|
Name |
Accession |
Description |
Interval |
E-value |
| EPSP_synthase |
cd01556 |
EPSP synthase domain. 3-phosphoshikimate 1-carboxyvinyltransferase ... |
406-834 |
1.41e-151 |
|
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: 468.19 E-value: 1.41e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 406 APPGSKSISNRALVLAALGSGTVRVKNLLHSDDTEVMLNALERLGAatfAWEDEGEVLVVNGNGGKMQASPTELYLGNAG 485
Cdd:cd01556 6 TVPGSKSISHRALLLAALAEGESRIENLLDSDDTLATLEALRALGA---KIEEEGGTVEIVGGGGLGLPPEAVLDCGNSG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 486 TASRFLTSVATLSGKGSVdyniLTGNNRMKQRPIGDLVDALTINGAQVEYLEKAGSLPLKIaaSGGFKGGRINLAAKVSS 565
Cdd:cd01556 83 TTMRLLTGLLALQGGDSV----LTGDESLRKRPMGRLVDALRQLGAEIEGREGGGYPPLIG--GGGLKGGEVEIPGAVSS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 566 QYVSSLLMCAPYAKEPVTLKLvgGRPISLSYIEMTTAMMRSFGIDVQKSTTEEWTYHiPQGSYnNPPEYVIESDASSATY 645
Cdd:cd01556 157 QFKSALLLAAPLAEGPTTIII--GELESKPYIDHTERMLRAFGAEVEVDGYRTITVK-GGQKY-KGPEYTVEGDASSAAF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 646 PLAIAAVTGTTCTVPNIGSASlqGDARFaVEVLRPMGCKVEQTATsTTVTGPADGVLRPLpNVDMEPMTDAFLGASVLAA 725
Cdd:cd01556 233 FLAAAAITGSEIVIKNVGLNS--GDTGI-IDVLKEMGADIEIGNE-DTVVVESGGKLKGI-DIDGNDIPDEAPTLAVLAA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 726 IAQGEggnhaTRIYGIANQRVKECNRIEAMRVELAKFGVVCREHPDGLEIDGidrSTLRHPAGGVFCYDDHRVAFSFSIL 805
Cdd:cd01556 308 FAEGP-----TRIRNAAELRVKESDRIAAMATELRKLGADVEETEDGLIIEG---GPLKGAGVEVYTYGDHRIAMSFAIA 379
|
410 420
....*....|....*....|....*....
gi 327507643 806 SLVAPTPTLILEKECVGKTWPTYWDALKQ 834
Cdd:cd01556 380 GLVAEGGVTIEDPECVAKSFPNFFEDLES 408
|
|
| aroA |
TIGR01356 |
3-phosphoshikimate 1-carboxyvinyltransferase; This model represents ... |
406-834 |
2.02e-138 |
|
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: 432.86 E-value: 2.02e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 406 APPGSKSISNRALVLAALGSGTVRVKNLLHSDDTEVMLNALERLGAATfawEDEGEVLVVNGNGGKMQASptELYLGNAG 485
Cdd:TIGR01356 4 RAPGSKSITHRALILAALAEGETRVRNLLRSEDTLATLDALRALGAKI---EDGGEVAVIEGVGGKEPQA--ELDLGNSG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 486 TASRFLTSVATLSGKGSVdyniLTGNNRMKQRPIGDLVDALTINGAQVEYLEKAGSLPLKIaaSGGFKGGRINLAAKVSS 565
Cdd:TIGR01356 79 TTARLLTGVLALADGEVV----LTGDESLRKRPMGRLVDALRQLGAEISSLEGGGSLPLTI--SGPLPGGIVYISGSASS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 566 QYVSSLLMCAPyAKEPVTLKLVGGRPISLSYIEMTTAMMRSFGIDVQKSTTEewTYHIPQGSYNNPPEYVIESDASSATY 645
Cdd:TIGR01356 153 QYKSALLLAAP-ALQAVGITIVGEPLKSRPYIEITLDLLGSFGVEVERSDGR--KIVVPGGQKYGPQGYDVPGDYSSAAF 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 646 PLAIAAVTGTTCTVPNIGSASLQGDARFaVEVLRPMGCKVEQTATSTTVTGPADgvLRPLpNVDMEPMTDAFLGASVLAA 725
Cdd:TIGR01356 230 FLAAAAITGGRVTLENLGINPTQGDKAI-IIVLEEMGADIEVEEDDLIVEGASG--LKGI-KIDMDDMIDELPTLAVLAA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 726 IAQGEggnhaTRIYGIANQRVKECNRIEAMRVELAKFGVVCREHPDGLEIDGidRSTLRhpAGGVFCYDDHRVAFSFSIL 805
Cdd:TIGR01356 306 FAEGV-----TRITGAEELRVKESDRIAAIAEELRKLGVDVEEFEDGLYIRG--KKELK--GAVVDTFGDHRIAMAFAVA 376
|
410 420
....*....|....*....|....*....
gi 327507643 806 SLVAPTPTLILEKECVGKTWPTYWDALKQ 834
Cdd:TIGR01356 377 GLVAEGEVLIDDPECVAKSFPSFFDVLER 405
|
|
| DHQS |
cd08195 |
Dehydroquinate synthase (DHQS) catalyzes the conversion of DAHP to DHQ in shikimate pathway ... |
25-387 |
3.00e-138 |
|
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: 429.94 E-value: 3.00e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 25 YIVQDLLTNLPS-------TTYVLVTDTNLGSIYREKFAKIFNEAAAalspapRLLTKEIPPGENSKSRQGKADIEDWML 97
Cdd:cd08195 5 LIGSGLLDKLGEllelkkgSKVVIVTDENVAKLYGELLLKSLEAAGF------KVEVIVIPAGEKSKSLETVERIYDFLL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 98 QQTCGRDTVIIALGGGVIGDLLGFVAATYMRGIRFVQVPTTLLAMVDSSIGGKTAIDTPLGKNLIGAIWQPHRIYIDIDF 177
Cdd:cd08195 79 EAGLDRDSLLIALGGGVVGDLAGFVASTYMRGIPFIQVPTTLLAQVDSSIGGKTGINLPGGKNLIGAFYQPKAVLIDPDF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 178 IDTLPEREFINGMAEVIKTAAISDEKEFAALEQHADAILKAarskpgkgRFDLVRQVVKdrivASARHKAFVVTADEREG 257
Cdd:cd08195 159 LKTLPEREFRSGLAEVIKYGLIADKELFEFLEKNLDKILAR--------DPEALEEIIA----RSVEIKADIVEEDEREK 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 258 GLRNLLNLGHSIGHAIEAILSPQVLHGECVAIGMVKELDLARYLGILKPVAVSRMVKCLSKYGLPTSLKDsrvrkhtagk 337
Cdd:cd08195 227 GLRAILNFGHTFGHAIESASGYKLLHGEAVAIGMVAAARLSVKLGLLSEEDLERIRALLKKLGLPTSIKD---------- 296
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 327507643 338 hCSLEQMMANMALDKKNDGPRKKVVLLSAIGQTYepKASVVSNEDIRAVL 387
Cdd:cd08195 297 -LDPEELLEAMKRDKKNRGGKIRFVLLKGIGKAV--IVDDVSEEEIREAL 343
|
|
| AroA |
COG0128 |
5-enolpyruvylshikimate-3-phosphate synthase [Amino acid transport and metabolism]; ... |
408-834 |
1.67e-135 |
|
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: 425.66 E-value: 1.67e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 408 PGSKSISNRALVLAALGSGTVRVKNLLHSDDTEVMLNALERLGaATFAWEDEGEVlVVNGNGGKMQASPTELYLGNAGTA 487
Cdd:COG0128 19 PGSKSISHRALLLAALAEGESTIRNLLESDDTLATLEALRALG-AEIEELDGGTL-RVTGVGGGLKEPDAVLDCGNSGTT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 488 SRFLTSVATLSGKGSVdyniLTGNNRMKQRPIGDLVDALTINGAQVEYLEKaGSLPLKIAAsGGFKGGRINLAAKVSSQY 567
Cdd:COG0128 97 MRLLTGLLALQPGEVV----LTGDESLRKRPMGRLLDPLRQLGARIESRGG-GYLPLTIRG-GPLKGGEYEIPGSASSQF 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 568 VSSLLMCAPYAKEPVTLKlVGGRPISLSYIEMTTAMMRSFGIDVQKSTTEEWTYHIPQgSYnNPPEYVIESDASSATYPL 647
Cdd:COG0128 171 KSALLLAGPLAEGGLEIT-VTGELESKPYRDHTERMLRAFGVEVEVEGYRRFTVPGGQ-RY-RPGDYTVPGDISSAAFFL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 648 AIAAVTGTTCTVPNIGSASLQGDARFaVEVLRPMGCKVEQTATSTTVTGpadGVLRPLpNVDMEPMTDAFLGASVLAAIA 727
Cdd:COG0128 248 AAAAITGSEVTVEGVGLNSTQGDTGI-LDILKEMGADIEIENDGITVRG---SPLKGI-DIDLSDIPDEAPTLAVLAAFA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 728 QGEggnhaTRIYGIANQRVKECNRIEAMRVELAKFGVVCREHPDGLEIDGidRSTLRhpaGGVF-CYDDHRVAFSFSILS 806
Cdd:COG0128 323 EGT-----TRIRGAAELRVKESDRIAAMATELRKLGADVEETEDGLIIEG--GPKLK---GAEVdSYGDHRIAMAFAVAG 392
|
410 420
....*....|....*....|....*...
gi 327507643 807 LVAPTPTLILEKECVGKTWPTYWDALKQ 834
Cdd:COG0128 393 LRAEGPVTIDDAECVAKSFPDFFELLES 420
|
|
| AroB |
COG0337 |
3-dehydroquinate synthetase [Amino acid transport and metabolism]; 3-dehydroquinate synthetase ... |
25-387 |
1.07e-128 |
|
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: 404.47 E-value: 1.07e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 25 YIVQDLLTNLPST--------TYVLVTDTNLGSIYREKFAKIFNEAAAALSPAprlltkEIPPGENSKSRQGKADIEDWM 96
Cdd:COG0337 16 RIGRGLLDELGELlaellkgrRVLVVTDENVAPLYGERLRAALEAAGFEVHLL------VLPDGEASKTLETLERILDAL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 97 LQQTCGRDTVIIALGGGVIGDLLGFVAATYMRGIRFVQVPTTLLAMVDSSIGGKTAIDTPLGKNLIGAIWQPHRIYIDID 176
Cdd:COG0337 90 LEAGLDRDDLVVALGGGVVGDLAGFAAATYLRGVPFIQVPTTLLAQVDSSVGGKTGVNHPGGKNLIGAFHQPRAVLIDLD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 177 FIDTLPEREFINGMAEVIKTAAISDEKEFAALEQHADAILkaarskpgKGRFDLVRQVVKDrivaSARHKAFVVTADERE 256
Cdd:COG0337 170 FLKTLPERELRAGLAEVIKYGLIADAEFFEWLEENADALL--------ARDPEALEEAIAR----SCEIKAEVVAADERE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 257 GGLRNLLNLGHSIGHAIEAILSPQVLHGECVAIGMVKELDLARYLGILKPVAVSRMVKCLSKYGLPTSLKDsrvrkhtag 336
Cdd:COG0337 238 SGLRALLNFGHTFGHAIEAATGYRLLHGEAVAIGMVFAARLSARLGLLSEEDVERIRALLEALGLPTRLPA--------- 308
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 327507643 337 khCSLEQMMANMALDKKNDGPRKKVVLLSAIGQTYEpkASVVSNEDIRAVL 387
Cdd:COG0337 309 --LDPEALLAAMKRDKKVRGGKLRFVLLRGIGKAVI--VDDVDEELLRAAL 355
|
|
| PRK02427 |
PRK02427 |
3-phosphoshikimate 1-carboxyvinyltransferase; Provisional |
389-834 |
2.56e-127 |
|
3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
Pssm-ID: 235037 [Multi-domain] Cd Length: 435 Bit Score: 403.75 E-value: 2.56e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 389 PSIEVIPGVPKDLNVVCAPPGSKSISNRALVLAALGSGTVRVKNLLHSDDTEVMLNALERLGAatfawEDEGEVLVVNGN 468
Cdd:PRK02427 1 MMMMLLIIPPSPLSGTVRVPGSKSISHRALLLAALAEGETTITNLLRSEDTLATLNALRALGV-----EIEDDEVVVEGV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 469 GGKMQASPTE-LYLGNAGTASRFLTSVATLSGKGSVdyniLTGNNRMKQRPIGDLVDALTINGAQVEYlEKAGSLPLKIa 547
Cdd:PRK02427 76 GGGGLKEPEDvLDCGNSGTTMRLLTGLLALQPGEVV----LTGDESLRKRPMGRLLDPLRQMGAKIEG-RDEGYLPLTI- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 548 aSGGFKGGRINLAAKVSSQYVSSLLMCAPYAKEPVTLKLVGGRPISLSYIEMTTAMMRSFGIDVQKSTTEEW-TYHIPQG 626
Cdd:PRK02427 150 -RGGKKGGPIEYDGPVSSQFVKSLLLLAPLFAEGDTETTVIEPLPSRPHTEITLRMLRAFGVEVENVEGWGYrRIVIKGG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 627 SYNNPPEYVIESDASSATYPLAIAAVT-GTTCTVPNIGSASLQGDARFaVEVLRPMGCKVEQTATSTTVTGPAD-----G 700
Cdd:PRK02427 229 QRLRGQDITVPGDPSSAAFFLAAAAITgGSEVTITNVGLNSTQGGKAI-IDVLEKMGADIEIENEREGGEPVGDirvrsS 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 701 VLRPLpNVDMEPMTDAFLGASVLAAIAQGEggnhaTRIYGIANQRVKECNRIEAMRVELAKFGVVCREHPDGLEIDGidr 780
Cdd:PRK02427 308 ELKGI-DIDIPDIIDEAPTLAVLAAFAEGT-----TVIRNAEELRVKETDRIAAMATELRKLGAEVEETEDGLIITG--- 378
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 327507643 781 stlRHPAGGVFCYDDHRVAFSFSILSLVAPTPTLILEKECVGKTWPTYWDALKQ 834
Cdd:PRK02427 379 ---GPLAGVVDSYGDHRIAMAFAIAGLAAEGPVTIDDPECVAKSFPDFFEDLAS 429
|
|
| DHQ_synthase |
pfam01761 |
3-dehydroquinate synthase; The 3-dehydroquinate synthase EC:4.6.1.3 domain is present in ... |
77-354 |
8.85e-124 |
|
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: 387.24 E-value: 8.85e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 77 IPPGENSKSRQGKADIEDWMLQQTCGRDTVIIALGGGVIGDLLGFVAATYMRGIRFVQVPTTLLAMVDSSIGGKTAIDTP 156
Cdd:pfam01761 4 IPDGEKSKTLETLERIYDALLEAGLDRSSLLIALGGGVIGDLAGFVAATYMRGIRFIQVPTTLLAQVDSSVGGKTGINHP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 157 LGKNLIGAIWQPHRIYIDIDFIDTLPEREFINGMAEVIKTAAISDEKEFAALEQHADAILkaarskpgkgrfDLVRQVVK 236
Cdd:pfam01761 84 LGKNLIGAFYQPKAVLIDLDFLKTLPDREFRAGLAEVIKYGLIADAEFFEWLEENAEALL------------NLDPDALE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 237 DRIVASARHKAFVVTADEREGGLRNLLNLGHSIGHAIEAILSP-QVLHGECVAIGMVKELDLARYLGILKPVAVSRMVKC 315
Cdd:pfam01761 152 EAIARSCEVKADVVAQDEKESGLRALLNLGHTFGHAIEALSGYgALLHGEAVAIGMVLAARLSERLGLLDEADVERIRAL 231
|
250 260 270
....*....|....*....|....*....|....*....
gi 327507643 316 LSKYGLPTSLKDSrvrkhtagkhcSLEQMMANMALDKKN 354
Cdd:pfam01761 232 LKKYGLPTSLPDL-----------DVEQLLAAMARDKKV 259
|
|
| EPSP_synthase |
pfam00275 |
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase); |
398-832 |
5.05e-114 |
|
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);
Pssm-ID: 395213 Cd Length: 415 Bit Score: 366.62 E-value: 5.05e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 398 PKDLNVVCAPPGSKSISNRALVLAALGSGTVRVKNLLHSDDTEVMLNALERLGAATFAWEDEGEVLVVNGNGGKMQASP- 476
Cdd:pfam00275 3 GSRLSGEVKIPGSKSNSHRALILAALAAGESTITNLLDSDDTLTMLEALRALGAEIIKLDDEKSVVIVEGLGGSFEAPEd 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 477 TELYLGNAGTASRFLTSVATLSGKGSVdyniLTGNNRMKQRPIGDLVDALTINGAQVEYLEKAGSLPLKIAasgGFKGGR 556
Cdd:pfam00275 83 LVLDMGNSGTALRPLTGRLALQSGEVV----LPGDCSIGKRPMDRLLDALRQLGAEIEGREGYNYAPLKVR---GLRLGG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 557 INLAAKVSSQYVSSLLMCAP-YAKEPVTLKlvggRPISLSYIEMTTAMMRSFGIDVQKSTTEE-WTYHIPQGSYnnPPEY 634
Cdd:pfam00275 156 IHIDGDVSSQFVTSLLMLAAlLAEGTTTIE----NLASEPYIDDTENMLKKFGAKIEGSGTELsITVKGGEKLP--GQEY 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 635 VIESDASSATYPLAIAAVTGTTCTVPNIGSASLQGDaRFAVEVLRPMGCKVEQTATSTTVTGPadGVLRPLPnVDMEPMT 714
Cdd:pfam00275 230 RVEGDRSSAAYFLVAAAITGGTVTVENVGINSLQGD-EALLEILEKMGAEITQEEDADIVVGP--PGLRGKA-VDIRTAP 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 715 DAFLGASVLAAIAQGEggnhaTRIYGIANQRVKECNRIEAMRVELAKFGVVCREHPDGLEIDGIDrSTLRHpaGGVFCYD 794
Cdd:pfam00275 306 DPAPTTAVLAAFAEGT-----TRIEGISELRVKETDRLFAMATELRRLGADVEELPDGLIIIPAV-KELKG--AEVDSYG 377
|
410 420 430
....*....|....*....|....*....|....*...
gi 327507643 795 DHRVAFSFSILSLVAPTPTLILEKECVGKTWPTYWDAL 832
Cdd:pfam00275 378 DHRIAMALALAGLVAEGETIIDDIECTDRSFPDFEEKL 415
|
|
| aroB |
TIGR01357 |
3-dehydroquinate synthase; This model represents 3-dehydroquinate synthase, the enzyme ... |
40-387 |
2.33e-112 |
|
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: 359.25 E-value: 2.33e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 40 VLVTDTNLGSIYREKFAkifnEAAAALSPAPRLLTkeIPPGENSKSRQGKADIEDWMLQQTCGRDTVIIALGGGVIGDLL 119
Cdd:TIGR01357 24 VIITDETVADLYGDKLL----EALQALGYNVLKLT--VPDGEESKSLETVQRLYDQLLEAGLDRSSTIIALGGGVVGDLA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 120 GFVAATYMRGIRFVQVPTTLLAMVDSSIGGKTAIDTPLGKNLIGAIWQPHRIYIDIDFIDTLPEREFINGMAEVIKTAAI 199
Cdd:TIGR01357 98 GFVAATYMRGIRFIQVPTTLLAMVDSSVGGKTGINFPGGKNLIGTFYQPKAVLIDPDFLKTLPDRELRSGMAEVIKHGLI 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 200 SDEKEFAALEQHADAILkaaRSKPGKGRFDLVRQVVKDrivasarhKAFVVTADEREGGLRNLLNLGHSIGHAIEAILSP 279
Cdd:TIGR01357 178 ADAELFDELESNDKLRL---NLQELEHLEELIKRSIEV--------KASIVAEDEKESGLRAILNFGHTIGHAIEAEAGY 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 280 -QVLHGECVAIGMVKELDLARYLGILKPVAVSRMVKCLSKYGLPTSLKdsrvrkhtagKHCSLEQMMANMALDKKNDGPR 358
Cdd:TIGR01357 247 gKIPHGEAVAIGMVCEAKLSERLGLLPAELIERLVQLLKRYGLPTDLP----------KDLDVDELLNAMLNDKKNSGGK 316
|
330 340
....*....|....*....|....*....
gi 327507643 359 KKVVLLSAIGQTYEpkASVVSNEDIRAVL 387
Cdd:TIGR01357 317 IRFVLLEEIGKAAL--AREVPDEMVLELL 343
|
|
| Shik-DH-AROM |
TIGR01809 |
shikimate-5-dehydrogenase, fungal AROM-type; This model represents a clade of ... |
1282-1566 |
1.25e-75 |
|
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: 252.91 E-value: 1.25e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 1282 GEIPAKKFAIFGKPVSVSRSPAMHNTLFEQNGLPYVYTRLETDQAQDVKEFIRS--PDFGGASATIPLKLDIIPLIDEVL 1359
Cdd:TIGR01809 1 GNKGPKKAFIIGKPIAHSRSPHLHNAGYEILGLPDKTYEFETCSAEELKEVLSGfgPQFGGASVTIPLKFAILRFADEHT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 1360 NEAEIIGAVNTIIPVegkdGSTRLIGRNTDWSGIVRCLREAGAHSNEGESSALVIGGGGTARAAIYALHNMGFSTVYVLG 1439
Cdd:TIGR01809 81 DRASLIGSVNTLLRT----QNGIWKGDNTDWDGIAGALANIGKFEPLAGFRGLVIGAGGTSRAAVYALASLGVTDITVIN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 1440 RSPEKIQNMASTFPTGFDIRVLENASDIENIP---RVAVGTIPGDRPIEANMREILCTIFERSGRAADGksaaVLLEMAY 1516
Cdd:TIGR01809 157 RNPDKLSRLVDLGVQVGVITRLEGDSGGLAIEkaaEVLVSTVPADVPADYVDLFATVPFLLLKRKSSEG----IFLDAAY 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 327507643 1517 KPSVTPLMQLASDSGWTTIPGLEALVGQGVYQFEYWTGITPVYEVARNAV 1566
Cdd:TIGR01809 233 DPWPTPLVAIVSAAGWRVISGLQMLLHQGFAQFEQWTGMPAPREAMACAL 282
|
|
| PLN02834 |
PLN02834 |
3-dehydroquinate synthase |
30-364 |
6.45e-74 |
|
3-dehydroquinate synthase
Pssm-ID: 215448 Cd Length: 433 Bit Score: 253.54 E-value: 6.45e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 30 LLTNLPSTTYVLVTDTNLGSIYREKFAKIFneaaAALSPAPRLLTKEIPPGENSKSRQGKADIEDWMLQQTCGRDTVIIA 109
Cdd:PLN02834 94 LQRHVHGKRVLVVTNETVAPLYLEKVVEAL----TAKGPELTVESVILPDGEKYKDMETLMKVFDKALESRLDRRCTFVA 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 110 LGGGVIGDLLGFVAATYMRGIRFVQVPTTLLAMVDSSIGGKTAIDTPLGKNLIGAIWQPHRIYIDIDFIDTLPEREFING 189
Cdd:PLN02834 170 LGGGVIGDMCGFAAASYQRGVNFVQIPTTVMAQVDSSVGGKTGVNHPLGKNMIGAFYQPQCVLIDTDTLATLPDRELASG 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 190 MAEVIKTAAISDEKEFAALEQHADAILkaARsKPGKGRFDLVRqvvkdrivaSARHKAFVVTADEREGGLRNLLNLGHSI 269
Cdd:PLN02834 250 IAEVVKYGLIRDAEFFEWQEANMEKLL--AR-DPGALAYAIKR---------SCENKAEVVSLDEKESGLRATLNLGHTF 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 270 GHAIEAILSP-QVLHGECVAIGMVKELDLARYLGILKPVAVSRMVKCLSKYGLPTSLKDSrvrkhtagkhCSLEQMMANM 348
Cdd:PLN02834 318 GHAIETGPGYgEWLHGEAVAAGTVMAADMSYRLGWIDMSLVNRIFALLKRAKLPTNPPEK----------MTVEMFKSLM 387
|
330
....*....|....*.
gi 327507643 349 ALDKKNDGPRKKVVLL 364
Cdd:PLN02834 388 AVDKKVADGLLRLILL 403
|
|
| DHquinase_I |
pfam01487 |
Type I 3-dehydroquinase; Type I 3-dehydroquinase, (3-dehydroquinate dehydratase or DHQase.) ... |
1051-1278 |
5.79e-73 |
|
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: 242.85 E-value: 5.79e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 1051 SLTLTDLRDSGDLLRTVASGSDAVELRVDLLKDPSSgngipSAEYVAEQISFYRSRVSLPIVFTIRTVSQGGKfPNDAHD 1130
Cdd:pfam01487 3 PLTGKTLEEILEELESGKEGADLVELRVDLLEEPVE-----DAEDVSEQLALLRRVGDLPLIFTFRTKSEGGE-PDGSEE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 1131 AALELIMLAIRSGCEFIDLEITFPEDLLRKVAESK--AHAKIIASHHDPQGKLNWAngSWIQYYNKALQYG-DIIKLVGV 1207
Cdd:pfam01487 77 EYLELLRLALRLGVDYVDVELFLPEEILKELIEAKheGGTKVIGSYHDFEGTPSWE--ELISRYEKMQALGaDIVKIAVM 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 327507643 1208 AETLKDNTALREFKDWAEQAHpDVPVIAINMGDKGQLSRMLNGFL-TPVSHPAL--PFKAAPGQLSAAEIRKGL 1278
Cdd:pfam01487 155 AKSIEDVLALLRFTSEMKSLA-DKPLIAMSMGELGRISRVLGPIFgSPVTFAALglAEKSAPGQLTAKELREAL 227
|
|
| aroD |
TIGR01093 |
3-dehydroquinate dehydratase, type I; This model detects 3-dehydroquinate dehydratase, type I, ... |
1047-1278 |
9.85e-70 |
|
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: 233.81 E-value: 9.85e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 1047 SFFMSLTLTDLRDSGDLLRTVAS-GSDAVELRVDLLKDPSSGNgipSAEYVAEQISFyrSRVSLPIVFTIRTVSQGGKFP 1125
Cdd:TIGR01093 1 KIFVPLTAPDLEEALAEAEKICEkGADIVELRVDLLKDVSSNN---DVDALSEQLSE--LRVDKPLIFTIRTQSEGGKFP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 1126 NDAHDAALELIMLAIRSGCEFIDLEITFPEDLLRKVAES--KAHAKIIASHHDPQGKLNWANgsWIQYYNKALQY-GDII 1202
Cdd:TIGR01093 76 GNEEEYFEELKRAAESLGPDFVDIELFLPDDAVKELINIakKGGTKIIMSNHDFQKTPSWEE--IVERLRKALSYgADIV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 327507643 1203 KLVGVAETLKDNTALREFKDWAeQAHPDVPVIAINMGDKGQLSRMLNGFLTPVSHP-ALPFKAAPGQLSAAEIRKGL 1278
Cdd:TIGR01093 154 KIAVMANSKEDVLTLLSATNKV-DTHYDVPLITMSMGDRGKISRVLGAVFGSVLTFgSLGKASAPGQISVDDLRELL 229
|
|
| AroE |
COG0169 |
Shikimate 5-dehydrogenase [Amino acid transport and metabolism]; Shikimate 5-dehydrogenase is ... |
1287-1567 |
7.45e-66 |
|
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: 224.25 E-value: 7.45e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 1287 KKFAIFGKPVSVSRSPAMHNTLFEQNGLPYVYTRLETDqAQDVKEFI---RSPDFGGASATIPLKLDIIPLIDEVLNEAE 1363
Cdd:COG0169 5 RLYGVIGDPIAHSLSPAIHNAAFAALGLDAVYVAFDVP-PEDLAAAVaglRALGIRGLNVTIPHKEAAIPLLDELDPRAR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 1364 IIGAVNTIIPVEGkdgstRLIGRNTDWSGIVRCLREAGAhsNEGESSALVIGGGGTARAAIYALHNMGFSTVYVLGRSPE 1443
Cdd:COG0169 84 LIGAVNTVVFEDG-----RLIGDNTDGIGFVRALREAGV--DLAGKRVLVLGAGGAARAVAAALAEAGAAEITIVNRTPE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 1444 KIQNMASTFPtgfdIRVLENAsDIENIPRVA--------VGTIPGDR-PIEAnmrEILctifersgraadgKSAAVLLEM 1514
Cdd:COG0169 157 RAEALAARLG----VRAVPLD-DLAAALAGAdlvinatpLGMAGGDAlPLPA---SLL-------------APGAVVYDL 215
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 327507643 1515 AYKPSVTPLMQLASDSGWTTIPGLEALVGQGVYQFEYWTGITPVYEVARNAVL 1567
Cdd:COG0169 216 VYNPLETPLLRAARARGARVIDGLGMLVHQAAEAFELWTGVRPPVEAMRAALR 268
|
|
| DHQase_I |
cd00502 |
Type I 3-dehydroquinase, (3-dehydroquinate dehydratase or DHQase); Type I 3-dehydroquinase, ... |
1047-1280 |
1.87e-58 |
|
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: 201.41 E-value: 1.87e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 1047 SFFMSLTLTDLRDSGDLLRTVASGSDAVELRVDLLKDPSsgngipsAEYVAEQISFYRSRVSLPIVFTIRTVSQGGKFPn 1126
Cdd:cd00502 1 KICVPLTGPDLLEEALSLLELLLGADAVELRVDLLEDPS-------IDDVAEQLSLLRELTPLPIIFTVRTKSEGGNFE- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 1127 DAHDAALELIMLAIRSGCEFIDLEITF--PEDLLRKVAesKAHAKIIASHHDPQGKLNwaNGSWIQYYNKALQYG-DIIK 1203
Cdd:cd00502 73 GSEEEYLELLEEALKLGPDYVDIELDSalLEELINSRK--KGNTKIIGSYHDFSGTPS--DEELVSRLEKMAALGaDIVK 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 327507643 1204 LVGVAETLKDNTALREFKDWAEqAHPDVPVIAINMGDKGQLSRMLNG-FLTPVSHPALPFKAAPGQLSAAEIRKGLSI 1280
Cdd:cd00502 149 IAVMANSIEDNLRLLKFTRQVK-NLYDIPLIAINMGELGKLSRILSPvFGSPLTYASLPEPSAPGQLSVEELKQALSL 225
|
|
| aroE |
PRK00258 |
shikimate 5-dehydrogenase; Reviewed |
1287-1567 |
1.18e-57 |
|
shikimate 5-dehydrogenase; Reviewed
Pssm-ID: 234703 [Multi-domain] Cd Length: 278 Bit Score: 200.80 E-value: 1.18e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 1287 KKFAIFGKPVSVSRSPAMHNTLFEQNGLPYVYTRLETDqAQDVKEFIRS---PDFGGASATIPLKLDIIPLIDEVLNEAE 1363
Cdd:PRK00258 6 RLYAVIGNPIAHSKSPLIHNAAFKQLGLDGVYLAILVP-PEDLEDAVKGffaLGGRGANVTVPFKEAAFALADELSERAR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 1364 IIGAVNTIIPVEGkdgstRLIGRNTDWSGIVRCLREAGAHSNEGESsALVIGGGGTARAAIYALHNMGFSTVYVLGRSPE 1443
Cdd:PRK00258 85 LIGAVNTLVLEDG-----RLIGDNTDGIGFVRALEERLGVDLKGKR-ILILGAGGAARAVILPLLDLGVAEITIVNRTVE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 1444 KIQNMASTFPTGFDIRVLENASDIENIPRVAVGTIP----GDRPIEANMREILctifersgraadgKSAAVLLEMAYKPS 1519
Cdd:PRK00258 159 RAEELAKLFGALGKAELDLELQEELADFDLIINATSagmsGELPLPPLPLSLL-------------RPGTIVYDMIYGPL 225
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 327507643 1520 VTPLMQLASDSGWTTIPGLEALVGQGVYQFEYWTGITPVYEVARNAVL 1567
Cdd:PRK00258 226 PTPFLAWAKAQGARTIDGLGMLVHQAAEAFELWTGVRPPVEPMLAALR 273
|
|
| SK |
cd00464 |
Shikimate kinase (SK) is the fifth enzyme in the shikimate pathway, a seven-step biosynthetic ... |
861-1005 |
1.13e-48 |
|
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: 170.43 E-value: 1.13e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 861 SIVIIGMRGAGKTTTGRWAAKALNRKFIDLDVELEQTEGKTIPDLIKERGWKGFRDAELSLFKRALTerPTGHVFACGGG 940
Cdd:cd00464 1 NIVLIGMMGAGKTTVGRLLAKALGLPFVDLDELIEQRAGMSIPEIFAEEGEEGFRELEREVLLLLLT--KENAVIATGGG 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 327507643 941 IVEIAEARNilidYHKNKGNVLLVMRDIKKVMEFLNIDKTRPAY----IEDMMSVWLRRKPWYQECSNV 1005
Cdd:cd00464 79 AVLREENRR----LLLENGIVVWLDASPEELLERLARDKTRPLLqdedPERLRELLEEREPLYREVADL 143
|
|
| SKI |
pfam01202 |
Shikimate kinase; |
868-1031 |
2.77e-45 |
|
Shikimate kinase;
Pssm-ID: 426122 [Multi-domain] Cd Length: 159 Bit Score: 160.83 E-value: 2.77e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 868 RGAGKTTTGRWAAKALNRKFIDLDVELEQTEGKTIPDLIKERGWKGFRDAELSLFKRALTERptGHVFACGGGIVEIAEA 947
Cdd:pfam01202 1 MGAGKSTIGRLLAKALGLPFIDTDEEIEKRTGMSIAEIFEEEGEEGFRRLESEVLKELLAEH--GLVIATGGGAVLSEEN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 948 RNILidyhKNKGNVLLVMRDIKKVMEFLNIDKTRPAYIEDMMSVWLRRKPWYQECSNVQYYSRHSSSPELALAMDDFDRF 1027
Cdd:pfam01202 79 RDLL----KERGIVIYLDAPLEVLLERLKRDKTRPLLQNKDPEEELLELLFEERDPLYEEAADIVIDTDESSPEEVATEI 154
|
....
gi 327507643 1028 IQFV 1031
Cdd:pfam01202 155 LEAL 158
|
|
| NAD_bind_Shikimate_DH |
cd01065 |
NAD(P) binding domain of Shikimate dehydrogenase; Shikimate dehydrogenase (DH) is an amino ... |
1388-1554 |
9.59e-37 |
|
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: 136.25 E-value: 9.59e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 1388 TDWSGIVRCLREAGAHSNEGesSALVIGGGGTARAAIYALHNMGFSTVYVLGRSPEKIQNMASTFPTGFDIRVLENASDI 1467
Cdd:cd01065 1 TDGLGFVRALEEAGIELKGK--KVLILGAGGAARAVAYALAELGAAKIVIVNRTLEKAKALAERFGELGIAIAYLDLEEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 1468 ENIPRVAVGTIPGDrpieanMREILCTIFErsgrAADGKSAAVLLEMAYKPSVTPLMQLASDSGWTTIPGLEALVGQGVY 1547
Cdd:cd01065 79 LAEADLIINTTPVG------MKPGDELPLP----PSLLKPGGVVYDVVYNPLETPLLKEARALGAKTIDGLEMLVYQAAE 148
|
....*..
gi 327507643 1548 QFEYWTG 1554
Cdd:cd01065 149 AFELWTG 155
|
|
| AroK |
COG0703 |
Shikimate kinase [Amino acid transport and metabolism]; Shikimate kinase is part of the ... |
862-1005 |
3.33e-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: 3.33e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 862 IVIIGMRGAGKTTTGRWAAKALNRKFIDLDVELEQTEGKTIPDLIKERGWKGFRDAELSLFKRALTERPTghVFACGGGI 941
Cdd:COG0703 1 IVLIGMMGAGKSTVGRLLAKRLGLPFVDTDAEIEERAGMSIPEIFAEEGEAGFRELEREVLAELLEEENA--VIATGGGA 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 327507643 942 VEIAEARNILidyhKNKGNVLLVMRDIKKVMEFLNIDKTRP--------AYIEDMMSvwlRRKPWYQECSNV 1005
Cdd:COG0703 79 VLSPENRELL----KEHGTVVYLDASPETLLERLRRDDNRPllqgedprERLEELLA---EREPLYREVADI 143
|
|
| AroD |
COG0710 |
3-dehydroquinate dehydratase [Amino acid transport and metabolism]; 3-dehydroquinate ... |
1058-1283 |
3.97e-33 |
|
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: 128.87 E-value: 3.97e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 1058 RDSGDLLRTVA----SGSDAVELRVDLLKDPSsgngipsAEYVAEQISFYRSRVSLPIVFTIRTVSQGGKFPNDaHDAAL 1133
Cdd:COG0710 13 ATPEDLLAEAEaaarAGADLVELRLDYLEDPD-------LEELKELLEALREYGGLPLIFTFRTAEEGGEFEGS-EEERL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 1134 ELIMLAIRS-GCEFIDLEITFPEDLLRKVAES--KAHAKIIASHHD-----PQGKLnwangswIQYYNKALQYG-DIIKL 1204
Cdd:COG0710 85 ELLRAAADSaGVDLVDVELDTLEDDVDDLIEAarEAGVKVIVSYHDfektpSAEEL-------VEILEKMQELGaDIVKI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 1205 VGVAETLKDNTALREFKDWAEQaHPDVPVIAINMGDKGQLSR----MLNGFLT--PVSHPalpfkAAPGQLSAAEIRKGL 1278
Cdd:COG0710 158 AVMAKSPEDVLRLLEATLEAKE-ELDRPVITMAMGELGKISRilgpLFGSALTyaSVGEA-----SAPGQIDVEELRELL 231
|
....*
gi 327507643 1279 SIMGE 1283
Cdd:COG0710 232 ELLEA 236
|
|
| Shikimate_dh_N |
pfam08501 |
Shikimate dehydrogenase substrate binding domain; This domain is the substrate binding domain ... |
1291-1371 |
2.10e-27 |
|
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: 106.91 E-value: 2.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 1291 IFGKPVSVSRSPAMHNTLFEQNGLPYVYTRLET--DQAQDVKEFIRSPDFGGASATIPLKLDIIPLIDEVLNEAEIIGAV 1368
Cdd:pfam08501 1 VIGNPISHSLSPAIHNAAFKALGLNGVYVAFEVppDNLPDFVEGLRALGFRGLNVTIPHKEAAIPLLDELSPEAKAIGAV 80
|
...
gi 327507643 1369 NTI 1371
Cdd:pfam08501 81 NTI 83
|
|
| aroK |
PRK00131 |
shikimate kinase; Reviewed |
861-1004 |
5.15e-26 |
|
shikimate kinase; Reviewed
Pssm-ID: 234654 [Multi-domain] Cd Length: 175 Bit Score: 106.43 E-value: 5.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 861 SIVIIGMRGAGKTTTGRWAAKALNRKFIDLDVELEQTEGKTIPDLIKERGWKGFRDAElslfKRALTE--RPTGHVFACG 938
Cdd:PRK00131 6 NIVLIGFMGAGKSTIGRLLAKRLGYDFIDTDHLIEARAGKSIPEIFEEEGEAAFRELE----EEVLAEllARHNLVISTG 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 327507643 939 GGIVEIAEARNILIDYHKnkgNVLLVMrDIKKVMEFLNIDKTRP--------AYIEDMMSVwlrRKPWYQECSN 1004
Cdd:PRK00131 82 GGAVLREENRALLRERGT---VVYLDA-SFEELLRRLRRDRNRPllqtndpkEKLRDLYEE---RDPLYEEVAD 148
|
|
| aroD |
PRK02412 |
type I 3-dehydroquinate dehydratase; |
1068-1283 |
5.47e-18 |
|
type I 3-dehydroquinate dehydratase;
Pssm-ID: 235036 Cd Length: 253 Bit Score: 85.33 E-value: 5.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 1068 ASGSDAVELRVDLLKDPSSGNGIPSaeyVAEQIsfYRSRVSLPIVFTIRTVSQGGKFP-NDahDAALELIMLAIRSGC-E 1145
Cdd:PRK02412 39 KYDADIIEWRADFLEKISDVESVLA---AAPAI--REKFAGKPLLFTFRTAKEGGEIAlSD--EEYLALIKAVIKSGLpD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 1146 FIDLEITFPEDLLRK-VAESKAH-AKIIASHHD-----PQGKLnwangswIQYYNKALQYG-DIIKLVGVAETLKDN--- 1214
Cdd:PRK02412 112 YIDVELFSGKDVVKEmVAFAHEHgVKVVLSYHDfektpPKEEI-------VERLRKMESLGaDIVKIAVMPQSEQDVltl 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 327507643 1215 -TALREFKdwaeQAHPDVPVIAINMGDKGQLSRmLNG--FLTPVSHPALPFKAAPGQLSAAEIRKGLSIMGE 1283
Cdd:PRK02412 185 lNATREMK----ELYADQPLITMSMGKLGRISR-LAGevFGSSWTFASLDKASAPGQISVEDLRRILEILHK 251
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| EPSP_synthase |
cd01556 |
EPSP synthase domain. 3-phosphoshikimate 1-carboxyvinyltransferase ... |
406-834 |
1.41e-151 |
|
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: 468.19 E-value: 1.41e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 406 APPGSKSISNRALVLAALGSGTVRVKNLLHSDDTEVMLNALERLGAatfAWEDEGEVLVVNGNGGKMQASPTELYLGNAG 485
Cdd:cd01556 6 TVPGSKSISHRALLLAALAEGESRIENLLDSDDTLATLEALRALGA---KIEEEGGTVEIVGGGGLGLPPEAVLDCGNSG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 486 TASRFLTSVATLSGKGSVdyniLTGNNRMKQRPIGDLVDALTINGAQVEYLEKAGSLPLKIaaSGGFKGGRINLAAKVSS 565
Cdd:cd01556 83 TTMRLLTGLLALQGGDSV----LTGDESLRKRPMGRLVDALRQLGAEIEGREGGGYPPLIG--GGGLKGGEVEIPGAVSS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 566 QYVSSLLMCAPYAKEPVTLKLvgGRPISLSYIEMTTAMMRSFGIDVQKSTTEEWTYHiPQGSYnNPPEYVIESDASSATY 645
Cdd:cd01556 157 QFKSALLLAAPLAEGPTTIII--GELESKPYIDHTERMLRAFGAEVEVDGYRTITVK-GGQKY-KGPEYTVEGDASSAAF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 646 PLAIAAVTGTTCTVPNIGSASlqGDARFaVEVLRPMGCKVEQTATsTTVTGPADGVLRPLpNVDMEPMTDAFLGASVLAA 725
Cdd:cd01556 233 FLAAAAITGSEIVIKNVGLNS--GDTGI-IDVLKEMGADIEIGNE-DTVVVESGGKLKGI-DIDGNDIPDEAPTLAVLAA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 726 IAQGEggnhaTRIYGIANQRVKECNRIEAMRVELAKFGVVCREHPDGLEIDGidrSTLRHPAGGVFCYDDHRVAFSFSIL 805
Cdd:cd01556 308 FAEGP-----TRIRNAAELRVKESDRIAAMATELRKLGADVEETEDGLIIEG---GPLKGAGVEVYTYGDHRIAMSFAIA 379
|
410 420
....*....|....*....|....*....
gi 327507643 806 SLVAPTPTLILEKECVGKTWPTYWDALKQ 834
Cdd:cd01556 380 GLVAEGGVTIEDPECVAKSFPNFFEDLES 408
|
|
| aroA |
TIGR01356 |
3-phosphoshikimate 1-carboxyvinyltransferase; This model represents ... |
406-834 |
2.02e-138 |
|
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: 432.86 E-value: 2.02e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 406 APPGSKSISNRALVLAALGSGTVRVKNLLHSDDTEVMLNALERLGAATfawEDEGEVLVVNGNGGKMQASptELYLGNAG 485
Cdd:TIGR01356 4 RAPGSKSITHRALILAALAEGETRVRNLLRSEDTLATLDALRALGAKI---EDGGEVAVIEGVGGKEPQA--ELDLGNSG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 486 TASRFLTSVATLSGKGSVdyniLTGNNRMKQRPIGDLVDALTINGAQVEYLEKAGSLPLKIaaSGGFKGGRINLAAKVSS 565
Cdd:TIGR01356 79 TTARLLTGVLALADGEVV----LTGDESLRKRPMGRLVDALRQLGAEISSLEGGGSLPLTI--SGPLPGGIVYISGSASS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 566 QYVSSLLMCAPyAKEPVTLKLVGGRPISLSYIEMTTAMMRSFGIDVQKSTTEewTYHIPQGSYNNPPEYVIESDASSATY 645
Cdd:TIGR01356 153 QYKSALLLAAP-ALQAVGITIVGEPLKSRPYIEITLDLLGSFGVEVERSDGR--KIVVPGGQKYGPQGYDVPGDYSSAAF 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 646 PLAIAAVTGTTCTVPNIGSASLQGDARFaVEVLRPMGCKVEQTATSTTVTGPADgvLRPLpNVDMEPMTDAFLGASVLAA 725
Cdd:TIGR01356 230 FLAAAAITGGRVTLENLGINPTQGDKAI-IIVLEEMGADIEVEEDDLIVEGASG--LKGI-KIDMDDMIDELPTLAVLAA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 726 IAQGEggnhaTRIYGIANQRVKECNRIEAMRVELAKFGVVCREHPDGLEIDGidRSTLRhpAGGVFCYDDHRVAFSFSIL 805
Cdd:TIGR01356 306 FAEGV-----TRITGAEELRVKESDRIAAIAEELRKLGVDVEEFEDGLYIRG--KKELK--GAVVDTFGDHRIAMAFAVA 376
|
410 420
....*....|....*....|....*....
gi 327507643 806 SLVAPTPTLILEKECVGKTWPTYWDALKQ 834
Cdd:TIGR01356 377 GLVAEGEVLIDDPECVAKSFPSFFDVLER 405
|
|
| DHQS |
cd08195 |
Dehydroquinate synthase (DHQS) catalyzes the conversion of DAHP to DHQ in shikimate pathway ... |
25-387 |
3.00e-138 |
|
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: 429.94 E-value: 3.00e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 25 YIVQDLLTNLPS-------TTYVLVTDTNLGSIYREKFAKIFNEAAAalspapRLLTKEIPPGENSKSRQGKADIEDWML 97
Cdd:cd08195 5 LIGSGLLDKLGEllelkkgSKVVIVTDENVAKLYGELLLKSLEAAGF------KVEVIVIPAGEKSKSLETVERIYDFLL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 98 QQTCGRDTVIIALGGGVIGDLLGFVAATYMRGIRFVQVPTTLLAMVDSSIGGKTAIDTPLGKNLIGAIWQPHRIYIDIDF 177
Cdd:cd08195 79 EAGLDRDSLLIALGGGVVGDLAGFVASTYMRGIPFIQVPTTLLAQVDSSIGGKTGINLPGGKNLIGAFYQPKAVLIDPDF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 178 IDTLPEREFINGMAEVIKTAAISDEKEFAALEQHADAILKAarskpgkgRFDLVRQVVKdrivASARHKAFVVTADEREG 257
Cdd:cd08195 159 LKTLPEREFRSGLAEVIKYGLIADKELFEFLEKNLDKILAR--------DPEALEEIIA----RSVEIKADIVEEDEREK 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 258 GLRNLLNLGHSIGHAIEAILSPQVLHGECVAIGMVKELDLARYLGILKPVAVSRMVKCLSKYGLPTSLKDsrvrkhtagk 337
Cdd:cd08195 227 GLRAILNFGHTFGHAIESASGYKLLHGEAVAIGMVAAARLSVKLGLLSEEDLERIRALLKKLGLPTSIKD---------- 296
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 327507643 338 hCSLEQMMANMALDKKNDGPRKKVVLLSAIGQTYepKASVVSNEDIRAVL 387
Cdd:cd08195 297 -LDPEELLEAMKRDKKNRGGKIRFVLLKGIGKAV--IVDDVSEEEIREAL 343
|
|
| AroA |
COG0128 |
5-enolpyruvylshikimate-3-phosphate synthase [Amino acid transport and metabolism]; ... |
408-834 |
1.67e-135 |
|
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: 425.66 E-value: 1.67e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 408 PGSKSISNRALVLAALGSGTVRVKNLLHSDDTEVMLNALERLGaATFAWEDEGEVlVVNGNGGKMQASPTELYLGNAGTA 487
Cdd:COG0128 19 PGSKSISHRALLLAALAEGESTIRNLLESDDTLATLEALRALG-AEIEELDGGTL-RVTGVGGGLKEPDAVLDCGNSGTT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 488 SRFLTSVATLSGKGSVdyniLTGNNRMKQRPIGDLVDALTINGAQVEYLEKaGSLPLKIAAsGGFKGGRINLAAKVSSQY 567
Cdd:COG0128 97 MRLLTGLLALQPGEVV----LTGDESLRKRPMGRLLDPLRQLGARIESRGG-GYLPLTIRG-GPLKGGEYEIPGSASSQF 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 568 VSSLLMCAPYAKEPVTLKlVGGRPISLSYIEMTTAMMRSFGIDVQKSTTEEWTYHIPQgSYnNPPEYVIESDASSATYPL 647
Cdd:COG0128 171 KSALLLAGPLAEGGLEIT-VTGELESKPYRDHTERMLRAFGVEVEVEGYRRFTVPGGQ-RY-RPGDYTVPGDISSAAFFL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 648 AIAAVTGTTCTVPNIGSASLQGDARFaVEVLRPMGCKVEQTATSTTVTGpadGVLRPLpNVDMEPMTDAFLGASVLAAIA 727
Cdd:COG0128 248 AAAAITGSEVTVEGVGLNSTQGDTGI-LDILKEMGADIEIENDGITVRG---SPLKGI-DIDLSDIPDEAPTLAVLAAFA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 728 QGEggnhaTRIYGIANQRVKECNRIEAMRVELAKFGVVCREHPDGLEIDGidRSTLRhpaGGVF-CYDDHRVAFSFSILS 806
Cdd:COG0128 323 EGT-----TRIRGAAELRVKESDRIAAMATELRKLGADVEETEDGLIIEG--GPKLK---GAEVdSYGDHRIAMAFAVAG 392
|
410 420
....*....|....*....|....*...
gi 327507643 807 LVAPTPTLILEKECVGKTWPTYWDALKQ 834
Cdd:COG0128 393 LRAEGPVTIDDAECVAKSFPDFFELLES 420
|
|
| AroB |
COG0337 |
3-dehydroquinate synthetase [Amino acid transport and metabolism]; 3-dehydroquinate synthetase ... |
25-387 |
1.07e-128 |
|
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: 404.47 E-value: 1.07e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 25 YIVQDLLTNLPST--------TYVLVTDTNLGSIYREKFAKIFNEAAAALSPAprlltkEIPPGENSKSRQGKADIEDWM 96
Cdd:COG0337 16 RIGRGLLDELGELlaellkgrRVLVVTDENVAPLYGERLRAALEAAGFEVHLL------VLPDGEASKTLETLERILDAL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 97 LQQTCGRDTVIIALGGGVIGDLLGFVAATYMRGIRFVQVPTTLLAMVDSSIGGKTAIDTPLGKNLIGAIWQPHRIYIDID 176
Cdd:COG0337 90 LEAGLDRDDLVVALGGGVVGDLAGFAAATYLRGVPFIQVPTTLLAQVDSSVGGKTGVNHPGGKNLIGAFHQPRAVLIDLD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 177 FIDTLPEREFINGMAEVIKTAAISDEKEFAALEQHADAILkaarskpgKGRFDLVRQVVKDrivaSARHKAFVVTADERE 256
Cdd:COG0337 170 FLKTLPERELRAGLAEVIKYGLIADAEFFEWLEENADALL--------ARDPEALEEAIAR----SCEIKAEVVAADERE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 257 GGLRNLLNLGHSIGHAIEAILSPQVLHGECVAIGMVKELDLARYLGILKPVAVSRMVKCLSKYGLPTSLKDsrvrkhtag 336
Cdd:COG0337 238 SGLRALLNFGHTFGHAIEAATGYRLLHGEAVAIGMVFAARLSARLGLLSEEDVERIRALLEALGLPTRLPA--------- 308
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 327507643 337 khCSLEQMMANMALDKKNDGPRKKVVLLSAIGQTYEpkASVVSNEDIRAVL 387
Cdd:COG0337 309 --LDPEALLAAMKRDKKVRGGKLRFVLLRGIGKAVI--VDDVDEELLRAAL 355
|
|
| PRK02427 |
PRK02427 |
3-phosphoshikimate 1-carboxyvinyltransferase; Provisional |
389-834 |
2.56e-127 |
|
3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
Pssm-ID: 235037 [Multi-domain] Cd Length: 435 Bit Score: 403.75 E-value: 2.56e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 389 PSIEVIPGVPKDLNVVCAPPGSKSISNRALVLAALGSGTVRVKNLLHSDDTEVMLNALERLGAatfawEDEGEVLVVNGN 468
Cdd:PRK02427 1 MMMMLLIIPPSPLSGTVRVPGSKSISHRALLLAALAEGETTITNLLRSEDTLATLNALRALGV-----EIEDDEVVVEGV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 469 GGKMQASPTE-LYLGNAGTASRFLTSVATLSGKGSVdyniLTGNNRMKQRPIGDLVDALTINGAQVEYlEKAGSLPLKIa 547
Cdd:PRK02427 76 GGGGLKEPEDvLDCGNSGTTMRLLTGLLALQPGEVV----LTGDESLRKRPMGRLLDPLRQMGAKIEG-RDEGYLPLTI- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 548 aSGGFKGGRINLAAKVSSQYVSSLLMCAPYAKEPVTLKLVGGRPISLSYIEMTTAMMRSFGIDVQKSTTEEW-TYHIPQG 626
Cdd:PRK02427 150 -RGGKKGGPIEYDGPVSSQFVKSLLLLAPLFAEGDTETTVIEPLPSRPHTEITLRMLRAFGVEVENVEGWGYrRIVIKGG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 627 SYNNPPEYVIESDASSATYPLAIAAVT-GTTCTVPNIGSASLQGDARFaVEVLRPMGCKVEQTATSTTVTGPAD-----G 700
Cdd:PRK02427 229 QRLRGQDITVPGDPSSAAFFLAAAAITgGSEVTITNVGLNSTQGGKAI-IDVLEKMGADIEIENEREGGEPVGDirvrsS 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 701 VLRPLpNVDMEPMTDAFLGASVLAAIAQGEggnhaTRIYGIANQRVKECNRIEAMRVELAKFGVVCREHPDGLEIDGidr 780
Cdd:PRK02427 308 ELKGI-DIDIPDIIDEAPTLAVLAAFAEGT-----TVIRNAEELRVKETDRIAAMATELRKLGAEVEETEDGLIITG--- 378
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 327507643 781 stlRHPAGGVFCYDDHRVAFSFSILSLVAPTPTLILEKECVGKTWPTYWDALKQ 834
Cdd:PRK02427 379 ---GPLAGVVDSYGDHRIAMAFAIAGLAAEGPVTIDDPECVAKSFPDFFEDLAS 429
|
|
| DHQ_synthase |
pfam01761 |
3-dehydroquinate synthase; The 3-dehydroquinate synthase EC:4.6.1.3 domain is present in ... |
77-354 |
8.85e-124 |
|
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: 387.24 E-value: 8.85e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 77 IPPGENSKSRQGKADIEDWMLQQTCGRDTVIIALGGGVIGDLLGFVAATYMRGIRFVQVPTTLLAMVDSSIGGKTAIDTP 156
Cdd:pfam01761 4 IPDGEKSKTLETLERIYDALLEAGLDRSSLLIALGGGVIGDLAGFVAATYMRGIRFIQVPTTLLAQVDSSVGGKTGINHP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 157 LGKNLIGAIWQPHRIYIDIDFIDTLPEREFINGMAEVIKTAAISDEKEFAALEQHADAILkaarskpgkgrfDLVRQVVK 236
Cdd:pfam01761 84 LGKNLIGAFYQPKAVLIDLDFLKTLPDREFRAGLAEVIKYGLIADAEFFEWLEENAEALL------------NLDPDALE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 237 DRIVASARHKAFVVTADEREGGLRNLLNLGHSIGHAIEAILSP-QVLHGECVAIGMVKELDLARYLGILKPVAVSRMVKC 315
Cdd:pfam01761 152 EAIARSCEVKADVVAQDEKESGLRALLNLGHTFGHAIEALSGYgALLHGEAVAIGMVLAARLSERLGLLDEADVERIRAL 231
|
250 260 270
....*....|....*....|....*....|....*....
gi 327507643 316 LSKYGLPTSLKDSrvrkhtagkhcSLEQMMANMALDKKN 354
Cdd:pfam01761 232 LKKYGLPTSLPDL-----------DVEQLLAAMARDKKV 259
|
|
| EPSP_synthase |
pfam00275 |
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase); |
398-832 |
5.05e-114 |
|
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);
Pssm-ID: 395213 Cd Length: 415 Bit Score: 366.62 E-value: 5.05e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 398 PKDLNVVCAPPGSKSISNRALVLAALGSGTVRVKNLLHSDDTEVMLNALERLGAATFAWEDEGEVLVVNGNGGKMQASP- 476
Cdd:pfam00275 3 GSRLSGEVKIPGSKSNSHRALILAALAAGESTITNLLDSDDTLTMLEALRALGAEIIKLDDEKSVVIVEGLGGSFEAPEd 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 477 TELYLGNAGTASRFLTSVATLSGKGSVdyniLTGNNRMKQRPIGDLVDALTINGAQVEYLEKAGSLPLKIAasgGFKGGR 556
Cdd:pfam00275 83 LVLDMGNSGTALRPLTGRLALQSGEVV----LPGDCSIGKRPMDRLLDALRQLGAEIEGREGYNYAPLKVR---GLRLGG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 557 INLAAKVSSQYVSSLLMCAP-YAKEPVTLKlvggRPISLSYIEMTTAMMRSFGIDVQKSTTEE-WTYHIPQGSYnnPPEY 634
Cdd:pfam00275 156 IHIDGDVSSQFVTSLLMLAAlLAEGTTTIE----NLASEPYIDDTENMLKKFGAKIEGSGTELsITVKGGEKLP--GQEY 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 635 VIESDASSATYPLAIAAVTGTTCTVPNIGSASLQGDaRFAVEVLRPMGCKVEQTATSTTVTGPadGVLRPLPnVDMEPMT 714
Cdd:pfam00275 230 RVEGDRSSAAYFLVAAAITGGTVTVENVGINSLQGD-EALLEILEKMGAEITQEEDADIVVGP--PGLRGKA-VDIRTAP 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 715 DAFLGASVLAAIAQGEggnhaTRIYGIANQRVKECNRIEAMRVELAKFGVVCREHPDGLEIDGIDrSTLRHpaGGVFCYD 794
Cdd:pfam00275 306 DPAPTTAVLAAFAEGT-----TRIEGISELRVKETDRLFAMATELRRLGADVEELPDGLIIIPAV-KELKG--AEVDSYG 377
|
410 420 430
....*....|....*....|....*....|....*...
gi 327507643 795 DHRVAFSFSILSLVAPTPTLILEKECVGKTWPTYWDAL 832
Cdd:pfam00275 378 DHRIAMALALAGLVAEGETIIDDIECTDRSFPDFEEKL 415
|
|
| aroB |
TIGR01357 |
3-dehydroquinate synthase; This model represents 3-dehydroquinate synthase, the enzyme ... |
40-387 |
2.33e-112 |
|
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: 359.25 E-value: 2.33e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 40 VLVTDTNLGSIYREKFAkifnEAAAALSPAPRLLTkeIPPGENSKSRQGKADIEDWMLQQTCGRDTVIIALGGGVIGDLL 119
Cdd:TIGR01357 24 VIITDETVADLYGDKLL----EALQALGYNVLKLT--VPDGEESKSLETVQRLYDQLLEAGLDRSSTIIALGGGVVGDLA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 120 GFVAATYMRGIRFVQVPTTLLAMVDSSIGGKTAIDTPLGKNLIGAIWQPHRIYIDIDFIDTLPEREFINGMAEVIKTAAI 199
Cdd:TIGR01357 98 GFVAATYMRGIRFIQVPTTLLAMVDSSVGGKTGINFPGGKNLIGTFYQPKAVLIDPDFLKTLPDRELRSGMAEVIKHGLI 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 200 SDEKEFAALEQHADAILkaaRSKPGKGRFDLVRQVVKDrivasarhKAFVVTADEREGGLRNLLNLGHSIGHAIEAILSP 279
Cdd:TIGR01357 178 ADAELFDELESNDKLRL---NLQELEHLEELIKRSIEV--------KASIVAEDEKESGLRAILNFGHTIGHAIEAEAGY 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 280 -QVLHGECVAIGMVKELDLARYLGILKPVAVSRMVKCLSKYGLPTSLKdsrvrkhtagKHCSLEQMMANMALDKKNDGPR 358
Cdd:TIGR01357 247 gKIPHGEAVAIGMVCEAKLSERLGLLPAELIERLVQLLKRYGLPTDLP----------KDLDVDELLNAMLNDKKNSGGK 316
|
330 340
....*....|....*....|....*....
gi 327507643 359 KKVVLLSAIGQTYEpkASVVSNEDIRAVL 387
Cdd:TIGR01357 317 IRFVLLEEIGKAAL--AREVPDEMVLELL 343
|
|
| PRK11860 |
PRK11860 |
bifunctional 3-phosphoshikimate 1-carboxyvinyltransferase/cytidylate kinase; |
408-889 |
5.23e-101 |
|
bifunctional 3-phosphoshikimate 1-carboxyvinyltransferase/cytidylate kinase;
Pssm-ID: 237003 [Multi-domain] Cd Length: 661 Bit Score: 339.33 E-value: 5.23e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 408 PGSKSISNRALVLAALGSGTVRVKNLLHSDDTEVMLNALERLGAatfAWEDEGEVLVVNGNGGKMQASPTELYLGNAGTA 487
Cdd:PRK11860 22 PGSKSISNRVLLLAALSEGTTTVRDLLDSDDTRVMLDALRALGC---GVEQLGDTYRITGLGGQFPVKQADLFLGNAGTA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 488 SRFLTSVATLSGKgsvDYNiLTGNNRMKQRPIGDLVDALTINGAQVEYLEKAGSLPLKIAASGGFKGGRINLAAKVSSQY 567
Cdd:PRK11860 99 MRPLTAALALLGG---EYE-LSGVPRMHERPIGDLVDALRQLGCDIDYLGNEGFPPLRIGPAPLRLDAPIRVRGDVSSQF 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 568 VSSLLMCAPY-AKEPVTLKLVgGRPISLSYIEMTTAMMRSFGIDVQKsttEEWT-YHIPQGS-YNNPPEYVIESDASSAT 644
Cdd:PRK11860 175 LTALLMALPLvARRDITIEVV-GELISKPYIEITLNLLARFGIAVQR---EGWQrFTIPAGSrYRSPGEIHVEGDASSAS 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 645 YPLAIAAV-TGTTCTVPNIGSASLQGDARFAvEVLRPMGCKVEQTATSTTVTGPAdGVLRPLpNVDMEPMTDAFLGASVL 723
Cdd:PRK11860 251 YFIAAGAIaGGAPVRIEGVGRDSIQGDIRFA-EAARAMGAQVTSGPNWLEVRRGA-WPLKAI-DLDCNHIPDAAMTLAVM 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 724 AAIAQGeggnhATRIYGIANQRVKECNRIEAMRVELAKFGVVCREHPDGLEIDGIDRSTLRHPAgGVFCYDDHRVAFSFS 803
Cdd:PRK11860 328 ALYADG-----TTTLRNIASWRVKETDRIAAMATELRKLGATVEEGADYIRVTPPAQAADWKAA-AIHTYDDHRMAMCFS 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 804 ILSL-VAPTPTLILEKECVGKTWPTYWDALkqkFGVslkgkelAESEITHGPAdrsdasIVIIGMRGAGKTTTGRWAAKA 882
Cdd:PRK11860 402 LAAFnPAGLPVRINDPKCVAKTFPDYFEAL---FSV-------AQADADRVPV------ICIDGPTASGKGTVAARVAEA 465
|
....*..
gi 327507643 883 LNRKFID 889
Cdd:PRK11860 466 LGYHYLD 472
|
|
| PLN02338 |
PLN02338 |
3-phosphoshikimate 1-carboxyvinyltransferase |
408-833 |
1.05e-98 |
|
3-phosphoshikimate 1-carboxyvinyltransferase
Pssm-ID: 177972 [Multi-domain] Cd Length: 443 Bit Score: 325.16 E-value: 1.05e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 408 PGSKSISNRALVLAALGSGTVRVKNLLHSDDTEVMLNALERLGAaTFAWEDEGEVLVVNGNGGKMQAS-----PTELYLG 482
Cdd:PLN02338 19 PGSKSLSNRILLLAALSEGTTVVDNLLDSDDIRYMLGALKTLGL-NVEEDSENNRAVVEGCGGKFPVSgdskeDVELFLG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 483 NAGTASRFLTSVATLSGkGSVDYnILTGNNRMKQRPIGDLVDALTINGAQVEYLEKAGSLPLKIAASGGFKGGRINLAAK 562
Cdd:PLN02338 98 NAGTAMRPLTAAVTAAG-GNASY-VLDGVPRMRERPIGDLVDGLKQLGADVECTLGTNCPPVRVNAAGGLPGGKVKLSGS 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 563 VSSQYVSSLLMCAPYAKEPVTLKLVgGRPISLSYIEMTTAMMRSFGIDVQKSTTEEwTYHIPQG-SYNNPPEYVIESDAS 641
Cdd:PLN02338 176 ISSQYLTALLMAAPLALGDVEIEIV-DKLISVPYVEMTLKLMERFGVSVEHSDSWD-RFFIKGGqKYKSPGNAYVEGDAS 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 642 SATYPLAIAAVTGTTCTVPNIGSASLQGDARFAvEVLRPMGCKVEQTATSTTVTGPADGVL--RPLP--NVDMEPMTDAF 717
Cdd:PLN02338 254 SASYFLAGAAITGGTVTVEGCGTTSLQGDVKFA-EVLEKMGAKVEWTENSVTVTGPPRDAFggKHLKaiDVNMNKMPDVA 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 718 LGASVLAAIAQGeggnhATRIYGIANQRVKECNRIEAMRVELAKFGVVCREHPD--------GLEIDGIDrstlrhpagg 789
Cdd:PLN02338 333 MTLAVVALFADG-----PTAIRDVASWRVKETERMIAICTELRKLGATVEEGPDyciitppkKLKPAEID---------- 397
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 327507643 790 vfCYDDHRVAFSFSiLSLVAPTPTLILEKECVGKTWPTYWDALK 833
Cdd:PLN02338 398 --TYDDHRMAMAFS-LAACGDVPVTINDPGCTRKTFPTYFDVLE 438
|
|
| Shik-DH-AROM |
TIGR01809 |
shikimate-5-dehydrogenase, fungal AROM-type; This model represents a clade of ... |
1282-1566 |
1.25e-75 |
|
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: 252.91 E-value: 1.25e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 1282 GEIPAKKFAIFGKPVSVSRSPAMHNTLFEQNGLPYVYTRLETDQAQDVKEFIRS--PDFGGASATIPLKLDIIPLIDEVL 1359
Cdd:TIGR01809 1 GNKGPKKAFIIGKPIAHSRSPHLHNAGYEILGLPDKTYEFETCSAEELKEVLSGfgPQFGGASVTIPLKFAILRFADEHT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 1360 NEAEIIGAVNTIIPVegkdGSTRLIGRNTDWSGIVRCLREAGAHSNEGESSALVIGGGGTARAAIYALHNMGFSTVYVLG 1439
Cdd:TIGR01809 81 DRASLIGSVNTLLRT----QNGIWKGDNTDWDGIAGALANIGKFEPLAGFRGLVIGAGGTSRAAVYALASLGVTDITVIN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 1440 RSPEKIQNMASTFPTGFDIRVLENASDIENIP---RVAVGTIPGDRPIEANMREILCTIFERSGRAADGksaaVLLEMAY 1516
Cdd:TIGR01809 157 RNPDKLSRLVDLGVQVGVITRLEGDSGGLAIEkaaEVLVSTVPADVPADYVDLFATVPFLLLKRKSSEG----IFLDAAY 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 327507643 1517 KPSVTPLMQLASDSGWTTIPGLEALVGQGVYQFEYWTGITPVYEVARNAV 1566
Cdd:TIGR01809 233 DPWPTPLVAIVSAAGWRVISGLQMLLHQGFAQFEQWTGMPAPREAMACAL 282
|
|
| PLN02834 |
PLN02834 |
3-dehydroquinate synthase |
30-364 |
6.45e-74 |
|
3-dehydroquinate synthase
Pssm-ID: 215448 Cd Length: 433 Bit Score: 253.54 E-value: 6.45e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 30 LLTNLPSTTYVLVTDTNLGSIYREKFAKIFneaaAALSPAPRLLTKEIPPGENSKSRQGKADIEDWMLQQTCGRDTVIIA 109
Cdd:PLN02834 94 LQRHVHGKRVLVVTNETVAPLYLEKVVEAL----TAKGPELTVESVILPDGEKYKDMETLMKVFDKALESRLDRRCTFVA 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 110 LGGGVIGDLLGFVAATYMRGIRFVQVPTTLLAMVDSSIGGKTAIDTPLGKNLIGAIWQPHRIYIDIDFIDTLPEREFING 189
Cdd:PLN02834 170 LGGGVIGDMCGFAAASYQRGVNFVQIPTTVMAQVDSSVGGKTGVNHPLGKNMIGAFYQPQCVLIDTDTLATLPDRELASG 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 190 MAEVIKTAAISDEKEFAALEQHADAILkaARsKPGKGRFDLVRqvvkdrivaSARHKAFVVTADEREGGLRNLLNLGHSI 269
Cdd:PLN02834 250 IAEVVKYGLIRDAEFFEWQEANMEKLL--AR-DPGALAYAIKR---------SCENKAEVVSLDEKESGLRATLNLGHTF 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 270 GHAIEAILSP-QVLHGECVAIGMVKELDLARYLGILKPVAVSRMVKCLSKYGLPTSLKDSrvrkhtagkhCSLEQMMANM 348
Cdd:PLN02834 318 GHAIETGPGYgEWLHGEAVAAGTVMAADMSYRLGWIDMSLVNRIFALLKRAKLPTNPPEK----------MTVEMFKSLM 387
|
330
....*....|....*.
gi 327507643 349 ALDKKNDGPRKKVVLL 364
Cdd:PLN02834 388 AVDKKVADGLLRLILL 403
|
|
| DHquinase_I |
pfam01487 |
Type I 3-dehydroquinase; Type I 3-dehydroquinase, (3-dehydroquinate dehydratase or DHQase.) ... |
1051-1278 |
5.79e-73 |
|
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: 242.85 E-value: 5.79e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 1051 SLTLTDLRDSGDLLRTVASGSDAVELRVDLLKDPSSgngipSAEYVAEQISFYRSRVSLPIVFTIRTVSQGGKfPNDAHD 1130
Cdd:pfam01487 3 PLTGKTLEEILEELESGKEGADLVELRVDLLEEPVE-----DAEDVSEQLALLRRVGDLPLIFTFRTKSEGGE-PDGSEE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 1131 AALELIMLAIRSGCEFIDLEITFPEDLLRKVAESK--AHAKIIASHHDPQGKLNWAngSWIQYYNKALQYG-DIIKLVGV 1207
Cdd:pfam01487 77 EYLELLRLALRLGVDYVDVELFLPEEILKELIEAKheGGTKVIGSYHDFEGTPSWE--ELISRYEKMQALGaDIVKIAVM 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 327507643 1208 AETLKDNTALREFKDWAEQAHpDVPVIAINMGDKGQLSRMLNGFL-TPVSHPAL--PFKAAPGQLSAAEIRKGL 1278
Cdd:pfam01487 155 AKSIEDVLALLRFTSEMKSLA-DKPLIAMSMGELGRISRVLGPIFgSPVTFAALglAEKSAPGQLTAKELREAL 227
|
|
| DOIS |
cd08197 |
2-deoxy-scyllo-inosose synthase (DOIS) catalyzes carbocycle formation from ... |
23-387 |
3.78e-71 |
|
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: 242.87 E-value: 3.78e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 23 GTYIVQDLLTNLPST---TYVLVTDTNLGSIYREKFAKIFNEAAAalsPAPRLLtkeIPPGENSKSRQGKADIEDWMLQQ 99
Cdd:cd08197 7 GRGILESLLSILEELkadRHFLVTDSNVNDLYGDRLLEGLKKAGI---PVELLV---VPAGESNKTLSTLTELAERLIAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 100 TCGRDTVIIALGGGVIGDLLGFVAATYMRGIRFVQVPTTLLAMVDSSIGGKTAIDTPLGKNLIGAIWQPHRIYIDIDFID 179
Cdd:cd08197 81 GITRRSVIIALGGGVVGNIAGLLAGLLYRGIRLVHVPTTLLAQSDSVLSLKQAVNGKSGKNLVGSYYAPLFVFVDTEFLK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 180 TLPEREFINGMAEVIKTAAISDEKEFAALEQHADAILKAArskpgkgrFDLVRQVVKDrivaSARHKAFVVTAD--EREG 257
Cdd:cd08197 161 TLPPRQIRSGLCEAIKNALIQDPEFLDYLEDYLNSDLDYD--------PEFLEKVIDL----SIEAKLEVLSNDpyEKKE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 258 GLrnLLNLGHSIGHAIEAILSPQVLHGECVAIGMVKELDLARYLGILKPVAVSRMVKCLSKYGLPTSLKDsrvrkhtagk 337
Cdd:cd08197 229 GL--ILEYGHTVGHAIELLSGGELSHGEAVAIGMCVAAEISHLLGLLSEEDVDKHYELLEKIGLPTIIPD---------- 296
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 327507643 338 HCSLEQMMANMALDKK-----NDGPRKKVVLLSAIGQTYEPKASV---VSNEDIRAVL 387
Cdd:cd08197 297 GISVEAILEVIRYDNKrgyikADADTIRMVLLEKLGKPANPDGDYltpVPEEIVKEAL 354
|
|
| aroD |
TIGR01093 |
3-dehydroquinate dehydratase, type I; This model detects 3-dehydroquinate dehydratase, type I, ... |
1047-1278 |
9.85e-70 |
|
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: 233.81 E-value: 9.85e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 1047 SFFMSLTLTDLRDSGDLLRTVAS-GSDAVELRVDLLKDPSSGNgipSAEYVAEQISFyrSRVSLPIVFTIRTVSQGGKFP 1125
Cdd:TIGR01093 1 KIFVPLTAPDLEEALAEAEKICEkGADIVELRVDLLKDVSSNN---DVDALSEQLSE--LRVDKPLIFTIRTQSEGGKFP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 1126 NDAHDAALELIMLAIRSGCEFIDLEITFPEDLLRKVAES--KAHAKIIASHHDPQGKLNWANgsWIQYYNKALQY-GDII 1202
Cdd:TIGR01093 76 GNEEEYFEELKRAAESLGPDFVDIELFLPDDAVKELINIakKGGTKIIMSNHDFQKTPSWEE--IVERLRKALSYgADIV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 327507643 1203 KLVGVAETLKDNTALREFKDWAeQAHPDVPVIAINMGDKGQLSRMLNGFLTPVSHP-ALPFKAAPGQLSAAEIRKGL 1278
Cdd:TIGR01093 154 KIAVMANSKEDVLTLLSATNKV-DTHYDVPLITMSMGDRGKISRVLGAVFGSVLTFgSLGKASAPGQISVDDLRELL 229
|
|
| PRK11861 |
PRK11861 |
bifunctional prephenate dehydrogenase/3-phosphoshikimate 1-carboxyvinyltransferase; Provisional |
408-830 |
3.78e-67 |
|
bifunctional prephenate dehydrogenase/3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
Pssm-ID: 183343 [Multi-domain] Cd Length: 673 Bit Score: 241.15 E-value: 3.78e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 408 PGSKSISNRALVLAALGSGTVRVKNLLHSDDTEVMLNALERLGAATfawEDEGEVLVVNGNGGKMQASPTELYLGNAGTA 487
Cdd:PRK11861 258 PGSKSISNRVLLLAALAEGETTVTNLLDSDDTRVMLDALTKLGVKL---SRDGGTCVVGGTRGAFTAKTADLFLGNAGTA 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 488 SRFLTSVATLSGKgsvDYNIlTGNNRMKQRPIGDLVDALTINGAQVEYLEKAGSLPLKIAASGGFKGGRINLAAKVSSQY 567
Cdd:PRK11861 335 VRPLTAALAVNGG---EYRI-HGVPRMHERPIGDLVDGLRQIGARIDYEGNEGFPPLRIRPATISVDAPIRVRGDVSSQF 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 568 VSSLLMCAPY--AKEPVTLKLVGGRPISLSYIEMTTAMMRSFGIDVQKSTTEEWTyhIPQG-SYNNPPEYVIESDASSAT 644
Cdd:PRK11861 411 LTALLMTLPLvkAKDGASVVEIDGELISKPYIEITIKLMARFGVTVERDGWQRFT--VPAGvRYRSPGTIMVEGDASSAS 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 645 YPLAIAAVTGTTCTVPNIGSASLQGDARFAvEVLRPMGCKVEQTATSTTVTGPA--DGVLRPLpNVDMEPMTDAFLGASV 722
Cdd:PRK11861 489 YFLAAGALGGGPLRVEGVGRASIQGDVGFA-NALMQMGANVTMGDDWIEVRGIGhdHGRLAPI-DMDFNLIPDAAMTIAV 566
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 723 LAAIAQGeggnhATRIYGIANQRVKECNRIEAMRVELAKFGVVCREHPDGLEIDGIDRSTlrhPAGGVFCYDDHRVAFSF 802
Cdd:PRK11861 567 AALFADG-----PSTLRNIGSWRVKETDRIAAMATELRKVGATVEEGADYLVVTPPAQLT---PNASIDTYDDHRMAMCF 638
|
410 420
....*....|....*....|....*...
gi 327507643 803 SILSLvAPTPTLILEKECVGKTWPTYWD 830
Cdd:PRK11861 639 SLVSL-GGVPVRINDPKCVGKTFPDYFD 665
|
|
| AroE |
COG0169 |
Shikimate 5-dehydrogenase [Amino acid transport and metabolism]; Shikimate 5-dehydrogenase is ... |
1287-1567 |
7.45e-66 |
|
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: 224.25 E-value: 7.45e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 1287 KKFAIFGKPVSVSRSPAMHNTLFEQNGLPYVYTRLETDqAQDVKEFI---RSPDFGGASATIPLKLDIIPLIDEVLNEAE 1363
Cdd:COG0169 5 RLYGVIGDPIAHSLSPAIHNAAFAALGLDAVYVAFDVP-PEDLAAAVaglRALGIRGLNVTIPHKEAAIPLLDELDPRAR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 1364 IIGAVNTIIPVEGkdgstRLIGRNTDWSGIVRCLREAGAhsNEGESSALVIGGGGTARAAIYALHNMGFSTVYVLGRSPE 1443
Cdd:COG0169 84 LIGAVNTVVFEDG-----RLIGDNTDGIGFVRALREAGV--DLAGKRVLVLGAGGAARAVAAALAEAGAAEITIVNRTPE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 1444 KIQNMASTFPtgfdIRVLENAsDIENIPRVA--------VGTIPGDR-PIEAnmrEILctifersgraadgKSAAVLLEM 1514
Cdd:COG0169 157 RAEALAARLG----VRAVPLD-DLAAALAGAdlvinatpLGMAGGDAlPLPA---SLL-------------APGAVVYDL 215
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 327507643 1515 AYKPSVTPLMQLASDSGWTTIPGLEALVGQGVYQFEYWTGITPVYEVARNAVL 1567
Cdd:COG0169 216 VYNPLETPLLRAARARGARVIDGLGMLVHQAAEAFELWTGVRPPVEAMRAALR 268
|
|
| DHQ-like |
cd08169 |
Dehydroquinate synthase-like which includes dehydroquinate synthase, 2-deoxy-scyllo-inosose ... |
39-368 |
4.39e-61 |
|
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: 212.65 E-value: 4.39e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 39 YVLVTDTNLGSIYREKFAKIFnEAAAALSPAPrlltkeIPPGENSKSRQGKADIEDWMLQQTCGRDTVIIALGGGVIGDL 118
Cdd:cd08169 26 CLIIVDSGVPDLIVNYLAEYF-GYYLEVHVFI------IQGGEAYKTFQTVVEELERAAALHLNRHSAVVAVGGGATGDV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 119 LGFVAATYMRGIRFVQVPTTLLAMVDSSIGGKTAIDTPLGKNLIGAIWQPHRIYIDIDFIDTLPEREFINGMAEVIKTAA 198
Cdd:cd08169 99 VGFAAATYFRGIAFIRVPTTLLAQSDSSVGIKVGINTRGGKNLLGAFYPPRAVFADFSFLKTLPFRQVRAGMAELVKMAL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 199 ISDEKEFAALEQHADAIlkaarskpgkgRFDLVRQVvkDRIVASARH-KAFVVTADEREGGLRNLLNLGHSIGHAIEAIL 277
Cdd:cd08169 179 IADNDFFEFLEDKANSA-----------TVYSPEQL--EKLINKCISlKLDVVVADEDEQGKRRGLNYGHTFGHALELAS 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 278 SPQVLHGECVAIGMVKELDLARYLGILKPVAVSRMVKCLSKYGLPTSLKDSRvrkhtagkhcSLEQMMANMALDKKNDGP 357
Cdd:cd08169 246 GYKIPHGEAVAVGMAYAAKIANRLGLLPEHDVSRIIWLLNKLGLPLDHPLAL----------DPDSLYEYLESDKKSLYG 315
|
330
....*....|.
gi 327507643 358 RKKVVLLSAIG 368
Cdd:cd08169 316 NLGMILLSGVG 326
|
|
| EPT-like |
cd01554 |
Enol pyruvate transferases family includes EPSP synthases and UDP-N-acetylglucosamine ... |
408-833 |
2.81e-59 |
|
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: 210.54 E-value: 2.81e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 408 PGSKSISNRALVLAALGSGTVRVKNLLHSDDTEVMLNALERLGAatfAWEDEGEVLVVNGNGGKMQASPT-ELYLGNAGT 486
Cdd:cd01554 8 PGDKSISHRSLIFASLAEGETKVYNILRGEDVLSTMQVLRDLGV---EIEDKDGVITIQGVGMAGLKAPQnALNLGNSGT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 487 ASRFLTSVATLsGKGSVdynILTGNNRMKQRPIGDLVDALTINGAQVEYLEKAGSLPLKIaaSGGFKGGRINLAAKVSSQ 566
Cdd:cd01554 85 AIRLISGVLAG-ADFEV---ELFGDDSLSKRPMDRVTLPLKKMGASISGQEERDLPPLLK--GGKNLGPIHYEDPIASAQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 567 YVSSLLMCAPYAKEPVTLKLVGGRPislsYIEMTTAMMRSFGIDVQKSTTEEWTYHIPQgSYNNpPEYVIESDASSATYP 646
Cdd:cd01554 159 VKSALMFAALLAKGETVIIEAAKEP----TINHTENMLQTFGGHISVQGTKKIVVQGPQ-KLTG-QKYVVPGDISSAAFF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 647 LAIAAVTGTTCTVPNIGSASlqGDARFAvEVLRPMGCKVEQTATSTTVT-GPADGVlrplpNVDMEP---MTDAFLGASV 722
Cdd:cd01554 233 LVAAAIAPGRLVLQNVGINE--TRTGII-DVLRAMGAKIEIGEDTISVEsSDLKAT-----EICGALiprLIDELPIIAL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 723 LAAIAQGeggnhATRIYGIANQRVKECNRIEAMRVELAKFGVVCREHPDGLEIDGIDRSTlrhpAGGVFCYDDHRVAFSF 802
Cdd:cd01554 305 LALQAQG-----TTVIKDAEELKVKETDRIFVVADELNSMGADIEPTADGMIIKGKEKLH----GARVNTFGDHRIGMMT 375
|
410 420 430
....*....|....*....|....*....|.
gi 327507643 803 SILSLVAPTPTLILEKECVGKTWPTYWDALK 833
Cdd:cd01554 376 ALAALVADGEVELDRAEAINTSYPSFFDDLE 406
|
|
| DHQase_I |
cd00502 |
Type I 3-dehydroquinase, (3-dehydroquinate dehydratase or DHQase); Type I 3-dehydroquinase, ... |
1047-1280 |
1.87e-58 |
|
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: 201.41 E-value: 1.87e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 1047 SFFMSLTLTDLRDSGDLLRTVASGSDAVELRVDLLKDPSsgngipsAEYVAEQISFYRSRVSLPIVFTIRTVSQGGKFPn 1126
Cdd:cd00502 1 KICVPLTGPDLLEEALSLLELLLGADAVELRVDLLEDPS-------IDDVAEQLSLLRELTPLPIIFTVRTKSEGGNFE- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 1127 DAHDAALELIMLAIRSGCEFIDLEITF--PEDLLRKVAesKAHAKIIASHHDPQGKLNwaNGSWIQYYNKALQYG-DIIK 1203
Cdd:cd00502 73 GSEEEYLELLEEALKLGPDYVDIELDSalLEELINSRK--KGNTKIIGSYHDFSGTPS--DEELVSRLEKMAALGaDIVK 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 327507643 1204 LVGVAETLKDNTALREFKDWAEqAHPDVPVIAINMGDKGQLSRMLNG-FLTPVSHPALPFKAAPGQLSAAEIRKGLSI 1280
Cdd:cd00502 149 IAVMANSIEDNLRLLKFTRQVK-NLYDIPLIAINMGELGKLSRILSPvFGSPLTYASLPEPSAPGQLSVEELKQALSL 225
|
|
| aroE |
PRK00258 |
shikimate 5-dehydrogenase; Reviewed |
1287-1567 |
1.18e-57 |
|
shikimate 5-dehydrogenase; Reviewed
Pssm-ID: 234703 [Multi-domain] Cd Length: 278 Bit Score: 200.80 E-value: 1.18e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 1287 KKFAIFGKPVSVSRSPAMHNTLFEQNGLPYVYTRLETDqAQDVKEFIRS---PDFGGASATIPLKLDIIPLIDEVLNEAE 1363
Cdd:PRK00258 6 RLYAVIGNPIAHSKSPLIHNAAFKQLGLDGVYLAILVP-PEDLEDAVKGffaLGGRGANVTVPFKEAAFALADELSERAR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 1364 IIGAVNTIIPVEGkdgstRLIGRNTDWSGIVRCLREAGAHSNEGESsALVIGGGGTARAAIYALHNMGFSTVYVLGRSPE 1443
Cdd:PRK00258 85 LIGAVNTLVLEDG-----RLIGDNTDGIGFVRALEERLGVDLKGKR-ILILGAGGAARAVILPLLDLGVAEITIVNRTVE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 1444 KIQNMASTFPTGFDIRVLENASDIENIPRVAVGTIP----GDRPIEANMREILctifersgraadgKSAAVLLEMAYKPS 1519
Cdd:PRK00258 159 RAEELAKLFGALGKAELDLELQEELADFDLIINATSagmsGELPLPPLPLSLL-------------RPGTIVYDMIYGPL 225
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 327507643 1520 VTPLMQLASDSGWTTIPGLEALVGQGVYQFEYWTGITPVYEVARNAVL 1567
Cdd:PRK00258 226 PTPFLAWAKAQGARTIDGLGMLVHQAAEAFELWTGVRPPVEPMLAALR 273
|
|
| PRK14021 |
PRK14021 |
bifunctional shikimate kinase/3-dehydroquinate synthase; Provisional |
77-369 |
5.41e-52 |
|
bifunctional shikimate kinase/3-dehydroquinate synthase; Provisional
Pssm-ID: 184458 [Multi-domain] Cd Length: 542 Bit Score: 193.15 E-value: 5.41e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 77 IPPGENSKSRQGKADIEDWMLQQTCGRDTVIIALGGGVIGDLLGFVAATYMRGIRFVQVPTTLLAMVDSSIGGKTAIDTP 156
Cdd:PRK14021 243 IPDAEAGKTIEVANGIWQRLGNEGFTRSDAIVGLGGGAATDLAGFVAATWMRGIRYVNCPTSLLAMVDASTGGKTGINTP 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 157 LGKNLIGAIWQPHRIYIDIDFIDTLPEREFINGMAEVIKTAAISDEKEFAALEQHADAIlkaaRSKPGKGRFDL-VRQVV 235
Cdd:PRK14021 323 QGKNLVGSFYTPAGVLADTKTLATLPNDIFIEGLGEVAKSGFIRDPEILRILEDHAAEL----RAFDGSTFLGSpLEDVV 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 236 KDRIVASARHKAFVVTADEREGGLRNLLNLGHSIGHAIEAILSPQVLHGECVAIGMVKELDLARYLGILKPVAVSRMVKC 315
Cdd:PRK14021 399 AELIERTVKVKAYHVSSDLKEAGLREFLNYGHTLGHAIEKLEHFRWRHGNAVAVGMVYAAELAHLLGYIDQDLVDYHRSL 478
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 327507643 316 LSKYGLPTSLKDSrvrkhtagkhcSLEQMMANMALDKKNDGPRKKVVLLSAIGQ 369
Cdd:PRK14021 479 LASLGLPTSWNGG-----------SFDDVLALMHRDKKARGNELRFVVLDEIGH 521
|
|
| EEVS |
cd08199 |
2-epi-5-epi-valiolone synthase (EEVS); 2-epi-5-epi-valiolone synthase catalyzes the ... |
40-369 |
8.97e-52 |
|
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: 186.58 E-value: 8.97e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 40 VLVTDTNLGSIYREKFAKIFNEAAAALspapRLLTkeIPPGENSKSRQGKADIEDWMLQQTCGRDTVIIALGGGVIGDLL 119
Cdd:cd08199 30 LVVVDENVDRLYGARIRAYFAAHGIEA----TILV--LPGGEANKTMETVLRIVDALDDFGLDRREPVIAIGGGVLLDVV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 120 GFVAATYMRGIRFVQVPTTLLAMVDSSIGGKTAIDTPLGKNLIGAIWQPHRIYIDIDFIDTLPEREFINGMAEVIKTAAI 199
Cdd:cd08199 104 GFAASLYRRGVPYIRVPTTLLGLVDAGVGIKTGVNFGGHKNRLGAYYPPVATLLDRSFLKTLPRRHIRNGLAEIIKMALV 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 200 SDEKEFAALEQHADAILKAarskpgkgRFDLvrQVVKDRIVasarHKAFVVTADE-----REGGLRNLLNLGHSIGHAIE 274
Cdd:cd08199 184 KDAELFELLEEHGAALVET--------RFFQ--DEVADEII----RRAIQGMLEElapnlWEHDLERLVDFGHTFSPILE 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 275 AILSPQVLHGECVAIGMVKELDLARYLGILKPVAVSRMVKCLSKYGLPTSlkdsrvrkHTagkHCSLEQMM-ANMALDKK 353
Cdd:cd08199 250 MAAAPELLHGEAVAIDMALSAVLAYRRGLLSEEELDRILRLMRRLGLPVW--------HP---LCTPDLLWrALEDIVKH 318
|
330
....*....|....*.
gi 327507643 354 NDGpRKKVVLLSAIGQ 369
Cdd:cd08199 319 RDG-LQRLPLPKGIGE 333
|
|
| SK |
cd00464 |
Shikimate kinase (SK) is the fifth enzyme in the shikimate pathway, a seven-step biosynthetic ... |
861-1005 |
1.13e-48 |
|
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: 170.43 E-value: 1.13e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 861 SIVIIGMRGAGKTTTGRWAAKALNRKFIDLDVELEQTEGKTIPDLIKERGWKGFRDAELSLFKRALTerPTGHVFACGGG 940
Cdd:cd00464 1 NIVLIGMMGAGKTTVGRLLAKALGLPFVDLDELIEQRAGMSIPEIFAEEGEEGFRELEREVLLLLLT--KENAVIATGGG 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 327507643 941 IVEIAEARNilidYHKNKGNVLLVMRDIKKVMEFLNIDKTRPAY----IEDMMSVWLRRKPWYQECSNV 1005
Cdd:cd00464 79 AVLREENRR----LLLENGIVVWLDASPEELLERLARDKTRPLLqdedPERLRELLEEREPLYREVADL 143
|
|
| SKI |
pfam01202 |
Shikimate kinase; |
868-1031 |
2.77e-45 |
|
Shikimate kinase;
Pssm-ID: 426122 [Multi-domain] Cd Length: 159 Bit Score: 160.83 E-value: 2.77e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 868 RGAGKTTTGRWAAKALNRKFIDLDVELEQTEGKTIPDLIKERGWKGFRDAELSLFKRALTERptGHVFACGGGIVEIAEA 947
Cdd:pfam01202 1 MGAGKSTIGRLLAKALGLPFIDTDEEIEKRTGMSIAEIFEEEGEEGFRRLESEVLKELLAEH--GLVIATGGGAVLSEEN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 948 RNILidyhKNKGNVLLVMRDIKKVMEFLNIDKTRPAYIEDMMSVWLRRKPWYQECSNVQYYSRHSSSPELALAMDDFDRF 1027
Cdd:pfam01202 79 RDLL----KERGIVIYLDAPLEVLLERLKRDKTRPLLQNKDPEEELLELLFEERDPLYEEAADIVIDTDESSPEEVATEI 154
|
....
gi 327507643 1028 IQFV 1031
Cdd:pfam01202 155 LEAL 158
|
|
| PLN02520 |
PLN02520 |
bifunctional 3-dehydroquinate dehydratase/shikimate dehydrogenase |
1061-1555 |
4.16e-43 |
|
bifunctional 3-dehydroquinate dehydratase/shikimate dehydrogenase
Pssm-ID: 178135 [Multi-domain] Cd Length: 529 Bit Score: 166.09 E-value: 4.16e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 1061 GDLLRTVASGSDAVELRVDLLKDPSSGNGIPsaeyvaeqisFYRSRVSLPIVFTIRTVSQGGKFPNDaHDAALELIMLAI 1140
Cdd:PLN02520 39 IEMAKAKELGADLVEIRLDFLKNFNPREDLK----------TLIKQSPLPTLVTYRPKWEGGQYEGD-ENKRQDALRLAM 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 1141 RSGCEFIDLEITFPEDLLRKVAESK-AHAKIIASHHDPQgklNWANGSWIQYYNKALQY--GDIIKLVGVAETLKDNTal 1217
Cdd:PLN02520 108 ELGADYVDVELKVAHEFINSISGKKpEKCKVIVSSHNYE---NTPSVEELGNLVARIQAtgADIVKIATTALDITDVA-- 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 1218 REFKdwaEQAHPDVPVIAINMGDKGQLSRML----NGFLTPVSHPAlPFKAAPGQLSAAEIRKGLSIMGEIP-AKKFAIF 1292
Cdd:PLN02520 183 RMFQ---ITVHSQVPTIGLVMGERGLISRILcpkfGGYLTFGTLEA-GKVSAPGQPTIKDLLDLYNFRQIGPdTKVYGII 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 1293 GKPVSVSRSPAMHNTLFEQNGLPYVYTRLETDqaqDVKEFIR---SPDFGGASATIPLKLDIIPLIDEVLNEAEIIGAVN 1369
Cdd:PLN02520 259 GKPVGHSKSPILHNEAFKSVGFNGVYVHLLVD---DLAKFLQtysSPDFAGFSCTIPHKEDALKCCDEVDPIAKSIGAIN 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 1370 TII--PVEGKdgstrLIGRNTDWSGIVRCLREA--GAHSNEGESSAL------VIGGGGTARAAIYALHNMGfSTVYVLG 1439
Cdd:PLN02520 336 TIIrrPSDGK-----LVGYNTDYIGAISAIEDGlrASGSSPASGSPLagklfvVIGAGGAGKALAYGAKEKG-ARVVIAN 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 1440 RSPEKIQNMASTFpTGFDIR-------------VLENASDIENIPRVAVGTIPgdrpieanmREILctifersgraadgK 1506
Cdd:PLN02520 410 RTYERAKELADAV-GGQALTladlenfhpeegmILANTTSVGMQPNVDETPIS---------KHAL-------------K 466
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 327507643 1507 SAAVLLEMAYKPSVTPLMQLASDSGWTTIPGLEALVGQGVYQFEYWTGI 1555
Cdd:PLN02520 467 HYSLVFDAVYTPKITRLLREAEESGAIIVSGTEMFIRQAYEQFERFTGL 515
|
|
| aroE |
TIGR00507 |
shikimate dehydrogenase; This model finds proteins from prokaryotes and functionally ... |
1287-1568 |
1.89e-39 |
|
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: 148.33 E-value: 1.89e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 1287 KKFAIFGKPVSVSRSPAMHNTLFEQNGLPYVYTRLET--DQAQDVKEFIRSPDFGGASATIPLKLDIIPLIDEVLNEAEI 1364
Cdd:TIGR00507 1 KLYGVIGNPIAHSKSPLIHNAFFKQLGLEGPYIAFLVppDDLEDALSGFFALGFKGANVTSPFKERAFQFLDEIDGRAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 1365 IGAVNTIIPVEGKdgstrLIGRNTDWSGIVRCLREAGAHSNegESSALVIGGGGTARAAIYALHNMGfSTVYVLGRSPEK 1444
Cdd:TIGR00507 81 AGAVNTLVLEDGK-----LVGYNTDGIGLVSDLEQLIPLRP--NQNVLIIGAGGAAKAVALELLKAD-CNVIIANRTVSK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 1445 IQNMASTFP-TGFDIRVLENASDIENIPRVAVGTIPGDRPieanmreilcTIFERSGRAADGKSAAVLLEMAYKPSVTPL 1523
Cdd:TIGR00507 153 AEELAERFQrYGEIQAFSMDELPLHRVDLIINATSAGMSG----------NIDEPPVPAEYLKEGKLVYDLVYNPLETPF 222
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 327507643 1524 MQLASDSGWTTIPGLEALVGQGVYQFEYWTGITPVYEVARNAVLG 1568
Cdd:TIGR00507 223 LAEAKSLGTKTIDGLGMLVYQAALSFELWTGVEPDIEKMFEQLIS 267
|
|
| NAD_bind_Shikimate_DH |
cd01065 |
NAD(P) binding domain of Shikimate dehydrogenase; Shikimate dehydrogenase (DH) is an amino ... |
1388-1554 |
9.59e-37 |
|
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: 136.25 E-value: 9.59e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 1388 TDWSGIVRCLREAGAHSNEGesSALVIGGGGTARAAIYALHNMGFSTVYVLGRSPEKIQNMASTFPTGFDIRVLENASDI 1467
Cdd:cd01065 1 TDGLGFVRALEEAGIELKGK--KVLILGAGGAARAVAYALAELGAAKIVIVNRTLEKAKALAERFGELGIAIAYLDLEEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 1468 ENIPRVAVGTIPGDrpieanMREILCTIFErsgrAADGKSAAVLLEMAYKPSVTPLMQLASDSGWTTIPGLEALVGQGVY 1547
Cdd:cd01065 79 LAEADLIINTTPVG------MKPGDELPLP----PSLLKPGGVVYDVVYNPLETPLLKEARALGAKTIDGLEMLVYQAAE 148
|
....*..
gi 327507643 1548 QFEYWTG 1554
Cdd:cd01065 149 AFELWTG 155
|
|
| aroB |
PRK06203 |
3-dehydroquinate synthase; Reviewed |
59-372 |
9.50e-36 |
|
3-dehydroquinate synthase; Reviewed
Pssm-ID: 235740 Cd Length: 389 Bit Score: 141.19 E-value: 9.50e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 59 FNEAAAALSPAPRLltkeIPPGENSK-SRQGKADIEDWMLQQTCGRDTVIIALGGGVIGDLLGFVAATYMRGIRFVQVPT 137
Cdd:PRK06203 70 AHADVLELVAEPLV----VPGGEAAKnDPALVEALHAAINRHGIDRHSYVLAIGGGAVLDMVGYAAATAHRGVRLIRIPT 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 138 TLLAMVDSSIGGKTAIDTPLGKNLIGAIWQPHRIYIDIDFIDTLPEREFINGMAEVIKTAAISDEKEFAALEQHADAIlk 217
Cdd:PRK06203 146 TVLAQNDSGVGVKNGINAFGKKNFLGTFAPPYAVINDFAFLTTLPDRDWRAGLAEAVKVALIKDAAFFDWLEAHAAAL-- 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 218 aarskpgkGRFDLvrQVVKDRIVASAR-HKAFVVTA-DEREGGLRNLLNLGHSIGHAIEAILSPQVLHGECVAIGMVkeL 295
Cdd:PRK06203 224 --------AARDP--EAMEELIYRCAElHLEHIAGGgDPFEFGSSRPLDFGHWSAHKLEQLTNYALRHGEAVAIGIA--L 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 296 DlARY---LGILKPVAVSRMVKCLSKYGLPTSlkdsrvrkH-----TAGKHCSLEQmmanmALD--KKNDGPRKKVVLLS 365
Cdd:PRK06203 292 D-SLYsylLGLLSEAEAQRILALLRALGFPLY--------HpalatRDSKGRELLK-----GLEefREHLGGRLTITLLT 357
|
....*..
gi 327507643 366 AIGQTYE 372
Cdd:PRK06203 358 GIGRGIE 364
|
|
| DHQS-like |
cd08198 |
Dehydroquinate synthase (DHQS) catalyzes the conversion of DAHP to DHQ in shikimate pathway ... |
103-324 |
2.14e-35 |
|
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: 139.24 E-value: 2.14e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 103 RDTVIIALGGGVIGDLLGFVAATYMRGIRFVQVPTTLLAMVDSSIGGKTAIDTPLGKNLIGAIWQPHRIYIDIDFIDTLP 182
Cdd:cd08198 99 RHSYVVVIGGGAVLDAVGFAAAIAHRGIRLIRVPTTVLAQNDSGVGVKNGINFFGKKNFLGTFAPPFAVINDFDFLETLP 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 183 EREFINGMAEVIKTAAISDEKEFAALEQHADAILkaarskpgKGRFDLVRQVVK-------DRIVASarhkafvvtADER 255
Cdd:cd08198 179 DRDWRSGIAEAVKVALIKDASFFEWLERNAAALR--------QRDPDAMEKLIRrcaelhlDHIAAS---------GDPF 241
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 327507643 256 EGGLRNLLNLGHSIGHAIEAILSPQVLHGECVAIGMVkeLD--LARYLGILKPVAVSRMVKCLSKYGLPTS 324
Cdd:cd08198 242 ETGSARPLDFGHWSAHKLEQLSGYALRHGEAVAIGIA--LDslYARLLGLLSREDFDRILALLQNLGLPLW 310
|
|
| AroK |
COG0703 |
Shikimate kinase [Amino acid transport and metabolism]; Shikimate kinase is part of the ... |
862-1005 |
3.33e-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: 3.33e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 862 IVIIGMRGAGKTTTGRWAAKALNRKFIDLDVELEQTEGKTIPDLIKERGWKGFRDAELSLFKRALTERPTghVFACGGGI 941
Cdd:COG0703 1 IVLIGMMGAGKSTVGRLLAKRLGLPFVDTDAEIEERAGMSIPEIFAEEGEAGFRELEREVLAELLEEENA--VIATGGGA 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 327507643 942 VEIAEARNILidyhKNKGNVLLVMRDIKKVMEFLNIDKTRP--------AYIEDMMSvwlRRKPWYQECSNV 1005
Cdd:COG0703 79 VLSPENRELL----KEHGTVVYLDASPETLLERLRRDDNRPllqgedprERLEELLA---EREPLYREVADI 143
|
|
| PRK14806 |
PRK14806 |
bifunctional cyclohexadienyl dehydrogenase/ 3-phosphoshikimate 1-carboxyvinyltransferase; ... |
408-840 |
3.91e-34 |
|
bifunctional cyclohexadienyl dehydrogenase/ 3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
Pssm-ID: 237820 [Multi-domain] Cd Length: 735 Bit Score: 141.67 E-value: 3.91e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 408 PGSKSISNRALVLAALGSGTVRVKNLLHSDDTEVMLNALERLGaATFAWEDEGEVlVVNGNGGK-MQASPTELYLGNAGT 486
Cdd:PRK14806 319 PGDKSISHRSIMLGSLAEGVTEVEGFLEGEDALATLQAFRDMG-VVIEGPHNGRV-TIHGVGLHgLKAPPGPLYMGNSGT 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 487 ASRFLTSVatLSGKgSVDyNILTGNNRMKQRPIGDLVDALTINGAQVEYLEKaGSLPLKIAASGGFKGGRINLAAkVSSQ 566
Cdd:PRK14806 397 SMRLLSGL--LAAQ-SFD-SVLTGDASLSKRPMERVAKPLREMGAVIETGEE-GRPPLSIRGGQRLKGIHYDLPM-ASAQ 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 567 YVSSLLMCAPYAK------EPVTlklvggrpiSLSYIEMttaMMRSFGIDVQkstTEEWTYHIPQGSYNNPPEYVIESDA 640
Cdd:PRK14806 471 VKSCLLLAGLYAEgetsvtEPAP---------TRDHTER---MLRGFGYPVK---VEGNTISVEGGGKLTATDIEVPADI 535
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 641 SSATYPLAIAAVT-GTTCTVPNIGSASlqgdARFAV-EVLRPMGCKVEqTATSTTVTGP--ADGVLR--PLPNVDMEP-- 712
Cdd:PRK14806 536 SSAAFFLVAASIAeGSELTLEHVGINP----TRTGViDILKLMGADIT-LENEREVGGEpvADIRVRgaRLKGIDIPEdq 610
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 713 ---MTDAFLGASVLAAIAQGEggnhaTRIYGIANQRVKECNRIEAMRVELAKFGVVCREHPDGLEIDGidrstlRHPAGG 789
Cdd:PRK14806 611 vplAIDEFPVLFVAAACAEGR-----TVLTGAEELRVKESDRIQVMADGLKTLGIDCEPTPDGIIIEG------GIFGGG 679
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 327507643 790 -VFCYDDHRVAFSFSILSLVAPTPTLILEKECVGKTWPTYwDALKQKFGVSL 840
Cdd:PRK14806 680 eVESHGDHRIAMSFSVASLRASGPITIHDCANVATSFPNF-LELANQVGIRI 730
|
|
| AroD |
COG0710 |
3-dehydroquinate dehydratase [Amino acid transport and metabolism]; 3-dehydroquinate ... |
1058-1283 |
3.97e-33 |
|
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: 128.87 E-value: 3.97e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 1058 RDSGDLLRTVA----SGSDAVELRVDLLKDPSsgngipsAEYVAEQISFYRSRVSLPIVFTIRTVSQGGKFPNDaHDAAL 1133
Cdd:COG0710 13 ATPEDLLAEAEaaarAGADLVELRLDYLEDPD-------LEELKELLEALREYGGLPLIFTFRTAEEGGEFEGS-EEERL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 1134 ELIMLAIRS-GCEFIDLEITFPEDLLRKVAES--KAHAKIIASHHD-----PQGKLnwangswIQYYNKALQYG-DIIKL 1204
Cdd:COG0710 85 ELLRAAADSaGVDLVDVELDTLEDDVDDLIEAarEAGVKVIVSYHDfektpSAEEL-------VEILEKMQELGaDIVKI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 1205 VGVAETLKDNTALREFKDWAEQaHPDVPVIAINMGDKGQLSR----MLNGFLT--PVSHPalpfkAAPGQLSAAEIRKGL 1278
Cdd:COG0710 158 AVMAKSPEDVLRLLEATLEAKE-ELDRPVITMAMGELGKISRilgpLFGSALTyaSVGEA-----SAPGQIDVEELRELL 231
|
....*
gi 327507643 1279 SIMGE 1283
Cdd:COG0710 232 ELLEA 236
|
|
| PRK13951 |
PRK13951 |
bifunctional shikimate kinase AroK/3-dehydroquinate synthase AroB; |
53-304 |
2.15e-31 |
|
bifunctional shikimate kinase AroK/3-dehydroquinate synthase AroB;
Pssm-ID: 172457 [Multi-domain] Cd Length: 488 Bit Score: 130.41 E-value: 2.15e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 53 EKFAKIFNEAAaalsPAPRLLtkeIPPGENSKSRQGKADIEDWMLQQTCGRDTVIIALGGGVIGDLLGFVAATYMRGIRF 132
Cdd:PRK13951 194 ERVEKIYGRYL----PENRLL---FPDGEEVKTLEHVSRAYYELVRMDFPRGKTIAGVGGGALTDFTGFVASTFKRGVGL 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 133 VQVPTTLLAMVDSSIGGKTAIDTPLGKNLIGAIWQPHRIYIDIDFIDTLPEREFINGMAEVIKTAAIS--DEKEFAALEQ 210
Cdd:PRK13951 267 SFYPTTLLAQVDASVGGKNAIDFAGVKNVVGTFRMPDYVIIDPTVTLSMDEGRFEEGVVEAFKMTILSgrGVELFDEPEK 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 211 hadaILKAarskpgkgRFDLVRQVVKdrivASARHKAFVVTADEREGGLRNLLNLGHSIGHAIEAILSpqVLHGECVAIG 290
Cdd:PRK13951 347 ----IEKR--------NLRVLSEMVK----ISVEEKARIVMEDPYDMGLRHALNLGHTLGHVYEMLEG--VPHGIAVAWG 408
|
250
....*....|....
gi 327507643 291 MVKELDLARYLGIL 304
Cdd:PRK13951 409 IEKETMYLYRKGIV 422
|
|
| Shikimate_dh_N |
pfam08501 |
Shikimate dehydrogenase substrate binding domain; This domain is the substrate binding domain ... |
1291-1371 |
2.10e-27 |
|
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: 106.91 E-value: 2.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 1291 IFGKPVSVSRSPAMHNTLFEQNGLPYVYTRLET--DQAQDVKEFIRSPDFGGASATIPLKLDIIPLIDEVLNEAEIIGAV 1368
Cdd:pfam08501 1 VIGNPISHSLSPAIHNAAFKALGLNGVYVAFEVppDNLPDFVEGLRALGFRGLNVTIPHKEAAIPLLDELSPEAKAIGAV 80
|
...
gi 327507643 1369 NTI 1371
Cdd:pfam08501 81 NTI 83
|
|
| aroK |
PRK00131 |
shikimate kinase; Reviewed |
861-1004 |
5.15e-26 |
|
shikimate kinase; Reviewed
Pssm-ID: 234654 [Multi-domain] Cd Length: 175 Bit Score: 106.43 E-value: 5.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 861 SIVIIGMRGAGKTTTGRWAAKALNRKFIDLDVELEQTEGKTIPDLIKERGWKGFRDAElslfKRALTE--RPTGHVFACG 938
Cdd:PRK00131 6 NIVLIGFMGAGKSTIGRLLAKRLGYDFIDTDHLIEARAGKSIPEIFEEEGEAAFRELE----EEVLAEllARHNLVISTG 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 327507643 939 GGIVEIAEARNILIDYHKnkgNVLLVMrDIKKVMEFLNIDKTRP--------AYIEDMMSVwlrRKPWYQECSN 1004
Cdd:PRK00131 82 GGAVLREENRALLRERGT---VVYLDA-SFEELLRRLRRDRNRPllqtndpkEKLRDLYEE---RDPLYEEVAD 148
|
|
| PRK12548 |
PRK12548 |
shikimate dehydrogenase; |
1289-1561 |
4.79e-24 |
|
shikimate dehydrogenase;
Pssm-ID: 183585 [Multi-domain] Cd Length: 289 Bit Score: 104.05 E-value: 4.79e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 1289 FAIFGKPVSVSRSPAMHNTLFEQNGLPYVYTRLET--DQAQDVKEFIRSPDFGGASATIPLKLDIIPLIDEVLNEAEIIG 1366
Cdd:PRK12548 12 LGLIGSPVGHSGSPAMYNYSFQKAGLDYAYLAFDIpvDKVPDAIKAIKTFNMRGANVTMPCKSEAAKYMDELSPAARIIG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 1367 AVNTIIPVEGKdgstrLIGRNTDWSGIVRCLREAGAhsnEGESSALVIGGGGTARAAIY---ALHnmGFSTVYVLGRSPE 1443
Cdd:PRK12548 92 AVNTIVNDDGK-----LTGHITDGLGFVRNLREHGV---DVKGKKLTVIGAGGAATAIQvqcALD--GAKEITIFNIKDD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 1444 KIQNMASTFPTgfdIR-----VLENASDIENIPRV----------AVGTIPGDRPIEaNMREILCTIFERSGraadgksa 1508
Cdd:PRK12548 162 FYERAEQTAEK---IKqevpeCIVNVYDLNDTEKLkaeiassdilVNATLVGMKPND-GETNIKDTSVFRKD-------- 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 327507643 1509 AVLLEMAYKPSVTPLMQLASDSGWTTIPGLEALVGQGVYQFEYWTGI-TPVYEV 1561
Cdd:PRK12548 230 LVVADTVYNPKKTKLLEDAEAAGCKTVGGLGMLLWQGAEAYKLYTGKdMPVEEV 283
|
|
| PRK12550 |
PRK12550 |
shikimate 5-dehydrogenase; Reviewed |
1305-1566 |
5.82e-24 |
|
shikimate 5-dehydrogenase; Reviewed
Pssm-ID: 183587 [Multi-domain] Cd Length: 272 Bit Score: 103.50 E-value: 5.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 1305 HNTLFEQNGLPYVYTRLET-DQAQDVKEfIRSPDFGGASATIPLKLDIIPLIDEVLNEAEIIGAVNTIIPVEGkdgstRL 1383
Cdd:PRK12550 27 HNYLYEALGLNFLYKAFTTtDLTAAIGG-VRALGIRGCAVSMPFKEAVIPLVDELDPSAQAIESVNTIVNTDG-----HL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 1384 IGRNTDWSGIVRCLREagaHSNEGESSALVIGGGGTARAAIYALHNMGFSTVYVLGRSPEKIQNMASTFptGFDIRvlen 1463
Cdd:PRK12550 101 KAYNTDYIAIAKLLAS---YQVPPDLVVALRGSGGMAKAVAAALRDAGFTDGTIVARNEKTGKALAELY--GYEWR---- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 1464 aSDIENI-PRVAVGTIPgdrpieanmreilctIFERSGRAADGKS--------AAVLLEMAYKPSVTPLMQLASDSGWTT 1534
Cdd:PRK12550 172 -PDLGGIeADILVNVTP---------------IGMAGGPEADKLAfpeaeidaASVVFDVVALPAETPLIRYARARGKTV 235
|
250 260 270
....*....|....*....|....*....|..
gi 327507643 1535 IPGLEALVGQGVYQFEYWTGITPVYEVARNAV 1566
Cdd:PRK12550 236 ITGAEVIALQAVEQFVLYTGVRPSDELIAEAA 267
|
|
| aroDE |
PRK09310 |
bifunctional 3-dehydroquinate dehydratase/shikimate dehydrogenase; |
1072-1552 |
2.38e-22 |
|
bifunctional 3-dehydroquinate dehydratase/shikimate dehydrogenase;
Pssm-ID: 137204 [Multi-domain] Cd Length: 477 Bit Score: 102.57 E-value: 2.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 1072 DAVELRVDLLKDPSSgngipsaeyvaEQISFYRSRVSLPIVfTIRtvsqggKFPNDAHDAALELIMLAIRSGCEFIDLEI 1151
Cdd:PRK09310 26 DCIELRVDLLLSLSD-----------LELKKLIELAPIPIL-TWK------KHESCSQAAWIDKMQSLAKLNPNYLDIDK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 1152 TFPEDLLRKVAESKAHAKIIASHHDPQgklnwaNGSWIQYYNKAL-QYGDIIKLVGVAETLKDntALREFKdwaEQAHPD 1230
Cdd:PRK09310 88 DFPKEALIRIRKLHPKIKIILSYHTSE------HEDIIQLYNEMLaSAADYYKIAVSSSSSTD--LLNIIH---QKRSLP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 1231 VPVIAINMGDKGQLSRMLNGFLTPVSHPALPFKA---APGQLSAAEIR----KGLSIMGEIpakkFAIFGKPVSVSRSPA 1303
Cdd:PRK09310 157 ENTTVLCMGGMGRPSRILSPLLQNAFNYAAGIGAppvAPGQLSLEHLLfynyANLSAQSPI----YGLIGDPVDRSISHL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 1304 MHNTLFEQNGLPYVYTRLETDqAQDVKEF---IRSPDFGGASATIPLKLDIIPLIDEVLNEAEIIGAVNTIIPVEGKdgs 1380
Cdd:PRK09310 233 SHNPLFSQLSLNCPYIKLPLT-PQELPKFfstIRDLPFLGLSVTMPLKTAVLDFLDKLDPSVKLCGSCNTLVFRNGK--- 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 1381 trLIGRNTDWSGIVRCLREAGAHSNEGESSalVIGGGGTARaAIYALHNMGFSTVYVLGRSPEKIQNMASTFP-TGFDIR 1459
Cdd:PRK09310 309 --IEGYNTDGEGLFSLLKQKNIPLNNQHVA--IVGAGGAAK-AIATTLARAGAELLIFNRTKAHAEALASRCQgKAFPLE 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 1460 VLENASDIENIprvaVGTIPGDrpieanmreilCTIFERsgraadgkSAAVLLEMAYKPSVTPLMQLASDSGWTTIPGLE 1539
Cdd:PRK09310 384 SLPELHRIDII----INCLPPS-----------VTIPKA--------FPPCVVDINTLPKHSPYTQYARSQGSSIIYGYE 440
|
490
....*....|...
gi 327507643 1540 ALVGQGVYQFEYW 1552
Cdd:PRK09310 441 MFAEQALLQFRLW 453
|
|
| PRK12749 |
PRK12749 |
quinate/shikimate dehydrogenase; Reviewed |
1295-1554 |
1.74e-21 |
|
quinate/shikimate dehydrogenase; Reviewed
Pssm-ID: 183721 [Multi-domain] Cd Length: 288 Bit Score: 96.61 E-value: 1.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 1295 PVSVSRSPAMHNTLFEQNGLPYVYTRLETDQAQ--DVKEFIRSPDFGGASATIPLKLDIIPLIDEVLNEAEIIGAVNTII 1372
Cdd:PRK12749 16 PIRHSLSPEMQNKALEKAGLPFTYMAFEVDNDSfpGAIEGLKALKMRGTGVSMPNKQLACEYVDELTPAAKLVGAINTIV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 1373 pveGKDGSTRliGRNTDWSGIVRCLREAGaHSNEGESSALV-IGGGGTARAAIYALHnmGFSTVYVLGRSPEKIQNMASt 1451
Cdd:PRK12749 96 ---NDDGYLR--GYNTDGTGHIRAIKESG-FDIKGKTMVLLgAGGASTAIGAQGAIE--GLKEIKLFNRRDEFFDKALA- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 1452 fptgFDIRVLENASDIENIPRVA----------------VGTIPGDRPIEaNMREILCTIFERSGraadgksaAVLLEMA 1515
Cdd:PRK12749 167 ----FAQRVNENTDCVVTVTDLAdqqafaealasadiltNGTKVGMKPLE-NESLVNDISLLHPG--------LLVTECV 233
|
250 260 270
....*....|....*....|....*....|....*....
gi 327507643 1516 YKPSVTPLMQLASDSGWTTIPGLEALVGQGVYQFEYWTG 1554
Cdd:PRK12749 234 YNPHMTKLLQQAQQAGCKTIDGYGMLLWQGAEQFTLWTG 272
|
|
| DHQ_Fe-ADH |
cd07766 |
Dehydroquinate synthase-like (DHQ-like) and iron-containing alcohol dehydrogenases (Fe-ADH); ... |
103-332 |
4.00e-21 |
|
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: 95.12 E-value: 4.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 103 RDTVIIALGGGVIGDLLGFVAATYMRGIRFVQVPTTLLAmvDSSIGGKTAIDTPLGKNL-IGAIWQPHRIYIDIDFIDTL 181
Cdd:cd07766 77 EADAVIAVGGGSTLDTAKAVAALLNRGIPFIIVPTTAST--DSEVSPKSVITDKGGKNKqVGPHYNPDVVFVDTDITKGL 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 182 PEREFINGMAEVIKTAAISdEKEFAALEQHADAILkaarSKPGkgrfdlvrqvvkdrivasarhkafvvtaderegglrn 261
Cdd:cd07766 155 PPRQVASGGVDALAHAVEL-EKVVEAATLAGMGLF----ESPG------------------------------------- 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 327507643 262 lLNLGHSIGHAIEAILspQVLHGECVAIGMVKELDLARYLGILKPVAVSRMVKCLSKYGLPTSLKDSRVRK 332
Cdd:cd07766 193 -LGLAHAIGHALTAFE--GIPHGEAVAVGLPYVLKVANDMNPEPEAAIEAVFKFLEDLGLPTHLADLGVSK 260
|
|
| PRK12549 |
PRK12549 |
shikimate 5-dehydrogenase; Reviewed |
1293-1557 |
4.60e-21 |
|
shikimate 5-dehydrogenase; Reviewed
Pssm-ID: 183586 [Multi-domain] Cd Length: 284 Bit Score: 95.35 E-value: 4.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 1293 GKPVSVSRSPAMHNTLFEQNGLPYVYTRLETDQ----AQDVKEFIRSP---DFGGASATIPLKLDIIPLIDEVLNEAEII 1365
Cdd:PRK12549 12 GAGIQASLSPAMHEAEGDAQGLRYVYRLIDLDAlgltADALPELLDAAermGFAGLNITHPCKQAVIPHLDELSDDARAL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 1366 GAVNTIIPvegKDGstRLIGRNTDWSGIVRCLRE--AGAhsneGESSALVIGGGGTARAAIYALHNMGFSTVYVLGRSPE 1443
Cdd:PRK12549 92 GAVNTVVF---RDG--RRIGHNTDWSGFAESFRRglPDA----SLERVVQLGAGGAGAAVAHALLTLGVERLTIFDVDPA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 1444 K----IQNMASTFPTGfdirvlenasdienipRVAVGTipgdrPIEANMREilctifersgraADGKSAAVLLEMA---- 1515
Cdd:PRK12549 163 RaaalADELNARFPAA----------------RATAGS-----DLAAALAA------------ADGLVHATPTGMAkhpg 209
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 1516 ------------------YKPSVTPLMQLASDSGWTTIPGLEALVGQGVYQFEYWTGITP 1557
Cdd:PRK12549 210 lplpaellrpglwvadivYFPLETELLRAARALGCRTLDGGGMAVFQAVDAFELFTGREP 269
|
|
| PRK14027 |
PRK14027 |
quinate/shikimate dehydrogenase (NAD+); |
1289-1567 |
6.01e-21 |
|
quinate/shikimate dehydrogenase (NAD+);
Pssm-ID: 172521 [Multi-domain] Cd Length: 283 Bit Score: 94.72 E-value: 6.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 1289 FAIFGKPVSVSRSPAMHNTLFEQNGLPYVYTRLET--DQA--QDVKEFI---RSPDFGGASATIPLKLDIIPLIDEVLNE 1361
Cdd:PRK14027 7 LGLIGQGLDLSRTPAMHEAEGLAQGRATVYRRIDTlgSRAsgQDLKTLLdaaLYLGFNGLNITHPYKQAVLPLLDEVSEQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 1362 AEIIGAVNTIipVEGKDGSTRliGRNTDWSGIVRCLREagAHSNEGESSALVIGGGGTARAAIYALHNMGFSTVYVLGRS 1441
Cdd:PRK14027 87 ATQLGAVNTV--VIDATGHTT--GHNTDVSGFGRGMEE--GLPNAKLDSVVQVGAGGVGNAVAYALVTHGVQKLQVADLD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 1442 PEKIQNMASTF--PTGFDIRVLENASDIENIPRVAVGTIpgdRPIEANMREILCTIFERSGRAADGKSAAVLlemaYKPS 1519
Cdd:PRK14027 161 TSRAQALADVInnAVGREAVVGVDARGIEDVIAAADGVV---NATPMGMPAHPGTAFDVSCLTKDHWVGDVV----YMPI 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 327507643 1520 VTPLMQLASDSGWTTIPGLEALVGQGVYQFEYWTGITPVYEVARNAVL 1567
Cdd:PRK14027 234 ETELLKAARALGCETLDGTRMAIHQAVDAFRLFTGLEPDVSRMRETFL 281
|
|
| PRK14021 |
PRK14021 |
bifunctional shikimate kinase/3-dehydroquinate synthase; Provisional |
863-1035 |
3.72e-18 |
|
bifunctional shikimate kinase/3-dehydroquinate synthase; Provisional
Pssm-ID: 184458 [Multi-domain] Cd Length: 542 Bit Score: 89.92 E-value: 3.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 863 VIIGMRGAGKTTTGRWAAKALNRKFIDLDVELEQTEGKTIPDLIKERGWKGFRDAELSLFKRALTErpTGHVFACGGGIV 942
Cdd:PRK14021 10 VIIGMMGAGKTRVGKEVAQMMRLPFADADVEIEREIGMSIPSYFEEYGEPAFREVEADVVADMLED--FDGIFSLGGGAP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 943 EIAEARNILIDYHKNKGNVLLVMRDIKKVMEFLNIDKTRPAYIEDMMSVWLR----RKPWYQECSNVQYYSrHSSSPELA 1018
Cdd:PRK14021 88 MTPSTQHALASYIAHGGRVVYLDADPKEAMERANRGGGRPMLNGDANKRWKKlfkqRDPVFRQVANVHVHT-RGLTPQAA 166
|
170
....*....|....*....
gi 327507643 1019 L--AMDDFDRFIQFVSGKT 1035
Cdd:PRK14021 167 AkkLIDMVAERTVHVTGAG 185
|
|
| aroD |
PRK02412 |
type I 3-dehydroquinate dehydratase; |
1068-1283 |
5.47e-18 |
|
type I 3-dehydroquinate dehydratase;
Pssm-ID: 235036 Cd Length: 253 Bit Score: 85.33 E-value: 5.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 1068 ASGSDAVELRVDLLKDPSSGNGIPSaeyVAEQIsfYRSRVSLPIVFTIRTVSQGGKFP-NDahDAALELIMLAIRSGC-E 1145
Cdd:PRK02412 39 KYDADIIEWRADFLEKISDVESVLA---AAPAI--REKFAGKPLLFTFRTAKEGGEIAlSD--EEYLALIKAVIKSGLpD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 1146 FIDLEITFPEDLLRK-VAESKAH-AKIIASHHD-----PQGKLnwangswIQYYNKALQYG-DIIKLVGVAETLKDN--- 1214
Cdd:PRK02412 112 YIDVELFSGKDVVKEmVAFAHEHgVKVVLSYHDfektpPKEEI-------VERLRKMESLGaDIVKIAVMPQSEQDVltl 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 327507643 1215 -TALREFKdwaeQAHPDVPVIAINMGDKGQLSRmLNG--FLTPVSHPALPFKAAPGQLSAAEIRKGLSIMGE 1283
Cdd:PRK02412 185 lNATREMK----ELYADQPLITMSMGKLGRISR-LAGevFGSSWTFASLDKASAPGQISVEDLRRILEILHK 251
|
|
| aroL |
PRK03731 |
shikimate kinase AroL; |
862-1016 |
6.88e-18 |
|
shikimate kinase AroL;
Pssm-ID: 235153 [Multi-domain] Cd Length: 171 Bit Score: 82.68 E-value: 6.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 862 IVIIGMRGAGKTTTGRWAAKALNRKFIDLDVELEQTEGKTIPDLIKERGWKGFRDAElSLFKRALTErpTGHVFACGGGI 941
Cdd:PRK03731 5 LFLVGARGCGKTTVGMALAQALGYRFVDTDQWLQSTSNMTVAEIVEREGWAGFRARE-SAALEAVTA--PSTVIATGGGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 942 VEIAEARniliDYHKNKGNVL--------LVMRdikkVMEFLNIDKtRP-----AYIEDMMSVWLRRKPWYQECSNvqYY 1008
Cdd:PRK03731 82 ILTEENR----HFMRNNGIVIylcapvsvLANR----LEANPEEDQ-RPtltgkPISEEVAEVLAEREALYREVAH--HI 150
|
....*...
gi 327507643 1009 SRHSSSPE 1016
Cdd:PRK03731 151 IDATQPPS 158
|
|
| PRK13947 |
PRK13947 |
shikimate kinase; Provisional |
862-942 |
2.42e-15 |
|
shikimate kinase; Provisional
Pssm-ID: 184412 [Multi-domain] Cd Length: 171 Bit Score: 75.51 E-value: 2.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 862 IVIIGMRGAGKTTTGRWAAKALNRKFIDLDVELEQTEGKTIPDLIKERGWKGFRDAELSLFKRAltERPTGHVFACGGGI 941
Cdd:PRK13947 4 IVLIGFMGTGKTTVGKRVATTLSFGFIDTDKEIEKMTGMTVAEIFEKDGEVRFRSEEKLLVKKL--ARLKNLVIATGGGV 81
|
.
gi 327507643 942 V 942
Cdd:PRK13947 82 V 82
|
|
| PRK13946 |
PRK13946 |
shikimate kinase; Provisional |
861-940 |
9.46e-15 |
|
shikimate kinase; Provisional
Pssm-ID: 184411 [Multi-domain] Cd Length: 184 Bit Score: 74.19 E-value: 9.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 861 SIVIIGMRGAGKTTTGRWAAKALNRKFIDLDVELEQTEGKTIPDLIKERGWKGFRDAELSLFKRALTERPtgHVFACGGG 940
Cdd:PRK13946 12 TVVLVGLMGAGKSTVGRRLATMLGLPFLDADTEIERAARMTIAEIFAAYGEPEFRDLERRVIARLLKGGP--LVLATGGG 89
|
|
| PRK13951 |
PRK13951 |
bifunctional shikimate kinase AroK/3-dehydroquinate synthase AroB; |
862-1001 |
1.48e-14 |
|
bifunctional shikimate kinase AroK/3-dehydroquinate synthase AroB;
Pssm-ID: 172457 [Multi-domain] Cd Length: 488 Bit Score: 78.41 E-value: 1.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 862 IVIIGMRGAGKTTTGRWAAKALNRKFIDLDVELEQTEGKTIPDLIKERGWKGFRDAELSLFkRALTERpTGHVFACGGGI 941
Cdd:PRK13951 3 IFLVGMMGSGKSTIGKRVSEVLDLQFIDMDEEIERREGRSVRRIFEEDGEEYFRLKEKELL-RELVER-DNVVVATGGGV 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 327507643 942 VEIAEARNILidyhkNKGNVLLVMRDIKKVMEFLNIDkTRPAYI---EDMMSVWLRRKPWYQE 1001
Cdd:PRK13951 81 VIDPENRELL-----KKEKTLFLYAPPEVLMERVTTE-NRPLLRegkERIREIWERRKQFYTE 137
|
|
| aroK |
PRK05057 |
shikimate kinase AroK; |
862-1005 |
3.89e-14 |
|
shikimate kinase AroK;
Pssm-ID: 235335 [Multi-domain] Cd Length: 172 Bit Score: 72.05 E-value: 3.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 862 IVIIGMRGAGKTTTGRWAAKALNRKFIDLDVELEQTEGKTIPDLIKERGWKGFRDAELSLFKRaLTERpTGHVFACGGGI 941
Cdd:PRK05057 7 IFLVGPMGAGKSTIGRQLAQQLNMEFYDSDQEIEKRTGADIGWVFDVEGEEGFRDREEKVINE-LTEK-QGIVLATGGGS 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 327507643 942 VEIAEARNILidyhKNKGNVLLVMRDIKKVMEFLNIDKTRP--------AYIEDMMSVwlrRKPWYQECSNV 1005
Cdd:PRK05057 85 VKSRETRNRL----SARGVVVYLETTIEKQLARTQRDKKRPllqvddprEVLEALANE---RNPLYEEIADV 149
|
|
| PRK08154 |
PRK08154 |
anaerobic benzoate catabolism transcriptional regulator; Reviewed |
825-942 |
5.09e-11 |
|
anaerobic benzoate catabolism transcriptional regulator; Reviewed
Pssm-ID: 236167 [Multi-domain] Cd Length: 309 Bit Score: 65.75 E-value: 5.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 825 WPTYWDALKQKFGVSL-KGKELAESEITHGPADRSDASIVIIGMRGAGKTTTGRWAAKALNRKFIDLDVELEQTEGKTIP 903
Cdd:PRK08154 98 WLLIRELLEQASPAQLaRVRDALSGMLGAGRRAARRRRIALIGLRGAGKSTLGRMLAARLGVPFVELNREIEREAGLSVS 177
|
90 100 110
....*....|....*....|....*....|....*....
gi 327507643 904 DLIKERGWKGFRDAELSLFKRALTERPTGhVFACGGGIV 942
Cdd:PRK08154 178 EIFALYGQEGYRRLERRALERLIAEHEEM-VLATGGGIV 215
|
|
| PRK13949 |
PRK13949 |
shikimate kinase; Provisional |
860-918 |
1.02e-09 |
|
shikimate kinase; Provisional
Pssm-ID: 140006 [Multi-domain] Cd Length: 169 Bit Score: 58.97 E-value: 1.02e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 327507643 860 ASIVIIGMRGAGKTTTGRWAAKALNRKFIDLDVELEQTEGKTIPDLIKERGWKGFRDAE 918
Cdd:PRK13949 2 ARIFLVGYMGAGKTTLGKALARELGLSFIDLDFFIENRFHKTVGDIFAERGEAVFRELE 60
|
|
| SDH_C |
pfam18317 |
Shikimate 5'-dehydrogenase C-terminal domain; This domain is found in the C-terminal region of ... |
1537-1567 |
1.78e-07 |
|
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: 48.57 E-value: 1.78e-07
10 20 30
....*....|....*....|....*....|.
gi 327507643 1537 GLEALVGQGVYQFEYWTGITPVYEVARNAVL 1567
Cdd:pfam18317 1 GLGMLVEQGAEQFELWTGREPPVEVMREALL 31
|
|
| PRK13948 |
PRK13948 |
shikimate kinase; Provisional |
856-952 |
8.09e-07 |
|
shikimate kinase; Provisional
Pssm-ID: 184413 [Multi-domain] Cd Length: 182 Bit Score: 50.94 E-value: 8.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 856 DRSDASIVIIGMRGAGKTTTGRWAAKALNRKFIDLDVELEQTEGKTIPDLIKERGWKGFRDAELSLFKRALteRPTGHVF 935
Cdd:PRK13948 7 ERPVTWVALAGFMGTGKSRIGWELSRALMLHFIDTDRYIERVTGKSIPEIFRHLGEAYFRRCEAEVVRRLT--RLDYAVI 84
|
90
....*....|....*..
gi 327507643 936 ACGGGIVEIAEARNILI 952
Cdd:PRK13948 85 SLGGGTFMHEENRRKLL 101
|
|
| Fe-ADH_2 |
pfam13685 |
Iron-containing alcohol dehydrogenase; |
29-288 |
8.41e-07 |
|
Iron-containing alcohol dehydrogenase;
Pssm-ID: 404557 [Multi-domain] Cd Length: 251 Bit Score: 51.92 E-value: 8.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 29 DLLTNLPSTTYVLVTDTNLGSIYREKFAKIFNEAAaalspaprlLTKEIPPGENsksrqGKADIEDWMLQQTCGRDT--- 105
Cdd:pfam13685 12 EYLAELGFRRVALVADANTYAAAGRKVAESLKRAG---------IEVETRLEVA-----GNADMETAEKLVGALRERdad 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 106 VIIALGGGVIGDLLGFVAATymRGIRFVQVPTTllAMVD------SSI---GGKTAIDT--PLGknligaiwqphrIYID 174
Cdd:pfam13685 78 AVVGVGGGTVIDLAKYAAFK--LGKPFISVPTA--ASNDgfaspgASLtvdGKKRSIPAaaPFG------------VIAD 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 175 IDFIDTLPEREFINGMAEVI-KTAAISDEK--------EFAALEQHADAILKAARSKPGKGRFDLVRQVVKDRIVASArh 245
Cdd:pfam13685 142 TDVIAAAPRRLLASGVGDLLaKITAVADWElahaeevaAPLALLSAAMVMNFADRPLRDPGDIEALAELLSALAMGGA-- 219
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 327507643 246 kAFVVTADEREgglrnllnlgHSIGHAIEAILSPQVLHGECVA 288
Cdd:pfam13685 220 -GSSRPASGSE----------HLISHALDMIAPKQALHGEQVG 251
|
|
| GldA |
COG0371 |
Glycerol dehydrogenase or related enzyme, iron-containing ADH family [Energy production and ... |
23-327 |
2.96e-06 |
|
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: 51.32 E-value: 2.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 23 GTYIVQ-DLLTNLPS------TTYVLVTDTNLGSIYREKFAKIFNEAAAALspaprllTKEIPPGENSKS---------R 86
Cdd:COG0371 7 RRYVQGeGALDELGEyladlgKRALIITGPTALKAAGDRLEESLEDAGIEV-------EVEVFGGECSEEeierlaeeaK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 87 QGKADiedwmlqqtcgrdtVIIALGGGVIGDLLGFVAatYMRGIRFVQVPTTllAMVD------SSI---GGKTAIDTPL 157
Cdd:COG0371 80 EQGAD--------------VIIGVGGGKALDTAKAVA--YRLGLPVVSVPTI--ASTDapasplSVIyteDGAFDGYSFL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 158 GKNligaiwqPHRIYIDIDFIDTLPEREFINGMAEVI--KTAA----ISDEK-------EFAA---------LEQHADAI 215
Cdd:COG0371 142 AKN-------PDLVLVDTDIIAKAPVRLLAAGIGDALakWYEArdwsLAHRDlageyytEAAValarlcaetLLEYGEAA 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 216 LKAARSKpgkGRFDLVRQVVKDRIVASArhkafVVTADEREGGlrnllNLG--HSIGHAIEAIL-SPQVLHGECVAIG-M 291
Cdd:COG0371 215 IKAVEAG---VVTPALERVVEANLLLSG-----LAMGIGSSRP-----GSGaaHAIHNGLTALPeTHHALHGEKVAFGtL 281
|
330 340 350
....*....|....*....|....*....|....*.
gi 327507643 292 VkeldLARYLGilKPVAVSRMVKCLSKYGLPTSLKD 327
Cdd:COG0371 282 V----QLVLEG--RPEEIEELLDFLRSVGLPTTLAD 311
|
|
| PLN02199 |
PLN02199 |
shikimate kinase |
861-942 |
1.40e-05 |
|
shikimate kinase
Pssm-ID: 177850 [Multi-domain] Cd Length: 303 Bit Score: 48.93 E-value: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 861 SIVIIGMRGAGKTTTGRWAAKALNRKFIDLDVELEQT-EGKTIPDLIKERGWKGFRDAELSLFKRALTERPTghVFACGG 939
Cdd:PLN02199 104 SMYLVGMMGSGKTTVGKLMSKVLGYTFFDCDTLIEQAmNGTSVAEIFVHHGENFFRGKETDALKKLSSRYQV--VVSTGG 181
|
...
gi 327507643 940 GIV 942
Cdd:PLN02199 182 GAV 184
|
|
| Gro1PDH |
cd08173 |
Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) catalyzes the reversible conversion between ... |
103-327 |
1.63e-04 |
|
Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) catalyzes the reversible conversion between dihydroxyacetone phosphate and glycerol-1-phosphate using either NADH or NADPH as a coenzyme; Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH, EC 1.1.1.261) plays an important role in the formation of the enantiomeric configuration of the glycerophosphate backbone (sn-glycerol-1-phosphate) of archaeal ether lipids. It catalyzes the reversible conversion between dihydroxyacetone phosphate and glycerol-1-phosphate using either NADH or NADPH as a coenzyme. The activity is zinc-dependent. One characteristic feature of archaea is that their cellular membrane has an ether linkage between the glycerol backbone and the hydrocarbon residues. The polar lipids of the members of Archaea consist of di- and tetra-ethers of glycerol with isoprenoid alcohols bound at the sn-2 and sn-3 positions of the glycerol moiety. The archaeal polar lipids have the enantiomeric configuration of a glycerophosphate backbone [sn-glycerol-1-phosphate (G-1-P)] that is the mirror image structure of the bacterial or eukaryal counterpart [sn-glycerol- 3-phosphate (G-3-P)]. The absolute stereochemistry of the glycerol moiety in all archaeal polar lipids is opposite to that of glycerol ester lipids in bacteria and eukarya.
Pssm-ID: 341452 Cd Length: 343 Bit Score: 45.62 E-value: 1.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 103 RDTVIIALGGGVIGDllgfVA--ATYMRGIRFVQVPTTL-----------LAMVDSSIGGKTaiDTPLGknligaiwqph 169
Cdd:cd08173 80 KADFIIGVGGGKVID----VAkyAAYKLNLPFISIPTSAshdgiaspfasIKGGDKPYSIKA--KAPIA----------- 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 170 rIYIDIDFIDTLPEREFINGMAEVI-KTAAISD---------EK--EFAA-LEQHADAILKAARSKPGKGRFDLVRQVVK 236
Cdd:cd08173 143 -IIADTEIISKAPKRLLAAGCGDLIsNITAVKDwrlahrlkgEYysEYAAsLALMSAKLIIENADLIKPGLEEGVRTVVK 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 237 DRI---VA-----SARhkafVVTADEregglrnllnlgHSIGHAIEAILSPQVLHGECVAIGMVkeldLARYL--GILKp 306
Cdd:cd08173 222 ALIssgVAmsiagSSR----PASGSE------------HLFSHALDKLAPGPALHGEQCGVGTI----MMAYLhgGDWK- 280
|
250 260
....*....|....*....|.
gi 327507643 307 vavsRMVKCLSKYGLPTSLKD 327
Cdd:cd08173 281 ----EIREALKKIGAPTTAKE 297
|
|
| EPT_RTPC-like |
cd01553 |
This domain family includes the Enolpyruvate transferase (EPT) family and the RNA 3' phosphate ... |
637-833 |
2.79e-04 |
|
This domain family includes the Enolpyruvate transferase (EPT) family and the RNA 3' phosphate cyclase family (RTPC). These 2 families differ in that EPT is formed by 3 repeats of an alpha-beta structural domain while RTPC has 3 similar repeats with a 4th slightly different domain inserted between the 2nd and 3rd repeat. They evidently share the same active site location, although the catalytic residues differ.
Pssm-ID: 238794 Cd Length: 211 Bit Score: 43.81 E-value: 2.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 637 ESDASSATYPLAIAAVTGTTCTVPNIGSAS-----LQGDARFaVEVLRPMG----CKVEQTATSTTVT-GPADGVlrplp 706
Cdd:cd01553 7 KGGGQILRSFLVLAAISGGPITVTGIRPDRakpglLRQHLTF-LKALEKICgatvEGGELGSDRISFRpGTVRGG----- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 707 NVDMEPMTDAFLG---ASVLAAIAQGEGGNHATRIYGI-ANQRVKECNRIEAMRVELAKFGVVCREhpdgleidGIDRST 782
Cdd:cd01553 81 DVRFAIGSAGSCTdvlQTILPLLLFAKGPTRLTVTGGTdNPSAPPADFIRFVLEPELAKIGAHQEE--------TLLRHG 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 327507643 783 LRHPAGGVFCYDDHRVA-FSFS-----ILSLVAPTPTLILEKECVGKTWPTYWDALK 833
Cdd:cd01553 153 FYPAGGGVVATEVSPVEkLNTAqlrqlVLPMLLASGAVEFTVAHPSCHLLTNFAVLE 209
|
|
| hemA |
PRK00045 |
glutamyl-tRNA reductase; Reviewed |
1410-1453 |
1.25e-03 |
|
glutamyl-tRNA reductase; Reviewed
Pssm-ID: 234592 [Multi-domain] Cd Length: 423 Bit Score: 43.25 E-value: 1.25e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 327507643 1410 SALVIGGGGTARAAIYALHNMGFSTVYVLGRSPEKIQNMASTFP 1453
Cdd:PRK00045 184 KVLVIGAGEMGELVAKHLAEKGVRKITVANRTLERAEELAEEFG 227
|
|
| G1PDH |
cd08175 |
Glycerol-1-phosphate dehydrogenase (G1PDH) catalyzes the reversible reduction of ... |
30-327 |
2.55e-03 |
|
Glycerol-1-phosphate dehydrogenase (G1PDH) catalyzes the reversible reduction of dihydroxyacetone phosphate (DHAP) to glycerol-1-phosphate (G1P) in an NADH-dependent manner; Glycerol-1-phosphate dehydrogenase (G1PDH) plays a role in the synthesis of phosphoglycerolipids in Gram-positive bacterial species. It catalyzes the reversibly reduction of dihydroxyacetone phosphate (DHAP) to glycerol-1-phosphate (G1P) in a NADH-dependent manner. Its activity requires a Ni++ ion. In Bacillus subtilis, it has been described as AraM gene in L-arabinose (ara) operon. AraM protein forms homodimer.
Pssm-ID: 341454 Cd Length: 340 Bit Score: 41.73 E-value: 2.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 30 LLTNLPSTTYVLVTDTNlgsIYR---EKFAKIFNEAAAALSPAPRLLTKEIPPGEnsksrqgkADIEDWMLQqTCGRDTV 106
Cdd:cd08175 18 LKELFGGKKVLVVADEN---TYAaagEEVEAALEEAGVTVCLLIFPGEGDLIADE--------AAVGKVLLE-LEKDTDL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 107 IIALGGGVIGDLLGFVAatYMRGIRFVQVPTTllAMVD------SSI---GGKTAIDTPLgknligaiwqPHRIYIDIDF 177
Cdd:cd08175 86 IIAVGSGTINDLTKYAA--YKLGIPYISVPTA--PSMDgytssgAPIivdGVKKTFPAHA----------PKAIFADLDV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 178 IDTLPEREFINGMAEVI-KTAAISDEK--EFAALEQHADAIlkaarskpgkgrFDLVRQVVKDRIVASARhkafvVTADE 254
Cdd:cd08175 152 LANAPQRMIAAGFGDLLgKYTALADWKlsHLLGGEYYCPEV------------ADLVQEALEKCLDNAEG-----IAARD 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 255 REgGLRNLLN-----------LGHS---------IGHAIE--AILS--PQVLHGECVAIGMVKELDLarYLGILKPvAVS 310
Cdd:cd08175 215 PE-AIEALMEalilsglamqlVGNSrpasgaehhLSHYWEmeFLRLgkPPVLHGEKVGVGTLLIAAL--YILEQLP-PPE 290
|
330
....*....|....*..
gi 327507643 311 RMVKCLSKYGLPTSLKD 327
Cdd:cd08175 291 ELRELLRKAGAPTTPED 307
|
|
| AAA_18 |
pfam13238 |
AAA domain; |
862-975 |
8.39e-03 |
|
AAA domain;
Pssm-ID: 433052 [Multi-domain] Cd Length: 128 Bit Score: 38.18 E-value: 8.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327507643 862 IVIIGMRGAGKTTTGRWAAKALNRkfidldveleqteGKTIPDLIKERGWKGFRDAELSLFKRALTERpTGHVFACGGGI 941
Cdd:pfam13238 1 ILITGTPGVGKTTLAKELSKRLGF-------------GDNVRDLALENGLVLGDDPETRESKRLDEDK-LDRLLDLLEEN 66
|
90 100 110
....*....|....*....|....*....|....
gi 327507643 942 VEIAEARNILIDYHknkGNVLLVMRDIKKVMEFL 975
Cdd:pfam13238 67 AALEEGGNLIIDGH---LAELEPERAKDLVGIVL 97
|
|
| |
