVGIKTGVNFGGHKNRLGAYYPPVATLLDRSFLKTLPRRHIRNGLAEIIKMALVKDAEL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684960172 197 YHWLKEEVQTLADLR--DEKLIH-ILTKAIpvkanIVSQDETEKGVRAH-----LNFGHTLGHALEKELGYGnITHGDGV 268
Cdd:cd08199 189 FELLEEHGAALVETRffQDEVADeIIRRAI-----QGMLEELAPNLWEHdlerlVDFGHTFSPILEMAAAPE-LLHGEAV 262
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1684960172 269 AVGMLFAIFLSEQvyKVDLAYEDMKQWF---LRYGYPKMPRDLNVERLVQLMKQDKKANAGAIHMVLMQEYG 337
Cdd:cd08199 263 AIDMALSAVLAYR--RGLLSEEELDRILrlmRRLGLPVWHPLCTPDLLWRALEDIVKHRDGLQRLPLPKGIG 332
|
|
| DHQS-like |
cd08198 |
Dehydroquinate synthase (DHQS) catalyzes the conversion of DAHP to DHQ in shikimate pathway ... |
39-272 |
4.12e-41 |
|
Dehydroquinate synthase (DHQS) catalyzes the conversion of DAHP to DHQ in shikimate pathway for aromatic compounds synthesis; This family contains dehydroquinate synthase-like proteins. 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. The activity of DHQS requires NAD as cofactor. Proteins of this family share sequence similarity and functional motifs with that of dehydroquinate synthase, but the specific function has not been characterized.
Pssm-ID: 341477 Cd Length: 366 Bit Score: 147.72 E-value: 4.12e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684960172 39 VMIISDEAVASLH---LQTVVDALQIEQKVF-----SFVVPSGEKEK-SFENFYAAHTSALENKLDRNSLIVALGGGMIG 109
Cdd:cd08198 33 VLFVIDSGVAAAHpalVKQIERYFQAHPDRLelvapPLIVPGGEAVKnDPALVEEILSAIHDHGLDRHSYVVVIGGGAVL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684960172 110 DLAGFVAASFMRGIRFVQVPTTLLAH-DSAVGGKVAINHPLGKNMIGAFHQPEAVVYHTPFLQSLSEKEWRSGYAEVIKH 188
Cdd:cd08198 113 DAVGFAAAIAHRGIRLIRVPTTVLAQnDSGVGVKNGINFFGKKNFLGTFAPPFAVINDFDFLETLPDRDWRSGIAEAVKV 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684960172 189 ALIGNVKLYHWLKEEVQTLADlRD----EKLI---------HILTkaipvkanivSQDETEKGVRAHLNFGHTLGHALEK 255
Cdd:cd08198 193 ALIKDASFFEWLERNAAALRQ-RDpdamEKLIrrcaelhldHIAA----------SGDPFETGSARPLDFGHWSAHKLEQ 261
|
250
....*....|....*..
gi 1684960172 256 ELGYGnITHGDGVAVGM 272
Cdd:cd08198 262 LSGYA-LRHGEAVAIGI 277
|
|
| aroB |
PRK06203 |
3-dehydroquinate synthase; Reviewed |
69-272 |
4.74e-40 |
|
3-dehydroquinate synthase; Reviewed
Pssm-ID: 235740 Cd Length: 389 Bit Score: 145.42 E-value: 4.74e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684960172 69 VVPSGEKEK-SFENFYAAHTSALENKLDRNSLIVALGGGMIGDLAGFVAASFMRGIRFVQVPTTLLAH-DSAVGGKVAIN 146
Cdd:PRK06203 83 VVPGGEAAKnDPALVEALHAAINRHGIDRHSYVLAIGGGAVLDMVGYAAATAHRGVRLIRIPTTVLAQnDSGVGVKNGIN 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684960172 147 HPLGKNMIGAFHQPEAVVYHTPFLQSLSEKEWRSGYAEVIKHALIGNVKLYHWLKEEVQTLADlRD----EKLI------ 216
Cdd:PRK06203 163 AFGKKNFLGTFAPPYAVINDFAFLTTLPDRDWRAGLAEAVKVALIKDAAFFDWLEAHAAALAA-RDpeamEELIyrcael 241
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1684960172 217 ---HILTkaipvkanivSQDETEKGVRAHLNFGHTLGHALEkELGYGNITHGDGVAVGM 272
Cdd:PRK06203 242 hleHIAG----------GGDPFEFGSSRPLDFGHWSAHKLE-QLTNYALRHGEAVAIGI 289
|
|
| PRK13951 |
PRK13951 |
bifunctional shikimate kinase AroK/3-dehydroquinate synthase AroB; |
68-344 |
1.24e-37 |
|
bifunctional shikimate kinase AroK/3-dehydroquinate synthase AroB;
Pssm-ID: 172457 [Multi-domain] Cd Length: 488 Bit Score: 140.81 E-value: 1.24e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684960172 68 FVVPSGEKEKSFENFYAAHTSALENKLDRNSLIVALGGGMIGDLAGFVAASFMRGIRFVQVPTTLLAH-DSAVGGKVAIN 146
Cdd:PRK13951 209 LLFPDGEEVKTLEHVSRAYYELVRMDFPRGKTIAGVGGGALTDFTGFVASTFKRGVGLSFYPTTLLAQvDASVGGKNAID 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684960172 147 HPLGKNMIGAFHQPEAVVYHTPFLQSLSEKEWRSGYAEVIKHALIGNVKLYhwLKEEVQTLADLRDEKLIHILTKAIPVK 226
Cdd:PRK13951 289 FAGVKNVVGTFRMPDYVIIDPTVTLSMDEGRFEEGVVEAFKMTILSGRGVE--LFDEPEKIEKRNLRVLSEMVKISVEEK 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684960172 227 ANIVSQDETEKGVRAHLNFGHTLGHALEKELGygnITHGDGVAVGMLFAIflsEQVYKVDLAYEDMKQWF---LRYGYPK 303
Cdd:PRK13951 367 ARIVMEDPYDMGLRHALNLGHTLGHVYEMLEG---VPHGIAVAWGIEKET---MYLYRKGIVPKETMRWIvekVKQIVPI 440
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1684960172 304 MPRDLNVERLVQLMKQDKKANAGA-IHMVLMQEYGVVNVVSI 344
Cdd:PRK13951 441 PVPSVDVEKARNLILNDKKILKGSrVRLPYVKEIGKIEFLEV 482
|
|
| DHQ_Fe-ADH |
cd07766 |
Dehydroquinate synthase-like (DHQ-like) and iron-containing alcohol dehydrogenases (Fe-ADH); ... |
39-317 |
8.47e-26 |
|
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: 104.37 E-value: 8.47e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684960172 39 VMIISDEAVASLHLQTVVDALQIEQKVFSFVVPSGEKekSFENFYAAHTSALENKLDrnsLIVALGGGMIGDLAGFVAAS 118
Cdd:cd07766 25 ALVVSDEGVVKGVGEKVADSLKKGLAVAIFDFVGENP--TFEEVKNAVERARAAEAD---AVIAVGGGSTLDTAKAVAAL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684960172 119 FMRGIRFVQVPTTLLAhDSAVGGKVAINHPLGKN-MIGAFHQPEAVVYHTPFLQSLSEKEWRSGYAEVIKHALIGnvkly 197
Cdd:cd07766 100 LNRGIPFIIVPTTAST-DSEVSPKSVITDKGGKNkQVGPHYNPDVVFVDTDITKGLPPRQVASGGVDALAHAVEL----- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684960172 198 hwlkeevqtladlrdEKLIHILTKAIPVKANIVSqdetekgvrahLNFGHTLGHALEKELGygnITHGDGVAVGMLFAIF 277
Cdd:cd07766 174 ---------------EKVVEAATLAGMGLFESPG-----------LGLAHAIGHALTAFEG---IPHGEAVAVGLPYVLK 224
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1684960172 278 LSEQVY-KVDLAYEDMKQWFLRYGYPKMPRDLNV-----ERLVQLM 317
Cdd:cd07766 225 VANDMNpEPEAAIEAVFKFLEDLGLPTHLADLGVskediPKLAEKA 270
|
|
| egsA |
PRK00843 |
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed |
14-203 |
7.07e-08 |
|
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed
Pssm-ID: 179139 Cd Length: 350 Bit Score: 53.74 E-value: 7.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684960172 14 DVHVGKEALSHLITIVQNMQPAvSNVMIISDEAVASLHLQTVVDALQIEQKVFSFVVpsgeKEKSFENFYAAHTSALENK 93
Cdd:PRK00843 13 DVVVGHGVLDDIGDVCSDLKLT-GRALIVTGPTTKKIAGDRVEENLEDAGDVEVVIV----DEATMEEVEKVEEKAKDVN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684960172 94 LDrnsLIVALGGGMIGDLAGFvaASFMRGIRFVQVPTTlLAHDSAVGGKVAINHpLGKNMIGAFHQPEAVVYHTpflQSL 173
Cdd:PRK00843 88 AG---FLIGVGGGKVIDVAKL--AAYRLGIPFISVPTA-ASHDGIASPRASIKG-GGKPVSVKAKPPLAVIADT---EII 157
|
170 180 190
....*....|....*....|....*....|....
gi 1684960172 174 SEKEWR---SGYAEVI-KHALIGNVKLYHWLKEE 203
Cdd:PRK00843 158 AKAPYRllaAGCGDIIsNYTAVKDWRLAHRLRGE 191
|
|
| G1PDH-like |
cd08174 |
Glycerol-1-phosphate dehydrogenase-like; These glycerol-1-phosphate dehydrogenase-like ... |
17-312 |
3.40e-06 |
|
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: 48.29 E-value: 3.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684960172 17 VGKEALSHLITIVQNMQPAVSNVMIISDEAVASLHLQTVVDALQIEQKVFSFVVPSGEkekSFEnfYAAHTSALENKLDr 96
Cdd:cd08174 6 IEEGALEHLGKYLADRNQGFGKVAIVTGEGIDELLGEDILESLEEAGEIVTVEENTDN---SAE--ELAEKAFSLPKVD- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684960172 97 nsLIVALGGGMIGDLAGFVAasFMRGIRFVQVPTTlLAHDS-----AV----GGKVAinhpLGKNMigafhqPEAVVYHT 167
Cdd:cd08174 80 --AIVGIGGGKVLDVAKYAA--FLSKLPFISVPTS-LSNDGiaspvAVlkvdGKRKS----LGAKM------PYGVIVDL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684960172 168 PFLQSLSEKEWRSGYAEvikhaLIGNVK-LYHWL------KEEVQTLA-----------------DLRDEKLIHILTKAI 223
Cdd:cd08174 145 DVIKSAPRRLILAGIGD-----LISNITaLYDWKlaeekgGEPVDDFAyllsrtaadsllntpgkDIKDDEFLKELAESL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684960172 224 pVKANI----------VSQDEtekgvrahlnfgHTLGHALEKeLGYGNITHGDGVAVGMLFAIFLSEQvykvdlAYEDMK 293
Cdd:cd08174 220 -VLSGIameiagssrpASGSE------------HLISHALDK-LFPGPALHGIQVGLGTYFMSFLQGQ------RYEEIR 279
|
330
....*....|....*....
gi 1684960172 294 QWFLRYGYPKMPRDLNVER 312
Cdd:cd08174 280 DVLKRTGFPLNPSDLGLTK 298
|
|
| EutG |
COG1454 |
Alcohol dehydrogenase, class IV [Energy production and conversion]; |
1-131 |
7.60e-06 |
|
Alcohol dehydrogenase, class IV [Energy production and conversion];
Pssm-ID: 441063 [Multi-domain] Cd Length: 381 Bit Score: 47.42 E-value: 7.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684960172 1 MGNIHIQTKskeydVHVGKEALSHLITIVQNMqpAVSNVMIISDEAVASL-HLQTVVDALQ---IEQKVFSFVVPsgekE 76
Cdd:COG1454 2 MFTFRLPTR-----IVFGAGALAELGEELKRL--GAKRALIVTDPGLAKLgLLDRVLDALEaagIEVVVFDDVEP----N 70
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1684960172 77 KSFENFYAAHTSALENKLDrnsLIVALGGG--M---------------IGDLAGFVAASfMRGIRFVQVPTT 131
Cdd:COG1454 71 PTVETVEAGAAAAREFGAD---VVIALGGGsaIdaakaiallatnpgdLEDYLGIKKVP-GPPLPLIAIPTT 138
|
|
| Fe-ADH |
cd08551 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains large ... |
15-149 |
7.48e-05 |
|
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: 44.36 E-value: 7.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684960172 15 VHVGKEALSHLITIVQNMQpaVSNVMIISDEAVASL-HLQTVVDALQ---IEQKVFSFVVPsgekEKSFENFYAAHTSAL 90
Cdd:cd08551 4 IVFGAGALARLGEELKALG--GKKVLLVTDPGLVKAgLLDKVLESLKaagIEVEVFDDVEP----NPTVETVEAAAELAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684960172 91 ENKLDrnsLIVALGGG--MigDLAGfvAASFM------------------RGIRFVQVPTT-----------LLAhDSAV 139
Cdd:cd08551 78 EEGAD---LVIAVGGGsvL--DTAK--AIAVLatnggsirdyegigkvpkPGLPLIAIPTTagtgsevtpnaVIT-DPET 149
|
170
....*....|
gi 1684960172 140 GGKVAINHPL 149
Cdd:cd08551 150 GRKMGIVSPY 159
|
|
| Fe-ADH |
pfam00465 |
Iron-containing alcohol dehydrogenase; |
15-312 |
8.22e-05 |
|
Iron-containing alcohol dehydrogenase;
Pssm-ID: 425696 [Multi-domain] Cd Length: 362 Bit Score: 44.13 E-value: 8.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684960172 15 VHVGKEALSHLITIVQNMQpavSNVMIISDEAVASL-HLQTVVDALQ---IEQKVFSFVVPsgekEKSFENFYAAHTSAL 90
Cdd:pfam00465 4 IVFGAGALAELGEELKRLG---ARALIVTDPGSLKSgLLDKVLASLEeagIEVVVFDGVEP----EPTLEEVDEAAALAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684960172 91 ENKLDrnsLIVALGGGMIGDLAGFVAA---------SFMRG-------IRFVQVPTTlLAHDSAVGGKVAINHPLGKNMI 154
Cdd:pfam00465 77 EAGAD---VIIAVGGGSVIDTAKAIALlltnpgdvwDYLGGkpltkpaLPLIAIPTT-AGTGSEVTPLAVITDTETGEKL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684960172 155 GAFH---QPEAVVYHTPFLQSLSEKEWRSGyaevikhalIGNVkLYHWLKEEVQTLA-DLRD---EKLIHILTKAIPVka 227
Cdd:pfam00465 153 GIFSpklLPDLAILDPELTLTLPPRLTAAT---------GMDA-LAHAVEAYVSKGAnPLTDalaLEAIRLIAENLPR-- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684960172 228 niVSQDETEKGVRAHL------------NFGHTLGHALEKELGYG-NITHGDGVAV----GMLF--------------AI 276
Cdd:pfam00465 221 --AVADGEDLEARENMllastlaglafsNAGLGAAHALAHALGGRyGIPHGLANAIllpyVLRFnapaapeklaqlarAL 298
|
330 340 350
....*....|....*....|....*....|....*.
gi 1684960172 277 FLSEQVYKVDLAYEDMKQWFLRYGYPKMPRDLNVER 312
Cdd:pfam00465 299 GEDSDEEAAEEAIEALRELLRELGLPTTLSELGVTE 334
|
|
| Fe-ADH-like |
cd08194 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
15-106 |
9.64e-05 |
|
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: 44.06 E-value: 9.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684960172 15 VHVGKEALSHLITIVQNMqpAVSNVMIISDEAVASL-HLQTVVDALQ---IEQKVFSFVVPsgekEKSFENFYAAHTSAL 90
Cdd:cd08194 4 IIIGGGALEELGEEAASL--GGKRALIVTDKVMVKLgLVDKVTQLLAeagIAYAVFDDVVS----EPTDEMVEEGLALYK 77
|
90
....*....|....*.
gi 1684960172 91 ENKLDrnsLIVALGGG 106
Cdd:cd08194 78 EGGCD---FIVALGGG 90
|
|
| Gro1PDH |
cd08173 |
Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) catalyzes the reversible conversion between ... |
15-278 |
1.56e-04 |
|
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: 43.31 E-value: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684960172 15 VHVGKEALSHLITIVQNMQPAvSNVMIISDEAVASLHLQTVVDALQIEQKVFSFV-VPSGEKEKSFENFYAahtsalENK 93
Cdd:cd08173 5 VVVGHGAINKIGEVLKKLLLG-KRALIITGPNTYKIAGKRVEDLLESSGVEVVIVdIATIEEAAEVEKVKK------LIK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684960172 94 LDRNSLIVALGGGMIGDLAGfvAASFMRGIRFVQVPTTlLAHDSAVGGKVAINHPLGKNMIGAfHQPEAVVYHTpflqsl 173
Cdd:cd08173 78 ESKADFIIGVGGGKVIDVAK--YAAYKLNLPFISIPTS-ASHDGIASPFASIKGGDKPYSIKA-KAPIAIIADT------ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684960172 174 sekewrsgyaEVIKHA-----------LIGNV------KLYHWLKEE-----VQTLADLRDEkliHILTKAIPVKANIvs 231
Cdd:cd08173 148 ----------EIISKApkrllaagcgdLISNItavkdwRLAHRLKGEyyseyAASLALMSAK---LIIENADLIKPGL-- 212
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1684960172 232 QDETEKGVRAHLNFG----------------HTLGHALEKeLGYGNITHGDGVAVGMLFAIFL 278
Cdd:cd08173 213 EEGVRTVVKALISSGvamsiagssrpasgseHLFSHALDK-LAPGPALHGEQCGVGTIMMAYL 274
|
|
| Fe-ADH-like |
cd08196 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
15-131 |
1.81e-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: 341475 [Multi-domain] Cd Length: 367 Bit Score: 42.95 E-value: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684960172 15 VHVGKEALSHLITIVQNMQpaVSNVMIISDE-AVASLHLQTVVDAL-QIEQKVFSFVVPsgekEKSFENFYAAHTSALEN 92
Cdd:cd08196 9 IIFGEGILKELPDIIKELG--GKRGLLVTDPsFIKSGLAKRIVESLkGRIVAVFSDVEP----NPTVENVDKCARLAREN 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1684960172 93 KLDrnsLIVALGGGMIGDLAGFVAA---------SFM--------RGIRFVQVPTT 131
Cdd:cd08196 83 GAD---FVIAIGGGSVLDTAKAAAClaktdgsieDYLegkkkipkKGLPLIAIPTT 135
|
|
| Fe-ADH-like |
cd14862 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
17-148 |
8.09e-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: 341484 [Multi-domain] Cd Length: 375 Bit Score: 41.06 E-value: 8.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684960172 17 VGKEALSHLITIVQnmqpavSNVMIISDEAVASL-HLQTVVDALQ---IEQKVFSFVVPsgekEKSFENFYAAHTSALEN 92
Cdd:cd14862 11 FGEDALSHLEQLSG------KRALIVTDKVLVKLgLLKKVLKRLLqagFEVEVFDEVEP----EPPLETVLKGAEAMREF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684960172 93 KLDrnsLIVALGGGMIGDLA------------GFVAASFM------RGIRFVQVPTT----------LLAHDSAVGGKVA 144
Cdd:cd14862 81 EPD---LIIALGGGSVMDAAkaawvlyerpdlDPEDISPLdllglrKKAKLIAIPTTsgtgseatwaIVLTDTEEPRKIA 157
|
....
gi 1684960172 145 INHP 148
Cdd:cd14862 158 VANP 161
|
|
| G1PDH |
cd08175 |
Glycerol-1-phosphate dehydrogenase (G1PDH) catalyzes the reversible reduction of ... |
14-312 |
2.72e-03 |
|
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: 39.42 E-value: 2.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684960172 14 DVHVGKEALSHLITIVQNMQPAvSNVMIISDE---AVASlhlQTVVDALQIEQKVFSFVVPSGEkeksfENFYAAHtSAL 90
Cdd:cd08175 3 EIVIGEGALKKLPEYLKELFGG-KKVLVVADEntyAAAG---EEVEAALEEAGVTVCLLIFPGE-----GDLIADE-AAV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684960172 91 ENKLDR----NSLIVALGGGMIGDLAGFVaaSFMRGIRFVQVPTTllahdSAVGGKVAINHPLgknMIGAF------HQP 160
Cdd:cd08175 73 GKVLLElekdTDLIIAVGSGTINDLTKYA--AYKLGIPYISVPTA-----PSMDGYTSSGAPI---IVDGVkktfpaHAP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684960172 161 EAVVYHTPFL----QSLSekewRSGYAEVI-K----------HALIG---------NVKLYhwLKEEVQTLADL--RDEK 214
Cdd:cd08175 143 KAIFADLDVLanapQRMI----AAGFGDLLgKytaladwklsHLLGGeyycpevadLVQEA--LEKCLDNAEGIaaRDPE 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684960172 215 LIHILTKAIpvkanIVSqdetekGVrAHLNFG---------HTLGHALEKE---LGYGNITHGDGVAVGMLF--AIFLSE 280
Cdd:cd08175 217 AIEALMEAL-----ILS------GL-AMQLVGnsrpasgaeHHLSHYWEMEflrLGKPPVLHGEKVGVGTLLiaALYILE 284
|
330 340 350
....*....|....*....|....*....|..
gi 1684960172 281 QVYkvdlAYEDMKQWFLRYGYPKMPRDLNVER 312
Cdd:cd08175 285 QLP----PPEELRELLRKAGAPTTPEDLGIDR 312
|
|
| GldA |
COG0371 |
Glycerol dehydrogenase or related enzyme, iron-containing ADH family [Energy production and ... |
15-139 |
2.76e-03 |
|
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: 39.38 E-value: 2.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1684960172 15 VHVGKEALSHLITIVQNMQpavSNVMIISDEAVASLHLQTVVDALQIEQKVFSFVVPSGEKekSFENFYAAHTSALENKL 94
Cdd:COG0371 9 YVQGEGALDELGEYLADLG---KRALIITGPTALKAAGDRLEESLEDAGIEVEVEVFGGEC--SEEEIERLAEEAKEQGA 83
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1684960172 95 DrnsLIVALGGGMIGDLAGFVAasFMRGIRFVQVPTTlLAHDSAV 139
Cdd:COG0371 84 D---VIIGVGGGKALDTAKAVA--YRLGLPVVSVPTI-ASTDAPA 122
|
|
| |
