|
Name |
Accession |
Description |
Interval |
E-value |
| AroB |
COG0337 |
3-dehydroquinate synthetase [Amino acid transport and metabolism]; 3-dehydroquinate synthetase ... |
1-353 |
5.20e-153 |
|
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: 434.52 E-value: 5.20e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446448964 1 MGNIHIQTKSKEYDVHVGKEVLSNLTTIVQNMQPAvSNVMIISDEAVASLHLQTVIDALQVEQ-HVFSFVVPSGEKEKSF 79
Cdd:COG0337 1 MQTLTVNLGERSYDIRIGRGLLDELGELLAELLKG-RRVLVVTDENVAPLYGERLRAALEAAGfEVHLLVLPDGEASKTL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446448964 80 ENFYAAHTSALENKLDRNSLILALGGGMIGDLAGFVAASFMRGIRFVQVPTTLLAH-DSAVGGKVAINHPLGKNMIGAFH 158
Cdd:COG0337 80 ETLERILDALLEAGLDRDDLVVALGGGVVGDLAGFAAATYLRGVPFIQVPTTLLAQvDSSVGGKTGVNHPGGKNLIGAFH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446448964 159 QPEAVVYHTPFLQSLPEKEWRSGYAEVIKHALIGDVELYHWLKEEVQTLADLHDEKLIHILTKAIPVKANVVSQDETEKG 238
Cdd:COG0337 160 QPRAVLIDLDFLKTLPERELRAGLAEVIKYGLIADAEFFEWLEENADALLARDPEALEEAIARSCEIKAEVVAADERESG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446448964 239 VRAHLNFGHTLGHALEKELGYgNITHGDGVAVGMLFAIFLSEQVYKVDLA-YEDMKQWFLKYGYPKMPGDLNVERLVQLM 317
Cdd:COG0337 240 LRALLNFGHTFGHAIEAATGY-RLLHGEAVAIGMVFAARLSARLGLLSEEdVERIRALLEALGLPTRLPALDPEALLAAM 318
|
330 340 350
....*....|....*....|....*....|....*..
gi 446448964 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 |
2.22e-148 |
|
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: 422.24 E-value: 2.22e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446448964 12 EYDVHVGKEVLSNLTTIVQNMQPavSNVMIISDEAVASLHLQTVIDAL-QVEQHVFSFVVPSGEKEKSFENFYAAHTSAL 90
Cdd:cd08195 1 SYPILIGSGLLDKLGELLELKKG--SKVVIVTDENVAKLYGELLLKSLeAAGFKVEVIVIPAGEKSKSLETVERIYDFLL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446448964 91 ENKLDRNSLILALGGGMIGDLAGFVAASFMRGIRFVQVPTTLLAH-DSAVGGKVAINHPLGKNMIGAFHQPEAVVYHTPF 169
Cdd:cd08195 79 EAGLDRDSLLIALGGGVVGDLAGFVASTYMRGIPFIQVPTTLLAQvDSSIGGKTGINLPGGKNLIGAFYQPKAVLIDPDF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446448964 170 LQSLPEKEWRSGYAEVIKHALIGDVELYHWLKEEVQTLADLHDEKLIHILTKAIPVKANVVSQDETEKGVRAHLNFGHTL 249
Cdd:cd08195 159 LKTLPEREFRSGLAEVIKYGLIADKELFEFLEKNLDKILARDPEALEEIIARSVEIKADIVEEDEREKGLRAILNFGHTF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446448964 250 GHALEKELGYGnITHGDGVAVGMLFAIFLSEQVYKVDLA-YEDMKQWFLKYGYPKMPGDLNVERLVQLMKQDKKANAGAI 328
Cdd:cd08195 239 GHAIESASGYK-LLHGEAVAIGMVAAARLSVKLGLLSEEdLERIRALLKKLGLPTSIKDLDPEELLEAMKRDKKNRGGKI 317
|
330 340
....*....|....*....|....*.
gi 446448964 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 |
7.70e-135 |
|
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: 384.93 E-value: 7.70e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446448964 67 SFVVPSGEKEKSFENFYAAHTSALENKLDRNSLILALGGGMIGDLAGFVAASFMRGIRFVQVPTTLLAH-DSAVGGKVAI 145
Cdd:pfam01761 1 TIVIPDGEKSKTLETLERIYDALLEAGLDRSSLLIALGGGVIGDLAGFVAATYMRGIRFIQVPTTLLAQvDSSVGGKTGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446448964 146 NHPLGKNMIGAFHQPEAVVYHTPFLQSLPEKEWRSGYAEVIKHALIGDVELYHWLKEEVQTLADLHDEKLIHILTKAIPV 225
Cdd:pfam01761 81 NHPLGKNLIGAFYQPKAVLIDLDFLKTLPDREFRAGLAEVIKYGLIADAEFFEWLEENAEALLNLDPDALEEAIARSCEV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446448964 226 KANVVSQDETEKGVRAHLNFGHTLGHALEKELGYGNITHGDGVAVGMLFAIFLSEQVYKVDLAY-EDMKQWFLKYGYPKM 304
Cdd:pfam01761 161 KADVVAQDEKESGLRALLNLGHTFGHAIEALSGYGALLHGEAVAIGMVLAARLSERLGLLDEADvERIRALLKKYGLPTS 240
|
250
....*....|....*....
gi 446448964 305 PGDLNVERLVQLMKQDKKA 323
Cdd:pfam01761 241 LPDLDVEQLLAAMARDKKV 259
|
|
| aroB |
TIGR01357 |
3-dehydroquinate synthase; This model represents 3-dehydroquinate synthase, the enzyme ... |
13-337 |
4.65e-125 |
|
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: 363.11 E-value: 4.65e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446448964 13 YDVHVGKEVLSNLTTIVQNMQPavsnVMIISDEAVASLHLQTVIDALQ-VEQHVFSFVVPSGEKEKSFENFYAAHTSALE 91
Cdd:TIGR01357 1 YPVHVGEGLLDQLVEELAEPSK----LVIITDETVADLYGDKLLEALQaLGYNVLKLTVPDGEESKSLETVQRLYDQLLE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446448964 92 NKLDRNSLILALGGGMIGDLAGFVAASFMRGIRFVQVPTTLLAH-DSAVGGKVAINHPLGKNMIGAFHQPEAVVYHTPFL 170
Cdd:TIGR01357 77 AGLDRSSTIIALGGGVVGDLAGFVAATYMRGIRFIQVPTTLLAMvDSSVGGKTGINFPGGKNLIGTFYQPKAVLIDPDFL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446448964 171 QSLPEKEWRSGYAEVIKHALIGDVELYHWLKEEVQTLADLHDEKLIH-ILTKAIPVKANVVSQDETEKGVRAHLNFGHTL 249
Cdd:TIGR01357 157 KTLPDRELRSGMAEVIKHGLIADAELFDELESNDKLRLNLQELEHLEeLIKRSIEVKASIVAEDEKESGLRAILNFGHTI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446448964 250 GHALEKELGYGNITHGDGVAVGMLFAIFLSEQVYKVDLA-YEDMKQWFLKYGYP-KMPGDLNVERLVQLMKQDKKANAGA 327
Cdd:TIGR01357 237 GHAIEAEAGYGKIPHGEAVAIGMVCEAKLSERLGLLPAElIERLVQLLKRYGLPtDLPKDLDVDELLNAMLNDKKNSGGK 316
|
330
....*....|
gi 446448964 328 IHMVLMQEYG 337
Cdd:TIGR01357 317 IRFVLLEEIG 326
|
|
| PLN02834 |
PLN02834 |
3-dehydroquinate synthase |
10-358 |
1.12e-94 |
|
3-dehydroquinate synthase
Pssm-ID: 215448 Cd Length: 433 Bit Score: 288.98 E-value: 1.12e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446448964 10 SKEYDVHVGKEVLSNlTTIVQNMQPAvSNVMIISDEAVASLHLQTVIDALQ---VEQHVFSFVVPSGEKEKSFENFYAAH 86
Cdd:PLN02834 76 DRSYPIYIGSGLLDH-GELLQRHVHG-KRVLVVTNETVAPLYLEKVVEALTakgPELTVESVILPDGEKYKDMETLMKVF 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446448964 87 TSALENKLDRNSLILALGGGMIGDLAGFVAASFMRGIRFVQVPTTLLAH-DSAVGGKVAINHPLGKNMIGAFHQPEAVVY 165
Cdd:PLN02834 154 DKALESRLDRRCTFVALGGGVIGDMCGFAAASYQRGVNFVQIPTTVMAQvDSSVGGKTGVNHPLGKNMIGAFYQPQCVLI 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446448964 166 HTPFLQSLPEKEWRSGYAEVIKHALIGDVELYHWLKEEVQTLADLHDEKLIHILTKAIPVKANVVSQDETEKGVRAHLNF 245
Cdd:PLN02834 234 DTDTLATLPDRELASGIAEVVKYGLIRDAEFFEWQEANMEKLLARDPGALAYAIKRSCENKAEVVSLDEKESGLRATLNL 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446448964 246 GHTLGHALEKELGYGNITHGDGVAVGMLFAIFLSEQVYKVDLAYED-----MKQWFLkygyPKMPGD-LNVERLVQLMKQ 319
Cdd:PLN02834 314 GHTFGHAIETGPGYGEWLHGEAVAAGTVMAADMSYRLGWIDMSLVNrifalLKRAKL----PTNPPEkMTVEMFKSLMAV 389
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 446448964 320 DKKANAGAIHMVLMQ-EYGvvNVVSISD---ETVHIALEAFQK 358
Cdd:PLN02834 390 DKKVADGLLRLILLKgELG--NCVFTGDfdrEALEETLRAFCK 430
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| AroB |
COG0337 |
3-dehydroquinate synthetase [Amino acid transport and metabolism]; 3-dehydroquinate synthetase ... |
1-353 |
5.20e-153 |
|
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: 434.52 E-value: 5.20e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446448964 1 MGNIHIQTKSKEYDVHVGKEVLSNLTTIVQNMQPAvSNVMIISDEAVASLHLQTVIDALQVEQ-HVFSFVVPSGEKEKSF 79
Cdd:COG0337 1 MQTLTVNLGERSYDIRIGRGLLDELGELLAELLKG-RRVLVVTDENVAPLYGERLRAALEAAGfEVHLLVLPDGEASKTL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446448964 80 ENFYAAHTSALENKLDRNSLILALGGGMIGDLAGFVAASFMRGIRFVQVPTTLLAH-DSAVGGKVAINHPLGKNMIGAFH 158
Cdd:COG0337 80 ETLERILDALLEAGLDRDDLVVALGGGVVGDLAGFAAATYLRGVPFIQVPTTLLAQvDSSVGGKTGVNHPGGKNLIGAFH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446448964 159 QPEAVVYHTPFLQSLPEKEWRSGYAEVIKHALIGDVELYHWLKEEVQTLADLHDEKLIHILTKAIPVKANVVSQDETEKG 238
Cdd:COG0337 160 QPRAVLIDLDFLKTLPERELRAGLAEVIKYGLIADAEFFEWLEENADALLARDPEALEEAIARSCEIKAEVVAADERESG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446448964 239 VRAHLNFGHTLGHALEKELGYgNITHGDGVAVGMLFAIFLSEQVYKVDLA-YEDMKQWFLKYGYPKMPGDLNVERLVQLM 317
Cdd:COG0337 240 LRALLNFGHTFGHAIEAATGY-RLLHGEAVAIGMVFAARLSARLGLLSEEdVERIRALLEALGLPTRLPALDPEALLAAM 318
|
330 340 350
....*....|....*....|....*....|....*..
gi 446448964 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 |
2.22e-148 |
|
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: 422.24 E-value: 2.22e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446448964 12 EYDVHVGKEVLSNLTTIVQNMQPavSNVMIISDEAVASLHLQTVIDAL-QVEQHVFSFVVPSGEKEKSFENFYAAHTSAL 90
Cdd:cd08195 1 SYPILIGSGLLDKLGELLELKKG--SKVVIVTDENVAKLYGELLLKSLeAAGFKVEVIVIPAGEKSKSLETVERIYDFLL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446448964 91 ENKLDRNSLILALGGGMIGDLAGFVAASFMRGIRFVQVPTTLLAH-DSAVGGKVAINHPLGKNMIGAFHQPEAVVYHTPF 169
Cdd:cd08195 79 EAGLDRDSLLIALGGGVVGDLAGFVASTYMRGIPFIQVPTTLLAQvDSSIGGKTGINLPGGKNLIGAFYQPKAVLIDPDF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446448964 170 LQSLPEKEWRSGYAEVIKHALIGDVELYHWLKEEVQTLADLHDEKLIHILTKAIPVKANVVSQDETEKGVRAHLNFGHTL 249
Cdd:cd08195 159 LKTLPEREFRSGLAEVIKYGLIADKELFEFLEKNLDKILARDPEALEEIIARSVEIKADIVEEDEREKGLRAILNFGHTF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446448964 250 GHALEKELGYGnITHGDGVAVGMLFAIFLSEQVYKVDLA-YEDMKQWFLKYGYPKMPGDLNVERLVQLMKQDKKANAGAI 328
Cdd:cd08195 239 GHAIESASGYK-LLHGEAVAIGMVAAARLSVKLGLLSEEdLERIRALLKKLGLPTSIKDLDPEELLEAMKRDKKNRGGKI 317
|
330 340
....*....|....*....|....*.
gi 446448964 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 |
7.70e-135 |
|
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: 384.93 E-value: 7.70e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446448964 67 SFVVPSGEKEKSFENFYAAHTSALENKLDRNSLILALGGGMIGDLAGFVAASFMRGIRFVQVPTTLLAH-DSAVGGKVAI 145
Cdd:pfam01761 1 TIVIPDGEKSKTLETLERIYDALLEAGLDRSSLLIALGGGVIGDLAGFVAATYMRGIRFIQVPTTLLAQvDSSVGGKTGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446448964 146 NHPLGKNMIGAFHQPEAVVYHTPFLQSLPEKEWRSGYAEVIKHALIGDVELYHWLKEEVQTLADLHDEKLIHILTKAIPV 225
Cdd:pfam01761 81 NHPLGKNLIGAFYQPKAVLIDLDFLKTLPDREFRAGLAEVIKYGLIADAEFFEWLEENAEALLNLDPDALEEAIARSCEV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446448964 226 KANVVSQDETEKGVRAHLNFGHTLGHALEKELGYGNITHGDGVAVGMLFAIFLSEQVYKVDLAY-EDMKQWFLKYGYPKM 304
Cdd:pfam01761 161 KADVVAQDEKESGLRALLNLGHTFGHAIEALSGYGALLHGEAVAIGMVLAARLSERLGLLDEADvERIRALLKKYGLPTS 240
|
250
....*....|....*....
gi 446448964 305 PGDLNVERLVQLMKQDKKA 323
Cdd:pfam01761 241 LPDLDVEQLLAAMARDKKV 259
|
|
| aroB |
TIGR01357 |
3-dehydroquinate synthase; This model represents 3-dehydroquinate synthase, the enzyme ... |
13-337 |
4.65e-125 |
|
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: 363.11 E-value: 4.65e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446448964 13 YDVHVGKEVLSNLTTIVQNMQPavsnVMIISDEAVASLHLQTVIDALQ-VEQHVFSFVVPSGEKEKSFENFYAAHTSALE 91
Cdd:TIGR01357 1 YPVHVGEGLLDQLVEELAEPSK----LVIITDETVADLYGDKLLEALQaLGYNVLKLTVPDGEESKSLETVQRLYDQLLE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446448964 92 NKLDRNSLILALGGGMIGDLAGFVAASFMRGIRFVQVPTTLLAH-DSAVGGKVAINHPLGKNMIGAFHQPEAVVYHTPFL 170
Cdd:TIGR01357 77 AGLDRSSTIIALGGGVVGDLAGFVAATYMRGIRFIQVPTTLLAMvDSSVGGKTGINFPGGKNLIGTFYQPKAVLIDPDFL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446448964 171 QSLPEKEWRSGYAEVIKHALIGDVELYHWLKEEVQTLADLHDEKLIH-ILTKAIPVKANVVSQDETEKGVRAHLNFGHTL 249
Cdd:TIGR01357 157 KTLPDRELRSGMAEVIKHGLIADAELFDELESNDKLRLNLQELEHLEeLIKRSIEVKASIVAEDEKESGLRAILNFGHTI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446448964 250 GHALEKELGYGNITHGDGVAVGMLFAIFLSEQVYKVDLA-YEDMKQWFLKYGYP-KMPGDLNVERLVQLMKQDKKANAGA 327
Cdd:TIGR01357 237 GHAIEAEAGYGKIPHGEAVAIGMVCEAKLSERLGLLPAElIERLVQLLKRYGLPtDLPKDLDVDELLNAMLNDKKNSGGK 316
|
330
....*....|
gi 446448964 328 IHMVLMQEYG 337
Cdd:TIGR01357 317 IRFVLLEEIG 326
|
|
| PLN02834 |
PLN02834 |
3-dehydroquinate synthase |
10-358 |
1.12e-94 |
|
3-dehydroquinate synthase
Pssm-ID: 215448 Cd Length: 433 Bit Score: 288.98 E-value: 1.12e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446448964 10 SKEYDVHVGKEVLSNlTTIVQNMQPAvSNVMIISDEAVASLHLQTVIDALQ---VEQHVFSFVVPSGEKEKSFENFYAAH 86
Cdd:PLN02834 76 DRSYPIYIGSGLLDH-GELLQRHVHG-KRVLVVTNETVAPLYLEKVVEALTakgPELTVESVILPDGEKYKDMETLMKVF 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446448964 87 TSALENKLDRNSLILALGGGMIGDLAGFVAASFMRGIRFVQVPTTLLAH-DSAVGGKVAINHPLGKNMIGAFHQPEAVVY 165
Cdd:PLN02834 154 DKALESRLDRRCTFVALGGGVIGDMCGFAAASYQRGVNFVQIPTTVMAQvDSSVGGKTGVNHPLGKNMIGAFYQPQCVLI 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446448964 166 HTPFLQSLPEKEWRSGYAEVIKHALIGDVELYHWLKEEVQTLADLHDEKLIHILTKAIPVKANVVSQDETEKGVRAHLNF 245
Cdd:PLN02834 234 DTDTLATLPDRELASGIAEVVKYGLIRDAEFFEWQEANMEKLLARDPGALAYAIKRSCENKAEVVSLDEKESGLRATLNL 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446448964 246 GHTLGHALEKELGYGNITHGDGVAVGMLFAIFLSEQVYKVDLAYED-----MKQWFLkygyPKMPGD-LNVERLVQLMKQ 319
Cdd:PLN02834 314 GHTFGHAIETGPGYGEWLHGEAVAAGTVMAADMSYRLGWIDMSLVNrifalLKRAKL----PTNPPEkMTVEMFKSLMAV 389
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 446448964 320 DKKANAGAIHMVLMQ-EYGvvNVVSISD---ETVHIALEAFQK 358
Cdd:PLN02834 390 DKKVADGLLRLILLKgELG--NCVFTGDfdrEALEETLRAFCK 430
|
|
| DOIS |
cd08197 |
2-deoxy-scyllo-inosose synthase (DOIS) catalyzes carbocycle formation from ... |
12-354 |
3.59e-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: 254.05 E-value: 3.59e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446448964 12 EYDVHVGKEVLSNLTTIVQNMqpAVSNVMIISDEAVASLHLQTVIDAL-QVEQHVFSFVVPSGEKEKSFENFYAAHTSAL 90
Cdd:cd08197 1 LTDIYLGRGILESLLSILEEL--KADRHFLVTDSNVNDLYGDRLLEGLkKAGIPVELLVVPAGESNKTLSTLTELAERLI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446448964 91 ENKLDRNSLILALGGGMIGDLAGFVAASFMRGIRFVQVPTTLLA-HDSAVGGKVAINHPLGKNMIGAFHQPEAVVYHTPF 169
Cdd:cd08197 79 AAGITRRSVIIALGGGVVGNIAGLLAGLLYRGIRLVHVPTTLLAqSDSVLSLKQAVNGKSGKNLVGSYYAPLFVFVDTEF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446448964 170 LQSLPEKEWRSGYAEVIKHALIGDVELYHWLKEEVQTLADLHDEKLIHILTKAIPVKANVVSQDETEKGVRAHLNFGHTL 249
Cdd:cd08197 159 LKTLPPRQIRSGLCEAIKNALIQDPEFLDYLEDYLNSDLDYDPEFLEKVIDLSIEAKLEVLSNDPYEKKEGLILEYGHTV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446448964 250 GHALEKeLGYGNITHGDGVAVGMLFAI-------FLSEQVykVDLAYEDMKqwflKYGYPKM-PGDLNVERLVQLMKQDK 321
Cdd:cd08197 239 GHAIEL-LSGGELSHGEAVAIGMCVAAeishllgLLSEED--VDKHYELLE----KIGLPTIiPDGISVEAILEVIRYDN 311
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 446448964 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 |
5.00e-80 |
|
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: 247.70 E-value: 5.00e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446448964 12 EYDVHVGKEVLSNLTTIVQNMQPAVSnvMIISDEAVASLHLQTVIDALQVEQHVFSFVVPSGEKEKSFENFYAAHTSALE 91
Cdd:cd08169 1 EYPVFFGEGVFESVNSYIPRDAFDQC--LIIVDSGVPDLIVNYLAEYFGYYLEVHVFIIQGGEAYKTFQTVVEELERAAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446448964 92 NKLDRNSLILALGGGMIGDLAGFVAASFMRGIRFVQVPTTLLAH-DSAVGGKVAINHPLGKNMIGAFHQPEAVVYHTPFL 170
Cdd:cd08169 79 LHLNRHSAVVAVGGGATGDVVGFAAATYFRGIAFIRVPTTLLAQsDSSVGIKVGINTRGGKNLLGAFYPPRAVFADFSFL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446448964 171 QSLPEKEWRSGYAEVIKHALIGDVELYHWL-----KEEVQTLADLhdEKLIHiltKAIPVKANVVSQDETEKGVRAHLNF 245
Cdd:cd08169 159 KTLPFRQVRAGMAELVKMALIADNDFFEFLedkanSATVYSPEQL--EKLIN---KCISLKLDVVVADEDEQGKRRGLNY 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446448964 246 GHTLGHALEKELGYGnITHGDGVAVGMLFAIFLSEQVYKVDLAYEDMKQWFL-KYGYP-KMPGDLNVERLVQLMKQDKKA 323
Cdd:cd08169 234 GHTFGHALELASGYK-IPHGEAVAVGMAYAAKIANRLGLLPEHDVSRIIWLLnKLGLPlDHPLALDPDSLYEYLESDKKS 312
|
330
....*....|....
gi 446448964 324 NAGAIHMVLMQEYG 337
Cdd:cd08169 313 LYGNLGMILLSGVG 326
|
|
| PRK14021 |
PRK14021 |
bifunctional shikimate kinase/3-dehydroquinate synthase; Provisional |
4-358 |
8.92e-51 |
|
bifunctional shikimate kinase/3-dehydroquinate synthase; Provisional
Pssm-ID: 184458 [Multi-domain] Cd Length: 542 Bit Score: 177.36 E-value: 8.92e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446448964 4 IHIQTKSKE-YDVHVGKEVLSNLttiVQNMQPAVSNVMIISDEAVA--SLHLQTVIDalQVEQHVFSFVVPSGEKEKSFE 80
Cdd:PRK14021 179 VHVTGAGIEpYDVRIGEGAMNHL---PQVLGPKPVKVALIHTQPVQrhSDRARTLLR--QGGYEVSDIVIPDAEAGKTIE 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446448964 81 NFYAAHTSALENKLDRNSLILALGGGMIGDLAGFVAASFMRGIRFVQVPTTLLAH-DSAVGGKVAINHPLGKNMIGAFHQ 159
Cdd:PRK14021 254 VANGIWQRLGNEGFTRSDAIVGLGGGAATDLAGFVAATWMRGIRYVNCPTSLLAMvDASTGGKTGINTPQGKNLVGSFYT 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446448964 160 PEAVVYHTPFLQSLPEKEWRSGYAEVIKHALIGDVELYHWLKEEVQTL----------ADLHDeKLIHILTKAIPVKANV 229
Cdd:PRK14021 334 PAGVLADTKTLATLPNDIFIEGLGEVAKSGFIRDPEILRILEDHAAELrafdgstflgSPLED-VVAELIERTVKVKAYH 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446448964 230 VSQDETEKGVRAHLNFGHTLGHALEKeLGYGNITHGDGVAVGMLFAIFLSEQVYKVDLAYEDMKQWFL-KYGYPKMPGDL 308
Cdd:PRK14021 413 VSSDLKEAGLREFLNYGHTLGHAIEK-LEHFRWRHGNAVAVGMVYAAELAHLLGYIDQDLVDYHRSLLaSLGLPTSWNGG 491
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 446448964 309 NVERLVQLMKQDKKANAGAIHMVLMQEYGvvNVVSISDETVHIALEAFQK 358
Cdd:PRK14021 492 SFDDVLALMHRDKKARGNELRFVVLDEIG--HPVHLDNPPAEAVEEAFRR 539
|
|
| EEVS |
cd08199 |
2-epi-5-epi-valiolone synthase (EEVS); 2-epi-5-epi-valiolone synthase catalyzes the ... |
12-337 |
4.86e-47 |
|
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: 163.08 E-value: 4.86e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446448964 12 EYDVHVGKEVLS--NlTTIVQNMQPAVSNVMIISDEAVASLH---LQTVIDALQVEQHVFsfVVPSGEKEKSFENFYAAH 86
Cdd:cd08199 1 SYDVVLVDDLFDpeN-PTLADAYGRPGRRRLVVVDENVDRLYgarIRAYFAAHGIEATIL--VLPGGEANKTMETVLRIV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446448964 87 TSALENKLDRNSLILALGGGMIGDLAGFVAASFMRGIRFVQVPTTLLAH-DSAVGGKVAINHPLGKNMIGAFHQPEAVVY 165
Cdd:cd08199 78 DALDDFGLDRREPVIAIGGGVLLDVVGFAASLYRRGVPYIRVPTTLLGLvDAGVGIKTGVNFGGHKNRLGAYYPPVATLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446448964 166 HTPFLQSLPEKEWRSGYAEVIKHALIGDVELYHWLKEEVQTLADLHDEklihiltkaipvkANVVSQDETEKGVRAHLN- 244
Cdd:cd08199 158 DRSFLKTLPRRHIRNGLAEIIKMALVKDAELFELLEEHGAALVETRFF-------------QDEVADEIIRRAIQGMLEe 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446448964 245 ---------------FGHTLGHALEKELGYGnITHGDGVAVGMLFAIFLSEQvyKVDLAYEDMKQWF---LKYGYPKMPG 306
Cdd:cd08199 225 lapnlwehdlerlvdFGHTFSPILEMAAAPE-LLHGEAVAIDMALSAVLAYR--RGLLSEEELDRILrlmRRLGLPVWHP 301
|
330 340 350
....*....|....*....|....*....|.
gi 446448964 307 DLNVERLVQLMKQDKKANAGAIHMVLMQEYG 337
Cdd:cd08199 302 LCTPDLLWRALEDIVKHRDGLQRLPLPKGIG 332
|
|
| aroB |
PRK06203 |
3-dehydroquinate synthase; Reviewed |
12-272 |
4.64e-43 |
|
3-dehydroquinate synthase; Reviewed
Pssm-ID: 235740 Cd Length: 389 Bit Score: 153.51 E-value: 4.64e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446448964 12 EYDVHVGKEV--LSN---LTTIVQNMQPAVSNVMIISDEAVASLH--LQTVIDA-LQVEQHVFS-----FVVPSGEKEK- 77
Cdd:PRK06203 13 EYPVYFTRDLfsPENpllAEVLAADGEGKPKKVLVVIDSGVLRAHpdLLEQITAyFAAHADVLElvaepLVVPGGEAAKn 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446448964 78 SFENFYAAHTSALENKLDRNSLILALGGGMIGDLAGFVAASFMRGIRFVQVPTTLLAH-DSAVGGKVAINHPLGKNMIGA 156
Cdd:PRK06203 93 DPALVEALHAAINRHGIDRHSYVLAIGGGAVLDMVGYAAATAHRGVRLIRIPTTVLAQnDSGVGVKNGINAFGKKNFLGT 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446448964 157 FHQPEAVVYHTPFLQSLPEKEWRSGYAEVIKHALIGDVELYHWLKEEVQTL---------------ADLHdekLIHILTk 221
Cdd:PRK06203 173 FAPPYAVINDFAFLTTLPDRDWRAGLAEAVKVALIKDAAFFDWLEAHAAALaardpeameeliyrcAELH---LEHIAG- 248
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 446448964 222 aipvkanvvSQDETEKGVRAHLNFGHTLGHALEkELGYGNITHGDGVAVGM 272
Cdd:PRK06203 249 ---------GGDPFEFGSSRPLDFGHWSAHKLE-QLTNYALRHGEAVAIGI 289
|
|
| DHQS-like |
cd08198 |
Dehydroquinate synthase (DHQS) catalyzes the conversion of DAHP to DHQ in shikimate pathway ... |
39-272 |
1.08e-42 |
|
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: 151.95 E-value: 1.08e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446448964 39 VMIISDEAVASLH---LQTVIDALQVEQHVF-----SFVVPSGEKEK-SFENFYAAHTSALENKLDRNSLILALGGGMIG 109
Cdd:cd08198 33 VLFVIDSGVAAAHpalVKQIERYFQAHPDRLelvapPLIVPGGEAVKnDPALVEEILSAIHDHGLDRHSYVVVIGGGAVL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446448964 110 DLAGFVAASFMRGIRFVQVPTTLLAH-DSAVGGKVAINHPLGKNMIGAFHQPEAVVYHTPFLQSLPEKEWRSGYAEVIKH 188
Cdd:cd08198 113 DAVGFAAAIAHRGIRLIRVPTTVLAQnDSGVGVKNGINFFGKKNFLGTFAPPFAVINDFDFLETLPDRDWRSGIAEAVKV 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446448964 189 ALIGDVELYHWLKEEVQTLADlHD----EKLI---------HILTkaipvkanvvSQDETEKGVRAHLNFGHTLGHALEK 255
Cdd:cd08198 193 ALIKDASFFEWLERNAAALRQ-RDpdamEKLIrrcaelhldHIAA----------SGDPFETGSARPLDFGHWSAHKLEQ 261
|
250
....*....|....*..
gi 446448964 256 ELGYGnITHGDGVAVGM 272
Cdd:cd08198 262 LSGYA-LRHGEAVAIGI 277
|
|
| PRK13951 |
PRK13951 |
bifunctional shikimate kinase AroK/3-dehydroquinate synthase AroB; |
68-344 |
1.56e-37 |
|
bifunctional shikimate kinase AroK/3-dehydroquinate synthase AroB;
Pssm-ID: 172457 [Multi-domain] Cd Length: 488 Bit Score: 140.81 E-value: 1.56e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446448964 68 FVVPSGEKEKSFENFYAAHTSALENKLDRNSLILALGGGMIGDLAGFVAASFMRGIRFVQVPTTLLAH-DSAVGGKVAIN 146
Cdd:PRK13951 209 LLFPDGEEVKTLEHVSRAYYELVRMDFPRGKTIAGVGGGALTDFTGFVASTFKRGVGLSFYPTTLLAQvDASVGGKNAID 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446448964 147 HPLGKNMIGAFHQPEAVVYHTPFLQSLPEKEWRSGYAEVIKHALIG--DVELYhwlkEEVQTLADLHDEKLIHILTKAIP 224
Cdd:PRK13951 289 FAGVKNVVGTFRMPDYVIIDPTVTLSMDEGRFEEGVVEAFKMTILSgrGVELF----DEPEKIEKRNLRVLSEMVKISVE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446448964 225 VKANVVSQDETEKGVRAHLNFGHTLGHALEKELGygnITHGDGVAVGMLFAIflsEQVYKVDLAYEDMKQWF---LKYGY 301
Cdd:PRK13951 365 EKARIVMEDPYDMGLRHALNLGHTLGHVYEMLEG---VPHGIAVAWGIEKET---MYLYRKGIVPKETMRWIvekVKQIV 438
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 446448964 302 PKMPGDLNVERLVQLMKQDKKANAGA-IHMVLMQEYGVVNVVSI 344
Cdd:PRK13951 439 PIPVPSVDVEKARNLILNDKKILKGSrVRLPYVKEIGKIEFLEV 482
|
|
| DHQ_Fe-ADH |
cd07766 |
Dehydroquinate synthase-like (DHQ-like) and iron-containing alcohol dehydrogenases (Fe-ADH); ... |
13-317 |
3.53e-27 |
|
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: 108.22 E-value: 3.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446448964 13 YDVHVGKEVLSNLTTIvqnMQPAVSNVMIISDEAVASLHLQTVIDALQVEQ--HVFSFVVPsgekEKSFENFYAAHTSAL 90
Cdd:cd07766 2 TRIVFGEGAIAKLGEI---KRRGFDRALVVSDEGVVKGVGEKVADSLKKGLavAIFDFVGE----NPTFEEVKNAVERAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446448964 91 ENKLDrnsLILALGGGMIGDLAGFVAASFMRGIRFVQVPTTLLAhDSAVGGKVAINHPLGKN-MIGAFHQPEAVVYHTPF 169
Cdd:cd07766 75 AAEAD---AVIAVGGGSTLDTAKAVAALLNRGIPFIIVPTTAST-DSEVSPKSVITDKGGKNkQVGPHYNPDVVFVDTDI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446448964 170 LQSLPEKEWRSGYAEVIKHALIGdvelyhwlkeevqtladlhdEKLIHILTKAIPVKANVVSqdetekgvrahLNFGHTL 249
Cdd:cd07766 151 TKGLPPRQVASGGVDALAHAVEL--------------------EKVVEAATLAGMGLFESPG-----------LGLAHAI 199
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446448964 250 GHALEKELGygnITHGDGVAVGMLFAIFLSEQVY-KVDLAYEDMKQWFLKYGYP-----KMPGDLNVERLVQLM 317
Cdd:cd07766 200 GHALTAFEG---IPHGEAVAVGLPYVLKVANDMNpEPEAAIEAVFKFLEDLGLPthladLGVSKEDIPKLAEKA 270
|
|
| egsA |
PRK00843 |
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed |
14-203 |
1.68e-10 |
|
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed
Pssm-ID: 179139 Cd Length: 350 Bit Score: 61.45 E-value: 1.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446448964 14 DVHVGKEVLSNLTTIVQNMQPAvSNVMIISDEAVASLHLQTVIDALQVEQHVFSFVVpsgeKEKSFENFYAAHTSALENK 93
Cdd:PRK00843 13 DVVVGHGVLDDIGDVCSDLKLT-GRALIVTGPTTKKIAGDRVEENLEDAGDVEVVIV----DEATMEEVEKVEEKAKDVN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446448964 94 LDrnsLILALGGGMIGDLAGFvaASFMRGIRFVQVPTTlLAHDSAVGGKVAINHpLGKNMIGAFHQPEAVVYHTPFLQSL 173
Cdd:PRK00843 88 AG---FLIGVGGGKVIDVAKL--AAYRLGIPFISVPTA-ASHDGIASPRASIKG-GGKPVSVKAKPPLAVIADTEIIAKA 160
|
170 180 190
....*....|....*....|....*....|.
gi 446448964 174 PEKEWRSGYAEVI-KHALIGDVELYHWLKEE 203
Cdd:PRK00843 161 PYRLLAAGCGDIIsNYTAVKDWRLAHRLRGE 191
|
|
| G1PDH_related |
cd08549 |
Glycerol-1-phosphate dehydrogenase and related proteins; This family contains bacterial and ... |
17-311 |
3.31e-09 |
|
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: 57.57 E-value: 3.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446448964 17 VGKEVLSNLTTIVQnmQPAVSNVMIISDEAVASLHLQTVIDALQVEQHVFSF-VVPSGEKEKSFENFYaahtsalenkld 95
Cdd:cd08549 6 VGDGAINKIEEILK--KLNLKRVLIITGKNTKAKYCRFFYDQLKTVCDIVYYdNIDNLEDELKKYTFY------------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446448964 96 rnSLILALGGGMIGDLAGFvaASFMRGIRFVQVPTTLlAHDSAVGGKVAINHPLGKNMIGAfHQPEAVVYHTPFLQSLPE 175
Cdd:cd08549 72 --DCVIGIGGGRSIDTGKY--LAYKLKIPFISVPTSA-SNDGIASPIVSLRIPGVKKTFMA-DAPIAIIADTEIIKKSPR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446448964 176 KEWRSGYAEVI-KHALIGDVELYHWLKEE-------------VQTLAD-----LHDEKLIHILTKAI---PVKANVVSQD 233
Cdd:cd08549 146 RLLSAGIGDLVsNITAVLDWKLAHKEKGEkysefaailsktsAKELVSyvlkaSDLEEYHRVLVKALvgsGIAMAIAGSS 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446448964 234 ETEKGVRahlnfgHTLGHALEKEL---GYGNITHGDGVAVGMLFAIFLSEQVYKVDLA-YEDMKQWFLKYGYPKMPGDLN 309
Cdd:cd08549 226 RPASGSE------HLFSHALDKLKeeyLNINVLHGEQVGVGTIIMSYLHEKENKKLSGlHERIKMILKKVGAPTTAKQLG 299
|
..
gi 446448964 310 VE 311
Cdd:cd08549 300 ID 301
|
|
| Gro1PDH |
cd08173 |
Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) catalyzes the reversible conversion between ... |
15-278 |
1.77e-06 |
|
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: 49.09 E-value: 1.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446448964 15 VHVGKEVLSNLTTIVQNMQPAvSNVMIISDEAVASLHLQTVIDALQVEQHVFSFV-VPSGEKEKSFENFYAahtsalENK 93
Cdd:cd08173 5 VVVGHGAINKIGEVLKKLLLG-KRALIITGPNTYKIAGKRVEDLLESSGVEVVIVdIATIEEAAEVEKVKK------LIK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446448964 94 LDRNSLILALGGGMIGDLAGfvAASFMRGIRFVQVPTTlLAHDSAVGGKVAINHPLGKNMIGAfHQPEAVVYHTPFLQSL 173
Cdd:cd08173 78 ESKADFIIGVGGGKVIDVAK--YAAYKLNLPFISIPTS-ASHDGIASPFASIKGGDKPYSIKA-KAPIAIIADTEIISKA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446448964 174 PEKEWRSGYAEVI-KHALIGDVELYHWLKEE-----VQTLADL--------------HDEKLIHILTKAIpvkanVVSqd 233
Cdd:cd08173 154 PKRLLAAGCGDLIsNITAVKDWRLAHRLKGEyyseyAASLALMsakliienadlikpGLEEGVRTVVKAL-----ISS-- 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 446448964 234 etekGVRA-------------HLnfghtLGHALEKeLGYGNITHGDGVAVGMLFAIFL 278
Cdd:cd08173 227 ----GVAMsiagssrpasgseHL-----FSHALDK-LAPGPALHGEQCGVGTIMMAYL 274
|
|
| Fe-ADH |
pfam00465 |
Iron-containing alcohol dehydrogenase; |
15-312 |
4.64e-06 |
|
Iron-containing alcohol dehydrogenase;
Pssm-ID: 425696 [Multi-domain] Cd Length: 362 Bit Score: 47.98 E-value: 4.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446448964 15 VHVGKEVLSNLTTIVQNMQpavSNVMIISDEAVASL-HLQTVIDALQ---VEQHVFSFVVPsgekEKSFENFYAAHTSAL 90
Cdd:pfam00465 4 IVFGAGALAELGEELKRLG---ARALIVTDPGSLKSgLLDKVLASLEeagIEVVVFDGVEP----EPTLEEVDEAAALAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446448964 91 ENKLDrnsLILALGGGMIGDLAGFVAA---------SFMRG-------IRFVQVPTTlLAHDSAVGGKVAINHPLGKNMI 154
Cdd:pfam00465 77 EAGAD---VIIAVGGGSVIDTAKAIALlltnpgdvwDYLGGkpltkpaLPLIAIPTT-AGTGSEVTPLAVITDTETGEKL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446448964 155 GAFH---QPEAVVYHTPFLQSLPEKEWRSGyaevikhalIGDVeLYHWLKEEVQT----LADLHDEKLIHILTKAIPvka 227
Cdd:pfam00465 153 GIFSpklLPDLAILDPELTLTLPPRLTAAT---------GMDA-LAHAVEAYVSKganpLTDALALEAIRLIAENLP--- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446448964 228 nVVSQDETEKGVRAHL------------NFGHTLGHALEKELGYG-NITHGDGVAV----GMLF--------------AI 276
Cdd:pfam00465 220 -RAVADGEDLEARENMllastlaglafsNAGLGAAHALAHALGGRyGIPHGLANAIllpyVLRFnapaapeklaqlarAL 298
|
330 340 350
....*....|....*....|....*....|....*.
gi 446448964 277 FLSEQVYKVDLAYEDMKQWFLKYGYPKMPGDLNVER 312
Cdd:pfam00465 299 GEDSDEEAAEEAIEALRELLRELGLPTTLSELGVTE 334
|
|
| G1PDH-like |
cd08174 |
Glycerol-1-phosphate dehydrogenase-like; These glycerol-1-phosphate dehydrogenase-like ... |
17-312 |
2.57e-05 |
|
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: 45.59 E-value: 2.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446448964 17 VGKEVLSNLTTIVQNMQPAVSNVMIISDEAVASLHLQTVIDALQVEQHVFSFVVPSGEkekSFEnfYAAHTSALENKLDr 96
Cdd:cd08174 6 IEEGALEHLGKYLADRNQGFGKVAIVTGEGIDELLGEDILESLEEAGEIVTVEENTDN---SAE--ELAEKAFSLPKVD- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446448964 97 nsLILALGGGMIGDLAGFVAasFMRGIRFVQVPTTlLAHDS-----AV----GGKVAinhpLGKNMigafhqPEAVVYHT 167
Cdd:cd08174 80 --AIVGIGGGKVLDVAKYAA--FLSKLPFISVPTS-LSNDGiaspvAVlkvdGKRKS----LGAKM------PYGVIVDL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446448964 168 PFLQSLPEKEWRSGyaevikhalIGDV-----ELYHWL------KEEVQTLA-----------------DLHDEKLIHIL 219
Cdd:cd08174 145 DVIKSAPRRLILAG---------IGDLisnitALYDWKlaeekgGEPVDDFAyllsrtaadsllntpgkDIKDDEFLKEL 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446448964 220 TKAI--------------PvkanvVSQDEtekgvrahlnfgHTLGHALEKeLGYGNITHGDGVAVGMLFAIFLSEQvykv 285
Cdd:cd08174 216 AESLvlsgiameiagssrP-----ASGSE------------HLISHALDK-LFPGPALHGIQVGLGTYFMSFLQGQ---- 273
|
330 340
....*....|....*....|....*..
gi 446448964 286 dlAYEDMKQWFLKYGYPKMPGDLNVER 312
Cdd:cd08174 274 --RYEEIRDVLKRTGFPLNPSDLGLTK 298
|
|
| GldA |
COG0371 |
Glycerol dehydrogenase or related enzyme, iron-containing ADH family [Energy production and ... |
15-312 |
7.86e-04 |
|
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: 40.92 E-value: 7.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446448964 15 VHVGKEVLSNLTTIVQNMQpavSNVMIISDE---AVASLHLQTVIDALQVEQHVFSFvvpsgEKEKSFENFYAAHTSALE 91
Cdd:COG0371 9 YVQGEGALDELGEYLADLG---KRALIITGPtalKAAGDRLEESLEDAGIEVEVEVF-----GGECSEEEIERLAEEAKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446448964 92 NKLDrnsLILALGGGMIGDLAGFVAasFMRGIRFVQVPTTlLAHDSAVGGKVAINHPLGKNMIGAF--HQPEAVVYHTPF 169
Cdd:COG0371 81 QGAD---VIIGVGGGKALDTAKAVA--YRLGLPVVSVPTI-ASTDAPASPLSVIYTEDGAFDGYSFlaKNPDLVLVDTDI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446448964 170 LQSLPEKEWRSGyaevikhalIGDV-----ELYHW------LKEEVQT-----LADLHDEKLIHILTKAI-PVKANVVSq 232
Cdd:COG0371 155 IAKAPVRLLAAG---------IGDAlakwyEARDWslahrdLAGEYYTeaavaLARLCAETLLEYGEAAIkAVEAGVVT- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446448964 233 DETEK---------GV-------RAHLNFGHTLGHALEKELGYGNITHGDGVAVGMLFAIFLSEQvykvDLAYEDMKQWF 296
Cdd:COG0371 225 PALERvveanlllsGLamgigssRPGSGAAHAIHNGLTALPETHHALHGEKVAFGTLVQLVLEGR----PEEIEELLDFL 300
|
330
....*....|....*.
gi 446448964 297 LKYGYPKMPGDLNVER 312
Cdd:COG0371 301 RSVGLPTTLADLGLDD 316
|
|
| |
