|
Name |
Accession |
Description |
Interval |
E-value |
| EPSP_synthase |
cd01556 |
EPSP synthase domain. 3-phosphoshikimate 1-carboxyvinyltransferase ... |
418-845 |
7.33e-138 |
|
EPSP synthase domain. 3-phosphoshikimate 1-carboxyvinyltransferase (5-enolpyruvylshikimate-3-phosphate synthase) (EC 2.5.1.19) catalyses the reaction between shikimate-3-phosphate (S3P) and phosphoenolpyruvate (PEP) to form 5-enolpyruvylshkimate-3-phosphate (EPSP), an intermediate in the shikimate pathway leading to aromatic amino acid biosynthesis. The reaction is phosphoenolpyruvate + 3-phosphoshikimate = phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate. It is found in bacteria and plants but not animals. The enzyme is the target of the widely used herbicide glyphosate, which has been shown to occupy the active site. In bacteria and plants, it is a single domain protein, while in fungi, the domain is found as part of a multidomain protein with functions that are all part of the shikimate pathway.
Pssm-ID: 238797 Cd Length: 409 Bit Score: 431.98 E-value: 7.33e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 418 PGSKSISNRALVLAALGKGTCRLKNLLHSDDTQVMMAALNELkGASfaWEDAGETLVVKGGEGSLSVPPKgkELYLGNAG 497
Cdd:cd01556 8 PGSKSISHRALLLAALAEGESRIENLLDSDDTLATLEALRAL-GAK--IEEEGGTVEIVGGGGLGLPPEA--VLDCGNSG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 498 TAARFLTTVCTLVQsspqdnaEYTVITGNARMKQRPIGPLVTALQANGSKIDFLESEGCLPLaIAPQGLKGSQLQLAASV 577
Cdd:cd01556 83 TTMRLLTGLLALQG-------GDSVLTGDESLRKRPMGRLVDALRQLGAEIEGREGGGYPPL-IGGGGLKGGEVEIPGAV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 578 SSQYVSSILLCAPYAEEPITLELigGQVISQPYIDMTVAMMKTFGVDVVRRKDpvtgkflDVYEIPKAVYTNPPEYNIES 657
Cdd:cd01556 155 SSQFKSALLLAAPLAEGPTTIII--GELESKPYIDHTERMLRAFGAEVEVDGY-------RTITVKGGQKYKGPEYTVEG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 658 DASSATYPLAIAAVTGTSCTIQNIGSASlqGDAKFAkEVLEKMGCQVSQTAtETTVQGPPIGQLKAIEeVDMEVMTDAFL 737
Cdd:cd01556 226 DASSAAFFLAAAAITGSEIVIKNVGLNS--GDTGII-DVLKEMGADIEIGN-EDTVVVESGGKLKGID-IDGNDIPDEAP 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 738 TATALAAVANGKTRIIGIANQRVKECNRIRAMIDELAKFGVETIELDDGLEIIGKPIsdLKRGVSVHCYDDHRVAMAFSV 817
Cdd:cd01556 301 TLAVLAAFAEGPTRIRNAAELRVKESDRIAAMATELRKLGADVEETEDGLIIEGGPL--KGAGVEVYTYGDHRIAMSFAI 378
|
410 420
....*....|....*....|....*....
gi 170096704 818 LSTV-VEGTIIEEKRCVEKTWPNWWDDLE 845
Cdd:cd01556 379 AGLVaEGGVTIEDPECVAKSFPNFFEDLE 407
|
|
| DHQS |
cd08195 |
Dehydroquinate synthase (DHQS) catalyzes the conversion of DAHP to DHQ in shikimate pathway ... |
16-397 |
7.66e-136 |
|
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: 423.78 E-value: 7.66e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 16 SIHCGFHLIPYIAQtVLSNLPSSTYVLVTDTNVANFHLTAFEKEFEQRisslptsstKPRFLSLVIPPGETSKSREGKAN 95
Cdd:cd08195 3 PILIGSGLLDKLGE-LLELKKGSKVVIVTDENVAKLYGELLLKSLEAA---------GFKVEVIVIPAGEKSKSLETVER 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 96 IEDFLLLHRCTRDSVILALGGGVIGDLVGFVAATFMRGVRFVQIPTTLLAMVDSSVGGKTAIDTPHGKNLIGAFWQPEYI 175
Cdd:cd08195 73 IYDFLLEAGLDRDSLLIALGGGVVGDLAGFVASTYMRGIPFIQVPTTLLAQVDSSIGGKTGINLPGGKNLIGAFYQPKAV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 176 FIDAAFLETLPSREFSNGMAEVVKTAAIWNEAEFISLESRSADIFAAIqtpsadyagrskqtrsiaQELLLSVIVGSISV 255
Cdd:cd08195 153 LIDPDFLKTLPEREFRSGLAEVIKYGLIADKELFEFLEKNLDKILARD------------------PEALEEIIARSVEI 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 256 KAHIVTIDERETGLRNLVNFGHTIGHAIEAVLTPTILHGECVSVGMILEGEISRQMGILSQVGVGRLNRCLKAYNLPVTL 335
Cdd:cd08195 215 KADIVEEDEREKGLRAILNFGHTFGHAIESASGYKLLHGEAVAIGMVAAARLSVKLGLLSEEDLERIRALLKKLGLPTSI 294
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 170096704 336 ADpriaslpaaklLTVERLLDIMRIDKKNSGPEKKIVILSRIGATYepKATVVPDSIIAKTL 397
Cdd:cd08195 295 KD-----------LDPEELLEAMKRDKKNRGGKIRFVLLKGIGKAV--IVDDVSEEEIREAL 343
|
|
| AroA |
COG0128 |
5-enolpyruvylshikimate-3-phosphate synthase [Amino acid transport and metabolism]; ... |
418-845 |
2.00e-129 |
|
5-enolpyruvylshikimate-3-phosphate synthase [Amino acid transport and metabolism]; 5-enolpyruvylshikimate-3-phosphate synthase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis
Pssm-ID: 439898 Cd Length: 421 Bit Score: 409.48 E-value: 2.00e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 418 PGSKSISNRALVLAALGKGTCRLKNLLHSDDTQVMMAALNELkGASFAWEDaGETLVVKGGEGSLSVPPKgkELYLGNAG 497
Cdd:COG0128 19 PGSKSISHRALLLAALAEGESTIRNLLESDDTLATLEALRAL-GAEIEELD-GGTLRVTGVGGGLKEPDA--VLDCGNSG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 498 TAARFLTTVCTLvqsspQDNaeYTVITGNARMKQRPIGPLVTALQANGSKIDFLEsEGCLPLAIAPQGLKGSQLQLAASV 577
Cdd:COG0128 95 TTMRLLTGLLAL-----QPG--EVVLTGDESLRKRPMGRLLDPLRQLGARIESRG-GGYLPLTIRGGPLKGGEYEIPGSA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 578 SSQYVSSILLCAPYAEEPITLELIGGqVISQPYIDMTVAMMKTFGVDVVRRKDpvtgkflDVYEIPKAVYTNPPEYNIES 657
Cdd:COG0128 167 SSQFKSALLLAGPLAEGGLEITVTGE-LESKPYRDHTERMLRAFGVEVEVEGY-------RRFTVPGGQRYRPGDYTVPG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 658 DASSATYPLAIAAVTGTSCTIQNIGSASLQGDAKFAkEVLEKMGCQVSQTATETTVQGppiGQLKAIEeVDMEVMTDAFL 737
Cdd:COG0128 239 DISSAAFFLAAAAITGSEVTVEGVGLNSTQGDTGIL-DILKEMGADIEIENDGITVRG---SPLKGID-IDLSDIPDEAP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 738 TATALAAVANGKTRIIGIANQRVKECNRIRAMIDELAKFGVETIELDDGLEIIGKPisDLKrGVSVHCYDDHRVAMAFSV 817
Cdd:COG0128 314 TLAVLAAFAEGTTRIRGAAELRVKESDRIAAMATELRKLGADVEETEDGLIIEGGP--KLK-GAEVDSYGDHRIAMAFAV 390
|
410 420
....*....|....*....|....*....
gi 170096704 818 LSTVVEG-TIIEEKRCVEKTWPNWWDDLE 845
Cdd:COG0128 391 AGLRAEGpVTIDDAECVAKSFPDFFELLE 419
|
|
| AroB |
COG0337 |
3-dehydroquinate synthetase [Amino acid transport and metabolism]; 3-dehydroquinate synthetase ... |
17-397 |
3.18e-129 |
|
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: 406.40 E-value: 3.18e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 17 IHCGFHLIPYIAQTVLSNLPSSTYVLVTDTNVANFHLTAFEKEFEQRisslptsstKPRFLSLVIPPGETSKSREGKANI 96
Cdd:COG0337 15 IRIGRGLLDELGELLAELLKGRRVLVVTDENVAPLYGERLRAALEAA---------GFEVHLLVLPDGEASKTLETLERI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 97 EDFLLLHRCTRDSVILALGGGVIGDLVGFVAATFMRGVRFVQIPTTLLAMVDSSVGGKTAIDTPHGKNLIGAFWQPEYIF 176
Cdd:COG0337 86 LDALLEAGLDRDDLVVALGGGVVGDLAGFAAATYLRGVPFIQVPTTLLAQVDSSVGGKTGVNHPGGKNLIGAFHQPRAVL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 177 IDAAFLETLPSREFSNGMAEVVKTAAIWNEAEFISLESRSADIFAaiqtpsadyagrskqtrsIAQELLLSVIVGSISVK 256
Cdd:COG0337 166 IDLDFLKTLPERELRAGLAEVIKYGLIADAEFFEWLEENADALLA------------------RDPEALEEAIARSCEIK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 257 AHIVTIDERETGLRNLVNFGHTIGHAIEAVLTPTILHGECVSVGMILEGEISRQMGILSQVGVGRLNRCLKAYNLPVTLA 336
Cdd:COG0337 228 AEVVAADERESGLRALLNFGHTFGHAIEAATGYRLLHGEAVAIGMVFAARLSARLGLLSEEDVERIRALLEALGLPTRLP 307
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 170096704 337 DpriaslpaaklLTVERLLDIMRIDKKNSGPEKKIVILSRIGATYEpkATVVPDSIIAKTL 397
Cdd:COG0337 308 A-----------LDPEALLAAMKRDKKVRGGKLRFVLLRGIGKAVI--VDDVDEELLRAAL 355
|
|
| DHQ_synthase |
pfam01761 |
3-dehydroquinate synthase; The 3-dehydroquinate synthase EC:4.6.1.3 domain is present in ... |
78-364 |
4.17e-123 |
|
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: 385.70 E-value: 4.17e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 78 SLVIPPGETSKSREGKANIEDFLLLHRCTRDSVILALGGGVIGDLVGFVAATFMRGVRFVQIPTTLLAMVDSSVGGKTAI 157
Cdd:pfam01761 1 TIVIPDGEKSKTLETLERIYDALLEAGLDRSSLLIALGGGVIGDLAGFVAATYMRGIRFIQVPTTLLAQVDSSVGGKTGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 158 DTPHGKNLIGAFWQPEYIFIDAAFLETLPSREFSNGMAEVVKTAAIWNEAEFISLESRSADIFAAIQTPSADYAGRskqt 237
Cdd:pfam01761 81 NHPLGKNLIGAFYQPKAVLIDLDFLKTLPDREFRAGLAEVIKYGLIADAEFFEWLEENAEALLNLDPDALEEAIAR---- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 238 rsiaqelllsvivgSISVKAHIVTIDERETGLRNLVNFGHTIGHAIEAVLTP-TILHGECVSVGMILEGEISRQMGILSQ 316
Cdd:pfam01761 157 --------------SCEVKADVVAQDEKESGLRALLNLGHTFGHAIEALSGYgALLHGEAVAIGMVLAARLSERLGLLDE 222
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 170096704 317 VGVGRLNRCLKAYNLPVTLADpriaslpaaklLTVERLLDIMRIDKKN 364
Cdd:pfam01761 223 ADVERIRALLKKYGLPTSLPD-----------LDVEQLLAAMARDKKV 259
|
|
| aroA |
TIGR01356 |
3-phosphoshikimate 1-carboxyvinyltransferase; This model represents ... |
418-845 |
7.71e-122 |
|
3-phosphoshikimate 1-carboxyvinyltransferase; This model represents 3-phosphoshikimate-1-carboxyvinyltransferase (aroA), which catalyzes the sixth of seven steps in the shikimate pathway of the biosynthesis of chorimate. Chorismate is last common precursor of all three aromatic amino acids. Sequences scoring between the trusted and noise cutoffs include fragmentary and aberrant sequences in which generally well-conserved motifs are missing or altererd, but no example of a protein known to have a different function. [Amino acid biosynthesis, Aromatic amino acid family]
Pssm-ID: 273574 Cd Length: 409 Bit Score: 388.17 E-value: 7.71e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 418 PGSKSISNRALVLAALGKGTCRLKNLLHSDDTQVMMAALNELkGASFawEDAGETLVVKGGEGslsvPPKGKELYLGNAG 497
Cdd:TIGR01356 6 PGSKSITHRALILAALAEGETRVRNLLRSEDTLATLDALRAL-GAKI--EDGGEVAVIEGVGG----KEPQAELDLGNSG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 498 TAARFLTTVCTLVqsspqdnAEYTVITGNARMKQRPIGPLVTALQANGSKIDFLESEGCLPLAIApQGLKGSQLQLAASV 577
Cdd:TIGR01356 79 TTARLLTGVLALA-------DGEVVLTGDESLRKRPMGRLVDALRQLGAEISSLEGGGSLPLTIS-GPLPGGIVYISGSA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 578 SSQYVSSILLCAPyAEEPITLELIGGQVISQPYIDMTVAMMKTFGVDVVRRKDpvtgkflDVYEIPKAVYTNPPEYNIES 657
Cdd:TIGR01356 151 SSQYKSALLLAAP-ALQAVGITIVGEPLKSRPYIEITLDLLGSFGVEVERSDG-------RKIVVPGGQKYGPQGYDVPG 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 658 DASSATYPLAIAAVTGTSCTIQNIGSASLQGDAKFAkEVLEKMGCQVSQTATETTVQGPPigQLKAIEeVDMEVMTDAFL 737
Cdd:TIGR01356 223 DYSSAAFFLAAAAITGGRVTLENLGINPTQGDKAII-IVLEEMGADIEVEEDDLIVEGAS--GLKGIK-IDMDDMIDELP 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 738 TATALAAVANGKTRIIGIANQRVKECNRIRAMIDELAKFGVETIELDDGLEIIGKpiSDLKRGVsVHCYDDHRVAMAFSV 817
Cdd:TIGR01356 299 TLAVLAAFAEGVTRITGAEELRVKESDRIAAIAEELRKLGVDVEEFEDGLYIRGK--KELKGAV-VDTFGDHRIAMAFAV 375
|
410 420
....*....|....*....|....*....
gi 170096704 818 LSTVVEG-TIIEEKRCVEKTWPNWWDDLE 845
Cdd:TIGR01356 376 AGLVAEGeVLIDDPECVAKSFPSFFDVLE 404
|
|
| PRK02427 |
PRK02427 |
3-phosphoshikimate 1-carboxyvinyltransferase; Provisional |
418-845 |
1.59e-112 |
|
3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
Pssm-ID: 235037 [Multi-domain] Cd Length: 435 Bit Score: 363.69 E-value: 1.59e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 418 PGSKSISNRALVLAALGKGTCRLKNLLHSDDTQVMMAALNELkGASFAWEdageTLVVKGGEGSLSVPPKGkELYLGNAG 497
Cdd:PRK02427 20 PGSKSISHRALLLAALAEGETTITNLLRSEDTLATLNALRAL-GVEIEDD----EVVVEGVGGGGLKEPED-VLDCGNSG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 498 TAARFLTTVCTLvqsspQDNaeYTVITGNARMKQRPIGPLVTALQANGSKIDFlESEGCLPLAIAPqGLKGSQLQLAASV 577
Cdd:PRK02427 94 TTMRLLTGLLAL-----QPG--EVVLTGDESLRKRPMGRLLDPLRQMGAKIEG-RDEGYLPLTIRG-GKKGGPIEYDGPV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 578 SSQYVSSILLCAPYAEEPITLELIGGQVISQPYIDMTVAMMKTFGVDVVRRKDPVTGKFldvYEIPKAVYTnPPEYNIES 657
Cdd:PRK02427 165 SSQFVKSLLLLAPLFAEGDTETTVIEPLPSRPHTEITLRMLRAFGVEVENVEGWGYRRI---VIKGGQRLR-GQDITVPG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 658 DASSATYPLAIAAVTGTSC-TIQNIGSASLQGDAKFAkEVLEKMGCQVsqTATETTVQGPPIG-------QLKAIEeVDM 729
Cdd:PRK02427 241 DPSSAAFFLAAAAITGGSEvTITNVGLNSTQGGKAII-DVLEKMGADI--EIENEREGGEPVGdirvrssELKGID-IDI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 730 -----EVMT--------DafltatalaavanGKTRIIGIANQRVKECNRIRAMIDELAKFGVETIELDDGLEIIGKPisd 796
Cdd:PRK02427 317 pdiidEAPTlavlaafaE-------------GTTVIRNAEELRVKETDRIAAMATELRKLGAEVEETEDGLIITGGP--- 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 170096704 797 lkRGVSVHCYDDHRVAMAFSVLSTVVEG-TIIEEKRCVEKTWPNWWDDLE 845
Cdd:PRK02427 381 --LAGVVDSYGDHRIAMAFAIAGLAAEGpVTIDDPECVAKSFPDFFEDLA 428
|
|
| EPSP_synthase |
pfam00275 |
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase); |
418-844 |
4.19e-110 |
|
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);
Pssm-ID: 395213 Cd Length: 415 Bit Score: 356.22 E-value: 4.19e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 418 PGSKSISNRALVLAALGKGTCRLKNLLHSDDTQVMMAALNELKGASFAWEDAGETLVVKGGEGSLSvPPKGKELYLGNAG 497
Cdd:pfam00275 13 PGSKSNSHRALILAALAAGESTITNLLDSDDTLTMLEALRALGAEIIKLDDEKSVVIVEGLGGSFE-APEDLVLDMGNSG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 498 TAARFLTTVCTLVQSspqdnaeYTVITGNARMKQRPIGPLVTALQANGSKIDFLESEGCLPLAIAPQGLKGSQLQlaASV 577
Cdd:pfam00275 92 TALRPLTGRLALQSG-------EVVLPGDCSIGKRPMDRLLDALRQLGAEIEGREGYNYAPLKVRGLRLGGIHID--GDV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 578 SSQYVSSILLCAP-YAEEPITLEliggQVISQPYIDMTVAMMKTFGVDVvrRKDPVTGKFldvYEIPKAVYTnPPEYNIE 656
Cdd:pfam00275 163 SSQFVTSLLMLAAlLAEGTTTIE----NLASEPYIDDTENMLKKFGAKI--EGSGTELSI---TVKGGEKLP-GQEYRVE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 657 SDASSATYPLAIAAVTGTSCTIQNIGSASLQGDaKFAKEVLEKMGCQVSQTATETTVQGPPigqLKAIEEVDMEVMTDAF 736
Cdd:pfam00275 233 GDRSSAAYFLVAAAITGGTVTVENVGINSLQGD-EALLEILEKMGAEITQEEDADIVVGPP---GLRGKAVDIRTAPDPA 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 737 LTATALAAVANGKTRIIGIANQRVKECNRIRAMIDELAKFGVETIELDDGLEIIGkPISDLKrGVSVHCYDDHRVAMAFS 816
Cdd:pfam00275 309 PTTAVLAAFAEGTTRIEGISELRVKETDRLFAMATELRRLGADVEELPDGLIIIP-AVKELK-GAEVDSYGDHRIAMALA 386
|
410 420
....*....|....*....|....*....
gi 170096704 817 VLSTVVEG-TIIEEKRCVEKTWPNWWDDL 844
Cdd:pfam00275 387 LAGLVAEGeTIIDDIECTDRSFPDFEEKL 415
|
|
| aroB |
TIGR01357 |
3-dehydroquinate synthase; This model represents 3-dehydroquinate synthase, the enzyme ... |
17-397 |
1.80e-109 |
|
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: 351.55 E-value: 1.80e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 17 IHCGFHLIPYIAQTVLsnlPSSTYVLVTDTNVANFHLTAFEKEFEQRISSLptsstkprfLSLVIPPGETSKSREGKANI 96
Cdd:TIGR01357 3 VHVGEGLLDQLVEELA---EPSKLVIITDETVADLYGDKLLEALQALGYNV---------LKLTVPDGEESKSLETVQRL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 97 EDFLLLHRCTRDSVILALGGGVIGDLVGFVAATFMRGVRFVQIPTTLLAMVDSSVGGKTAIDTPHGKNLIGAFWQPEYIF 176
Cdd:TIGR01357 71 YDQLLEAGLDRSSTIIALGGGVVGDLAGFVAATYMRGIRFIQVPTTLLAMVDSSVGGKTGINFPGGKNLIGTFYQPKAVL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 177 IDAAFLETLPSREFSNGMAEVVKTAAIWNeaefislesrsADIFAAIQTPSADyaGRSKQTRSIAQELllsvIVGSISVK 256
Cdd:TIGR01357 151 IDPDFLKTLPDRELRSGMAEVIKHGLIAD-----------AELFDELESNDKL--RLNLQELEHLEEL----IKRSIEVK 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 257 AHIVTIDERETGLRNLVNFGHTIGHAIEAVLTPT-ILHGECVSVGMILEGEISRQMGILSQVGVGRLNRCLKAYNLPVTL 335
Cdd:TIGR01357 214 ASIVAEDEKESGLRAILNFGHTIGHAIEAEAGYGkIPHGEAVAIGMVCEAKLSERLGLLPAELIERLVQLLKRYGLPTDL 293
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 170096704 336 adpriaslpaAKLLTVERLLDIMRIDKKNSGPEKKIVILSRIGATYEPKatVVPDSIIAKTL 397
Cdd:TIGR01357 294 ----------PKDLDVDELLNAMLNDKKNSGGKIRFVLLEEIGKAALAR--EVPDEMVLELL 343
|
|
| AroE |
COG0169 |
Shikimate 5-dehydrogenase [Amino acid transport and metabolism]; Shikimate 5-dehydrogenase is ... |
1310-1591 |
8.16e-76 |
|
Shikimate 5-dehydrogenase [Amino acid transport and metabolism]; Shikimate 5-dehydrogenase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis
Pssm-ID: 439939 [Multi-domain] Cd Length: 270 Bit Score: 252.75 E-value: 8.16e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 1310 QRFYLFGTPIAHSMSPTLHNTGFEILGLPHHYELLETK--EVAEEIKiAIGDSAFGGASVTIPYKLDVIPLLDKLSPAAE 1387
Cdd:COG0169 5 RLYGVIGDPIAHSLSPAIHNAAFAALGLDAVYVAFDVPpeDLAAAVA-GLRALGIRGLNVTIPHKEAAIPLLDELDPRAR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 1388 AIGAVNTIIPRttgSGRmLVGDNTDWLGIKACITEQLSSKPIHAALVIGAGGTARAAIYALSALNVGDIYLYNRTTSKAY 1467
Cdd:COG0169 84 LIGAVNTVVFE---DGR-LIGDNTDGIGFVRALREAGVDLAGKRVLVLGAGGAARAVAAALAEAGAAEITIVNRTPERAE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 1468 ELAHAFPhAPVHVLEQLGQWPNGAVppcVIVSTVPASATTTEEetsgILLPSKLFdyrDGPAVVIDMAYKPAETPLLRLA 1547
Cdd:COG0169 160 ALAARLG-VRAVPLDDLAAALAGAD---LVINATPLGMAGGDA----LPLPASLL---APGAVVYDLVYNPLETPLLRAA 228
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 170096704 1548 KTAGdnWATVPGLEVLLEQGYVQFEMWTGRRCPKELVAKWLGRL 1591
Cdd:COG0169 229 RARG--ARVIDGLGMLVHQAAEAFELWTGVRPPVEAMRAALRAL 270
|
|
| PLN02834 |
PLN02834 |
3-dehydroquinate synthase |
33-364 |
9.09e-76 |
|
3-dehydroquinate synthase
Pssm-ID: 215448 Cd Length: 433 Bit Score: 258.93 E-value: 9.09e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 33 SNLPSSTYVLVTDTNVANFHLtafekefEQRISSLPTSSTKPRFLSLVIPPGETSKSREGKANIEDFLLLHRCTRDSVIL 112
Cdd:PLN02834 96 RHVHGKRVLVVTNETVAPLYL-------EKVVEALTAKGPELTVESVILPDGEKYKDMETLMKVFDKALESRLDRRCTFV 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 113 ALGGGVIGDLVGFVAATFMRGVRFVQIPTTLLAMVDSSVGGKTAIDTPHGKNLIGAFWQPEYIFIDAAFLETLPSREFSN 192
Cdd:PLN02834 169 ALGGGVIGDMCGFAAASYQRGVNFVQIPTTVMAQVDSSVGGKTGVNHPLGKNMIGAFYQPQCVLIDTDTLATLPDRELAS 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 193 GMAEVVKTAAIwNEAEFISLESRSADIFAAIQTPSADYAgrskqtrsiaqelllsvIVGSISVKAHIVTIDERETGLRNL 272
Cdd:PLN02834 249 GIAEVVKYGLI-RDAEFFEWQEANMEKLLARDPGALAYA-----------------IKRSCENKAEVVSLDEKESGLRAT 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 273 VNFGHTIGHAIEAVL-TPTILHGECVSVGMILEGEISRQMGILSQVGVGRLNRCLKAYNLPVTLADPriaslpaaklLTV 351
Cdd:PLN02834 311 LNLGHTFGHAIETGPgYGEWLHGEAVAAGTVMAADMSYRLGWIDMSLVNRIFALLKRAKLPTNPPEK----------MTV 380
|
330
....*....|...
gi 170096704 352 ERLLDIMRIDKKN 364
Cdd:PLN02834 381 EMFKSLMAVDKKV 393
|
|
| aroE |
PRK00258 |
shikimate 5-dehydrogenase; Reviewed |
1310-1584 |
2.97e-69 |
|
shikimate 5-dehydrogenase; Reviewed
Pssm-ID: 234703 [Multi-domain] Cd Length: 278 Bit Score: 234.31 E-value: 2.97e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 1310 QRFYLFGTPIAHSMSPTLHNTGFEILGLPHHYELLETKEVAEEIKI-AIGDSAFGGASVTIPYKLDVIPLLDKLSPAAEA 1388
Cdd:PRK00258 6 RLYAVIGNPIAHSKSPLIHNAAFKQLGLDGVYLAILVPPEDLEDAVkGFFALGGRGANVTVPFKEAAFALADELSERARL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 1389 IGAVNTIIPRTTGsgrmLVGDNTDWLGIKACITEQLSSKPIHA-ALVIGAGGTARAAIYALSALNVGDIYLYNRTTSKAY 1467
Cdd:PRK00258 86 IGAVNTLVLEDGR----LIGDNTDGIGFVRALEERLGVDLKGKrILILGAGGAARAVILPLLDLGVAEITIVNRTVERAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 1468 ELAHAFPHAPVHVLEQLGQWPNGAVPpcVIVSTVPASATtteEETSGILLPSKLFDYRdgpAVVIDMAYKPAETPLLRLA 1547
Cdd:PRK00258 162 ELAKLFGALGKAELDLELQEELADFD--LIINATSAGMS---GELPLPPLPLSLLRPG---TIVYDMIYGPLPTPFLAWA 233
|
250 260 270
....*....|....*....|....*....|....*..
gi 170096704 1548 KTAGDnwATVPGLEVLLEQGYVQFEMWTGRRCPKELV 1584
Cdd:PRK00258 234 KAQGA--RTIDGLGMLVHQAAEAFELWTGVRPPVEPM 268
|
|
| Shik-DH-AROM |
TIGR01809 |
shikimate-5-dehydrogenase, fungal AROM-type; This model represents a clade of ... |
1305-1585 |
4.56e-68 |
|
shikimate-5-dehydrogenase, fungal AROM-type; This model represents a clade of shikimate-5-dehydrogenases found in Corynebacterium, Mycobacteria and fungi. The fungal sequences are pentafunctional proteins known as AroM which contain the central five seven steps in the chorismate biosynthesis pathway. The Corynebacterium and Mycobacterial sequences represent the sole shikimate-5-dehydrogenases in species which otherwise have every enzyme of the chorismate biosynthesis pathway. [Amino acid biosynthesis, Aromatic amino acid family]
Pssm-ID: 273813 [Multi-domain] Cd Length: 282 Bit Score: 231.34 E-value: 4.56e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 1305 GLLPAQRFYLFGTPIAHSMSPTLHNTGFEILGLPHHYELLETkEVAEEIK--IAIGDSAFGGASVTIPYKLDVIPLLDKL 1382
Cdd:TIGR01809 1 GNKGPKKAFIIGKPIAHSRSPHLHNAGYEILGLPDKTYEFET-CSAEELKevLSGFGPQFGGASVTIPLKFAILRFADEH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 1383 SPAAEAIGAVNTIIPrtTGSGRmLVGDNTDWLGI-KACITEQLSSKPIH-AALVIGAGGTARAAIYALSALNVGDIYLYN 1460
Cdd:TIGR01809 80 TDRASLIGSVNTLLR--TQNGI-WKGDNTDWDGIaGALANIGKFEPLAGfRGLVIGAGGTSRAAVYALASLGVTDITVIN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 1461 RTTSKAYELAHAFPHapVHVLEQL-----GQWPNGAVPpcVIVSTVPASATTTEEETSgILLPSKLFDYRDGPAVVIDMA 1535
Cdd:TIGR01809 157 RNPDKLSRLVDLGVQ--VGVITRLegdsgGLAIEKAAE--VLVSTVPADVPADYVDLF-ATVPFLLLKRKSSEGIFLDAA 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 170096704 1536 YKPAETPLLRLAKTAgdNWATVPGLEVLLEQGYVQFEMWTGRRCPKELVA 1585
Cdd:TIGR01809 232 YDPWPTPLVAIVSAA--GWRVISGLQMLLHQGFAQFEQWTGMPAPREAMA 279
|
|
| DHquinase_I |
pfam01487 |
Type I 3-dehydroquinase; Type I 3-dehydroquinase, (3-dehydroquinate dehydratase or DHQase.) ... |
1068-1301 |
5.99e-62 |
|
Type I 3-dehydroquinase; Type I 3-dehydroquinase, (3-dehydroquinate dehydratase or DHQase.) catalyzes the cis-dehydration of 3-dehydroquinate via a covalent imine intermediate giving dehydroshikimate. Dehydroquinase functions in the shikimate pathway which is involved in the biosynthesis of aromatic amino acids. Type II 3-dehydroquinase catalyzes the trans-dehydration of 3-dehydroshikimate see pfam01220.
Pssm-ID: 426287 Cd Length: 227 Bit Score: 211.26 E-value: 5.99e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 1068 FLCLTYPDVTQSFPVIHELTQGVDAIELRVDLLRASkdydsieysIPTLAYVSSQVAALRRVTSLPIVFTVRTQSQGGSf 1147
Cdd:pfam01487 1 CVPLTGKTLEEILEELESGKEGADLVELRVDLLEEP---------VEDAEDVSEQLALLRRVGDLPLIFTFRTKSEGGE- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 1148 PDAAEKEAVELLKLALRLGVEYVDVEISLSEKKIKELVSLK--GSSHMIASWHDWSGNMIWDgpVVKEKYDAAARFG-DI 1224
Cdd:pfam01487 71 PDGSEEEYLELLRLALRLGVDYVDVELFLPEEILKELIEAKheGGTKVIGSYHDFEGTPSWE--ELISRYEKMQALGaDI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 1225 IKIVGKANSIQDNFTLYNFVSKVNSTAgSKPFIAINMGLEGQMSRVLNSTL-SPVSHPLL--PSKAAPGQLSFKQIQNAL 1301
Cdd:pfam01487 149 VKIAVMAKSIEDVLALLRFTSEMKSLA-DKPLIAMSMGELGRISRVLGPIFgSPVTFAALglAEKSAPGQLTAKELREAL 227
|
|
| DHQase_I |
cd00502 |
Type I 3-dehydroquinase, (3-dehydroquinate dehydratase or DHQase); Type I 3-dehydroquinase, ... |
1066-1303 |
7.25e-61 |
|
Type I 3-dehydroquinase, (3-dehydroquinate dehydratase or DHQase); Type I 3-dehydroquinase, (3-dehydroquinate dehydratase or DHQase). Catalyzes the cis-dehydration of 3-dehydroquinate via a covalent imine intermediate to produce dehydroshikimate. Dehydroquinase is the third enzyme in the shikimate pathway, which is involved in the biosynthesis of aromatic amino acids. Type I DHQase exists as a homodimer. Type II 3-dehydroquinase also catalyzes the same overall reaction, but is unrelated in terms of sequence and structure, and utilizes a completely different reaction mechanism.
Pssm-ID: 188633 Cd Length: 225 Bit Score: 208.35 E-value: 7.25e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 1066 SYFLCLTYPD-VTQSFPVIhELTQGVDAIELRVDLLraskdydsieySIPTLAYVSSQVAALRRVTSLPIVFTVRTQSQG 1144
Cdd:cd00502 1 KICVPLTGPDlLEEALSLL-ELLLGADAVELRVDLL-----------EDPSIDDVAEQLSLLRELTPLPIIFTVRTKSEG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 1145 GSFPDAaEKEAVELLKLALRLGVEYVDVEisLSEKKIKELVS--LKGSSHMIASWHDWSGnmIWDGPVVKEKYDAAARFG 1222
Cdd:cd00502 69 GNFEGS-EEEYLELLEEALKLGPDYVDIE--LDSALLEELINsrKKGNTKIIGSYHDFSG--TPSDEELVSRLEKMAALG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 1223 -DIIKIVGKANSIQDNFTLYNFVSKVNSTAGsKPFIAINMGLEGQMSRVLN-STLSPVSHPLLPSKAAPGQLSFKQIQNA 1300
Cdd:cd00502 144 aDIVKIAVMANSIEDNLRLLKFTRQVKNLYD-IPLIAINMGELGKLSRILSpVFGSPLTYASLPEPSAPGQLSVEELKQA 222
|
...
gi 170096704 1301 LHL 1303
Cdd:cd00502 223 LSL 225
|
|
| aroD |
TIGR01093 |
3-dehydroquinate dehydratase, type I; This model detects 3-dehydroquinate dehydratase, type I, ... |
1066-1301 |
9.35e-53 |
|
3-dehydroquinate dehydratase, type I; This model detects 3-dehydroquinate dehydratase, type I, either as a monofunctional protein or as a domain of a larger, multifunctional protein. It is often found fused to shikimate 5-dehydrogenase (EC 1.1.1.25), and sometimes additional domains. Type II 3-dehydroquinate dehydratase, designated AroQ, is described by the model TIGR01088. [Amino acid biosynthesis, Aromatic amino acid family]
Pssm-ID: 273439 Cd Length: 229 Bit Score: 185.28 E-value: 9.35e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 1066 SYFLCLTYPDVTQSFPVIHELTQ-GVDAIELRVDLLRASKDYDSIEYsiptlayVSSQVAALRrvTSLPIVFTVRTQSQG 1144
Cdd:TIGR01093 1 KIFVPLTAPDLEEALAEAEKICEkGADIVELRVDLLKDVSSNNDVDA-------LSEQLSELR--VDKPLIFTIRTQSEG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 1145 GSFPDAAEKEAVELLKLALRLGVEYVDVEISLSEKKIKELVSL--KGSSHMIASWHDWSGNMIWDgpVVKEKYDAAARF- 1221
Cdd:TIGR01093 72 GKFPGNEEEYFEELKRAAESLGPDFVDIELFLPDDAVKELINIakKGGTKIIMSNHDFQKTPSWE--EIVERLRKALSYg 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 1222 GDIIKIVGKANSIQDNFTLYNFVSKVnSTAGSKPFIAINMGLEGQMSRVLNSTLSPVSHPL-LPSKAAPGQLSFKQIQNA 1300
Cdd:TIGR01093 150 ADIVKIAVMANSKEDVLTLLSATNKV-DTHYDVPLITMSMGDRGKISRVLGAVFGSVLTFGsLGKASAPGQISVDDLREL 228
|
.
gi 170096704 1301 L 1301
Cdd:TIGR01093 229 L 229
|
|
| SK |
cd00464 |
Shikimate kinase (SK) is the fifth enzyme in the shikimate pathway, a seven-step biosynthetic ... |
877-1018 |
1.38e-43 |
|
Shikimate kinase (SK) is the fifth enzyme in the shikimate pathway, a seven-step biosynthetic pathway which converts erythrose-4-phosphate to chorismic acid, found in bacteria, fungi and plants. Chorismic acid is a important intermediate in the synthesis of aromatic compounds, such as aromatic amino acids, p-aminobenzoic acid, folate and ubiquinone. Shikimate kinase catalyses the phosphorylation of the 3-hydroxyl group of shikimic acid using ATP.
Pssm-ID: 238260 [Multi-domain] Cd Length: 154 Bit Score: 155.79 E-value: 1.38e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 877 SIILIGMRGTGKTFVGNLAAATLSWTCLDADAYFETKHEMGVREFVHQKGWQAFRDAEFEVLRELiaEKSQGHVISLGGG 956
Cdd:cd00464 1 NIVLIGMMGAGKTTVGRLLAKALGLPFVDLDELIEQRAGMSIPEIFAEEGEEGFRELEREVLLLL--LTKENAVIATGGG 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 170096704 957 IVETPAARELLKEyaatKGPVVHIVRPIDEVIRYLNSEASRPAY----DEAIVDVFRRREPWFGEC 1018
Cdd:cd00464 79 AVLREENRRLLLE----NGIVVWLDASPEELLERLARDKTRPLLqdedPERLRELLEEREPLYREV 140
|
|
| NAD_bind_Shikimate_DH |
cd01065 |
NAD(P) binding domain of Shikimate dehydrogenase; Shikimate dehydrogenase (DH) is an amino ... |
1411-1576 |
1.22e-41 |
|
NAD(P) binding domain of Shikimate dehydrogenase; Shikimate dehydrogenase (DH) is an amino acid DH family member. Shikimate pathway links metabolism of carbohydrates to de novo biosynthesis of aromatic amino acids, quinones and folate. It is essential in plants, bacteria, and fungi but absent in mammals, thus making enzymes involved in this pathway ideal targets for broad spectrum antibiotics and herbicides. Shikimate DH catalyzes the reduction of 3-hydroshikimate to shikimate using the cofactor NADH. Amino acid DH-like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DHs, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.
Pssm-ID: 133443 [Multi-domain] Cd Length: 155 Bit Score: 150.50 E-value: 1.22e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 1411 TDWLGIKACITEQLSSKPIHAALVIGAGGTARAAIYALSALNVGDIYLYNRTTSKAYELAHAFPHAPvhVLEQLGQWPNG 1490
Cdd:cd01065 1 TDGLGFVRALEEAGIELKGKKVLILGAGGAARAVAYALAELGAAKIVIVNRTLEKAKALAERFGELG--IAIAYLDLEEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 1491 AVPPCVIVSTVPASATTTEEetsgILLPSKLFdyrDGPAVVIDMAYKPAETPLLRLAKTAGdnWATVPGLEVLLEQGYVQ 1570
Cdd:cd01065 79 LAEADLIINTTPVGMKPGDE----LPLPPSLL---KPGGVVYDVVYNPLETPLLKEARALG--AKTIDGLEMLVYQAAEA 149
|
....*.
gi 170096704 1571 FEMWTG 1576
Cdd:cd01065 150 FELWTG 155
|
|
| AroD |
COG0710 |
3-dehydroquinate dehydratase [Amino acid transport and metabolism]; 3-dehydroquinate ... |
1086-1305 |
4.40e-35 |
|
3-dehydroquinate dehydratase [Amino acid transport and metabolism]; 3-dehydroquinate dehydratase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis
Pssm-ID: 440474 Cd Length: 236 Bit Score: 134.65 E-value: 4.40e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 1086 LTQGVDAIELRVDLLRAskdydsieysiPTLAYVSSQVAALRRVTSLPIVFTVRTQSQGGSFPdAAEKEAVELLKLALRL 1165
Cdd:COG0710 26 ARAGADLVELRLDYLED-----------PDLEELKELLEALREYGGLPLIFTFRTAEEGGEFE-GSEEERLELLRAAADS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 1166 -GVEYVDVEISLSEKKIKELVSLKGSSH--MIASWHDWSGnmiwdGP---VVKEKYDAAARFG-DIIKIVGKANSIQDNF 1238
Cdd:COG0710 94 aGVDLVDVELDTLEDDVDDLIEAAREAGvkVIVSYHDFEK-----TPsaeELVEILEKMQELGaDIVKIAVMAKSPEDVL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 170096704 1239 TLYNFVSKVNSTAGsKPFIAINMGLEGQMSRVLNSTL-SPVSHPLLPSKAAPGQLSFKQIQNALHLLG 1305
Cdd:COG0710 169 RLLEATLEAKEELD-RPVITMAMGELGKISRILGPLFgSALTYASVGEASAPGQIDVEELRELLELLE 235
|
|
| AroK |
COG0703 |
Shikimate kinase [Amino acid transport and metabolism]; Shikimate kinase is part of the ... |
878-1021 |
3.37e-34 |
|
Shikimate kinase [Amino acid transport and metabolism]; Shikimate kinase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis
Pssm-ID: 440467 [Multi-domain] Cd Length: 165 Bit Score: 129.48 E-value: 3.37e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 878 IILIGMRGTGKTFVGNLAAATLSWTCLDADAYFETKHEMGVREFVHQKGWQAFRDAEFEVLRELIAEKsqGHVISLGGGI 957
Cdd:COG0703 1 IVLIGMMGAGKSTVGRLLAKRLGLPFVDTDAEIEERAGMSIPEIFAEEGEAGFRELEREVLAELLEEE--NAVIATGGGA 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 170096704 958 VETPAARELLKEYaatkGPVVHIVRPIDEVIRYLNSEASRPAYD-----EAIVDVFRRREPWFGECCSH 1021
Cdd:COG0703 79 VLSPENRELLKEH----GTVVYLDASPETLLERLRRDDNRPLLQgedprERLEELLAEREPLYREVADI 143
|
|
| SKI |
pfam01202 |
Shikimate kinase; |
884-1018 |
2.94e-32 |
|
Shikimate kinase;
Pssm-ID: 426122 [Multi-domain] Cd Length: 159 Bit Score: 123.46 E-value: 2.94e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 884 RGTGKTFVGNLAAATLSWTCLDADAYFETKHEMGVREFVHQKGWQAFRDAEFEVLRELIAEKsqGHVISLGGGIVETPAA 963
Cdd:pfam01202 1 MGAGKSTIGRLLAKALGLPFIDTDEEIEKRTGMSIAEIFEEEGEEGFRRLESEVLKELLAEH--GLVIATGGGAVLSEEN 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 170096704 964 RELLKEyaatKGPVVHIVRPIDEVIRYLNSEASRPAYDEAIVDVFRRREPWFGEC 1018
Cdd:pfam01202 79 RDLLKE----RGIVIYLDAPLEVLLERLKRDKTRPLLQNKDPEEELLELLFEERD 129
|
|
| Shikimate_dh_N |
pfam08501 |
Shikimate dehydrogenase substrate binding domain; This domain is the substrate binding domain ... |
1314-1395 |
3.98e-29 |
|
Shikimate dehydrogenase substrate binding domain; This domain is the substrate binding domain of shikimate dehydrogenase.
Pssm-ID: 400688 [Multi-domain] Cd Length: 83 Bit Score: 111.92 E-value: 3.98e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 1314 LFGTPIAHSMSPTLHNTGFEILGLPHHYELLETKEVA-EEIKIAIGDSAFGGASVTIPYKLDVIPLLDKLSPAAEAIGAV 1392
Cdd:pfam08501 1 VIGNPISHSLSPAIHNAAFKALGLNGVYVAFEVPPDNlPDFVEGLRALGFRGLNVTIPHKEAAIPLLDELSPEAKAIGAV 80
|
...
gi 170096704 1393 NTI 1395
Cdd:pfam08501 81 NTI 83
|
|
| aroK |
PRK00131 |
shikimate kinase; Reviewed |
877-1013 |
8.95e-24 |
|
shikimate kinase; Reviewed
Pssm-ID: 234654 [Multi-domain] Cd Length: 175 Bit Score: 99.88 E-value: 8.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 877 SIILIGMRGTGKTFVGNLAAATLSWTCLDADAYFETKHEMGVREFVHQKGWQAFRDAEFEVLRELIAEksQGHVISLGGG 956
Cdd:PRK00131 6 NIVLIGFMGAGKSTIGRLLAKRLGYDFIDTDHLIEARAGKSIPEIFEEEGEAAFRELEEEVLAELLAR--HNLVISTGGG 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 170096704 957 IVETPAARELLKEyaatKGPVVHIVRPIDEVIRYLNSEASRP-----AYDEAIVDVFRRREP 1013
Cdd:PRK00131 84 AVLREENRALLRE----RGTVVYLDASFEELLRRLRRDRNRPllqtnDPKEKLRDLYEERDP 141
|
|
| aroD |
PRK02412 |
type I 3-dehydroquinate dehydratase; |
1090-1305 |
5.51e-23 |
|
type I 3-dehydroquinate dehydratase;
Pssm-ID: 235036 Cd Length: 253 Bit Score: 99.97 E-value: 5.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 1090 VDAIELRVDLLRASKDYDSIEYSIPTLayvssqvaaLRRVTSLPIVFTVRTQSQGGSFPdAAEKEAVELLKLALRLG-VE 1168
Cdd:PRK02412 42 ADIIEWRADFLEKISDVESVLAAAPAI---------REKFAGKPLLFTFRTAKEGGEIA-LSDEEYLALIKAVIKSGlPD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 1169 YVDVEISLSEKKIKELVSL--KGSSHMIASWHDWSG-----NMIwdgpvvkEKYDAAARFG-DIIKIVGKANSIQDNFTL 1240
Cdd:PRK02412 112 YIDVELFSGKDVVKEMVAFahEHGVKVVLSYHDFEKtppkeEIV-------ERLRKMESLGaDIVKIAVMPQSEQDVLTL 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 170096704 1241 YNFVSKVNSTAGSKPFIAINMGLEGQMSRVLNSTL-SPVSHPLLPSKAAPGQLSFKQIQNALHLLG 1305
Cdd:PRK02412 185 LNATREMKELYADQPLITMSMGKLGRISRLAGEVFgSSWTFASLDKASAPGQISVEDLRRILEILH 250
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| EPSP_synthase |
cd01556 |
EPSP synthase domain. 3-phosphoshikimate 1-carboxyvinyltransferase ... |
418-845 |
7.33e-138 |
|
EPSP synthase domain. 3-phosphoshikimate 1-carboxyvinyltransferase (5-enolpyruvylshikimate-3-phosphate synthase) (EC 2.5.1.19) catalyses the reaction between shikimate-3-phosphate (S3P) and phosphoenolpyruvate (PEP) to form 5-enolpyruvylshkimate-3-phosphate (EPSP), an intermediate in the shikimate pathway leading to aromatic amino acid biosynthesis. The reaction is phosphoenolpyruvate + 3-phosphoshikimate = phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate. It is found in bacteria and plants but not animals. The enzyme is the target of the widely used herbicide glyphosate, which has been shown to occupy the active site. In bacteria and plants, it is a single domain protein, while in fungi, the domain is found as part of a multidomain protein with functions that are all part of the shikimate pathway.
Pssm-ID: 238797 Cd Length: 409 Bit Score: 431.98 E-value: 7.33e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 418 PGSKSISNRALVLAALGKGTCRLKNLLHSDDTQVMMAALNELkGASfaWEDAGETLVVKGGEGSLSVPPKgkELYLGNAG 497
Cdd:cd01556 8 PGSKSISHRALLLAALAEGESRIENLLDSDDTLATLEALRAL-GAK--IEEEGGTVEIVGGGGLGLPPEA--VLDCGNSG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 498 TAARFLTTVCTLVQsspqdnaEYTVITGNARMKQRPIGPLVTALQANGSKIDFLESEGCLPLaIAPQGLKGSQLQLAASV 577
Cdd:cd01556 83 TTMRLLTGLLALQG-------GDSVLTGDESLRKRPMGRLVDALRQLGAEIEGREGGGYPPL-IGGGGLKGGEVEIPGAV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 578 SSQYVSSILLCAPYAEEPITLELigGQVISQPYIDMTVAMMKTFGVDVVRRKDpvtgkflDVYEIPKAVYTNPPEYNIES 657
Cdd:cd01556 155 SSQFKSALLLAAPLAEGPTTIII--GELESKPYIDHTERMLRAFGAEVEVDGY-------RTITVKGGQKYKGPEYTVEG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 658 DASSATYPLAIAAVTGTSCTIQNIGSASlqGDAKFAkEVLEKMGCQVSQTAtETTVQGPPIGQLKAIEeVDMEVMTDAFL 737
Cdd:cd01556 226 DASSAAFFLAAAAITGSEIVIKNVGLNS--GDTGII-DVLKEMGADIEIGN-EDTVVVESGGKLKGID-IDGNDIPDEAP 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 738 TATALAAVANGKTRIIGIANQRVKECNRIRAMIDELAKFGVETIELDDGLEIIGKPIsdLKRGVSVHCYDDHRVAMAFSV 817
Cdd:cd01556 301 TLAVLAAFAEGPTRIRNAAELRVKESDRIAAMATELRKLGADVEETEDGLIIEGGPL--KGAGVEVYTYGDHRIAMSFAI 378
|
410 420
....*....|....*....|....*....
gi 170096704 818 LSTV-VEGTIIEEKRCVEKTWPNWWDDLE 845
Cdd:cd01556 379 AGLVaEGGVTIEDPECVAKSFPNFFEDLE 407
|
|
| DHQS |
cd08195 |
Dehydroquinate synthase (DHQS) catalyzes the conversion of DAHP to DHQ in shikimate pathway ... |
16-397 |
7.66e-136 |
|
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: 423.78 E-value: 7.66e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 16 SIHCGFHLIPYIAQtVLSNLPSSTYVLVTDTNVANFHLTAFEKEFEQRisslptsstKPRFLSLVIPPGETSKSREGKAN 95
Cdd:cd08195 3 PILIGSGLLDKLGE-LLELKKGSKVVIVTDENVAKLYGELLLKSLEAA---------GFKVEVIVIPAGEKSKSLETVER 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 96 IEDFLLLHRCTRDSVILALGGGVIGDLVGFVAATFMRGVRFVQIPTTLLAMVDSSVGGKTAIDTPHGKNLIGAFWQPEYI 175
Cdd:cd08195 73 IYDFLLEAGLDRDSLLIALGGGVVGDLAGFVASTYMRGIPFIQVPTTLLAQVDSSIGGKTGINLPGGKNLIGAFYQPKAV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 176 FIDAAFLETLPSREFSNGMAEVVKTAAIWNEAEFISLESRSADIFAAIqtpsadyagrskqtrsiaQELLLSVIVGSISV 255
Cdd:cd08195 153 LIDPDFLKTLPEREFRSGLAEVIKYGLIADKELFEFLEKNLDKILARD------------------PEALEEIIARSVEI 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 256 KAHIVTIDERETGLRNLVNFGHTIGHAIEAVLTPTILHGECVSVGMILEGEISRQMGILSQVGVGRLNRCLKAYNLPVTL 335
Cdd:cd08195 215 KADIVEEDEREKGLRAILNFGHTFGHAIESASGYKLLHGEAVAIGMVAAARLSVKLGLLSEEDLERIRALLKKLGLPTSI 294
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 170096704 336 ADpriaslpaaklLTVERLLDIMRIDKKNSGPEKKIVILSRIGATYepKATVVPDSIIAKTL 397
Cdd:cd08195 295 KD-----------LDPEELLEAMKRDKKNRGGKIRFVLLKGIGKAV--IVDDVSEEEIREAL 343
|
|
| AroA |
COG0128 |
5-enolpyruvylshikimate-3-phosphate synthase [Amino acid transport and metabolism]; ... |
418-845 |
2.00e-129 |
|
5-enolpyruvylshikimate-3-phosphate synthase [Amino acid transport and metabolism]; 5-enolpyruvylshikimate-3-phosphate synthase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis
Pssm-ID: 439898 Cd Length: 421 Bit Score: 409.48 E-value: 2.00e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 418 PGSKSISNRALVLAALGKGTCRLKNLLHSDDTQVMMAALNELkGASFAWEDaGETLVVKGGEGSLSVPPKgkELYLGNAG 497
Cdd:COG0128 19 PGSKSISHRALLLAALAEGESTIRNLLESDDTLATLEALRAL-GAEIEELD-GGTLRVTGVGGGLKEPDA--VLDCGNSG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 498 TAARFLTTVCTLvqsspQDNaeYTVITGNARMKQRPIGPLVTALQANGSKIDFLEsEGCLPLAIAPQGLKGSQLQLAASV 577
Cdd:COG0128 95 TTMRLLTGLLAL-----QPG--EVVLTGDESLRKRPMGRLLDPLRQLGARIESRG-GGYLPLTIRGGPLKGGEYEIPGSA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 578 SSQYVSSILLCAPYAEEPITLELIGGqVISQPYIDMTVAMMKTFGVDVVRRKDpvtgkflDVYEIPKAVYTNPPEYNIES 657
Cdd:COG0128 167 SSQFKSALLLAGPLAEGGLEITVTGE-LESKPYRDHTERMLRAFGVEVEVEGY-------RRFTVPGGQRYRPGDYTVPG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 658 DASSATYPLAIAAVTGTSCTIQNIGSASLQGDAKFAkEVLEKMGCQVSQTATETTVQGppiGQLKAIEeVDMEVMTDAFL 737
Cdd:COG0128 239 DISSAAFFLAAAAITGSEVTVEGVGLNSTQGDTGIL-DILKEMGADIEIENDGITVRG---SPLKGID-IDLSDIPDEAP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 738 TATALAAVANGKTRIIGIANQRVKECNRIRAMIDELAKFGVETIELDDGLEIIGKPisDLKrGVSVHCYDDHRVAMAFSV 817
Cdd:COG0128 314 TLAVLAAFAEGTTRIRGAAELRVKESDRIAAMATELRKLGADVEETEDGLIIEGGP--KLK-GAEVDSYGDHRIAMAFAV 390
|
410 420
....*....|....*....|....*....
gi 170096704 818 LSTVVEG-TIIEEKRCVEKTWPNWWDDLE 845
Cdd:COG0128 391 AGLRAEGpVTIDDAECVAKSFPDFFELLE 419
|
|
| AroB |
COG0337 |
3-dehydroquinate synthetase [Amino acid transport and metabolism]; 3-dehydroquinate synthetase ... |
17-397 |
3.18e-129 |
|
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: 406.40 E-value: 3.18e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 17 IHCGFHLIPYIAQTVLSNLPSSTYVLVTDTNVANFHLTAFEKEFEQRisslptsstKPRFLSLVIPPGETSKSREGKANI 96
Cdd:COG0337 15 IRIGRGLLDELGELLAELLKGRRVLVVTDENVAPLYGERLRAALEAA---------GFEVHLLVLPDGEASKTLETLERI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 97 EDFLLLHRCTRDSVILALGGGVIGDLVGFVAATFMRGVRFVQIPTTLLAMVDSSVGGKTAIDTPHGKNLIGAFWQPEYIF 176
Cdd:COG0337 86 LDALLEAGLDRDDLVVALGGGVVGDLAGFAAATYLRGVPFIQVPTTLLAQVDSSVGGKTGVNHPGGKNLIGAFHQPRAVL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 177 IDAAFLETLPSREFSNGMAEVVKTAAIWNEAEFISLESRSADIFAaiqtpsadyagrskqtrsIAQELLLSVIVGSISVK 256
Cdd:COG0337 166 IDLDFLKTLPERELRAGLAEVIKYGLIADAEFFEWLEENADALLA------------------RDPEALEEAIARSCEIK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 257 AHIVTIDERETGLRNLVNFGHTIGHAIEAVLTPTILHGECVSVGMILEGEISRQMGILSQVGVGRLNRCLKAYNLPVTLA 336
Cdd:COG0337 228 AEVVAADERESGLRALLNFGHTFGHAIEAATGYRLLHGEAVAIGMVFAARLSARLGLLSEEDVERIRALLEALGLPTRLP 307
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 170096704 337 DpriaslpaaklLTVERLLDIMRIDKKNSGPEKKIVILSRIGATYEpkATVVPDSIIAKTL 397
Cdd:COG0337 308 A-----------LDPEALLAAMKRDKKVRGGKLRFVLLRGIGKAVI--VDDVDEELLRAAL 355
|
|
| DHQ_synthase |
pfam01761 |
3-dehydroquinate synthase; The 3-dehydroquinate synthase EC:4.6.1.3 domain is present in ... |
78-364 |
4.17e-123 |
|
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: 385.70 E-value: 4.17e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 78 SLVIPPGETSKSREGKANIEDFLLLHRCTRDSVILALGGGVIGDLVGFVAATFMRGVRFVQIPTTLLAMVDSSVGGKTAI 157
Cdd:pfam01761 1 TIVIPDGEKSKTLETLERIYDALLEAGLDRSSLLIALGGGVIGDLAGFVAATYMRGIRFIQVPTTLLAQVDSSVGGKTGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 158 DTPHGKNLIGAFWQPEYIFIDAAFLETLPSREFSNGMAEVVKTAAIWNEAEFISLESRSADIFAAIQTPSADYAGRskqt 237
Cdd:pfam01761 81 NHPLGKNLIGAFYQPKAVLIDLDFLKTLPDREFRAGLAEVIKYGLIADAEFFEWLEENAEALLNLDPDALEEAIAR---- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 238 rsiaqelllsvivgSISVKAHIVTIDERETGLRNLVNFGHTIGHAIEAVLTP-TILHGECVSVGMILEGEISRQMGILSQ 316
Cdd:pfam01761 157 --------------SCEVKADVVAQDEKESGLRALLNLGHTFGHAIEALSGYgALLHGEAVAIGMVLAARLSERLGLLDE 222
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 170096704 317 VGVGRLNRCLKAYNLPVTLADpriaslpaaklLTVERLLDIMRIDKKN 364
Cdd:pfam01761 223 ADVERIRALLKKYGLPTSLPD-----------LDVEQLLAAMARDKKV 259
|
|
| aroA |
TIGR01356 |
3-phosphoshikimate 1-carboxyvinyltransferase; This model represents ... |
418-845 |
7.71e-122 |
|
3-phosphoshikimate 1-carboxyvinyltransferase; This model represents 3-phosphoshikimate-1-carboxyvinyltransferase (aroA), which catalyzes the sixth of seven steps in the shikimate pathway of the biosynthesis of chorimate. Chorismate is last common precursor of all three aromatic amino acids. Sequences scoring between the trusted and noise cutoffs include fragmentary and aberrant sequences in which generally well-conserved motifs are missing or altererd, but no example of a protein known to have a different function. [Amino acid biosynthesis, Aromatic amino acid family]
Pssm-ID: 273574 Cd Length: 409 Bit Score: 388.17 E-value: 7.71e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 418 PGSKSISNRALVLAALGKGTCRLKNLLHSDDTQVMMAALNELkGASFawEDAGETLVVKGGEGslsvPPKGKELYLGNAG 497
Cdd:TIGR01356 6 PGSKSITHRALILAALAEGETRVRNLLRSEDTLATLDALRAL-GAKI--EDGGEVAVIEGVGG----KEPQAELDLGNSG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 498 TAARFLTTVCTLVqsspqdnAEYTVITGNARMKQRPIGPLVTALQANGSKIDFLESEGCLPLAIApQGLKGSQLQLAASV 577
Cdd:TIGR01356 79 TTARLLTGVLALA-------DGEVVLTGDESLRKRPMGRLVDALRQLGAEISSLEGGGSLPLTIS-GPLPGGIVYISGSA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 578 SSQYVSSILLCAPyAEEPITLELIGGQVISQPYIDMTVAMMKTFGVDVVRRKDpvtgkflDVYEIPKAVYTNPPEYNIES 657
Cdd:TIGR01356 151 SSQYKSALLLAAP-ALQAVGITIVGEPLKSRPYIEITLDLLGSFGVEVERSDG-------RKIVVPGGQKYGPQGYDVPG 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 658 DASSATYPLAIAAVTGTSCTIQNIGSASLQGDAKFAkEVLEKMGCQVSQTATETTVQGPPigQLKAIEeVDMEVMTDAFL 737
Cdd:TIGR01356 223 DYSSAAFFLAAAAITGGRVTLENLGINPTQGDKAII-IVLEEMGADIEVEEDDLIVEGAS--GLKGIK-IDMDDMIDELP 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 738 TATALAAVANGKTRIIGIANQRVKECNRIRAMIDELAKFGVETIELDDGLEIIGKpiSDLKRGVsVHCYDDHRVAMAFSV 817
Cdd:TIGR01356 299 TLAVLAAFAEGVTRITGAEELRVKESDRIAAIAEELRKLGVDVEEFEDGLYIRGK--KELKGAV-VDTFGDHRIAMAFAV 375
|
410 420
....*....|....*....|....*....
gi 170096704 818 LSTVVEG-TIIEEKRCVEKTWPNWWDDLE 845
Cdd:TIGR01356 376 AGLVAEGeVLIDDPECVAKSFPSFFDVLE 404
|
|
| PRK02427 |
PRK02427 |
3-phosphoshikimate 1-carboxyvinyltransferase; Provisional |
418-845 |
1.59e-112 |
|
3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
Pssm-ID: 235037 [Multi-domain] Cd Length: 435 Bit Score: 363.69 E-value: 1.59e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 418 PGSKSISNRALVLAALGKGTCRLKNLLHSDDTQVMMAALNELkGASFAWEdageTLVVKGGEGSLSVPPKGkELYLGNAG 497
Cdd:PRK02427 20 PGSKSISHRALLLAALAEGETTITNLLRSEDTLATLNALRAL-GVEIEDD----EVVVEGVGGGGLKEPED-VLDCGNSG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 498 TAARFLTTVCTLvqsspQDNaeYTVITGNARMKQRPIGPLVTALQANGSKIDFlESEGCLPLAIAPqGLKGSQLQLAASV 577
Cdd:PRK02427 94 TTMRLLTGLLAL-----QPG--EVVLTGDESLRKRPMGRLLDPLRQMGAKIEG-RDEGYLPLTIRG-GKKGGPIEYDGPV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 578 SSQYVSSILLCAPYAEEPITLELIGGQVISQPYIDMTVAMMKTFGVDVVRRKDPVTGKFldvYEIPKAVYTnPPEYNIES 657
Cdd:PRK02427 165 SSQFVKSLLLLAPLFAEGDTETTVIEPLPSRPHTEITLRMLRAFGVEVENVEGWGYRRI---VIKGGQRLR-GQDITVPG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 658 DASSATYPLAIAAVTGTSC-TIQNIGSASLQGDAKFAkEVLEKMGCQVsqTATETTVQGPPIG-------QLKAIEeVDM 729
Cdd:PRK02427 241 DPSSAAFFLAAAAITGGSEvTITNVGLNSTQGGKAII-DVLEKMGADI--EIENEREGGEPVGdirvrssELKGID-IDI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 730 -----EVMT--------DafltatalaavanGKTRIIGIANQRVKECNRIRAMIDELAKFGVETIELDDGLEIIGKPisd 796
Cdd:PRK02427 317 pdiidEAPTlavlaafaE-------------GTTVIRNAEELRVKETDRIAAMATELRKLGAEVEETEDGLIITGGP--- 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 170096704 797 lkRGVSVHCYDDHRVAMAFSVLSTVVEG-TIIEEKRCVEKTWPNWWDDLE 845
Cdd:PRK02427 381 --LAGVVDSYGDHRIAMAFAIAGLAAEGpVTIDDPECVAKSFPDFFEDLA 428
|
|
| EPSP_synthase |
pfam00275 |
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase); |
418-844 |
4.19e-110 |
|
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);
Pssm-ID: 395213 Cd Length: 415 Bit Score: 356.22 E-value: 4.19e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 418 PGSKSISNRALVLAALGKGTCRLKNLLHSDDTQVMMAALNELKGASFAWEDAGETLVVKGGEGSLSvPPKGKELYLGNAG 497
Cdd:pfam00275 13 PGSKSNSHRALILAALAAGESTITNLLDSDDTLTMLEALRALGAEIIKLDDEKSVVIVEGLGGSFE-APEDLVLDMGNSG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 498 TAARFLTTVCTLVQSspqdnaeYTVITGNARMKQRPIGPLVTALQANGSKIDFLESEGCLPLAIAPQGLKGSQLQlaASV 577
Cdd:pfam00275 92 TALRPLTGRLALQSG-------EVVLPGDCSIGKRPMDRLLDALRQLGAEIEGREGYNYAPLKVRGLRLGGIHID--GDV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 578 SSQYVSSILLCAP-YAEEPITLEliggQVISQPYIDMTVAMMKTFGVDVvrRKDPVTGKFldvYEIPKAVYTnPPEYNIE 656
Cdd:pfam00275 163 SSQFVTSLLMLAAlLAEGTTTIE----NLASEPYIDDTENMLKKFGAKI--EGSGTELSI---TVKGGEKLP-GQEYRVE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 657 SDASSATYPLAIAAVTGTSCTIQNIGSASLQGDaKFAKEVLEKMGCQVSQTATETTVQGPPigqLKAIEEVDMEVMTDAF 736
Cdd:pfam00275 233 GDRSSAAYFLVAAAITGGTVTVENVGINSLQGD-EALLEILEKMGAEITQEEDADIVVGPP---GLRGKAVDIRTAPDPA 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 737 LTATALAAVANGKTRIIGIANQRVKECNRIRAMIDELAKFGVETIELDDGLEIIGkPISDLKrGVSVHCYDDHRVAMAFS 816
Cdd:pfam00275 309 PTTAVLAAFAEGTTRIEGISELRVKETDRLFAMATELRRLGADVEELPDGLIIIP-AVKELK-GAEVDSYGDHRIAMALA 386
|
410 420
....*....|....*....|....*....
gi 170096704 817 VLSTVVEG-TIIEEKRCVEKTWPNWWDDL 844
Cdd:pfam00275 387 LAGLVAEGeTIIDDIECTDRSFPDFEEKL 415
|
|
| aroB |
TIGR01357 |
3-dehydroquinate synthase; This model represents 3-dehydroquinate synthase, the enzyme ... |
17-397 |
1.80e-109 |
|
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: 351.55 E-value: 1.80e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 17 IHCGFHLIPYIAQTVLsnlPSSTYVLVTDTNVANFHLTAFEKEFEQRISSLptsstkprfLSLVIPPGETSKSREGKANI 96
Cdd:TIGR01357 3 VHVGEGLLDQLVEELA---EPSKLVIITDETVADLYGDKLLEALQALGYNV---------LKLTVPDGEESKSLETVQRL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 97 EDFLLLHRCTRDSVILALGGGVIGDLVGFVAATFMRGVRFVQIPTTLLAMVDSSVGGKTAIDTPHGKNLIGAFWQPEYIF 176
Cdd:TIGR01357 71 YDQLLEAGLDRSSTIIALGGGVVGDLAGFVAATYMRGIRFIQVPTTLLAMVDSSVGGKTGINFPGGKNLIGTFYQPKAVL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 177 IDAAFLETLPSREFSNGMAEVVKTAAIWNeaefislesrsADIFAAIQTPSADyaGRSKQTRSIAQELllsvIVGSISVK 256
Cdd:TIGR01357 151 IDPDFLKTLPDRELRSGMAEVIKHGLIAD-----------AELFDELESNDKL--RLNLQELEHLEEL----IKRSIEVK 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 257 AHIVTIDERETGLRNLVNFGHTIGHAIEAVLTPT-ILHGECVSVGMILEGEISRQMGILSQVGVGRLNRCLKAYNLPVTL 335
Cdd:TIGR01357 214 ASIVAEDEKESGLRAILNFGHTIGHAIEAEAGYGkIPHGEAVAIGMVCEAKLSERLGLLPAELIERLVQLLKRYGLPTDL 293
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 170096704 336 adpriaslpaAKLLTVERLLDIMRIDKKNSGPEKKIVILSRIGATYEPKatVVPDSIIAKTL 397
Cdd:TIGR01357 294 ----------PKDLDVDELLNAMLNDKKNSGGKIRFVLLEEIGKAALAR--EVPDEMVLELL 343
|
|
| PLN02338 |
PLN02338 |
3-phosphoshikimate 1-carboxyvinyltransferase |
418-845 |
5.55e-95 |
|
3-phosphoshikimate 1-carboxyvinyltransferase
Pssm-ID: 177972 [Multi-domain] Cd Length: 443 Bit Score: 314.76 E-value: 5.55e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 418 PGSKSISNRALVLAALGKGTCRLKNLLHSDDTQVMMAALNELkGASFAWEDAGETLVVKGGEGSLSVPPKGK---ELYLG 494
Cdd:PLN02338 19 PGSKSLSNRILLLAALSEGTTVVDNLLDSDDIRYMLGALKTL-GLNVEEDSENNRAVVEGCGGKFPVSGDSKedvELFLG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 495 NAGTAARFLTTVCTLVQSspqdNAEYtVITGNARMKQRPIGPLVTALQANGSKIDFLESEGCLPLAI-APQGLKGSQLQL 573
Cdd:PLN02338 98 NAGTAMRPLTAAVTAAGG----NASY-VLDGVPRMRERPIGDLVDGLKQLGADVECTLGTNCPPVRVnAAGGLPGGKVKL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 574 AASVSSQYVSSILLCAPYAEEPITLELIgGQVISQPYIDMTVAMMKTFGVDVVRRKDpvtgkfLDVYEIPKA-VYTNPPE 652
Cdd:PLN02338 173 SGSISSQYLTALLMAAPLALGDVEIEIV-DKLISVPYVEMTLKLMERFGVSVEHSDS------WDRFFIKGGqKYKSPGN 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 653 YNIESDASSATYPLAIAAVTGTSCTIQNIGSASLQGDAKFAkEVLEKMGCQVSQTATETTVQGPPI-----GQLKAIeEV 727
Cdd:PLN02338 246 AYVEGDASSASYFLAGAAITGGTVTVEGCGTTSLQGDVKFA-EVLEKMGAKVEWTENSVTVTGPPRdafggKHLKAI-DV 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 728 DMEVMTDAFLTATALAAVANGKTRIIGIANQRVKECNRIRAMIDELAKFGVETIELDDGLEIigKPISDLKRGvSVHCYD 807
Cdd:PLN02338 324 NMNKMPDVAMTLAVVALFADGPTAIRDVASWRVKETERMIAICTELRKLGATVEEGPDYCII--TPPKKLKPA-EIDTYD 400
|
410 420 430
....*....|....*....|....*....|....*...
gi 170096704 808 DHRVAMAFSVLSTVVEGTIIEEKRCVEKTWPNWWDDLE 845
Cdd:PLN02338 401 DHRMAMAFSLAACGDVPVTINDPGCTRKTFPTYFDVLE 438
|
|
| PRK11860 |
PRK11860 |
bifunctional 3-phosphoshikimate 1-carboxyvinyltransferase/cytidylate kinase; |
418-908 |
3.58e-89 |
|
bifunctional 3-phosphoshikimate 1-carboxyvinyltransferase/cytidylate kinase;
Pssm-ID: 237003 [Multi-domain] Cd Length: 661 Bit Score: 305.43 E-value: 3.58e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 418 PGSKSISNRALVLAALGKGTCRLKNLLHSDDTQVMMAALNELkgaSFAWEDAGETLVVKGGEGSLsvPPKGKELYLGNAG 497
Cdd:PRK11860 22 PGSKSISNRVLLLAALSEGTTTVRDLLDSDDTRVMLDALRAL---GCGVEQLGDTYRITGLGGQF--PVKQADLFLGNAG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 498 TAARFLTTVCTLVqsspqdNAEYTvITGNARMKQRPIGPLVTALQANGSKIDFLESEGCLPLAIAPQGLK-GSQLQLAAS 576
Cdd:PRK11860 97 TAMRPLTAALALL------GGEYE-LSGVPRMHERPIGDLVDALRQLGCDIDYLGNEGFPPLRIGPAPLRlDAPIRVRGD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 577 VSSQYVSSILLCAPY-AEEPITLELIGgQVISQPYIDMTVAMMKTFGVDVVRRKdpvtgkfLDVYEIPK-AVYTNPPEYN 654
Cdd:PRK11860 170 VSSQFLTALLMALPLvARRDITIEVVG-ELISKPYIEITLNLLARFGIAVQREG-------WQRFTIPAgSRYRSPGEIH 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 655 IESDASSATYPLAIAAV-TGTSCTIQNIGSASLQGDAKFAkEVLEKMGCQVSQTATETTVQGPPiGQLKAIEeVDMEVMT 733
Cdd:PRK11860 242 VEGDASSASYFIAAGAIaGGAPVRIEGVGRDSIQGDIRFA-EAARAMGAQVTSGPNWLEVRRGA-WPLKAID-LDCNHIP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 734 DAFLTATALAAVANGKTRIIGIANQRVKECNRIRAMIDELAKFGVETIELDDGLEIIGKPISDLKRGVSVHCYDDHRVAM 813
Cdd:PRK11860 319 DAAMTLAVMALYADGTTTLRNIASWRVKETDRIAAMATELRKLGATVEEGADYIRVTPPAQAADWKAAAIHTYDDHRMAM 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 814 AFSVLSTVVEGTI--IEEKRCVEKTWPNWWDDLenkigltvqgvdlasvaseasasGTINHDSAASIILIGMRG---TGK 888
Cdd:PRK11860 399 CFSLAAFNPAGLPvrINDPKCVAKTFPDYFEAL-----------------------FSVAQADADRVPVICIDGptaSGK 455
|
490 500
....*....|....*....|
gi 170096704 889 TFVGNLAAATLSWTCLDADA 908
Cdd:PRK11860 456 GTVAARVAEALGYHYLDSGA 475
|
|
| DOIS |
cd08197 |
2-deoxy-scyllo-inosose synthase (DOIS) catalyzes carbocycle formation from ... |
14-397 |
4.76e-79 |
|
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: 265.60 E-value: 4.76e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 14 KESIHCGFHLIPYIAqTVLSNLPSSTYVLVTDTNVANFHLTAFEKEFEQriSSLPTSStkprflsLVIPPGETSKSREGK 93
Cdd:cd08197 1 LTDIYLGRGILESLL-SILEELKADRHFLVTDSNVNDLYGDRLLEGLKK--AGIPVEL-------LVVPAGESNKTLSTL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 94 ANIEDFLLLHRCTRDSVILALGGGVIGDLVGFVAATFMRGVRFVQIPTTLLAMVDSSVGGKTAIDTPHGKNLIGAFWQPE 173
Cdd:cd08197 71 TELAERLIAAGITRRSVIIALGGGVVGNIAGLLAGLLYRGIRLVHVPTTLLAQSDSVLSLKQAVNGKSGKNLVGSYYAPL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 174 YIFIDAAFLETLPSREFSNGMAEVVKTAAIwNEAEFIslesrsaDIFAAIQTPSADYagrskqtrsiAQELLLSVIVGSI 253
Cdd:cd08197 151 FVFVDTEFLKTLPPRQIRSGLCEAIKNALI-QDPEFL-------DYLEDYLNSDLDY----------DPEFLEKVIDLSI 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 254 SVKAHIVTID--ERETGLrnLVNFGHTIGHAIEAVLTPTILHGECVSVGMILEGEISRQMGILSQVGVGRLNRCLKAYNL 331
Cdd:cd08197 213 EAKLEVLSNDpyEKKEGL--ILEYGHTVGHAIELLSGGELSHGEAVAIGMCVAAEISHLLGLLSEEDVDKHYELLEKIGL 290
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 170096704 332 PVTLADPriaslpaaklLTVERLLDIMRIDKK---NSGPEKKI--VILSRIGATYEPK---ATVVPDSIIAKTL 397
Cdd:cd08197 291 PTIIPDG----------ISVEAILEVIRYDNKrgyIKADADTIrmVLLEKLGKPANPDgdyLTPVPEEIVKEAL 354
|
|
| AroE |
COG0169 |
Shikimate 5-dehydrogenase [Amino acid transport and metabolism]; Shikimate 5-dehydrogenase is ... |
1310-1591 |
8.16e-76 |
|
Shikimate 5-dehydrogenase [Amino acid transport and metabolism]; Shikimate 5-dehydrogenase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis
Pssm-ID: 439939 [Multi-domain] Cd Length: 270 Bit Score: 252.75 E-value: 8.16e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 1310 QRFYLFGTPIAHSMSPTLHNTGFEILGLPHHYELLETK--EVAEEIKiAIGDSAFGGASVTIPYKLDVIPLLDKLSPAAE 1387
Cdd:COG0169 5 RLYGVIGDPIAHSLSPAIHNAAFAALGLDAVYVAFDVPpeDLAAAVA-GLRALGIRGLNVTIPHKEAAIPLLDELDPRAR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 1388 AIGAVNTIIPRttgSGRmLVGDNTDWLGIKACITEQLSSKPIHAALVIGAGGTARAAIYALSALNVGDIYLYNRTTSKAY 1467
Cdd:COG0169 84 LIGAVNTVVFE---DGR-LIGDNTDGIGFVRALREAGVDLAGKRVLVLGAGGAARAVAAALAEAGAAEITIVNRTPERAE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 1468 ELAHAFPhAPVHVLEQLGQWPNGAVppcVIVSTVPASATTTEEetsgILLPSKLFdyrDGPAVVIDMAYKPAETPLLRLA 1547
Cdd:COG0169 160 ALAARLG-VRAVPLDDLAAALAGAD---LVINATPLGMAGGDA----LPLPASLL---APGAVVYDLVYNPLETPLLRAA 228
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 170096704 1548 KTAGdnWATVPGLEVLLEQGYVQFEMWTGRRCPKELVAKWLGRL 1591
Cdd:COG0169 229 RARG--ARVIDGLGMLVHQAAEAFELWTGVRPPVEAMRAALRAL 270
|
|
| PLN02834 |
PLN02834 |
3-dehydroquinate synthase |
33-364 |
9.09e-76 |
|
3-dehydroquinate synthase
Pssm-ID: 215448 Cd Length: 433 Bit Score: 258.93 E-value: 9.09e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 33 SNLPSSTYVLVTDTNVANFHLtafekefEQRISSLPTSSTKPRFLSLVIPPGETSKSREGKANIEDFLLLHRCTRDSVIL 112
Cdd:PLN02834 96 RHVHGKRVLVVTNETVAPLYL-------EKVVEALTAKGPELTVESVILPDGEKYKDMETLMKVFDKALESRLDRRCTFV 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 113 ALGGGVIGDLVGFVAATFMRGVRFVQIPTTLLAMVDSSVGGKTAIDTPHGKNLIGAFWQPEYIFIDAAFLETLPSREFSN 192
Cdd:PLN02834 169 ALGGGVIGDMCGFAAASYQRGVNFVQIPTTVMAQVDSSVGGKTGVNHPLGKNMIGAFYQPQCVLIDTDTLATLPDRELAS 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 193 GMAEVVKTAAIwNEAEFISLESRSADIFAAIQTPSADYAgrskqtrsiaqelllsvIVGSISVKAHIVTIDERETGLRNL 272
Cdd:PLN02834 249 GIAEVVKYGLI-RDAEFFEWQEANMEKLLARDPGALAYA-----------------IKRSCENKAEVVSLDEKESGLRAT 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 273 VNFGHTIGHAIEAVL-TPTILHGECVSVGMILEGEISRQMGILSQVGVGRLNRCLKAYNLPVTLADPriaslpaaklLTV 351
Cdd:PLN02834 311 LNLGHTFGHAIETGPgYGEWLHGEAVAAGTVMAADMSYRLGWIDMSLVNRIFALLKRAKLPTNPPEK----------MTV 380
|
330
....*....|...
gi 170096704 352 ERLLDIMRIDKKN 364
Cdd:PLN02834 381 EMFKSLMAVDKKV 393
|
|
| aroE |
PRK00258 |
shikimate 5-dehydrogenase; Reviewed |
1310-1584 |
2.97e-69 |
|
shikimate 5-dehydrogenase; Reviewed
Pssm-ID: 234703 [Multi-domain] Cd Length: 278 Bit Score: 234.31 E-value: 2.97e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 1310 QRFYLFGTPIAHSMSPTLHNTGFEILGLPHHYELLETKEVAEEIKI-AIGDSAFGGASVTIPYKLDVIPLLDKLSPAAEA 1388
Cdd:PRK00258 6 RLYAVIGNPIAHSKSPLIHNAAFKQLGLDGVYLAILVPPEDLEDAVkGFFALGGRGANVTVPFKEAAFALADELSERARL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 1389 IGAVNTIIPRTTGsgrmLVGDNTDWLGIKACITEQLSSKPIHA-ALVIGAGGTARAAIYALSALNVGDIYLYNRTTSKAY 1467
Cdd:PRK00258 86 IGAVNTLVLEDGR----LIGDNTDGIGFVRALEERLGVDLKGKrILILGAGGAARAVILPLLDLGVAEITIVNRTVERAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 1468 ELAHAFPHAPVHVLEQLGQWPNGAVPpcVIVSTVPASATtteEETSGILLPSKLFDYRdgpAVVIDMAYKPAETPLLRLA 1547
Cdd:PRK00258 162 ELAKLFGALGKAELDLELQEELADFD--LIINATSAGMS---GELPLPPLPLSLLRPG---TIVYDMIYGPLPTPFLAWA 233
|
250 260 270
....*....|....*....|....*....|....*..
gi 170096704 1548 KTAGDnwATVPGLEVLLEQGYVQFEMWTGRRCPKELV 1584
Cdd:PRK00258 234 KAQGA--RTIDGLGMLVHQAAEAFELWTGVRPPVEPM 268
|
|
| Shik-DH-AROM |
TIGR01809 |
shikimate-5-dehydrogenase, fungal AROM-type; This model represents a clade of ... |
1305-1585 |
4.56e-68 |
|
shikimate-5-dehydrogenase, fungal AROM-type; This model represents a clade of shikimate-5-dehydrogenases found in Corynebacterium, Mycobacteria and fungi. The fungal sequences are pentafunctional proteins known as AroM which contain the central five seven steps in the chorismate biosynthesis pathway. The Corynebacterium and Mycobacterial sequences represent the sole shikimate-5-dehydrogenases in species which otherwise have every enzyme of the chorismate biosynthesis pathway. [Amino acid biosynthesis, Aromatic amino acid family]
Pssm-ID: 273813 [Multi-domain] Cd Length: 282 Bit Score: 231.34 E-value: 4.56e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 1305 GLLPAQRFYLFGTPIAHSMSPTLHNTGFEILGLPHHYELLETkEVAEEIK--IAIGDSAFGGASVTIPYKLDVIPLLDKL 1382
Cdd:TIGR01809 1 GNKGPKKAFIIGKPIAHSRSPHLHNAGYEILGLPDKTYEFET-CSAEELKevLSGFGPQFGGASVTIPLKFAILRFADEH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 1383 SPAAEAIGAVNTIIPrtTGSGRmLVGDNTDWLGI-KACITEQLSSKPIH-AALVIGAGGTARAAIYALSALNVGDIYLYN 1460
Cdd:TIGR01809 80 TDRASLIGSVNTLLR--TQNGI-WKGDNTDWDGIaGALANIGKFEPLAGfRGLVIGAGGTSRAAVYALASLGVTDITVIN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 1461 RTTSKAYELAHAFPHapVHVLEQL-----GQWPNGAVPpcVIVSTVPASATTTEEETSgILLPSKLFDYRDGPAVVIDMA 1535
Cdd:TIGR01809 157 RNPDKLSRLVDLGVQ--VGVITRLegdsgGLAIEKAAE--VLVSTVPADVPADYVDLF-ATVPFLLLKRKSSEGIFLDAA 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 170096704 1536 YKPAETPLLRLAKTAgdNWATVPGLEVLLEQGYVQFEMWTGRRCPKELVA 1585
Cdd:TIGR01809 232 YDPWPTPLVAIVSAA--GWRVISGLQMLLHQGFAQFEQWTGMPAPREAMA 279
|
|
| DHQ-like |
cd08169 |
Dehydroquinate synthase-like which includes dehydroquinate synthase, 2-deoxy-scyllo-inosose ... |
40-379 |
2.41e-63 |
|
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: 219.20 E-value: 2.41e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 40 YVLVTDTNVANFHLTAFEKEFEQRISSLPtsstkprflsLVIPPGETSKSREGKANIEDFLLLHRCTRDSVILALGGGVI 119
Cdd:cd08169 26 CLIIVDSGVPDLIVNYLAEYFGYYLEVHV----------FIIQGGEAYKTFQTVVEELERAAALHLNRHSAVVAVGGGAT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 120 GDLVGFVAATFMRGVRFVQIPTTLLAMVDSSVGGKTAIDTPHGKNLIGAFWQPEYIFIDAAFLETLPSREFSNGMAEVVK 199
Cdd:cd08169 96 GDVVGFAAATYFRGIAFIRVPTTLLAQSDSSVGIKVGINTRGGKNLLGAFYPPRAVFADFSFLKTLPFRQVRAGMAELVK 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 200 TAAIWNEAEFISLESRSADifAAIQTPsadyagrskqtrsiaqELLLSVIVGSISVKAHIVTIDERETGLRNLVNFGHTI 279
Cdd:cd08169 176 MALIADNDFFEFLEDKANS--ATVYSP----------------EQLEKLINKCISLKLDVVVADEDEQGKRRGLNYGHTF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 280 GHAIEAVLTPTILHGECVSVGMILEGEISRQMGILSQVGVGRLNRCLKAYNLPV---TLADPRIaslpaaklltverLLD 356
Cdd:cd08169 238 GHALELASGYKIPHGEAVAVGMAYAAKIANRLGLLPEHDVSRIIWLLNKLGLPLdhpLALDPDS-------------LYE 304
|
330 340
....*....|....*....|...
gi 170096704 357 IMRIDKKNSGPEKKIVILSRIGA 379
Cdd:cd08169 305 YLESDKKSLYGNLGMILLSGVGD 327
|
|
| DHquinase_I |
pfam01487 |
Type I 3-dehydroquinase; Type I 3-dehydroquinase, (3-dehydroquinate dehydratase or DHQase.) ... |
1068-1301 |
5.99e-62 |
|
Type I 3-dehydroquinase; Type I 3-dehydroquinase, (3-dehydroquinate dehydratase or DHQase.) catalyzes the cis-dehydration of 3-dehydroquinate via a covalent imine intermediate giving dehydroshikimate. Dehydroquinase functions in the shikimate pathway which is involved in the biosynthesis of aromatic amino acids. Type II 3-dehydroquinase catalyzes the trans-dehydration of 3-dehydroshikimate see pfam01220.
Pssm-ID: 426287 Cd Length: 227 Bit Score: 211.26 E-value: 5.99e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 1068 FLCLTYPDVTQSFPVIHELTQGVDAIELRVDLLRASkdydsieysIPTLAYVSSQVAALRRVTSLPIVFTVRTQSQGGSf 1147
Cdd:pfam01487 1 CVPLTGKTLEEILEELESGKEGADLVELRVDLLEEP---------VEDAEDVSEQLALLRRVGDLPLIFTFRTKSEGGE- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 1148 PDAAEKEAVELLKLALRLGVEYVDVEISLSEKKIKELVSLK--GSSHMIASWHDWSGNMIWDgpVVKEKYDAAARFG-DI 1224
Cdd:pfam01487 71 PDGSEEEYLELLRLALRLGVDYVDVELFLPEEILKELIEAKheGGTKVIGSYHDFEGTPSWE--ELISRYEKMQALGaDI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 1225 IKIVGKANSIQDNFTLYNFVSKVNSTAgSKPFIAINMGLEGQMSRVLNSTL-SPVSHPLL--PSKAAPGQLSFKQIQNAL 1301
Cdd:pfam01487 149 VKIAVMAKSIEDVLALLRFTSEMKSLA-DKPLIAMSMGELGRISRVLGPIFgSPVTFAALglAEKSAPGQLTAKELREAL 227
|
|
| PRK11861 |
PRK11861 |
bifunctional prephenate dehydrogenase/3-phosphoshikimate 1-carboxyvinyltransferase; Provisional |
418-842 |
1.27e-61 |
|
bifunctional prephenate dehydrogenase/3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
Pssm-ID: 183343 [Multi-domain] Cd Length: 673 Bit Score: 224.97 E-value: 1.27e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 418 PGSKSISNRALVLAALGKGTCRLKNLLHSDDTQVMMAALNELkGASFAWEdaGETLVVKGGEGSLSVppKGKELYLGNAG 497
Cdd:PRK11861 258 PGSKSISNRVLLLAALAEGETTVTNLLDSDDTRVMLDALTKL-GVKLSRD--GGTCVVGGTRGAFTA--KTADLFLGNAG 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 498 TAARFLTTVCTLvqsspqDNAEYTvITGNARMKQRPIGPLVTALQANGSKIDFLESEGCLPLAIAPQGLK-GSQLQLAAS 576
Cdd:PRK11861 333 TAVRPLTAALAV------NGGEYR-IHGVPRMHERPIGDLVDGLRQIGARIDYEGNEGFPPLRIRPATISvDAPIRVRGD 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 577 VSSQYVSSILLCAPY--AEEPITLELIGGQVISQPYIDMTVAMMKTFGVDVVRRKdpvtgkfLDVYEIPKAV-YTNPPEY 653
Cdd:PRK11861 406 VSSQFLTALLMTLPLvkAKDGASVVEIDGELISKPYIEITIKLMARFGVTVERDG-------WQRFTVPAGVrYRSPGTI 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 654 NIESDASSATYPLAIAAVTGTSCTIQNIGSASLQGDAKFAKEVLEkMGCQVSQTATETTVQ--GPPIGQLKAIeEVDMEV 731
Cdd:PRK11861 479 MVEGDASSASYFLAAGALGGGPLRVEGVGRASIQGDVGFANALMQ-MGANVTMGDDWIEVRgiGHDHGRLAPI-DMDFNL 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 732 MTDAFLTATALAAVANGKTRIIGIANQRVKECNRIRAMIDELAKFGVETIELDDGLEIigKPISDLKRGVSVHCYDDHRV 811
Cdd:PRK11861 557 IPDAAMTIAVAALFADGPSTLRNIGSWRVKETDRIAAMATELRKVGATVEEGADYLVV--TPPAQLTPNASIDTYDDHRM 634
|
410 420 430
....*....|....*....|....*....|.
gi 170096704 812 AMAFSVLSTVVEGTIIEEKRCVEKTWPNWWD 842
Cdd:PRK11861 635 AMCFSLVSLGGVPVRINDPKCVGKTFPDYFD 665
|
|
| DHQase_I |
cd00502 |
Type I 3-dehydroquinase, (3-dehydroquinate dehydratase or DHQase); Type I 3-dehydroquinase, ... |
1066-1303 |
7.25e-61 |
|
Type I 3-dehydroquinase, (3-dehydroquinate dehydratase or DHQase); Type I 3-dehydroquinase, (3-dehydroquinate dehydratase or DHQase). Catalyzes the cis-dehydration of 3-dehydroquinate via a covalent imine intermediate to produce dehydroshikimate. Dehydroquinase is the third enzyme in the shikimate pathway, which is involved in the biosynthesis of aromatic amino acids. Type I DHQase exists as a homodimer. Type II 3-dehydroquinase also catalyzes the same overall reaction, but is unrelated in terms of sequence and structure, and utilizes a completely different reaction mechanism.
Pssm-ID: 188633 Cd Length: 225 Bit Score: 208.35 E-value: 7.25e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 1066 SYFLCLTYPD-VTQSFPVIhELTQGVDAIELRVDLLraskdydsieySIPTLAYVSSQVAALRRVTSLPIVFTVRTQSQG 1144
Cdd:cd00502 1 KICVPLTGPDlLEEALSLL-ELLLGADAVELRVDLL-----------EDPSIDDVAEQLSLLRELTPLPIIFTVRTKSEG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 1145 GSFPDAaEKEAVELLKLALRLGVEYVDVEisLSEKKIKELVS--LKGSSHMIASWHDWSGnmIWDGPVVKEKYDAAARFG 1222
Cdd:cd00502 69 GNFEGS-EEEYLELLEEALKLGPDYVDIE--LDSALLEELINsrKKGNTKIIGSYHDFSG--TPSDEELVSRLEKMAALG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 1223 -DIIKIVGKANSIQDNFTLYNFVSKVNSTAGsKPFIAINMGLEGQMSRVLN-STLSPVSHPLLPSKAAPGQLSFKQIQNA 1300
Cdd:cd00502 144 aDIVKIAVMANSIEDNLRLLKFTRQVKNLYD-IPLIAINMGELGKLSRILSpVFGSPLTYASLPEPSAPGQLSVEELKQA 222
|
...
gi 170096704 1301 LHL 1303
Cdd:cd00502 223 LSL 225
|
|
| EEVS |
cd08199 |
2-epi-5-epi-valiolone synthase (EEVS); 2-epi-5-epi-valiolone synthase catalyzes the ... |
41-378 |
7.20e-57 |
|
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: 201.22 E-value: 7.20e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 41 VLVTDTNVANFHLTAFEKEFEQRISslptsstKPRFLslVIPPGETSKSREGKANIEDFLLLHRCTRDSVILALGGGVIG 120
Cdd:cd08199 30 LVVVDENVDRLYGARIRAYFAAHGI-------EATIL--VLPGGEANKTMETVLRIVDALDDFGLDRREPVIAIGGGVLL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 121 DLVGFVAATFMRGVRFVQIPTTLLAMVDSSVGGKTAIDTPHGKNLIGAFWQPEYIFIDAAFLETLPSREFSNGMAEVVKT 200
Cdd:cd08199 101 DVVGFAASLYRRGVPYIRVPTTLLGLVDAGVGIKTGVNFGGHKNRLGAYYPPVATLLDRSFLKTLPRRHIRNGLAEIIKM 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 201 AAIwneaefislesRSADIFAAIQTpsadYAGRSKQTRSIAQELLLSVIVGSIsvkahIVTIDE-----RETGLRNLVNF 275
Cdd:cd08199 181 ALV-----------KDAELFELLEE----HGAALVETRFFQDEVADEIIRRAI-----QGMLEElapnlWEHDLERLVDF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 276 GHTIGHAIEAVLTPTILHGECVSVGMILEGEISRQMGILSQVGVGRLNRCLKAYNLPVTLAdpriaslpaakLLTVERLL 355
Cdd:cd08199 241 GHTFSPILEMAAAPELLHGEAVAIDMALSAVLAYRRGLLSEEELDRILRLMRRLGLPVWHP-----------LCTPDLLW 309
|
330 340
....*....|....*....|...
gi 170096704 356 DIMRIDKKNSGPEKKIVILSRIG 378
Cdd:cd08199 310 RALEDIVKHRDGLQRLPLPKGIG 332
|
|
| aroD |
TIGR01093 |
3-dehydroquinate dehydratase, type I; This model detects 3-dehydroquinate dehydratase, type I, ... |
1066-1301 |
9.35e-53 |
|
3-dehydroquinate dehydratase, type I; This model detects 3-dehydroquinate dehydratase, type I, either as a monofunctional protein or as a domain of a larger, multifunctional protein. It is often found fused to shikimate 5-dehydrogenase (EC 1.1.1.25), and sometimes additional domains. Type II 3-dehydroquinate dehydratase, designated AroQ, is described by the model TIGR01088. [Amino acid biosynthesis, Aromatic amino acid family]
Pssm-ID: 273439 Cd Length: 229 Bit Score: 185.28 E-value: 9.35e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 1066 SYFLCLTYPDVTQSFPVIHELTQ-GVDAIELRVDLLRASKDYDSIEYsiptlayVSSQVAALRrvTSLPIVFTVRTQSQG 1144
Cdd:TIGR01093 1 KIFVPLTAPDLEEALAEAEKICEkGADIVELRVDLLKDVSSNNDVDA-------LSEQLSELR--VDKPLIFTIRTQSEG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 1145 GSFPDAAEKEAVELLKLALRLGVEYVDVEISLSEKKIKELVSL--KGSSHMIASWHDWSGNMIWDgpVVKEKYDAAARF- 1221
Cdd:TIGR01093 72 GKFPGNEEEYFEELKRAAESLGPDFVDIELFLPDDAVKELINIakKGGTKIIMSNHDFQKTPSWE--EIVERLRKALSYg 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 1222 GDIIKIVGKANSIQDNFTLYNFVSKVnSTAGSKPFIAINMGLEGQMSRVLNSTLSPVSHPL-LPSKAAPGQLSFKQIQNA 1300
Cdd:TIGR01093 150 ADIVKIAVMANSKEDVLTLLSATNKV-DTHYDVPLITMSMGDRGKISRVLGAVFGSVLTFGsLGKASAPGQISVDDLREL 228
|
.
gi 170096704 1301 L 1301
Cdd:TIGR01093 229 L 229
|
|
| EPT-like |
cd01554 |
Enol pyruvate transferases family includes EPSP synthases and UDP-N-acetylglucosamine ... |
418-845 |
7.39e-52 |
|
Enol pyruvate transferases family includes EPSP synthases and UDP-N-acetylglucosamine enolpyruvyl transferase. Both enzymes catalyze the reaction of enolpyruvyl transfer.
Pssm-ID: 238795 Cd Length: 408 Bit Score: 188.97 E-value: 7.39e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 418 PGSKSISNRALVLAALGKGTCRLKNLLHSDDTQVMMAALNELkGASFawEDAGETLVVKGGEGSLSVPPKgKELYLGNAG 497
Cdd:cd01554 8 PGDKSISHRSLIFASLAEGETKVYNILRGEDVLSTMQVLRDL-GVEI--EDKDGVITIQGVGMAGLKAPQ-NALNLGNSG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 498 TAARFLTTVCTLVQSSpqdnaeyTVITGNARMKQRPIGPLVTALQANGSKIDFLESEGCLPLAIApQGLKGSQLQLAASV 577
Cdd:cd01554 84 TAIRLISGVLAGADFE-------VELFGDDSLSKRPMDRVTLPLKKMGASISGQEERDLPPLLKG-GKNLGPIHYEDPIA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 578 SSQYVSSILLCAPYAEEPITLEliggQVISQPYIDMTVAMMKTFGVDV-VRRKDPVTGKFLDVYEIPKavytnppeYNIE 656
Cdd:cd01554 156 SAQVKSALMFAALLAKGETVII----EAAKEPTINHTENMLQTFGGHIsVQGTKKIVVQGPQKLTGQK--------YVVP 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 657 SDASSATYPLAIAAVTGTSCTIQNIGSASlqGDAKFAkEVLEKMGCQVSQTATETTVQgppIGQLKAIeEVDM---EVMT 733
Cdd:cd01554 224 GDISSAAFFLVAAAIAPGRLVLQNVGINE--TRTGII-DVLRAMGAKIEIGEDTISVE---SSDLKAT-EICGaliPRLI 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 734 DAFLTATALAAVANGKTRIIGIANQRVKECNRIRAMIDELAKFGVETIELDDGleIIGKPISDLKrGVSVHCYDDHRVAM 813
Cdd:cd01554 297 DELPIIALLALQAQGTTVIKDAEELKVKETDRIFVVADELNSMGADIEPTADG--MIIKGKEKLH-GARVNTFGDHRIGM 373
|
410 420 430
....*....|....*....|....*....|...
gi 170096704 814 AFSVLSTVVEGTI-IEEKRCVEKTWPNWWDDLE 845
Cdd:cd01554 374 MTALAALVADGEVeLDRAEAINTSYPSFFDDLE 406
|
|
| PRK14021 |
PRK14021 |
bifunctional shikimate kinase/3-dehydroquinate synthase; Provisional |
79-378 |
1.15e-50 |
|
bifunctional shikimate kinase/3-dehydroquinate synthase; Provisional
Pssm-ID: 184458 [Multi-domain] Cd Length: 542 Bit Score: 188.92 E-value: 1.15e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 79 LVIPPGETSKSREGKANIEDFLLLHRCTRDSVILALGGGVIGDLVGFVAATFMRGVRFVQIPTTLLAMVDSSVGGKTAID 158
Cdd:PRK14021 241 IVIPDAEAGKTIEVANGIWQRLGNEGFTRSDAIVGLGGGAATDLAGFVAATWMRGIRYVNCPTSLLAMVDASTGGKTGIN 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 159 TPHGKNLIGAFWQPEYIFIDAAFLETLPSREFSNGMAEVVKTAAIwNEAEFISLESRSADIFAAIQtpSADYAGrskqtr 238
Cdd:PRK14021 321 TPQGKNLVGSFYTPAGVLADTKTLATLPNDIFIEGLGEVAKSGFI-RDPEILRILEDHAAELRAFD--GSTFLG------ 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 239 SIAQELLLSVIVGSISVKAHIVTIDERETGLRNLVNFGHTIGHAIEAVLTPTILHGECVSVGMILEGEISRQMGILSQVG 318
Cdd:PRK14021 392 SPLEDVVAELIERTVKVKAYHVSSDLKEAGLREFLNYGHTLGHAIEKLEHFRWRHGNAVAVGMVYAAELAHLLGYIDQDL 471
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 319 VGRLNRCLKAYNLPVTLADPriaslpaakllTVERLLDIMRIDKKNSGPEKKIVILSRIG 378
Cdd:PRK14021 472 VDYHRSLLASLGLPTSWNGG-----------SFDDVLALMHRDKKARGNELRFVVLDEIG 520
|
|
| aroE |
TIGR00507 |
shikimate dehydrogenase; This model finds proteins from prokaryotes and functionally ... |
1314-1576 |
1.33e-48 |
|
shikimate dehydrogenase; This model finds proteins from prokaryotes and functionally equivalent domains from larger, multifunctional proteins of fungi and plants. Below the trusted cutoff of 180, but above the noise cutoff of 20, are the putative shikimate dehydrogenases of Thermotoga maritima and Mycobacterium tuberculosis, and uncharacterized paralogs of shikimate dehydrogenase from E. coli and H. influenzae. The related enzyme quinate 5-dehydrogenase scores below the noise cutoff. A neighbor-joining tree, constructed with quinate 5-dehydrogenases as the outgroup, shows the Clamydial homolog as clustering among the shikimate dehydrogenases, although the sequence is unusual in the degree of sequence divergence and the presence of an additional N-terminal domain. [Amino acid biosynthesis, Aromatic amino acid family]
Pssm-ID: 161904 [Multi-domain] Cd Length: 270 Bit Score: 174.53 E-value: 1.33e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 1314 LFGTPIAHSMSPTLHNTGFEILGLPHHYELLETKEVAEE-IKIAIGDSAFGGASVTIPYKLDVIPLLDKLSPAAEAIGAV 1392
Cdd:TIGR00507 5 VIGNPIAHSKSPLIHNAFFKQLGLEGPYIAFLVPPDDLEdALSGFFALGFKGANVTSPFKERAFQFLDEIDGRAKLAGAV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 1393 NTIIPRttgsGRMLVGDNTDWLGIKACITEQLSSKPIHAALVIGAGGTARAAIYALSALNVgDIYLYNRTTSKAYELAHA 1472
Cdd:TIGR00507 85 NTLVLE----DGKLVGYNTDGIGLVSDLEQLIPLRPNQNVLIIGAGGAAKAVALELLKADC-NVIIANRTVSKAEELAER 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 1473 FPHapvhvLEQLGQWPNGAVPP---CVIVSTVPASAttteeeTSGILLPSKLFDYRDGPAVVIDMAYKPAETPLLRLAKT 1549
Cdd:TIGR00507 160 FQR-----YGEIQAFSMDELPLhrvDLIINATSAGM------SGNIDEPPVPAEYLKEGKLVYDLVYNPLETPFLAEAKS 228
|
250 260
....*....|....*....|....*..
gi 170096704 1550 AGDNwaTVPGLEVLLEQGYVQFEMWTG 1576
Cdd:TIGR00507 229 LGTK--TIDGLGMLVYQAALSFELWTG 253
|
|
| PLN02520 |
PLN02520 |
bifunctional 3-dehydroquinate dehydratase/shikimate dehydrogenase |
1089-1591 |
1.23e-47 |
|
bifunctional 3-dehydroquinate dehydratase/shikimate dehydrogenase
Pssm-ID: 178135 [Multi-domain] Cd Length: 529 Bit Score: 179.96 E-value: 1.23e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 1089 GVDAIELRVDLLRASKDYDSIEysiptlayvssqvaALRRVTSLPIVFTVRTQSQGGSFpDAAEKEAVELLKLALRLGVE 1168
Cdd:PLN02520 48 GADLVEIRLDFLKNFNPREDLK--------------TLIKQSPLPTLVTYRPKWEGGQY-EGDENKRQDALRLAMELGAD 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 1169 YVDVEISLSEKKIKELVSLK-GSSHMIASWHDWSGNmiwdgPVVKEKYDAAARF----GDIIKIVGKANSIQDNFTLYNF 1243
Cdd:PLN02520 113 YVDVELKVAHEFINSISGKKpEKCKVIVSSHNYENT-----PSVEELGNLVARIqatgADIVKIATTALDITDVARMFQI 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 1244 VskVNSTAgskPFIAINMGLEGQMSRVLNSTLSP-VSHPLLPSKA--APGQLSFKQIQNALHLLGLLPAQRFY-LFGTPI 1319
Cdd:PLN02520 188 T--VHSQV---PTIGLVMGERGLISRILCPKFGGyLTFGTLEAGKvsAPGQPTIKDLLDLYNFRQIGPDTKVYgIIGKPV 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 1320 AHSMSPTLHNTGFEILGLPHHYELLETKEVAEEIKiAIGDSAFGGASVTIPYKLDVIPLLDKLSPAAEAIGAVNTIIpRT 1399
Cdd:PLN02520 263 GHSKSPILHNEAFKSVGFNGVYVHLLVDDLAKFLQ-TYSSPDFAGFSCTIPHKEDALKCCDEVDPIAKSIGAINTII-RR 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 1400 TGSGRmLVGDNTDWLGIKACITEQL--------SSKPIHAAL--VIGAGGTARAAIYAlsALNVG-DIYLYNRTTSKAYE 1468
Cdd:PLN02520 341 PSDGK-LVGYNTDYIGAISAIEDGLrasgsspaSGSPLAGKLfvVIGAGGAGKALAYG--AKEKGaRVVIANRTYERAKE 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 1469 LAHAFpHAPVHVLEQLGQW-PNGAVppcVIVSTVPASATTTEEETSgilLPSKLFDYRdgpAVVIDMAYKPAETPLLRLA 1547
Cdd:PLN02520 418 LADAV-GGQALTLADLENFhPEEGM---ILANTTSVGMQPNVDETP---ISKHALKHY---SLVFDAVYTPKITRLLREA 487
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 170096704 1548 KTAGDnwATVPGLEVLLEQGYVQFEMWTGRRCPKELVAKWLGRL 1591
Cdd:PLN02520 488 EESGA--IIVSGTEMFIRQAYEQFERFTGLPAPKELFREIMSKY 529
|
|
| SK |
cd00464 |
Shikimate kinase (SK) is the fifth enzyme in the shikimate pathway, a seven-step biosynthetic ... |
877-1018 |
1.38e-43 |
|
Shikimate kinase (SK) is the fifth enzyme in the shikimate pathway, a seven-step biosynthetic pathway which converts erythrose-4-phosphate to chorismic acid, found in bacteria, fungi and plants. Chorismic acid is a important intermediate in the synthesis of aromatic compounds, such as aromatic amino acids, p-aminobenzoic acid, folate and ubiquinone. Shikimate kinase catalyses the phosphorylation of the 3-hydroxyl group of shikimic acid using ATP.
Pssm-ID: 238260 [Multi-domain] Cd Length: 154 Bit Score: 155.79 E-value: 1.38e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 877 SIILIGMRGTGKTFVGNLAAATLSWTCLDADAYFETKHEMGVREFVHQKGWQAFRDAEFEVLRELiaEKSQGHVISLGGG 956
Cdd:cd00464 1 NIVLIGMMGAGKTTVGRLLAKALGLPFVDLDELIEQRAGMSIPEIFAEEGEEGFRELEREVLLLL--LTKENAVIATGGG 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 170096704 957 IVETPAARELLKEyaatKGPVVHIVRPIDEVIRYLNSEASRPAY----DEAIVDVFRRREPWFGEC 1018
Cdd:cd00464 79 AVLREENRRLLLE----NGIVVWLDASPEELLERLARDKTRPLLqdedPERLRELLEEREPLYREV 140
|
|
| NAD_bind_Shikimate_DH |
cd01065 |
NAD(P) binding domain of Shikimate dehydrogenase; Shikimate dehydrogenase (DH) is an amino ... |
1411-1576 |
1.22e-41 |
|
NAD(P) binding domain of Shikimate dehydrogenase; Shikimate dehydrogenase (DH) is an amino acid DH family member. Shikimate pathway links metabolism of carbohydrates to de novo biosynthesis of aromatic amino acids, quinones and folate. It is essential in plants, bacteria, and fungi but absent in mammals, thus making enzymes involved in this pathway ideal targets for broad spectrum antibiotics and herbicides. Shikimate DH catalyzes the reduction of 3-hydroshikimate to shikimate using the cofactor NADH. Amino acid DH-like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DHs, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.
Pssm-ID: 133443 [Multi-domain] Cd Length: 155 Bit Score: 150.50 E-value: 1.22e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 1411 TDWLGIKACITEQLSSKPIHAALVIGAGGTARAAIYALSALNVGDIYLYNRTTSKAYELAHAFPHAPvhVLEQLGQWPNG 1490
Cdd:cd01065 1 TDGLGFVRALEEAGIELKGKKVLILGAGGAARAVAYALAELGAAKIVIVNRTLEKAKALAERFGELG--IAIAYLDLEEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 1491 AVPPCVIVSTVPASATTTEEetsgILLPSKLFdyrDGPAVVIDMAYKPAETPLLRLAKTAGdnWATVPGLEVLLEQGYVQ 1570
Cdd:cd01065 79 LAEADLIINTTPVGMKPGDE----LPLPPSLL---KPGGVVYDVVYNPLETPLLKEARALG--AKTIDGLEMLVYQAAEA 149
|
....*.
gi 170096704 1571 FEMWTG 1576
Cdd:cd01065 150 FELWTG 155
|
|
| DHQS-like |
cd08198 |
Dehydroquinate synthase (DHQS) catalyzes the conversion of DAHP to DHQ in shikimate pathway ... |
79-333 |
1.94e-38 |
|
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: 148.49 E-value: 1.94e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 79 LVIPPGETSKSreGKANIEDFL---LLHRCTRDSVILALGGGVIGDLVGFVAATFMRGVRFVQIPTTLLAMVDSSVGGKT 155
Cdd:cd08198 70 LIVPGGEAVKN--DPALVEEILsaiHDHGLDRHSYVVVIGGGAVLDAVGFAAAIAHRGIRLIRVPTTVLAQNDSGVGVKN 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 156 AIDTPHGKNLIGAFWQPEYIFIDAAFLETLPSREFSNGMAEVVKTAAIWNEAEFISLEsRSADIFAAIQTPSADYAGRsk 235
Cdd:cd08198 148 GINFFGKKNFLGTFAPPFAVINDFDFLETLPDRDWRSGIAEAVKVALIKDASFFEWLE-RNAAALRQRDPDAMEKLIR-- 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 236 qtRSIaqELLLsvivgsisvkAHIVTI-DERETGLRNLVNFGHTIGHAIEAVLTPTILHGECVSVGMILEGEISRQMGIL 314
Cdd:cd08198 225 --RCA--ELHL----------DHIAASgDPFETGSARPLDFGHWSAHKLEQLSGYALRHGEAVAIGIALDSLYARLLGLL 290
|
250
....*....|....*....
gi 170096704 315 SQVGVGRLNRCLKAYNLPV 333
Cdd:cd08198 291 SREDFDRILALLQNLGLPL 309
|
|
| aroB |
PRK06203 |
3-dehydroquinate synthase; Reviewed |
79-333 |
8.98e-38 |
|
3-dehydroquinate synthase; Reviewed
Pssm-ID: 235740 Cd Length: 389 Bit Score: 146.97 E-value: 8.98e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 79 LVIPPGETSKSREGKAN-IEDFLLLHRCTRDSVILALGGGVIGDLVGFVAATFMRGVRFVQIPTTLLAMVDSSVGGKTAI 157
Cdd:PRK06203 82 LVVPGGEAAKNDPALVEaLHAAINRHGIDRHSYVLAIGGGAVLDMVGYAAATAHRGVRLIRIPTTVLAQNDSGVGVKNGI 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 158 DTPHGKNLIGAFWQPEYIFIDAAFLETLPSREFSNGMAEVVKTAAIwNEAEFISLESRSADIFAAIQTPSADYAGRskqt 237
Cdd:PRK06203 162 NAFGKKNFLGTFAPPYAVINDFAFLTTLPDRDWRAGLAEAVKVALI-KDAAFFDWLEAHAAALAARDPEAMEELIY---- 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 238 RSiaQELLLSVIVGSisvkahivtIDERETGLRNLVNFGHTIGHAIEAVLTPTILHGECVSVGMILEGEISRQMGILSQV 317
Cdd:PRK06203 237 RC--AELHLEHIAGG---------GDPFEFGSSRPLDFGHWSAHKLEQLTNYALRHGEAVAIGIALDSLYSYLLGLLSEA 305
|
250
....*....|....*.
gi 170096704 318 GVGRLNRCLKAYNLPV 333
Cdd:PRK06203 306 EAQRILALLRALGFPL 321
|
|
| AroD |
COG0710 |
3-dehydroquinate dehydratase [Amino acid transport and metabolism]; 3-dehydroquinate ... |
1086-1305 |
4.40e-35 |
|
3-dehydroquinate dehydratase [Amino acid transport and metabolism]; 3-dehydroquinate dehydratase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis
Pssm-ID: 440474 Cd Length: 236 Bit Score: 134.65 E-value: 4.40e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 1086 LTQGVDAIELRVDLLRAskdydsieysiPTLAYVSSQVAALRRVTSLPIVFTVRTQSQGGSFPdAAEKEAVELLKLALRL 1165
Cdd:COG0710 26 ARAGADLVELRLDYLED-----------PDLEELKELLEALREYGGLPLIFTFRTAEEGGEFE-GSEEERLELLRAAADS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 1166 -GVEYVDVEISLSEKKIKELVSLKGSSH--MIASWHDWSGnmiwdGP---VVKEKYDAAARFG-DIIKIVGKANSIQDNF 1238
Cdd:COG0710 94 aGVDLVDVELDTLEDDVDDLIEAAREAGvkVIVSYHDFEK-----TPsaeELVEILEKMQELGaDIVKIAVMAKSPEDVL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 170096704 1239 TLYNFVSKVNSTAGsKPFIAINMGLEGQMSRVLNSTL-SPVSHPLLPSKAAPGQLSFKQIQNALHLLG 1305
Cdd:COG0710 169 RLLEATLEAKEELD-RPVITMAMGELGKISRILGPLFgSALTYASVGEASAPGQIDVEELRELLELLE 235
|
|
| AroK |
COG0703 |
Shikimate kinase [Amino acid transport and metabolism]; Shikimate kinase is part of the ... |
878-1021 |
3.37e-34 |
|
Shikimate kinase [Amino acid transport and metabolism]; Shikimate kinase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis
Pssm-ID: 440467 [Multi-domain] Cd Length: 165 Bit Score: 129.48 E-value: 3.37e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 878 IILIGMRGTGKTFVGNLAAATLSWTCLDADAYFETKHEMGVREFVHQKGWQAFRDAEFEVLRELIAEKsqGHVISLGGGI 957
Cdd:COG0703 1 IVLIGMMGAGKSTVGRLLAKRLGLPFVDTDAEIEERAGMSIPEIFAEEGEAGFRELEREVLAELLEEE--NAVIATGGGA 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 170096704 958 VETPAARELLKEYaatkGPVVHIVRPIDEVIRYLNSEASRPAYD-----EAIVDVFRRREPWFGECCSH 1021
Cdd:COG0703 79 VLSPENRELLKEH----GTVVYLDASPETLLERLRRDDNRPLLQgedprERLEELLAEREPLYREVADI 143
|
|
| SKI |
pfam01202 |
Shikimate kinase; |
884-1018 |
2.94e-32 |
|
Shikimate kinase;
Pssm-ID: 426122 [Multi-domain] Cd Length: 159 Bit Score: 123.46 E-value: 2.94e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 884 RGTGKTFVGNLAAATLSWTCLDADAYFETKHEMGVREFVHQKGWQAFRDAEFEVLRELIAEKsqGHVISLGGGIVETPAA 963
Cdd:pfam01202 1 MGAGKSTIGRLLAKALGLPFIDTDEEIEKRTGMSIAEIFEEEGEEGFRRLESEVLKELLAEH--GLVIATGGGAVLSEEN 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 170096704 964 RELLKEyaatKGPVVHIVRPIDEVIRYLNSEASRPAYDEAIVDVFRRREPWFGEC 1018
Cdd:pfam01202 79 RDLLKE----RGIVIYLDAPLEVLLERLKRDKTRPLLQNKDPEEELLELLFEERD 129
|
|
| PRK13951 |
PRK13951 |
bifunctional shikimate kinase AroK/3-dehydroquinate synthase AroB; |
79-316 |
7.48e-32 |
|
bifunctional shikimate kinase AroK/3-dehydroquinate synthase AroB;
Pssm-ID: 172457 [Multi-domain] Cd Length: 488 Bit Score: 131.56 E-value: 7.48e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 79 LVIPPGETSKSREGKANIEDFLLLHRCTRDSVILALGGGVIGDLVGFVAATFMRGVRFVQIPTTLLAMVDSSVGGKTAID 158
Cdd:PRK13951 209 LLFPDGEEVKTLEHVSRAYYELVRMDFPRGKTIAGVGGGALTDFTGFVASTFKRGVGLSFYPTTLLAQVDASVGGKNAID 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 159 TPHGKNLIGAFWQPEYIFIDAAFLETLPSREFSNGMAEVVKTAAiwneaefisLESRSADIFAAIQtpsadyagrSKQTR 238
Cdd:PRK13951 289 FAGVKNVVGTFRMPDYVIIDPTVTLSMDEGRFEEGVVEAFKMTI---------LSGRGVELFDEPE---------KIEKR 350
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 170096704 239 SIaqELLLSVIVGSISVKAHIVTIDERETGLRNLVNFGHTIGHAIEAvlTPTILHGECVSVGMILEGEISRQMGILSQ 316
Cdd:PRK13951 351 NL--RVLSEMVKISVEEKARIVMEDPYDMGLRHALNLGHTLGHVYEM--LEGVPHGIAVAWGIEKETMYLYRKGIVPK 424
|
|
| PRK14806 |
PRK14806 |
bifunctional cyclohexadienyl dehydrogenase/ 3-phosphoshikimate 1-carboxyvinyltransferase; ... |
418-853 |
6.66e-31 |
|
bifunctional cyclohexadienyl dehydrogenase/ 3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
Pssm-ID: 237820 [Multi-domain] Cd Length: 735 Bit Score: 131.66 E-value: 6.66e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 418 PGSKSISNRALVLAALGKGTCRLKNLLHSDDTQVMMAALNELkGASFAWEDAGETLVVKGGEGSLSVPPKgkELYLGNAG 497
Cdd:PRK14806 319 PGDKSISHRSIMLGSLAEGVTEVEGFLEGEDALATLQAFRDM-GVVIEGPHNGRVTIHGVGLHGLKAPPG--PLYMGNSG 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 498 TAARFLTTVCTlVQSSPqdnaeyTVITGNARMKQRPIGPLVTALQANGSKIDflESEGCL-PLAI-APQGLKGSQLQLAA 575
Cdd:PRK14806 396 TSMRLLSGLLA-AQSFD------SVLTGDASLSKRPMERVAKPLREMGAVIE--TGEEGRpPLSIrGGQRLKGIHYDLPM 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 576 SvSSQYVSSILLCAPYAEepitleliGGQVISQPYI--DMTVAMMKTFGVDVVRRKDPVTgkfldVYEIPKAVYTNppeY 653
Cdd:PRK14806 467 A-SAQVKSCLLLAGLYAE--------GETSVTEPAPtrDHTERMLRGFGYPVKVEGNTIS-----VEGGGKLTATD---I 529
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 654 NIESDASSATYPLAIAAVT-GTSCTIQNIG-----SASLqgdakfakEVLEKMGCQVSqTATETTVQGPPIG-------Q 720
Cdd:PRK14806 530 EVPADISSAAFFLVAASIAeGSELTLEHVGinptrTGVI--------DILKLMGADIT-LENEREVGGEPVAdirvrgaR 600
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 721 LKAIE--EVDMEVMTDAFLTATALAAVANGKTRIIGIANQRVKECNRIRAMIDELAKFGVETIELDDGLEIIGKPIsdlk 798
Cdd:PRK14806 601 LKGIDipEDQVPLAIDEFPVLFVAAACAEGRTVLTGAEELRVKESDRIQVMADGLKTLGIDCEPTPDGIIIEGGIF---- 676
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 170096704 799 RGVSVHCYDDHRVAMAFSVLSTVVEGTI-IEEKRCVEKTWPNwWDDLENKIGLTVQ 853
Cdd:PRK14806 677 GGGEVESHGDHRIAMSFSVASLRASGPItIHDCANVATSFPN-FLELANQVGIRIE 731
|
|
| PRK12548 |
PRK12548 |
shikimate dehydrogenase; |
1314-1586 |
2.92e-29 |
|
shikimate dehydrogenase;
Pssm-ID: 183585 [Multi-domain] Cd Length: 289 Bit Score: 119.46 E-value: 2.92e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 1314 LFGTPIAHSMSPTLHNTGFEILGLPHHYELLETK--EVAEEIKiAIGDSAFGGASVTIPYKLDVIPLLDKLSPAAEAIGA 1391
Cdd:PRK12548 14 LIGSPVGHSGSPAMYNYSFQKAGLDYAYLAFDIPvdKVPDAIK-AIKTFNMRGANVTMPCKSEAAKYMDELSPAARIIGA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 1392 VNTIIprtTGSGRmLVGDNTDWLGIKACITE---QLSSKPIhaaLVIGAGGTArAAIYALSAL---------NVGDIYlY 1459
Cdd:PRK12548 93 VNTIV---NDDGK-LTGHITDGLGFVRNLREhgvDVKGKKL---TVIGAGGAA-TAIQVQCALdgakeitifNIKDDF-Y 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 1460 NRTTSKAYELAHAFPHAPVHV-----LEQLGQwpngavppCVIVSTVPASATTT----EEETSGILLPSKLfdyRDGpAV 1530
Cdd:PRK12548 164 ERAEQTAEKIKQEVPECIVNVydlndTEKLKA--------EIASSDILVNATLVgmkpNDGETNIKDTSVF---RKD-LV 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 170096704 1531 VIDMAYKPAETPLLRLAKTAGDNwaTVPGLEVLLEQGYVQFEMWTGRRCPKELVAK 1586
Cdd:PRK12548 232 VADTVYNPKKTKLLEDAEAAGCK--TVGGLGMLLWQGAEAYKLYTGKDMPVEEVKE 285
|
|
| Shikimate_dh_N |
pfam08501 |
Shikimate dehydrogenase substrate binding domain; This domain is the substrate binding domain ... |
1314-1395 |
3.98e-29 |
|
Shikimate dehydrogenase substrate binding domain; This domain is the substrate binding domain of shikimate dehydrogenase.
Pssm-ID: 400688 [Multi-domain] Cd Length: 83 Bit Score: 111.92 E-value: 3.98e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 1314 LFGTPIAHSMSPTLHNTGFEILGLPHHYELLETKEVA-EEIKIAIGDSAFGGASVTIPYKLDVIPLLDKLSPAAEAIGAV 1392
Cdd:pfam08501 1 VIGNPISHSLSPAIHNAAFKALGLNGVYVAFEVPPDNlPDFVEGLRALGFRGLNVTIPHKEAAIPLLDELSPEAKAIGAV 80
|
...
gi 170096704 1393 NTI 1395
Cdd:pfam08501 81 NTI 83
|
|
| aroDE |
PRK09310 |
bifunctional 3-dehydroquinate dehydratase/shikimate dehydrogenase; |
1090-1574 |
8.41e-29 |
|
bifunctional 3-dehydroquinate dehydratase/shikimate dehydrogenase;
Pssm-ID: 137204 [Multi-domain] Cd Length: 477 Bit Score: 122.21 E-value: 8.41e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 1090 VDAIELRVDLLrASKDYDSIEYSIpTLAYVSsqVAALRRVTSL-PIVFTVRTQSqggsfpdaaekeavellkLAlRLGVE 1168
Cdd:PRK09310 25 VDCIELRVDLL-LSLSDLELKKLI-ELAPIP--ILTWKKHESCsQAAWIDKMQS------------------LA-KLNPN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 1169 YVDVEISLSEKKIKELVSLKGSSHMIASWHDWSGNmiwDGPVVKEKYDAAArfGDIIKIVGKANSIQDnftLYNFVSKVN 1248
Cdd:PRK09310 82 YLDIDKDFPKEALIRIRKLHPKIKIILSYHTSEHE---DIIQLYNEMLASA--ADYYKIAVSSSSSTD---LLNIIHQKR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 1249 STAgsKPFIAINMGLEGQMSRVLNSTLS-PVSH--PLLPSKAAPGQLSFKQIQnALHLLGLLPAQRFY-LFGTPIAHSMS 1324
Cdd:PRK09310 154 SLP--ENTTVLCMGGMGRPSRILSPLLQnAFNYaaGIGAPPVAPGQLSLEHLL-FYNYANLSAQSPIYgLIGDPVDRSIS 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 1325 PTLHNTGFEILGLPHHY-ELLETKEVAEEIKIAIGDSAFGGASVTIPYKLDVIPLLDKLSPAAEAIGAVNTIIPRTtgsg 1403
Cdd:PRK09310 231 HLSHNPLFSQLSLNCPYiKLPLTPQELPKFFSTIRDLPFLGLSVTMPLKTAVLDFLDKLDPSVKLCGSCNTLVFRN---- 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 1404 RMLVGDNTDWLGIKACITE-QLSSKPIHAALViGAGGTARaAIYALSALNVGDIYLYNRTTSKAYELA-----HAFPhap 1477
Cdd:PRK09310 307 GKIEGYNTDGEGLFSLLKQkNIPLNNQHVAIV-GAGGAAK-AIATTLARAGAELLIFNRTKAHAEALAsrcqgKAFP--- 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 1478 vhvLEQLGQWPNGAvppcVIVSTVPASATtteeetsgilLPSKLfdyrdgPAVVIDMAYKPAETPLLRLAKTAGDNwaTV 1557
Cdd:PRK09310 382 ---LESLPELHRID----IIINCLPPSVT----------IPKAF------PPCVVDINTLPKHSPYTQYARSQGSS--II 436
|
490
....*....|....*..
gi 170096704 1558 PGLEVLLEQGYVQFEMW 1574
Cdd:PRK09310 437 YGYEMFAEQALLQFRLW 453
|
|
| PRK12549 |
PRK12549 |
shikimate 5-dehydrogenase; Reviewed |
1314-1578 |
1.93e-27 |
|
shikimate 5-dehydrogenase; Reviewed
Pssm-ID: 183586 [Multi-domain] Cd Length: 284 Bit Score: 113.84 E-value: 1.93e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 1314 LFGTPIAHSMSPTLHNTGFEILGLPHHYELLE------TKEVAEEIKIAIGDSAFGGASVTIPYKLDVIPLLDKLSPAAE 1387
Cdd:PRK12549 10 LIGAGIQASLSPAMHEAEGDAQGLRYVYRLIDldalglTADALPELLDAAERMGFAGLNITHPCKQAVIPHLDELSDDAR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 1388 AIGAVNTIIPRttgSGRmLVGDNTDWLGIKACITEQLSSKPIHAALVIGAGGTARAAIYALSALNVGDIYLY----NRTT 1463
Cdd:PRK12549 90 ALGAVNTVVFR---DGR-RIGHNTDWSGFAESFRRGLPDASLERVVQLGAGGAGAAVAHALLTLGVERLTIFdvdpARAA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 1464 SKAYELAHAFPHAPVHVLEQLGQwpngAVPPC--VIVST------VPASATTTEeetsgiLLPSKLFdyrdgpavVIDMA 1535
Cdd:PRK12549 166 ALADELNARFPAARATAGSDLAA----ALAAAdgLVHATptgmakHPGLPLPAE------LLRPGLW--------VADIV 227
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 170096704 1536 YKPAETPLLRLAKTAGdnWATVPGLEVLLEQGYVQFEMWTGRR 1578
Cdd:PRK12549 228 YFPLETELLRAARALG--CRTLDGGGMAVFQAVDAFELFTGRE 268
|
|
| PRK12550 |
PRK12550 |
shikimate 5-dehydrogenase; Reviewed |
1328-1586 |
2.08e-27 |
|
shikimate 5-dehydrogenase; Reviewed
Pssm-ID: 183587 [Multi-domain] Cd Length: 272 Bit Score: 113.51 E-value: 2.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 1328 HNTGFEILGLPHHYELLETKEVAEEIKiaiGDSAFG--GASVTIPYKLDVIPLLDKLSPAAEAIGAVNTIIpRTTGsgrM 1405
Cdd:PRK12550 27 HNYLYEALGLNFLYKAFTTTDLTAAIG---GVRALGirGCAVSMPFKEAVIPLVDELDPSAQAIESVNTIV-NTDG---H 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 1406 LVGDNTDWLGIKACITE-QLSskPIHAALVIGAGGTARAAIYAL--SALNVGDIYLYNRTTSKAyeLAhafphapvhvlE 1482
Cdd:PRK12550 100 LKAYNTDYIAIAKLLASyQVP--PDLVVALRGSGGMAKAVAAALrdAGFTDGTIVARNEKTGKA--LA-----------E 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 1483 QLG-QWPN--GAVPPCVIVSTVPASATTTEEETSgILLPSKLFDYRDgpaVVIDMAYKPAETPLLRLAKTAGDnwATVPG 1559
Cdd:PRK12550 165 LYGyEWRPdlGGIEADILVNVTPIGMAGGPEADK-LAFPEAEIDAAS---VVFDVVALPAETPLIRYARARGK--TVITG 238
|
250 260
....*....|....*....|....*..
gi 170096704 1560 LEVLLEQGYVQFEMWTGRRCPKELVAK 1586
Cdd:PRK12550 239 AEVIALQAVEQFVLYTGVRPSDELIAE 265
|
|
| aroK |
PRK00131 |
shikimate kinase; Reviewed |
877-1013 |
8.95e-24 |
|
shikimate kinase; Reviewed
Pssm-ID: 234654 [Multi-domain] Cd Length: 175 Bit Score: 99.88 E-value: 8.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 877 SIILIGMRGTGKTFVGNLAAATLSWTCLDADAYFETKHEMGVREFVHQKGWQAFRDAEFEVLRELIAEksQGHVISLGGG 956
Cdd:PRK00131 6 NIVLIGFMGAGKSTIGRLLAKRLGYDFIDTDHLIEARAGKSIPEIFEEEGEAAFRELEEEVLAELLAR--HNLVISTGGG 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 170096704 957 IVETPAARELLKEyaatKGPVVHIVRPIDEVIRYLNSEASRP-----AYDEAIVDVFRRREP 1013
Cdd:PRK00131 84 AVLREENRALLRE----RGTVVYLDASFEELLRRLRRDRNRPllqtnDPKEKLRDLYEERDP 141
|
|
| aroD |
PRK02412 |
type I 3-dehydroquinate dehydratase; |
1090-1305 |
5.51e-23 |
|
type I 3-dehydroquinate dehydratase;
Pssm-ID: 235036 Cd Length: 253 Bit Score: 99.97 E-value: 5.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 1090 VDAIELRVDLLRASKDYDSIEYSIPTLayvssqvaaLRRVTSLPIVFTVRTQSQGGSFPdAAEKEAVELLKLALRLG-VE 1168
Cdd:PRK02412 42 ADIIEWRADFLEKISDVESVLAAAPAI---------REKFAGKPLLFTFRTAKEGGEIA-LSDEEYLALIKAVIKSGlPD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 1169 YVDVEISLSEKKIKELVSL--KGSSHMIASWHDWSG-----NMIwdgpvvkEKYDAAARFG-DIIKIVGKANSIQDNFTL 1240
Cdd:PRK02412 112 YIDVELFSGKDVVKEMVAFahEHGVKVVLSYHDFEKtppkeEIV-------ERLRKMESLGaDIVKIAVMPQSEQDVLTL 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 170096704 1241 YNFVSKVNSTAGSKPFIAINMGLEGQMSRVLNSTL-SPVSHPLLPSKAAPGQLSFKQIQNALHLLG 1305
Cdd:PRK02412 185 LNATREMKELYADQPLITMSMGKLGRISRLAGEVFgSSWTFASLDKASAPGQISVEDLRRILEILH 250
|
|
| PRK12749 |
PRK12749 |
quinate/shikimate dehydrogenase; Reviewed |
1314-1589 |
1.40e-21 |
|
quinate/shikimate dehydrogenase; Reviewed
Pssm-ID: 183721 [Multi-domain] Cd Length: 288 Bit Score: 97.00 E-value: 1.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 1314 LFGTPIAHSMSPTLHNTGFEILGLPHHYELLETKEVAEEIKIAiGDSAFG--GASVTIPYKLDVIPLLDKLSPAAEAIGA 1391
Cdd:PRK12749 12 LMAYPIRHSLSPEMQNKALEKAGLPFTYMAFEVDNDSFPGAIE-GLKALKmrGTGVSMPNKQLACEYVDELTPAAKLVGA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 1392 VNTIIprttGSGRMLVGDNTDWLGIKACITEQLSSKPIHAALVIGAGGtARAAIYALSALN-VGDIYLYNRtTSKAYELA 1470
Cdd:PRK12749 91 INTIV----NDDGYLRGYNTDGTGHIRAIKESGFDIKGKTMVLLGAGG-ASTAIGAQGAIEgLKEIKLFNR-RDEFFDKA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 1471 HAFPH---------APVHVLEQLGQWPNGAVPPCVIVSTVPASATTTEEET----SGILLPSKLfdyrdgpavVIDMAYK 1537
Cdd:PRK12749 165 LAFAQrvnentdcvVTVTDLADQQAFAEALASADILTNGTKVGMKPLENESlvndISLLHPGLL---------VTECVYN 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 170096704 1538 PAETPLLRLAKTAGdnWATVPGLEVLLEQGYVQFEMWTGRRCPKELVAKWLG 1589
Cdd:PRK12749 236 PHMTKLLQQAQQAG--CKTIDGYGMLLWQGAEQFTLWTGKDFPLEYVKQVMG 285
|
|
| DHQ_Fe-ADH |
cd07766 |
Dehydroquinate synthase-like (DHQ-like) and iron-containing alcohol dehydrogenases (Fe-ADH); ... |
95-337 |
6.28e-20 |
|
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: 91.66 E-value: 6.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 95 NIEDFLLLHRCTRDSVILALGGGVIGDLVGFVAATFMRGVRFVQIPTTLLAmvDSSVGGKTAIDTPHGKNL-IGAFWQPE 173
Cdd:cd07766 65 EVKNAVERARAAEADAVIAVGGGSTLDTAKAVAALLNRGIPFIIVPTTAST--DSEVSPKSVITDKGGKNKqVGPHYNPD 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 174 YIFIDAAFLETLPSREFSNGMAEVVKTAAIwneaefislesRSADIFAAIQTpsadyagrskqtrsiaqELLLSVIVGSi 253
Cdd:cd07766 143 VVFVDTDITKGLPPRQVASGGVDALAHAVE-----------LEKVVEAATLA-----------------GMGLFESPGL- 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 254 svkahivtideretglrnlvNFGHTIGHAIEAVLtpTILHGECVSVGMILEGEISRQMGILSQVGVGRLNRCLKAYNLPV 333
Cdd:cd07766 194 --------------------GLAHAIGHALTAFE--GIPHGEAVAVGLPYVLKVANDMNPEPEAAIEAVFKFLEDLGLPT 251
|
....
gi 170096704 334 TLAD 337
Cdd:cd07766 252 HLAD 255
|
|
| aroL |
PRK03731 |
shikimate kinase AroL; |
878-1021 |
8.37e-19 |
|
shikimate kinase AroL;
Pssm-ID: 235153 [Multi-domain] Cd Length: 171 Bit Score: 85.38 E-value: 8.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 878 IILIGMRGTGKTFVGNLAAATLSWTCLDADAYFETKHEMGVREFVHQKGWQAFRDAEFEVLRELIAEKSqghVISLGGGI 957
Cdd:PRK03731 5 LFLVGARGCGKTTVGMALAQALGYRFVDTDQWLQSTSNMTVAEIVEREGWAGFRARESAALEAVTAPST---VIATGGGI 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 170096704 958 VETPAARELLKEyaatKGPVVHIVRPIDEVIRYL--NSEAS-RPAYD-----EAIVDVFRRREPWFGECCSH 1021
Cdd:PRK03731 82 ILTEENRHFMRN----NGIVIYLCAPVSVLANRLeaNPEEDqRPTLTgkpisEEVAEVLAEREALYREVAHH 149
|
|
| PRK13947 |
PRK13947 |
shikimate kinase; Provisional |
878-1015 |
1.04e-14 |
|
shikimate kinase; Provisional
Pssm-ID: 184412 [Multi-domain] Cd Length: 171 Bit Score: 73.59 E-value: 1.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 878 IILIGMRGTGKTFVGNLAAATLSWTCLDADAYFETKHEMGVREFVHQKGWQAFRDAEFEVLRELiaEKSQGHVISLGGGI 957
Cdd:PRK13947 4 IVLIGFMGTGKTTVGKRVATTLSFGFIDTDKEIEKMTGMTVAEIFEKDGEVRFRSEEKLLVKKL--ARLKNLVIATGGGV 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 170096704 958 VETPAARELLKeyaatKGPVVHIVRPIDEVI-RYLNSEASRPAY-----DEAIVDVFRRREPWF 1015
Cdd:PRK13947 82 VLNPENVVQLR-----KNGVVICLKARPEVIlRRVGKKKSRPLLmvgdpEERIKELLKEREPFY 140
|
|
| PRK14021 |
PRK14021 |
bifunctional shikimate kinase/3-dehydroquinate synthase; Provisional |
879-1051 |
1.10e-14 |
|
bifunctional shikimate kinase/3-dehydroquinate synthase; Provisional
Pssm-ID: 184458 [Multi-domain] Cd Length: 542 Bit Score: 79.13 E-value: 1.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 879 ILIGMRGTGKTFVGNLAAATLSWTCLDADAYFETKHEMGVREFVHQKGWQAFRDAEFEVLRELIaeKSQGHVISLGGGIV 958
Cdd:PRK14021 10 VIIGMMGAGKTRVGKEVAQMMRLPFADADVEIEREIGMSIPSYFEEYGEPAFREVEADVVADML--EDFDGIFSLGGGAP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 959 ETPAARELLKEYAATKGPVVHIVRPIDEVIRYLNSEASRPAY----DEAIVDVFRRREPWFGECCSHDFFNRfGDLPYSS 1034
Cdd:PRK14021 88 MTPSTQHALASYIAHGGRVVYLDADPKEAMERANRGGGRPMLngdaNKRWKKLFKQRDPVFRQVANVHVHTR-GLTPQAA 166
|
170
....*....|....*..
gi 170096704 1035 PKATSREIARFFNHITG 1051
Cdd:PRK14021 167 AKKLIDMVAERTVHVTG 183
|
|
| PRK14027 |
PRK14027 |
quinate/shikimate dehydrogenase (NAD+); |
1314-1576 |
1.33e-14 |
|
quinate/shikimate dehydrogenase (NAD+);
Pssm-ID: 172521 [Multi-domain] Cd Length: 283 Bit Score: 76.23 E-value: 1.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 1314 LFGTPIAHSMSPTLHNTGFEILGLPHHYELLET------KEVAEEIKIAIGDSAFGGASVTIPYKLDVIPLLDKLSPAAE 1387
Cdd:PRK14027 9 LIGQGLDLSRTPAMHEAEGLAQGRATVYRRIDTlgsrasGQDLKTLLDAALYLGFNGLNITHPYKQAVLPLLDEVSEQAT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 1388 AIGAVNTIIPRTTGSgrmLVGDNTDWLGIKACITEQLSSKPIHAALVIGAGGTARAAIYALSALNVGDIYLYNRTTSKAY 1467
Cdd:PRK14027 89 QLGAVNTVVIDATGH---TTGHNTDVSGFGRGMEEGLPNAKLDSVVQVGAGGVGNAVAYALVTHGVQKLQVADLDTSRAQ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 1468 ELAHAFPHA----PVHVLEQLGqwpngavppcvIVSTVPASATTTEEETSGILL-PSKLFDYR--DGPAVVIDMAYKPAE 1540
Cdd:PRK14027 166 ALADVINNAvgreAVVGVDARG-----------IEDVIAAADGVVNATPMGMPAhPGTAFDVSclTKDHWVGDVVYMPIE 234
|
250 260 270
....*....|....*....|....*....|....*.
gi 170096704 1541 TPLLRLAKTAGdnWATVPGLEVLLEQGYVQFEMWTG 1576
Cdd:PRK14027 235 TELLKAARALG--CETLDGTRMAIHQAVDAFRLFTG 268
|
|
| PRK13951 |
PRK13951 |
bifunctional shikimate kinase AroK/3-dehydroquinate synthase AroB; |
878-1017 |
4.52e-10 |
|
bifunctional shikimate kinase AroK/3-dehydroquinate synthase AroB;
Pssm-ID: 172457 [Multi-domain] Cd Length: 488 Bit Score: 64.15 E-value: 4.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 878 IILIGMRGTGKTFVGNLAAATLSWTCLDADAYFETKHEMGVREFVHQKGWQAFRDAEFEVLRELIaeKSQGHVISLGGGI 957
Cdd:PRK13951 3 IFLVGMMGSGKSTIGKRVSEVLDLQFIDMDEEIERREGRSVRRIFEEDGEEYFRLKEKELLRELV--ERDNVVVATGGGV 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 170096704 958 VETPAARELLKeyaatKGPVVHIVRPIDEVIRYLNSEaSRPAY---DEAIVDVFRRREPWFGE 1017
Cdd:PRK13951 81 VIDPENRELLK-----KEKTLFLYAPPEVLMERVTTE-NRPLLregKERIREIWERRKQFYTE 137
|
|
| PRK13948 |
PRK13948 |
shikimate kinase; Provisional |
880-978 |
1.28e-08 |
|
shikimate kinase; Provisional
Pssm-ID: 184413 [Multi-domain] Cd Length: 182 Bit Score: 56.34 E-value: 1.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 880 LIGMRGTGKTFVGNLAAATLSWTCLDADAYFETKHEMGVREFVHQKGWQAFRDAEFEVLRELIaeKSQGHVISLGGGIVE 959
Cdd:PRK13948 15 LAGFMGTGKSRIGWELSRALMLHFIDTDRYIERVTGKSIPEIFRHLGEAYFRRCEAEVVRRLT--RLDYAVISLGGGTFM 92
|
90
....*....|....*....
gi 170096704 960 TPAARELLKEyaatKGPVV 978
Cdd:PRK13948 93 HEENRRKLLS----RGPVV 107
|
|
| PRK13946 |
PRK13946 |
shikimate kinase; Provisional |
877-969 |
2.31e-08 |
|
shikimate kinase; Provisional
Pssm-ID: 184411 [Multi-domain] Cd Length: 184 Bit Score: 55.70 E-value: 2.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 877 SIILIGMRGTGKTFVGNLAAATLSWTCLDADAYFETKHEMGVREFVHQKGWQAFRDAEFEVLRELIaeKSQGHVISLGGG 956
Cdd:PRK13946 12 TVVLVGLMGAGKSTVGRRLATMLGLPFLDADTEIERAARMTIAEIFAAYGEPEFRDLERRVIARLL--KGGPLVLATGGG 89
|
90
....*....|...
gi 170096704 957 IVETPAARELLKE 969
Cdd:PRK13946 90 AFMNEETRAAIAE 102
|
|
| PRK08154 |
PRK08154 |
anaerobic benzoate catabolism transcriptional regulator; Reviewed |
878-967 |
2.86e-08 |
|
anaerobic benzoate catabolism transcriptional regulator; Reviewed
Pssm-ID: 236167 [Multi-domain] Cd Length: 309 Bit Score: 57.27 E-value: 2.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 878 IILIGMRGTGKTFVGNLAAATLSWTCLDADAYFETKHEMGVREFVHQKGWQAFRDAEFEVLRELIAEKSQGhVISLGGGI 957
Cdd:PRK08154 136 IALIGLRGAGKSTLGRMLAARLGVPFVELNREIEREAGLSVSEIFALYGQEGYRRLERRALERLIAEHEEM-VLATGGGI 214
|
90
....*....|
gi 170096704 958 VETPAARELL 967
Cdd:PRK08154 215 VSEPATFDLL 224
|
|
| hemA |
PRK00045 |
glutamyl-tRNA reductase; Reviewed |
1432-1535 |
2.04e-07 |
|
glutamyl-tRNA reductase; Reviewed
Pssm-ID: 234592 [Multi-domain] Cd Length: 423 Bit Score: 55.19 E-value: 2.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 1432 ALVIGAGGTARAAIYALSALNVGDIYLYNRTTSKAYELAHAFPhAPVHVLEQLGQWPNGAvpPCVIVSTvpaSATT---T 1508
Cdd:PRK00045 185 VLVIGAGEMGELVAKHLAEKGVRKITVANRTLERAEELAEEFG-GEAIPLDELPEALAEA--DIVISST---GAPHpiiG 258
|
90 100
....*....|....*....|....*..
gi 170096704 1509 EEEtsgilLPSKLFDYRDGPAVVIDMA 1535
Cdd:PRK00045 259 KGM-----VERALKARRHRPLLLVDLA 280
|
|
| PRK13949 |
PRK13949 |
shikimate kinase; Provisional |
876-956 |
5.75e-07 |
|
shikimate kinase; Provisional
Pssm-ID: 140006 [Multi-domain] Cd Length: 169 Bit Score: 51.27 E-value: 5.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 876 ASIILIGMRGTGKTFVGNLAAATLSWTCLDADAYFETKHEMGVREFVHQKGWQAFRDAEFEVLRELiaEKSQGHVISLGG 955
Cdd:PRK13949 2 ARIFLVGYMGAGKTTLGKALARELGLSFIDLDFFIENRFHKTVGDIFAERGEAVFRELERNMLHEV--AEFEDVVISTGG 79
|
.
gi 170096704 956 G 956
Cdd:PRK13949 80 G 80
|
|
| Fe-ADH_2 |
pfam13685 |
Iron-containing alcohol dehydrogenase; |
31-297 |
7.64e-07 |
|
Iron-containing alcohol dehydrogenase;
Pssm-ID: 404557 [Multi-domain] Cd Length: 251 Bit Score: 52.30 E-value: 7.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 31 VLSNLPSSTYVLVTDTNVanfhltafEKEFEQRIS-SLPTSSTKPRFLSLVIPPGETSksregkaNIEDFLLLHRCTRDS 109
Cdd:pfam13685 13 YLAELGFRRVALVADANT--------YAAAGRKVAeSLKRAGIEVETRLEVAGNADME-------TAEKLVGALRERDAD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 110 VILALGGGVIGDLVGFVAatFMRGVRFVQIPTTLlamvdsSVGGKTA----IDTPHGKNLIGAFWqPEYIFIDAAFLETL 185
Cdd:pfam13685 78 AVVGVGGGTVIDLAKYAA--FKLGKPFISVPTAA------SNDGFASpgasLTVDGKKRSIPAAA-PFGVIADTDVIAAA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 186 PSREFSNGMAEVV--KTAAIWNEAEFISLESRSADIF-AAIQTPSADYAGRSKQTRSIAQELLLSVIVG--SISVKAHiv 260
Cdd:pfam13685 149 PRRLLASGVGDLLakITAVADWELAHAEEVAAPLALLsAAMVMNFADRPLRDPGDIEALAELLSALAMGgaGSSRPAS-- 226
|
250 260 270
....*....|....*....|....*....|....*....
gi 170096704 261 tideretglrnlvnfG--HTIGHAIEAVLTPTILHGECV 297
Cdd:pfam13685 227 ---------------GseHLISHALDMIAPKQALHGEQV 250
|
|
| GldA |
COG0371 |
Glycerol dehydrogenase or related enzyme, iron-containing ADH family [Energy production and ... |
110-351 |
9.18e-07 |
|
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: 52.86 E-value: 9.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 110 VILALGGGVIGDLVGFVAatFMRGVRFVQIPTTllAMVDSSVGGKTAIDTPHGKNLIGAFW--QPEYIFIDAAFLETLPS 187
Cdd:COG0371 85 VIIGVGGGKALDTAKAVA--YRLGLPVVSVPTI--ASTDAPASPLSVIYTEDGAFDGYSFLakNPDLVLVDTDIIAKAPV 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 188 REFSNGMAEVVKTaaiWNEAEFISLESRSAdifaaIQTPSADYAgrskqtRSIAQ---ELLLSVIVGSI-SVKAHIVTid 263
Cdd:COG0371 161 RLLAAGIGDALAK---WYEARDWSLAHRDL-----AGEYYTEAA------VALARlcaETLLEYGEAAIkAVEAGVVT-- 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 264 erETGLR----NLV------NFG---------HTIGHAIEAVL-TPTILHGECVSVG----MILEGEISRQMGILsqvgv 319
Cdd:COG0371 225 --PALERvveaNLLlsglamGIGssrpgsgaaHAIHNGLTALPeTHHALHGEKVAFGtlvqLVLEGRPEEIEELL----- 297
|
250 260 270
....*....|....*....|....*....|..
gi 170096704 320 grlnRCLKAYNLPVTLADPRIASLPAAKLLTV 351
Cdd:COG0371 298 ----DFLRSVGLPTTLADLGLDDETEEELLTV 325
|
|
| SDH_C |
pfam18317 |
Shikimate 5'-dehydrogenase C-terminal domain; This domain is found in the C-terminal region of ... |
1559-1586 |
2.42e-06 |
|
Shikimate 5'-dehydrogenase C-terminal domain; This domain is found in the C-terminal region of Shikimate 5'-dehydrogenase (SDH) present in Methanocaldococcus jannaschii. SDH catalyzes the NADPH-dependent reduction of 3-dehydroshikimate to shikimate in the shikimate pathway. The domain is found just after the C-terminal domain (pfam01488) which is responsible for NADP binding.
Pssm-ID: 436404 [Multi-domain] Cd Length: 31 Bit Score: 45.49 E-value: 2.42e-06
10 20
....*....|....*....|....*...
gi 170096704 1559 GLEVLLEQGYVQFEMWTGRRCPKELVAK 1586
Cdd:pfam18317 1 GLGMLVEQGAEQFELWTGREPPVEVMRE 28
|
|
| PLN02199 |
PLN02199 |
shikimate kinase |
877-961 |
2.78e-06 |
|
shikimate kinase
Pssm-ID: 177850 [Multi-domain] Cd Length: 303 Bit Score: 51.24 E-value: 2.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 877 SIILIGMRGTGKTFVGNLAAATLSWTCLDADAYFETKHE-MGVREFVHQKGWQAFRDAEFEVLRELIAEKSQghVISLGG 955
Cdd:PLN02199 104 SMYLVGMMGSGKTTVGKLMSKVLGYTFFDCDTLIEQAMNgTSVAEIFVHHGENFFRGKETDALKKLSSRYQV--VVSTGG 181
|
....*.
gi 170096704 956 GIVETP 961
Cdd:PLN02199 182 GAVIRP 187
|
|
| HemA |
COG0373 |
Glutamyl-tRNA reductase [Coenzyme transport and metabolism]; Glutamyl-tRNA reductase is part ... |
1420-1535 |
3.78e-06 |
|
Glutamyl-tRNA reductase [Coenzyme transport and metabolism]; Glutamyl-tRNA reductase is part of the Pathway/BioSystem: Heme biosynthesis
Pssm-ID: 440142 [Multi-domain] Cd Length: 425 Bit Score: 51.27 E-value: 3.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 1420 ITEQLSSKPIhaaLVIGAGGTARAAIYALSALNVGDIYLYNRTTSKAYELAHAFPHAPVHvLEQLGQWPNGAvpPCVIVS 1499
Cdd:COG0373 176 IFGDLSGKTV---LVIGAGEMGELAARHLAAKGVKRITVANRTLERAEELAEEFGGEAVP-LEELPEALAEA--DIVISS 249
|
90 100 110
....*....|....*....|....*....|....*....
gi 170096704 1500 TvpaSATT---TEEetsgiLLPSKLFDYRDGPAVVIDMA 1535
Cdd:COG0373 250 T---GAPHpviTKE-----MVERALKKRRHRPLFLIDLA 280
|
|
| aroK |
PRK05057 |
shikimate kinase AroK; |
878-998 |
7.56e-06 |
|
shikimate kinase AroK;
Pssm-ID: 235335 [Multi-domain] Cd Length: 172 Bit Score: 47.79 E-value: 7.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 878 IILIGMRGTGKTFVGNLAAATLSWTCLDADAYFETKHEMGVREFVHQKGWQAFRDAEFEVLRELiAEKsQGHVISLGGGI 957
Cdd:PRK05057 7 IFLVGPMGAGKSTIGRQLAQQLNMEFYDSDQEIEKRTGADIGWVFDVEGEEGFRDREEKVINEL-TEK-QGIVLATGGGS 84
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 170096704 958 VETPAARELLkeyaATKGPVVHIVRPIDEVIRYLNSEASRP 998
Cdd:PRK05057 85 VKSRETRNRL----SARGVVVYLETTIEKQLARTQRDKKRP 121
|
|
| NAD_bind_Glutamyl_tRNA_reduct |
cd05213 |
NADP-binding domain of glutamyl-tRNA reductase; Glutamyl-tRNA reductase catalyzes the ... |
1432-1535 |
3.89e-04 |
|
NADP-binding domain of glutamyl-tRNA reductase; Glutamyl-tRNA reductase catalyzes the conversion of glutamyl-tRNA to glutamate-1-semialdehyde, initiating the synthesis of tetrapyrrole. Whereas tRNAs are generally associated with peptide bond formation in protein translation, here the tRNA activates glutamate in the initiation of tetrapyrrole biosynthesis in archaea, plants and many bacteria. In the first step, activated glutamate is reduced to glutamate-1-semi-aldehyde via the NADPH dependent glutamyl-tRNA reductase. Glutamyl-tRNA reductase forms a V-shaped dimer. Each monomer has 3 domains: an N-terminal catalytic domain, a classic nucleotide binding domain, and a C-terminal dimerization domain. Although the representative structure 1GPJ lacks a bound NADPH, a theoretical binding pocket has been described. (PMID 11172694). Amino acid dehydrogenase (DH)-like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.
Pssm-ID: 133452 [Multi-domain] Cd Length: 311 Bit Score: 44.56 E-value: 3.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 1432 ALVIGAGGTARAAIYALSALNVGDIYLYNRTTSKAYELAHAFPHAPVHVLEQLGQWPNGAVppcVIVSTvpaSATTTEEE 1511
Cdd:cd05213 181 VLVIGAGEMGELAAKHLAAKGVAEITIANRTYERAEELAKELGGNAVPLDELLELLNEADV---VISAT---GAPHYAKI 254
|
90 100
....*....|....*....|....
gi 170096704 1512 TSGILLPSklfdyRDGPAVVIDMA 1535
Cdd:cd05213 255 VERAMKKR-----SGKPRLIVDLA 273
|
|
| Shikimate_DH |
pfam01488 |
Shikimate / quinate 5-dehydrogenase; This family contains both shikimate and quinate ... |
1432-1535 |
5.51e-04 |
|
Shikimate / quinate 5-dehydrogenase; This family contains both shikimate and quinate dehydrogenases. Shikimate 5-dehydrogenase catalyzes the conversion of shikimate to 5-dehydroshikimate. This reaction is part of the shikimate pathway which is involved in the biosynthesis of aromatic amino acids. Quinate 5-dehydrogenase catalyzes the conversion of quinate to 5-dehydroquinate. This reaction is part of the quinate pathway where quinic acid is exploited as a source of carbon in prokaryotes and microbial eukaryotes. Both the shikimate and quinate pathways share two common pathway metabolites 3-dehydroquinate and dehydroshikimate.
Pssm-ID: 460229 [Multi-domain] Cd Length: 136 Bit Score: 41.79 E-value: 5.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 1432 ALVIGAGGTARAAIYALSALNVGDIYLYNRTTSKAYELAHAFPHAPVHVLEQLGQWPNGAvpPCVIVSTvpaSATT---T 1508
Cdd:pfam01488 15 VLLIGAGEMGELVAKHLLAKGAKEVTIANRTIERAQELAEKFGGVEALPLDDLKEYLAEA--DIVISAT---SSPTpiiT 89
|
90 100
....*....|....*....|....*..
gi 170096704 1509 EEETSGILLPsklfdyRDGPAVVIDMA 1535
Cdd:pfam01488 90 KEMVERALKP------RKKPLLFVDIA 110
|
|
| GntK |
COG3265 |
Gluconate kinase [Carbohydrate transport and metabolism]; Gluconate kinase is part of the ... |
877-909 |
1.62e-03 |
|
Gluconate kinase [Carbohydrate transport and metabolism]; Gluconate kinase is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway
Pssm-ID: 442496 [Multi-domain] Cd Length: 164 Bit Score: 40.88 E-value: 1.62e-03
10 20 30
....*....|....*....|....*....|...
gi 170096704 877 SIILIGMRGTGKTFVGNLAAATLSWTCLDADAY 909
Cdd:COG3265 3 VIVVMGVSGSGKSTVGQALAERLGWPFIDGDDF 35
|
|
| COG0645 |
COG0645 |
Predicted kinase, contains AAA domain [General function prediction only]; |
878-1014 |
3.10e-03 |
|
Predicted kinase, contains AAA domain [General function prediction only];
Pssm-ID: 440410 [Multi-domain] Cd Length: 164 Bit Score: 40.28 E-value: 3.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 878 IILIGMRGTGKTFVGNLAAATLSWTCLDADAyfETKHEMGvREFVHQKGWQAFRDAEFEVLRELIAEksqghVISLGGGI 957
Cdd:COG0645 2 ILVCGLPGSGKSTLARALAERLGAVRLRSDV--VRKRLFG-AGLAPLERSPEATARTYARLLALARE-----LLAAGRSV 73
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 170096704 958 V-----ETPAARELLKEYAATKGPVVHIVR---PIDEVIRYLNSEASRPAYDEAIVDVFRRR----EPW 1014
Cdd:COG0645 74 IldatfLRRAQREAFRALAEEAGAPFVLIWldaPEEVLRERLEARNAEGGDSDATWEVLERQlafeEPL 142
|
|
| hemA |
TIGR01035 |
glutamyl-tRNA reductase; This enzyme, together with glutamate-1-semialdehyde-2,1-aminomutase ... |
1420-1500 |
3.49e-03 |
|
glutamyl-tRNA reductase; This enzyme, together with glutamate-1-semialdehyde-2,1-aminomutase (TIGR00713), leads to the production of delta-amino-levulinic acid from Glu-tRNA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]
Pssm-ID: 273407 [Multi-domain] Cd Length: 417 Bit Score: 41.60 E-value: 3.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 1420 ITEQLSSKpihAALVIGAGGTARAAIYALSALNVGDIYLYNRTTSKAYELAHAFPHAPVHvLEQLgqwpNGAVPPC--VI 1497
Cdd:TIGR01035 174 IFGSLKGK---KALLIGAGEMGELVAKHLLRKGVGKILIANRTYERAEDLAKELGGEAVK-FEDL----EEYLAEAdiVI 245
|
...
gi 170096704 1498 VST 1500
Cdd:TIGR01035 246 SST 248
|
|
| PRK00625 |
PRK00625 |
shikimate kinase; Provisional |
878-991 |
9.40e-03 |
|
shikimate kinase; Provisional
Pssm-ID: 134335 [Multi-domain] Cd Length: 173 Bit Score: 38.97 E-value: 9.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170096704 878 IILIGMRGTGKTFVGNLAAATLSWTCLDAD----AYFETKHEMGVREFVHQKGWQAFRDAEFEVLRELIAEKSqghVISL 953
Cdd:PRK00625 3 IFLCGLPTVGKTSFGKALAKFLSLPFFDTDdlivSNYHGALYSSPKEIYQAYGEEGFCREEFLALTSLPVIPS---IVAL 79
|
90 100 110
....*....|....*....|....*....|....*...
gi 170096704 954 GGGIVETPAARELLKeyaaTKGPVVHIVRPIDEVIRYL 991
Cdd:PRK00625 80 GGGTLMIEPSYAHIR----NRGLLVLLSLPIATIYQRL 113
|
|
| |
