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Conserved domains on  [gi|2459786690|ref|XP_054125236|]
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uncharacterized protein EYB26_010016 [Talaromyces marneffei]

Protein Classification

pentafunctional AROM polypeptide( domain architecture ID 12959900)

pentafunctional AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
EPSP_synthase cd01556
EPSP synthase domain. 3-phosphoshikimate 1-carboxyvinyltransferase ...
406-834 1.31e-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: 468.58  E-value: 1.31e-151
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  406 APPGSKSISNRALVLAALGSGTVRVKNLLHSDDTEVMLNALERLGAatfAWEDEGEVLVVNGNGGKMQASPTELYLGNAG 485
Cdd:cd01556      6 TVPGSKSISHRALLLAALAEGESRIENLLDSDDTLATLEALRALGA---KIEEEGGTVEIVGGGGLGLPPEAVLDCGNSG 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  486 TASRFLTSVATLSGKGSVdyniLTGNNRMKQRPIGDLVDALTINGAQVEYLEKAGSLPLKIaaSGGFKGGRINLAAKVSS 565
Cdd:cd01556     83 TTMRLLTGLLALQGGDSV----LTGDESLRKRPMGRLVDALRQLGAEIEGREGGGYPPLIG--GGGLKGGEVEIPGAVSS 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  566 QYVSSLLMCAPYAKEPVTLKLvgGRPISLSYIEMTTAMMRSFGIDVQKSTTEEWTYHiPQGSYnNPPEYVIESDASSATY 645
Cdd:cd01556    157 QFKSALLLAAPLAEGPTTIII--GELESKPYIDHTERMLRAFGAEVEVDGYRTITVK-GGQKY-KGPEYTVEGDASSAAF 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  646 PLAIAAVTGTTCTVPNIGSASlqGDARFaVEVLRPMGCKVEQTATsTTVTGPADGVLRPLpNVDMEPMTDAFLGASVLAA 725
Cdd:cd01556    233 FLAAAAITGSEIVIKNVGLNS--GDTGI-IDVLKEMGADIEIGNE-DTVVVESGGKLKGI-DIDGNDIPDEAPTLAVLAA 307
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  726 IAQGEggnhaTRIYGIANQRVKECNRIEAMRVELAKFGVVCREHPDGLEIDGidrSTLRHPAGGVFCYDDHRVAFSFSIL 805
Cdd:cd01556    308 FAEGP-----TRIRNAAELRVKESDRIAAMATELRKLGADVEETEDGLIIEG---GPLKGAGVEVYTYGDHRIAMSFAIA 379
                          410       420
                   ....*....|....*....|....*....
gi 2459786690  806 SLVAPTPTLILEKECVGKTWPTYWDALKQ 834
Cdd:cd01556    380 GLVAEGGVTIEDPECVAKSFPNFFEDLES 408
DHQS cd08195
Dehydroquinate synthase (DHQS) catalyzes the conversion of DAHP to DHQ in shikimate pathway ...
25-387 2.52e-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: 2.52e-138
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690   25 YIVQDLLTNLPS-------TTYVLVTDTNLGSIYREKFAKIFNEAAAalspapRLLTKEIPPGENSKSRQGKADIEDWML 97
Cdd:cd08195      5 LIGSGLLDKLGEllelkkgSKVVIVTDENVAKLYGELLLKSLEAAGF------KVEVIVIPAGEKSKSLETVERIYDFLL 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690   98 QQTCGRDTVIIALGGGVIGDLLGFVAATYMRGIRFVQVPTTLLAMVDSSIGGKTAIDTPLGKNLIGAIWQPHRIYIDIDF 177
Cdd:cd08195     79 EAGLDRDSLLIALGGGVVGDLAGFVASTYMRGIPFIQVPTTLLAQVDSSIGGKTGINLPGGKNLIGAFYQPKAVLIDPDF 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  178 IDTLPEREFINGMAEVIKTAAISDEKEFAALEQHADAILKAarskpgkgRFDLVRQVVKdrivASARHKAFVVTADEREG 257
Cdd:cd08195    159 LKTLPEREFRSGLAEVIKYGLIADKELFEFLEKNLDKILAR--------DPEALEEIIA----RSVEIKADIVEEDEREK 226
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  258 GLRNLLNLGHSIGHAIEAILSPQVLHGECVAIGMVKELDLARYLGILKPVAVSRMVKCLSKYGLPTSLKDsrvrkhtagk 337
Cdd:cd08195    227 GLRAILNFGHTFGHAIESASGYKLLHGEAVAIGMVAAARLSVKLGLLSEEDLERIRALLKKLGLPTSIKD---------- 296
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|
gi 2459786690  338 hCSLEQMMANMALDKKNDGPRKKVVLLSAIGQTYepKASVVSNEDIRAVL 387
Cdd:cd08195    297 -LDPEELLEAMKRDKKNRGGKIRFVLLKGIGKAV--IVDDVSEEEIREAL 343
Shik-DH-AROM super family cl36977
shikimate-5-dehydrogenase, fungal AROM-type; This model represents a clade of ...
1282-1566 1.24e-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]


The actual alignment was detected with superfamily member TIGR01809:

Pssm-ID: 273813 [Multi-domain]  Cd Length: 282  Bit Score: 252.91  E-value: 1.24e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690 1282 GEIPAKKFAIFGKPVSVSRSPAMHNTLFEQNGLPYVYTRLETDQAQDVKEFIRS--PDFGGASATIPLKLDIIPLIDEVL 1359
Cdd:TIGR01809    1 GNKGPKKAFIIGKPIAHSRSPHLHNAGYEILGLPDKTYEFETCSAEELKEVLSGfgPQFGGASVTIPLKFAILRFADEHT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690 1360 NEAEIIGAVNTIIPVegkdGSTRLIGRNTDWSGIVRCLREAGAHSNEGESSALVIGGGGTARAAIYALHNMGFSTVYVLG 1439
Cdd:TIGR01809   81 DRASLIGSVNTLLRT----QNGIWKGDNTDWDGIAGALANIGKFEPLAGFRGLVIGAGGTSRAAVYALASLGVTDITVIN 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690 1440 RSPEKIQNMASTFPTGFDIRVLENASDIENIP---RVAVGTIPGDRPIEANMREILCTIFERSGRAADGksaaVLLEMAY 1516
Cdd:TIGR01809  157 RNPDKLSRLVDLGVQVGVITRLEGDSGGLAIEkaaEVLVSTVPADVPADYVDLFATVPFLLLKRKSSEG----IFLDAAY 232
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 2459786690 1517 KPSVTPLMQLASDSGWTTIPGLEALVGQGVYQFEYWTGITPVYEVARNAV 1566
Cdd:TIGR01809  233 DPWPTPLVAIVSAAGWRVISGLQMLLHQGFAQFEQWTGMPAPREAMACAL 282
DHquinase_I pfam01487
Type I 3-dehydroquinase; Type I 3-dehydroquinase, (3-dehydroquinate dehydratase or DHQase.) ...
1051-1278 5.73e-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: 5.73e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690 1051 SLTLTDLRDSGDLLRTVASGSDAVELRVDLLKDPSSgngipSAEYVAEQISFYRSRVSLPIVFTIRTVSQGGKfPNDAHD 1130
Cdd:pfam01487    3 PLTGKTLEEILEELESGKEGADLVELRVDLLEEPVE-----DAEDVSEQLALLRRVGDLPLIFTFRTKSEGGE-PDGSEE 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690 1131 AALELIMLAIRSGCEFIDLEITFPEDLLRKVAESK--AHAKIIASHHDPQGKLNWAngSWIQYYNKALQYG-DIIKLVGV 1207
Cdd:pfam01487   77 EYLELLRLALRLGVDYVDVELFLPEEILKELIEAKheGGTKVIGSYHDFEGTPSWE--ELISRYEKMQALGaDIVKIAVM 154
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2459786690 1208 AETLKDNTALREFKDWAEQAHpDVPVIAINMGDKGQLSRMLNGFL-TPVSHPAL--PFKAAPGQLSAAEIRKGL 1278
Cdd:pfam01487  155 AKSIEDVLALLRFTSEMKSLA-DKPLIAMSMGELGRISRVLGPIFgSPVTFAALglAEKSAPGQLTAKELREAL 227
SK cd00464
Shikimate kinase (SK) is the fifth enzyme in the shikimate pathway, a seven-step biosynthetic ...
861-1005 8.81e-49

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: 170.81  E-value: 8.81e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  861 SIVIIGMRGAGKTTTGRWAAKALNRKFIDLDVELEQTEGKTIPDLIKERGWQGFRDAELSLFKRALTerPTGHVFACGGG 940
Cdd:cd00464      1 NIVLIGMMGAGKTTVGRLLAKALGLPFVDLDELIEQRAGMSIPEIFAEEGEEGFRELEREVLLLLLT--KENAVIATGGG 78
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2459786690  941 IVEIAEARNilidYHKNKGNVLLVMRDIKKVMEFLNIDKTRPAY----IEDMMSVWLRRKPWYQECSNV 1005
Cdd:cd00464     79 AVLREENRR----LLLENGIVVWLDASPEELLERLARDKTRPLLqdedPERLRELLEEREPLYREVADL 143
 
Name Accession Description Interval E-value
EPSP_synthase cd01556
EPSP synthase domain. 3-phosphoshikimate 1-carboxyvinyltransferase ...
406-834 1.31e-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: 468.58  E-value: 1.31e-151
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  406 APPGSKSISNRALVLAALGSGTVRVKNLLHSDDTEVMLNALERLGAatfAWEDEGEVLVVNGNGGKMQASPTELYLGNAG 485
Cdd:cd01556      6 TVPGSKSISHRALLLAALAEGESRIENLLDSDDTLATLEALRALGA---KIEEEGGTVEIVGGGGLGLPPEAVLDCGNSG 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  486 TASRFLTSVATLSGKGSVdyniLTGNNRMKQRPIGDLVDALTINGAQVEYLEKAGSLPLKIaaSGGFKGGRINLAAKVSS 565
Cdd:cd01556     83 TTMRLLTGLLALQGGDSV----LTGDESLRKRPMGRLVDALRQLGAEIEGREGGGYPPLIG--GGGLKGGEVEIPGAVSS 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  566 QYVSSLLMCAPYAKEPVTLKLvgGRPISLSYIEMTTAMMRSFGIDVQKSTTEEWTYHiPQGSYnNPPEYVIESDASSATY 645
Cdd:cd01556    157 QFKSALLLAAPLAEGPTTIII--GELESKPYIDHTERMLRAFGAEVEVDGYRTITVK-GGQKY-KGPEYTVEGDASSAAF 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  646 PLAIAAVTGTTCTVPNIGSASlqGDARFaVEVLRPMGCKVEQTATsTTVTGPADGVLRPLpNVDMEPMTDAFLGASVLAA 725
Cdd:cd01556    233 FLAAAAITGSEIVIKNVGLNS--GDTGI-IDVLKEMGADIEIGNE-DTVVVESGGKLKGI-DIDGNDIPDEAPTLAVLAA 307
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  726 IAQGEggnhaTRIYGIANQRVKECNRIEAMRVELAKFGVVCREHPDGLEIDGidrSTLRHPAGGVFCYDDHRVAFSFSIL 805
Cdd:cd01556    308 FAEGP-----TRIRNAAELRVKESDRIAAMATELRKLGADVEETEDGLIIEG---GPLKGAGVEVYTYGDHRIAMSFAIA 379
                          410       420
                   ....*....|....*....|....*....
gi 2459786690  806 SLVAPTPTLILEKECVGKTWPTYWDALKQ 834
Cdd:cd01556    380 GLVAEGGVTIEDPECVAKSFPNFFEDLES 408
aroA TIGR01356
3-phosphoshikimate 1-carboxyvinyltransferase; This model represents ...
406-834 1.73e-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: 433.24  E-value: 1.73e-138
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  406 APPGSKSISNRALVLAALGSGTVRVKNLLHSDDTEVMLNALERLGAATfawEDEGEVLVVNGNGGKMQASptELYLGNAG 485
Cdd:TIGR01356    4 RAPGSKSITHRALILAALAEGETRVRNLLRSEDTLATLDALRALGAKI---EDGGEVAVIEGVGGKEPQA--ELDLGNSG 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  486 TASRFLTSVATLSGKGSVdyniLTGNNRMKQRPIGDLVDALTINGAQVEYLEKAGSLPLKIaaSGGFKGGRINLAAKVSS 565
Cdd:TIGR01356   79 TTARLLTGVLALADGEVV----LTGDESLRKRPMGRLVDALRQLGAEISSLEGGGSLPLTI--SGPLPGGIVYISGSASS 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  566 QYVSSLLMCAPyAKEPVTLKLVGGRPISLSYIEMTTAMMRSFGIDVQKSTTEewTYHIPQGSYNNPPEYVIESDASSATY 645
Cdd:TIGR01356  153 QYKSALLLAAP-ALQAVGITIVGEPLKSRPYIEITLDLLGSFGVEVERSDGR--KIVVPGGQKYGPQGYDVPGDYSSAAF 229
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  646 PLAIAAVTGTTCTVPNIGSASLQGDARFaVEVLRPMGCKVEQTATSTTVTGPADgvLRPLpNVDMEPMTDAFLGASVLAA 725
Cdd:TIGR01356  230 FLAAAAITGGRVTLENLGINPTQGDKAI-IIVLEEMGADIEVEEDDLIVEGASG--LKGI-KIDMDDMIDELPTLAVLAA 305
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  726 IAQGEggnhaTRIYGIANQRVKECNRIEAMRVELAKFGVVCREHPDGLEIDGidRSTLRhpAGGVFCYDDHRVAFSFSIL 805
Cdd:TIGR01356  306 FAEGV-----TRITGAEELRVKESDRIAAIAEELRKLGVDVEEFEDGLYIRG--KKELK--GAVVDTFGDHRIAMAFAVA 376
                          410       420
                   ....*....|....*....|....*....
gi 2459786690  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 2.52e-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: 2.52e-138
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690   25 YIVQDLLTNLPS-------TTYVLVTDTNLGSIYREKFAKIFNEAAAalspapRLLTKEIPPGENSKSRQGKADIEDWML 97
Cdd:cd08195      5 LIGSGLLDKLGEllelkkgSKVVIVTDENVAKLYGELLLKSLEAAGF------KVEVIVIPAGEKSKSLETVERIYDFLL 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690   98 QQTCGRDTVIIALGGGVIGDLLGFVAATYMRGIRFVQVPTTLLAMVDSSIGGKTAIDTPLGKNLIGAIWQPHRIYIDIDF 177
Cdd:cd08195     79 EAGLDRDSLLIALGGGVVGDLAGFVASTYMRGIPFIQVPTTLLAQVDSSIGGKTGINLPGGKNLIGAFYQPKAVLIDPDF 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  178 IDTLPEREFINGMAEVIKTAAISDEKEFAALEQHADAILKAarskpgkgRFDLVRQVVKdrivASARHKAFVVTADEREG 257
Cdd:cd08195    159 LKTLPEREFRSGLAEVIKYGLIADKELFEFLEKNLDKILAR--------DPEALEEIIA----RSVEIKADIVEEDEREK 226
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  258 GLRNLLNLGHSIGHAIEAILSPQVLHGECVAIGMVKELDLARYLGILKPVAVSRMVKCLSKYGLPTSLKDsrvrkhtagk 337
Cdd:cd08195    227 GLRAILNFGHTFGHAIESASGYKLLHGEAVAIGMVAAARLSVKLGLLSEEDLERIRALLKKLGLPTSIKD---------- 296
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|
gi 2459786690  338 hCSLEQMMANMALDKKNDGPRKKVVLLSAIGQTYepKASVVSNEDIRAVL 387
Cdd:cd08195    297 -LDPEELLEAMKRDKKNRGGKIRFVLLKGIGKAV--IVDDVSEEEIREAL 343
AroA COG0128
5-enolpyruvylshikimate-3-phosphate synthase [Amino acid transport and metabolism]; ...
408-834 1.62e-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: 1.62e-135
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  408 PGSKSISNRALVLAALGSGTVRVKNLLHSDDTEVMLNALERLGaATFAWEDEGEVlVVNGNGGKMQASPTELYLGNAGTA 487
Cdd:COG0128     19 PGSKSISHRALLLAALAEGESTIRNLLESDDTLATLEALRALG-AEIEELDGGTL-RVTGVGGGLKEPDAVLDCGNSGTT 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  488 SRFLTSVATLSGKGSVdyniLTGNNRMKQRPIGDLVDALTINGAQVEYLEKaGSLPLKIAAsGGFKGGRINLAAKVSSQY 567
Cdd:COG0128     97 MRLLTGLLALQPGEVV----LTGDESLRKRPMGRLLDPLRQLGARIESRGG-GYLPLTIRG-GPLKGGEYEIPGSASSQF 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  568 VSSLLMCAPYAKEPVTLKlVGGRPISLSYIEMTTAMMRSFGIDVQKSTTEEWTYHIPQgSYnNPPEYVIESDASSATYPL 647
Cdd:COG0128    171 KSALLLAGPLAEGGLEIT-VTGELESKPYRDHTERMLRAFGVEVEVEGYRRFTVPGGQ-RY-RPGDYTVPGDISSAAFFL 247
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  648 AIAAVTGTTCTVPNIGSASLQGDARFaVEVLRPMGCKVEQTATSTTVTGpadGVLRPLpNVDMEPMTDAFLGASVLAAIA 727
Cdd:COG0128    248 AAAAITGSEVTVEGVGLNSTQGDTGI-LDILKEMGADIEIENDGITVRG---SPLKGI-DIDLSDIPDEAPTLAVLAAFA 322
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  728 QGEggnhaTRIYGIANQRVKECNRIEAMRVELAKFGVVCREHPDGLEIDGidRSTLRhpaGGVF-CYDDHRVAFSFSILS 806
Cdd:COG0128    323 EGT-----TRIRGAAELRVKESDRIAAMATELRKLGADVEETEDGLIIEG--GPKLK---GAEVdSYGDHRIAMAFAVAG 392
                          410       420
                   ....*....|....*....|....*...
gi 2459786690  807 LVAPTPTLILEKECVGKTWPTYWDALKQ 834
Cdd:COG0128    393 LRAEGPVTIDDAECVAKSFPDFFELLES 420
AroB COG0337
3-dehydroquinate synthetase [Amino acid transport and metabolism]; 3-dehydroquinate synthetase ...
25-387 9.96e-129

3-dehydroquinate synthetase [Amino acid transport and metabolism]; 3-dehydroquinate synthetase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis


Pssm-ID: 440106  Cd Length: 355  Bit Score: 404.47  E-value: 9.96e-129
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690   25 YIVQDLLTNLPST--------TYVLVTDTNLGSIYREKFAKIFNEAAAALSPAprlltkEIPPGENSKSRQGKADIEDWM 96
Cdd:COG0337     16 RIGRGLLDELGELlaellkgrRVLVVTDENVAPLYGERLRAALEAAGFEVHLL------VLPDGEASKTLETLERILDAL 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690   97 LQQTCGRDTVIIALGGGVIGDLLGFVAATYMRGIRFVQVPTTLLAMVDSSIGGKTAIDTPLGKNLIGAIWQPHRIYIDID 176
Cdd:COG0337     90 LEAGLDRDDLVVALGGGVVGDLAGFAAATYLRGVPFIQVPTTLLAQVDSSVGGKTGVNHPGGKNLIGAFHQPRAVLIDLD 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  177 FIDTLPEREFINGMAEVIKTAAISDEKEFAALEQHADAILkaarskpgKGRFDLVRQVVKDrivaSARHKAFVVTADERE 256
Cdd:COG0337    170 FLKTLPERELRAGLAEVIKYGLIADAEFFEWLEENADALL--------ARDPEALEEAIAR----SCEIKAEVVAADERE 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  257 GGLRNLLNLGHSIGHAIEAILSPQVLHGECVAIGMVKELDLARYLGILKPVAVSRMVKCLSKYGLPTSLKDsrvrkhtag 336
Cdd:COG0337    238 SGLRALLNFGHTFGHAIEAATGYRLLHGEAVAIGMVFAARLSARLGLLSEEDVERIRALLEALGLPTRLPA--------- 308
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2459786690  337 khCSLEQMMANMALDKKNDGPRKKVVLLSAIGQTYEpkASVVSNEDIRAVL 387
Cdd:COG0337    309 --LDPEALLAAMKRDKKVRGGKLRFVLLRGIGKAVI--VDDVDEELLRAAL 355
PRK02427 PRK02427
3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
389-834 2.48e-127

3-phosphoshikimate 1-carboxyvinyltransferase; Provisional


Pssm-ID: 235037 [Multi-domain]  Cd Length: 435  Bit Score: 404.14  E-value: 2.48e-127
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  389 PSIEVIPGVPKDLNVVCAPPGSKSISNRALVLAALGSGTVRVKNLLHSDDTEVMLNALERLGAatfawEDEGEVLVVNGN 468
Cdd:PRK02427     1 MMMMLLIIPPSPLSGTVRVPGSKSISHRALLLAALAEGETTITNLLRSEDTLATLNALRALGV-----EIEDDEVVVEGV 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  469 GGKMQASPTE-LYLGNAGTASRFLTSVATLSGKGSVdyniLTGNNRMKQRPIGDLVDALTINGAQVEYlEKAGSLPLKIa 547
Cdd:PRK02427    76 GGGGLKEPEDvLDCGNSGTTMRLLTGLLALQPGEVV----LTGDESLRKRPMGRLLDPLRQMGAKIEG-RDEGYLPLTI- 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  548 aSGGFKGGRINLAAKVSSQYVSSLLMCAPYAKEPVTLKLVGGRPISLSYIEMTTAMMRSFGIDVQKSTTEEW-TYHIPQG 626
Cdd:PRK02427   150 -RGGKKGGPIEYDGPVSSQFVKSLLLLAPLFAEGDTETTVIEPLPSRPHTEITLRMLRAFGVEVENVEGWGYrRIVIKGG 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  627 SYNNPPEYVIESDASSATYPLAIAAVT-GTTCTVPNIGSASLQGDARFaVEVLRPMGCKVEQTATSTTVTGPAD-----G 700
Cdd:PRK02427   229 QRLRGQDITVPGDPSSAAFFLAAAAITgGSEVTITNVGLNSTQGGKAI-IDVLEKMGADIEIENEREGGEPVGDirvrsS 307
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  701 VLRPLpNVDMEPMTDAFLGASVLAAIAQGEggnhaTRIYGIANQRVKECNRIEAMRVELAKFGVVCREHPDGLEIDGidr 780
Cdd:PRK02427   308 ELKGI-DIDIPDIIDEAPTLAVLAAFAEGT-----TVIRNAEELRVKETDRIAAMATELRKLGAEVEETEDGLIITG--- 378
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2459786690  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 8.59e-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: 8.59e-124
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690   77 IPPGENSKSRQGKADIEDWMLQQTCGRDTVIIALGGGVIGDLLGFVAATYMRGIRFVQVPTTLLAMVDSSIGGKTAIDTP 156
Cdd:pfam01761    4 IPDGEKSKTLETLERIYDALLEAGLDRSSLLIALGGGVIGDLAGFVAATYMRGIRFIQVPTTLLAQVDSSVGGKTGINHP 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  157 LGKNLIGAIWQPHRIYIDIDFIDTLPEREFINGMAEVIKTAAISDEKEFAALEQHADAILkaarskpgkgrfDLVRQVVK 236
Cdd:pfam01761   84 LGKNLIGAFYQPKAVLIDLDFLKTLPDREFRAGLAEVIKYGLIADAEFFEWLEENAEALL------------NLDPDALE 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  237 DRIVASARHKAFVVTADEREGGLRNLLNLGHSIGHAIEAILSP-QVLHGECVAIGMVKELDLARYLGILKPVAVSRMVKC 315
Cdd:pfam01761  152 EAIARSCEVKADVVAQDEKESGLRALLNLGHTFGHAIEALSGYgALLHGEAVAIGMVLAARLSERLGLLDEADVERIRAL 231
                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 2459786690  316 LSKYGLPTSLKDSrvrkhtagkhcSLEQMMANMALDKKN 354
Cdd:pfam01761  232 LKKYGLPTSLPDL-----------DVEQLLAAMARDKKV 259
EPSP_synthase pfam00275
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);
398-832 4.81e-114

EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);


Pssm-ID: 395213  Cd Length: 415  Bit Score: 366.62  E-value: 4.81e-114
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  398 PKDLNVVCAPPGSKSISNRALVLAALGSGTVRVKNLLHSDDTEVMLNALERLGAATFAWEDEGEVLVVNGNGGKMQASP- 476
Cdd:pfam00275    3 GSRLSGEVKIPGSKSNSHRALILAALAAGESTITNLLDSDDTLTMLEALRALGAEIIKLDDEKSVVIVEGLGGSFEAPEd 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  477 TELYLGNAGTASRFLTSVATLSGKGSVdyniLTGNNRMKQRPIGDLVDALTINGAQVEYLEKAGSLPLKIAasgGFKGGR 556
Cdd:pfam00275   83 LVLDMGNSGTALRPLTGRLALQSGEVV----LPGDCSIGKRPMDRLLDALRQLGAEIEGREGYNYAPLKVR---GLRLGG 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  557 INLAAKVSSQYVSSLLMCAP-YAKEPVTLKlvggRPISLSYIEMTTAMMRSFGIDVQKSTTEE-WTYHIPQGSYnnPPEY 634
Cdd:pfam00275  156 IHIDGDVSSQFVTSLLMLAAlLAEGTTTIE----NLASEPYIDDTENMLKKFGAKIEGSGTELsITVKGGEKLP--GQEY 229
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  635 VIESDASSATYPLAIAAVTGTTCTVPNIGSASLQGDaRFAVEVLRPMGCKVEQTATSTTVTGPadGVLRPLPnVDMEPMT 714
Cdd:pfam00275  230 RVEGDRSSAAYFLVAAAITGGTVTVENVGINSLQGD-EALLEILEKMGAEITQEEDADIVVGP--PGLRGKA-VDIRTAP 305
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  715 DAFLGASVLAAIAQGEggnhaTRIYGIANQRVKECNRIEAMRVELAKFGVVCREHPDGLEIDGIDrSTLRHpaGGVFCYD 794
Cdd:pfam00275  306 DPAPTTAVLAAFAEGT-----TRIEGISELRVKETDRLFAMATELRRLGADVEELPDGLIIIPAV-KELKG--AEVDSYG 377
                          410       420       430
                   ....*....|....*....|....*....|....*...
gi 2459786690  795 DHRVAFSFSILSLVAPTPTLILEKECVGKTWPTYWDAL 832
Cdd:pfam00275  378 DHRIAMALALAGLVAEGETIIDDIECTDRSFPDFEEKL 415
aroB TIGR01357
3-dehydroquinate synthase; This model represents 3-dehydroquinate synthase, the enzyme ...
40-387 2.24e-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: 2.24e-112
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690   40 VLVTDTNLGSIYREKFAkifnEAAAALSPAPRLLTkeIPPGENSKSRQGKADIEDWMLQQTCGRDTVIIALGGGVIGDLL 119
Cdd:TIGR01357   24 VIITDETVADLYGDKLL----EALQALGYNVLKLT--VPDGEESKSLETVQRLYDQLLEAGLDRSSTIIALGGGVVGDLA 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  120 GFVAATYMRGIRFVQVPTTLLAMVDSSIGGKTAIDTPLGKNLIGAIWQPHRIYIDIDFIDTLPEREFINGMAEVIKTAAI 199
Cdd:TIGR01357   98 GFVAATYMRGIRFIQVPTTLLAMVDSSVGGKTGINFPGGKNLIGTFYQPKAVLIDPDFLKTLPDRELRSGMAEVIKHGLI 177
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  200 SDEKEFAALEQHADAILkaaRSKPGKGRFDLVRQVVKDrivasarhKAFVVTADEREGGLRNLLNLGHSIGHAIEAILSP 279
Cdd:TIGR01357  178 ADAELFDELESNDKLRL---NLQELEHLEELIKRSIEV--------KASIVAEDEKESGLRAILNFGHTIGHAIEAEAGY 246
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  280 -QVLHGECVAIGMVKELDLARYLGILKPVAVSRMVKCLSKYGLPTSLKdsrvrkhtagKHCSLEQMMANMALDKKNDGPR 358
Cdd:TIGR01357  247 gKIPHGEAVAIGMVCEAKLSERLGLLPAELIERLVQLLKRYGLPTDLP----------KDLDVDELLNAMLNDKKNSGGK 316
                          330       340
                   ....*....|....*....|....*....
gi 2459786690  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 1.24e-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: 1.24e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690 1282 GEIPAKKFAIFGKPVSVSRSPAMHNTLFEQNGLPYVYTRLETDQAQDVKEFIRS--PDFGGASATIPLKLDIIPLIDEVL 1359
Cdd:TIGR01809    1 GNKGPKKAFIIGKPIAHSRSPHLHNAGYEILGLPDKTYEFETCSAEELKEVLSGfgPQFGGASVTIPLKFAILRFADEHT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690 1360 NEAEIIGAVNTIIPVegkdGSTRLIGRNTDWSGIVRCLREAGAHSNEGESSALVIGGGGTARAAIYALHNMGFSTVYVLG 1439
Cdd:TIGR01809   81 DRASLIGSVNTLLRT----QNGIWKGDNTDWDGIAGALANIGKFEPLAGFRGLVIGAGGTSRAAVYALASLGVTDITVIN 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690 1440 RSPEKIQNMASTFPTGFDIRVLENASDIENIP---RVAVGTIPGDRPIEANMREILCTIFERSGRAADGksaaVLLEMAY 1516
Cdd:TIGR01809  157 RNPDKLSRLVDLGVQVGVITRLEGDSGGLAIEkaaEVLVSTVPADVPADYVDLFATVPFLLLKRKSSEG----IFLDAAY 232
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 2459786690 1517 KPSVTPLMQLASDSGWTTIPGLEALVGQGVYQFEYWTGITPVYEVARNAV 1566
Cdd:TIGR01809  233 DPWPTPLVAIVSAAGWRVISGLQMLLHQGFAQFEQWTGMPAPREAMACAL 282
PLN02834 PLN02834
3-dehydroquinate synthase
30-364 6.21e-74

3-dehydroquinate synthase


Pssm-ID: 215448  Cd Length: 433  Bit Score: 253.54  E-value: 6.21e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690   30 LLTNLPSTTYVLVTDTNLGSIYREKFAKIFneaaAALSPAPRLLTKEIPPGENSKSRQGKADIEDWMLQQTCGRDTVIIA 109
Cdd:PLN02834    94 LQRHVHGKRVLVVTNETVAPLYLEKVVEAL----TAKGPELTVESVILPDGEKYKDMETLMKVFDKALESRLDRRCTFVA 169
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  110 LGGGVIGDLLGFVAATYMRGIRFVQVPTTLLAMVDSSIGGKTAIDTPLGKNLIGAIWQPHRIYIDIDFIDTLPEREFING 189
Cdd:PLN02834   170 LGGGVIGDMCGFAAASYQRGVNFVQIPTTVMAQVDSSVGGKTGVNHPLGKNMIGAFYQPQCVLIDTDTLATLPDRELASG 249
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  190 MAEVIKTAAISDEKEFAALEQHADAILkaARsKPGKGRFDLVRqvvkdrivaSARHKAFVVTADEREGGLRNLLNLGHSI 269
Cdd:PLN02834   250 IAEVVKYGLIRDAEFFEWQEANMEKLL--AR-DPGALAYAIKR---------SCENKAEVVSLDEKESGLRATLNLGHTF 317
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  270 GHAIEAILSP-QVLHGECVAIGMVKELDLARYLGILKPVAVSRMVKCLSKYGLPTSLKDSrvrkhtagkhCSLEQMMANM 348
Cdd:PLN02834   318 GHAIETGPGYgEWLHGEAVAAGTVMAADMSYRLGWIDMSLVNRIFALLKRAKLPTNPPEK----------MTVEMFKSLM 387
                          330
                   ....*....|....*.
gi 2459786690  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 5.73e-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: 5.73e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690 1051 SLTLTDLRDSGDLLRTVASGSDAVELRVDLLKDPSSgngipSAEYVAEQISFYRSRVSLPIVFTIRTVSQGGKfPNDAHD 1130
Cdd:pfam01487    3 PLTGKTLEEILEELESGKEGADLVELRVDLLEEPVE-----DAEDVSEQLALLRRVGDLPLIFTFRTKSEGGE-PDGSEE 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690 1131 AALELIMLAIRSGCEFIDLEITFPEDLLRKVAESK--AHAKIIASHHDPQGKLNWAngSWIQYYNKALQYG-DIIKLVGV 1207
Cdd:pfam01487   77 EYLELLRLALRLGVDYVDVELFLPEEILKELIEAKheGGTKVIGSYHDFEGTPSWE--ELISRYEKMQALGaDIVKIAVM 154
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2459786690 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 8.86e-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: 8.86e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690 1047 SFFMSLTLTDLRDSGDLLRTVAS-GSDAVELRVDLLKDPSSGNgipSAEYVAEQISFyrSRVSLPIVFTIRTVSQGGKFP 1125
Cdd:TIGR01093    1 KIFVPLTAPDLEEALAEAEKICEkGADIVELRVDLLKDVSSNN---DVDALSEQLSE--LRVDKPLIFTIRTQSEGGKFP 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690 1126 NDAHDAALELIMLAIRSGCEFIDLEITFPEDLLRKVAES--KAHAKIIASHHDPQGKLNWANgsWIQYYNKALQY-GDII 1202
Cdd:TIGR01093   76 GNEEEYFEELKRAAESLGPDFVDIELFLPDDAVKELINIakKGGTKIIMSNHDFQKTPSWEE--IVERLRKALSYgADIV 153
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2459786690 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 2459786690 1287 KKFAIFGKPVSVSRSPAMHNTLFEQNGLPYVYTRLETDqAQDVKEFI---RSPDFGGASATIPLKLDIIPLIDEVLNEAE 1363
Cdd:COG0169      5 RLYGVIGDPIAHSLSPAIHNAAFAALGLDAVYVAFDVP-PEDLAAAVaglRALGIRGLNVTIPHKEAAIPLLDELDPRAR 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690 1364 IIGAVNTIIPVEGkdgstRLIGRNTDWSGIVRCLREAGAhsNEGESSALVIGGGGTARAAIYALHNMGFSTVYVLGRSPE 1443
Cdd:COG0169     84 LIGAVNTVVFEDG-----RLIGDNTDGIGFVRALREAGV--DLAGKRVLVLGAGGAARAVAAALAEAGAAEITIVNRTPE 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690 1444 KIQNMASTFPtgfdIRVLENAsDIENIPRVA--------VGTIPGDR-PIEAnmrEILctifersgraadgKSAAVLLEM 1514
Cdd:COG0169    157 RAEALAARLG----VRAVPLD-DLAAALAGAdlvinatpLGMAGGDAlPLPA---SLL-------------APGAVVYDL 215
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2459786690 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 1.81e-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: 1.81e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690 1047 SFFMSLTLTDLRDSGDLLRTVASGSDAVELRVDLLKDPSsgngipsAEYVAEQISFYRSRVSLPIVFTIRTVSQGGKFPn 1126
Cdd:cd00502      1 KICVPLTGPDLLEEALSLLELLLGADAVELRVDLLEDPS-------IDDVAEQLSLLRELTPLPIIFTVRTKSEGGNFE- 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690 1127 DAHDAALELIMLAIRSGCEFIDLEITF--PEDLLRKVAesKAHAKIIASHHDPQGKLNwaNGSWIQYYNKALQYG-DIIK 1203
Cdd:cd00502     73 GSEEEYLELLEEALKLGPDYVDIELDSalLEELINSRK--KGNTKIIGSYHDFSGTPS--DEELVSRLEKMAALGaDIVK 148
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2459786690 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 2459786690 1287 KKFAIFGKPVSVSRSPAMHNTLFEQNGLPYVYTRLETDqAQDVKEFIRS---PDFGGASATIPLKLDIIPLIDEVLNEAE 1363
Cdd:PRK00258     6 RLYAVIGNPIAHSKSPLIHNAAFKQLGLDGVYLAILVP-PEDLEDAVKGffaLGGRGANVTVPFKEAAFALADELSERAR 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690 1364 IIGAVNTIIPVEGkdgstRLIGRNTDWSGIVRCLREAGAHSNEGESsALVIGGGGTARAAIYALHNMGFSTVYVLGRSPE 1443
Cdd:PRK00258    85 LIGAVNTLVLEDG-----RLIGDNTDGIGFVRALEERLGVDLKGKR-ILILGAGGAARAVILPLLDLGVAEITIVNRTVE 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690 1444 KIQNMASTFPTGFDIRVLENASDIENIPRVAVGTIP----GDRPIEANMREILctifersgraadgKSAAVLLEMAYKPS 1519
Cdd:PRK00258   159 RAEELAKLFGALGKAELDLELQEELADFDLIINATSagmsGELPLPPLPLSLL-------------RPGTIVYDMIYGPL 225
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 2459786690 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 8.81e-49

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: 170.81  E-value: 8.81e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  861 SIVIIGMRGAGKTTTGRWAAKALNRKFIDLDVELEQTEGKTIPDLIKERGWQGFRDAELSLFKRALTerPTGHVFACGGG 940
Cdd:cd00464      1 NIVLIGMMGAGKTTVGRLLAKALGLPFVDLDELIEQRAGMSIPEIFAEEGEEGFRELEREVLLLLLT--KENAVIATGGG 78
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2459786690  941 IVEIAEARNilidYHKNKGNVLLVMRDIKKVMEFLNIDKTRPAY----IEDMMSVWLRRKPWYQECSNV 1005
Cdd:cd00464     79 AVLREENRR----LLLENGIVVWLDASPEELLERLARDKTRPLLqdedPERLRELLEEREPLYREVADL 143
SKI pfam01202
Shikimate kinase;
868-1031 2.33e-45

Shikimate kinase;


Pssm-ID: 426122 [Multi-domain]  Cd Length: 159  Bit Score: 161.21  E-value: 2.33e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  868 RGAGKTTTGRWAAKALNRKFIDLDVELEQTEGKTIPDLIKERGWQGFRDAELSLFKRALTERptGHVFACGGGIVEIAEA 947
Cdd:pfam01202    1 MGAGKSTIGRLLAKALGLPFIDTDEEIEKRTGMSIAEIFEEEGEEGFRRLESEVLKELLAEH--GLVIATGGGAVLSEEN 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  948 RNILidyhKNKGNVLLVMRDIKKVMEFLNIDKTRPAYIEDMMSVWLRRKPWYQECSNVQYYSRHSSSPELALAMDDFDRF 1027
Cdd:pfam01202   79 RDLL----KERGIVIYLDAPLEVLLERLKRDKTRPLLQNKDPEEELLELLFEERDPLYEEAADIVIDTDESSPEEVATEI 154

                   ....
gi 2459786690 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 9.31e-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: 9.31e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690 1388 TDWSGIVRCLREAGAHSNEGesSALVIGGGGTARAAIYALHNMGFSTVYVLGRSPEKIQNMASTFPTGFDIRVLENASDI 1467
Cdd:cd01065      1 TDGLGFVRALEEAGIELKGK--KVLILGAGGAARAVAYALAELGAAKIVIVNRTLEKAKALAERFGELGIAIAYLDLEEL 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690 1468 ENIPRVAVGTIPGDrpieanMREILCTIFErsgrAADGKSAAVLLEMAYKPSVTPLMQLASDSGWTTIPGLEALVGQGVY 1547
Cdd:cd01065     79 LAEADLIINTTPVG------MKPGDELPLP----PSLLKPGGVVYDVVYNPLETPLLKEARALGAKTIDGLEMLVYQAAE 148

                   ....*..
gi 2459786690 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 3.02e-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: 3.02e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  862 IVIIGMRGAGKTTTGRWAAKALNRKFIDLDVELEQTEGKTIPDLIKERGWQGFRDAELSLFKRALTERPTghVFACGGGI 941
Cdd:COG0703      1 IVLIGMMGAGKSTVGRLLAKRLGLPFVDTDAEIEERAGMSIPEIFAEEGEAGFRELEREVLAELLEEENA--VIATGGGA 78
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2459786690  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 3.82e-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: 3.82e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690 1058 RDSGDLLRTVA----SGSDAVELRVDLLKDPSsgngipsAEYVAEQISFYRSRVSLPIVFTIRTVSQGGKFPNDaHDAAL 1133
Cdd:COG0710     13 ATPEDLLAEAEaaarAGADLVELRLDYLEDPD-------LEELKELLEALREYGGLPLIFTFRTAEEGGEFEGS-EEERL 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690 1134 ELIMLAIRS-GCEFIDLEITFPEDLLRKVAES--KAHAKIIASHHD-----PQGKLnwangswIQYYNKALQYG-DIIKL 1204
Cdd:COG0710     85 ELLRAAADSaGVDLVDVELDTLEDDVDDLIEAarEAGVKVIVSYHDfektpSAEEL-------VEILEKMQELGaDIVKI 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690 1205 VGVAETLKDNTALREFKDWAEQaHPDVPVIAINMGDKGQLSR----MLNGFLT--PVSHPalpfkAAPGQLSAAEIRKGL 1278
Cdd:COG0710    158 AVMAKSPEDVLRLLEATLEAKE-ELDRPVITMAMGELGKISRilgpLFGSALTyaSVGEA-----SAPGQIDVEELRELL 231

                   ....*
gi 2459786690 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 2459786690 1291 IFGKPVSVSRSPAMHNTLFEQNGLPYVYTRLET--DQAQDVKEFIRSPDFGGASATIPLKLDIIPLIDEVLNEAEIIGAV 1368
Cdd:pfam08501    1 VIGNPISHSLSPAIHNAAFKALGLNGVYVAFEVppDNLPDFVEGLRALGFRGLNVTIPHKEAAIPLLDELSPEAKAIGAV 80

                   ...
gi 2459786690 1369 NTI 1371
Cdd:pfam08501   81 NTI 83
aroK PRK00131
shikimate kinase; Reviewed
861-1004 4.54e-26

shikimate kinase; Reviewed


Pssm-ID: 234654 [Multi-domain]  Cd Length: 175  Bit Score: 106.43  E-value: 4.54e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  861 SIVIIGMRGAGKTTTGRWAAKALNRKFIDLDVELEQTEGKTIPDLIKERGWQGFRDAElslfKRALTE--RPTGHVFACG 938
Cdd:PRK00131     6 NIVLIGFMGAGKSTIGRLLAKRLGYDFIDTDHLIEARAGKSIPEIFEEEGEAAFRELE----EEVLAEllARHNLVISTG 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2459786690  939 GGIVEIAEARNILIDYHKnkgNVLLVMrDIKKVMEFLNIDKTRP--------AYIEDMMSVwlrRKPWYQECSN 1004
Cdd:PRK00131    82 GGAVLREENRALLRERGT---VVYLDA-SFEELLRRLRRDRNRPllqtndpkEKLRDLYEE---RDPLYEEVAD 148
aroD PRK02412
type I 3-dehydroquinate dehydratase;
1068-1283 5.27e-18

type I 3-dehydroquinate dehydratase;


Pssm-ID: 235036  Cd Length: 253  Bit Score: 85.33  E-value: 5.27e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690 1068 ASGSDAVELRVDLLKDPSSGNGIPSaeyVAEQIsfYRSRVSLPIVFTIRTVSQGGKFP-NDahDAALELIMLAIRSGC-E 1145
Cdd:PRK02412    39 KYDADIIEWRADFLEKISDVESVLA---AAPAI--REKFAGKPLLFTFRTAKEGGEIAlSD--EEYLALIKAVIKSGLpD 111
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690 1146 FIDLEITFPEDLLRK-VAESKAH-AKIIASHHD-----PQGKLnwangswIQYYNKALQYG-DIIKLVGVAETLKDN--- 1214
Cdd:PRK02412   112 YIDVELFSGKDVVKEmVAFAHEHgVKVVLSYHDfektpPKEEI-------VERLRKMESLGaDIVKIAVMPQSEQDVltl 184
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2459786690 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 1.31e-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: 468.58  E-value: 1.31e-151
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  406 APPGSKSISNRALVLAALGSGTVRVKNLLHSDDTEVMLNALERLGAatfAWEDEGEVLVVNGNGGKMQASPTELYLGNAG 485
Cdd:cd01556      6 TVPGSKSISHRALLLAALAEGESRIENLLDSDDTLATLEALRALGA---KIEEEGGTVEIVGGGGLGLPPEAVLDCGNSG 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  486 TASRFLTSVATLSGKGSVdyniLTGNNRMKQRPIGDLVDALTINGAQVEYLEKAGSLPLKIaaSGGFKGGRINLAAKVSS 565
Cdd:cd01556     83 TTMRLLTGLLALQGGDSV----LTGDESLRKRPMGRLVDALRQLGAEIEGREGGGYPPLIG--GGGLKGGEVEIPGAVSS 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  566 QYVSSLLMCAPYAKEPVTLKLvgGRPISLSYIEMTTAMMRSFGIDVQKSTTEEWTYHiPQGSYnNPPEYVIESDASSATY 645
Cdd:cd01556    157 QFKSALLLAAPLAEGPTTIII--GELESKPYIDHTERMLRAFGAEVEVDGYRTITVK-GGQKY-KGPEYTVEGDASSAAF 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  646 PLAIAAVTGTTCTVPNIGSASlqGDARFaVEVLRPMGCKVEQTATsTTVTGPADGVLRPLpNVDMEPMTDAFLGASVLAA 725
Cdd:cd01556    233 FLAAAAITGSEIVIKNVGLNS--GDTGI-IDVLKEMGADIEIGNE-DTVVVESGGKLKGI-DIDGNDIPDEAPTLAVLAA 307
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  726 IAQGEggnhaTRIYGIANQRVKECNRIEAMRVELAKFGVVCREHPDGLEIDGidrSTLRHPAGGVFCYDDHRVAFSFSIL 805
Cdd:cd01556    308 FAEGP-----TRIRNAAELRVKESDRIAAMATELRKLGADVEETEDGLIIEG---GPLKGAGVEVYTYGDHRIAMSFAIA 379
                          410       420
                   ....*....|....*....|....*....
gi 2459786690  806 SLVAPTPTLILEKECVGKTWPTYWDALKQ 834
Cdd:cd01556    380 GLVAEGGVTIEDPECVAKSFPNFFEDLES 408
aroA TIGR01356
3-phosphoshikimate 1-carboxyvinyltransferase; This model represents ...
406-834 1.73e-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: 433.24  E-value: 1.73e-138
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  406 APPGSKSISNRALVLAALGSGTVRVKNLLHSDDTEVMLNALERLGAATfawEDEGEVLVVNGNGGKMQASptELYLGNAG 485
Cdd:TIGR01356    4 RAPGSKSITHRALILAALAEGETRVRNLLRSEDTLATLDALRALGAKI---EDGGEVAVIEGVGGKEPQA--ELDLGNSG 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  486 TASRFLTSVATLSGKGSVdyniLTGNNRMKQRPIGDLVDALTINGAQVEYLEKAGSLPLKIaaSGGFKGGRINLAAKVSS 565
Cdd:TIGR01356   79 TTARLLTGVLALADGEVV----LTGDESLRKRPMGRLVDALRQLGAEISSLEGGGSLPLTI--SGPLPGGIVYISGSASS 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  566 QYVSSLLMCAPyAKEPVTLKLVGGRPISLSYIEMTTAMMRSFGIDVQKSTTEewTYHIPQGSYNNPPEYVIESDASSATY 645
Cdd:TIGR01356  153 QYKSALLLAAP-ALQAVGITIVGEPLKSRPYIEITLDLLGSFGVEVERSDGR--KIVVPGGQKYGPQGYDVPGDYSSAAF 229
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  646 PLAIAAVTGTTCTVPNIGSASLQGDARFaVEVLRPMGCKVEQTATSTTVTGPADgvLRPLpNVDMEPMTDAFLGASVLAA 725
Cdd:TIGR01356  230 FLAAAAITGGRVTLENLGINPTQGDKAI-IIVLEEMGADIEVEEDDLIVEGASG--LKGI-KIDMDDMIDELPTLAVLAA 305
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  726 IAQGEggnhaTRIYGIANQRVKECNRIEAMRVELAKFGVVCREHPDGLEIDGidRSTLRhpAGGVFCYDDHRVAFSFSIL 805
Cdd:TIGR01356  306 FAEGV-----TRITGAEELRVKESDRIAAIAEELRKLGVDVEEFEDGLYIRG--KKELK--GAVVDTFGDHRIAMAFAVA 376
                          410       420
                   ....*....|....*....|....*....
gi 2459786690  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 2.52e-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: 2.52e-138
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690   25 YIVQDLLTNLPS-------TTYVLVTDTNLGSIYREKFAKIFNEAAAalspapRLLTKEIPPGENSKSRQGKADIEDWML 97
Cdd:cd08195      5 LIGSGLLDKLGEllelkkgSKVVIVTDENVAKLYGELLLKSLEAAGF------KVEVIVIPAGEKSKSLETVERIYDFLL 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690   98 QQTCGRDTVIIALGGGVIGDLLGFVAATYMRGIRFVQVPTTLLAMVDSSIGGKTAIDTPLGKNLIGAIWQPHRIYIDIDF 177
Cdd:cd08195     79 EAGLDRDSLLIALGGGVVGDLAGFVASTYMRGIPFIQVPTTLLAQVDSSIGGKTGINLPGGKNLIGAFYQPKAVLIDPDF 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  178 IDTLPEREFINGMAEVIKTAAISDEKEFAALEQHADAILKAarskpgkgRFDLVRQVVKdrivASARHKAFVVTADEREG 257
Cdd:cd08195    159 LKTLPEREFRSGLAEVIKYGLIADKELFEFLEKNLDKILAR--------DPEALEEIIA----RSVEIKADIVEEDEREK 226
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  258 GLRNLLNLGHSIGHAIEAILSPQVLHGECVAIGMVKELDLARYLGILKPVAVSRMVKCLSKYGLPTSLKDsrvrkhtagk 337
Cdd:cd08195    227 GLRAILNFGHTFGHAIESASGYKLLHGEAVAIGMVAAARLSVKLGLLSEEDLERIRALLKKLGLPTSIKD---------- 296
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|
gi 2459786690  338 hCSLEQMMANMALDKKNDGPRKKVVLLSAIGQTYepKASVVSNEDIRAVL 387
Cdd:cd08195    297 -LDPEELLEAMKRDKKNRGGKIRFVLLKGIGKAV--IVDDVSEEEIREAL 343
AroA COG0128
5-enolpyruvylshikimate-3-phosphate synthase [Amino acid transport and metabolism]; ...
408-834 1.62e-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: 1.62e-135
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  408 PGSKSISNRALVLAALGSGTVRVKNLLHSDDTEVMLNALERLGaATFAWEDEGEVlVVNGNGGKMQASPTELYLGNAGTA 487
Cdd:COG0128     19 PGSKSISHRALLLAALAEGESTIRNLLESDDTLATLEALRALG-AEIEELDGGTL-RVTGVGGGLKEPDAVLDCGNSGTT 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  488 SRFLTSVATLSGKGSVdyniLTGNNRMKQRPIGDLVDALTINGAQVEYLEKaGSLPLKIAAsGGFKGGRINLAAKVSSQY 567
Cdd:COG0128     97 MRLLTGLLALQPGEVV----LTGDESLRKRPMGRLLDPLRQLGARIESRGG-GYLPLTIRG-GPLKGGEYEIPGSASSQF 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  568 VSSLLMCAPYAKEPVTLKlVGGRPISLSYIEMTTAMMRSFGIDVQKSTTEEWTYHIPQgSYnNPPEYVIESDASSATYPL 647
Cdd:COG0128    171 KSALLLAGPLAEGGLEIT-VTGELESKPYRDHTERMLRAFGVEVEVEGYRRFTVPGGQ-RY-RPGDYTVPGDISSAAFFL 247
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  648 AIAAVTGTTCTVPNIGSASLQGDARFaVEVLRPMGCKVEQTATSTTVTGpadGVLRPLpNVDMEPMTDAFLGASVLAAIA 727
Cdd:COG0128    248 AAAAITGSEVTVEGVGLNSTQGDTGI-LDILKEMGADIEIENDGITVRG---SPLKGI-DIDLSDIPDEAPTLAVLAAFA 322
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  728 QGEggnhaTRIYGIANQRVKECNRIEAMRVELAKFGVVCREHPDGLEIDGidRSTLRhpaGGVF-CYDDHRVAFSFSILS 806
Cdd:COG0128    323 EGT-----TRIRGAAELRVKESDRIAAMATELRKLGADVEETEDGLIIEG--GPKLK---GAEVdSYGDHRIAMAFAVAG 392
                          410       420
                   ....*....|....*....|....*...
gi 2459786690  807 LVAPTPTLILEKECVGKTWPTYWDALKQ 834
Cdd:COG0128    393 LRAEGPVTIDDAECVAKSFPDFFELLES 420
AroB COG0337
3-dehydroquinate synthetase [Amino acid transport and metabolism]; 3-dehydroquinate synthetase ...
25-387 9.96e-129

3-dehydroquinate synthetase [Amino acid transport and metabolism]; 3-dehydroquinate synthetase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis


Pssm-ID: 440106  Cd Length: 355  Bit Score: 404.47  E-value: 9.96e-129
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690   25 YIVQDLLTNLPST--------TYVLVTDTNLGSIYREKFAKIFNEAAAALSPAprlltkEIPPGENSKSRQGKADIEDWM 96
Cdd:COG0337     16 RIGRGLLDELGELlaellkgrRVLVVTDENVAPLYGERLRAALEAAGFEVHLL------VLPDGEASKTLETLERILDAL 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690   97 LQQTCGRDTVIIALGGGVIGDLLGFVAATYMRGIRFVQVPTTLLAMVDSSIGGKTAIDTPLGKNLIGAIWQPHRIYIDID 176
Cdd:COG0337     90 LEAGLDRDDLVVALGGGVVGDLAGFAAATYLRGVPFIQVPTTLLAQVDSSVGGKTGVNHPGGKNLIGAFHQPRAVLIDLD 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  177 FIDTLPEREFINGMAEVIKTAAISDEKEFAALEQHADAILkaarskpgKGRFDLVRQVVKDrivaSARHKAFVVTADERE 256
Cdd:COG0337    170 FLKTLPERELRAGLAEVIKYGLIADAEFFEWLEENADALL--------ARDPEALEEAIAR----SCEIKAEVVAADERE 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  257 GGLRNLLNLGHSIGHAIEAILSPQVLHGECVAIGMVKELDLARYLGILKPVAVSRMVKCLSKYGLPTSLKDsrvrkhtag 336
Cdd:COG0337    238 SGLRALLNFGHTFGHAIEAATGYRLLHGEAVAIGMVFAARLSARLGLLSEEDVERIRALLEALGLPTRLPA--------- 308
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2459786690  337 khCSLEQMMANMALDKKNDGPRKKVVLLSAIGQTYEpkASVVSNEDIRAVL 387
Cdd:COG0337    309 --LDPEALLAAMKRDKKVRGGKLRFVLLRGIGKAVI--VDDVDEELLRAAL 355
PRK02427 PRK02427
3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
389-834 2.48e-127

3-phosphoshikimate 1-carboxyvinyltransferase; Provisional


Pssm-ID: 235037 [Multi-domain]  Cd Length: 435  Bit Score: 404.14  E-value: 2.48e-127
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  389 PSIEVIPGVPKDLNVVCAPPGSKSISNRALVLAALGSGTVRVKNLLHSDDTEVMLNALERLGAatfawEDEGEVLVVNGN 468
Cdd:PRK02427     1 MMMMLLIIPPSPLSGTVRVPGSKSISHRALLLAALAEGETTITNLLRSEDTLATLNALRALGV-----EIEDDEVVVEGV 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  469 GGKMQASPTE-LYLGNAGTASRFLTSVATLSGKGSVdyniLTGNNRMKQRPIGDLVDALTINGAQVEYlEKAGSLPLKIa 547
Cdd:PRK02427    76 GGGGLKEPEDvLDCGNSGTTMRLLTGLLALQPGEVV----LTGDESLRKRPMGRLLDPLRQMGAKIEG-RDEGYLPLTI- 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  548 aSGGFKGGRINLAAKVSSQYVSSLLMCAPYAKEPVTLKLVGGRPISLSYIEMTTAMMRSFGIDVQKSTTEEW-TYHIPQG 626
Cdd:PRK02427   150 -RGGKKGGPIEYDGPVSSQFVKSLLLLAPLFAEGDTETTVIEPLPSRPHTEITLRMLRAFGVEVENVEGWGYrRIVIKGG 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  627 SYNNPPEYVIESDASSATYPLAIAAVT-GTTCTVPNIGSASLQGDARFaVEVLRPMGCKVEQTATSTTVTGPAD-----G 700
Cdd:PRK02427   229 QRLRGQDITVPGDPSSAAFFLAAAAITgGSEVTITNVGLNSTQGGKAI-IDVLEKMGADIEIENEREGGEPVGDirvrsS 307
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  701 VLRPLpNVDMEPMTDAFLGASVLAAIAQGEggnhaTRIYGIANQRVKECNRIEAMRVELAKFGVVCREHPDGLEIDGidr 780
Cdd:PRK02427   308 ELKGI-DIDIPDIIDEAPTLAVLAAFAEGT-----TVIRNAEELRVKETDRIAAMATELRKLGAEVEETEDGLIITG--- 378
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2459786690  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 8.59e-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: 8.59e-124
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690   77 IPPGENSKSRQGKADIEDWMLQQTCGRDTVIIALGGGVIGDLLGFVAATYMRGIRFVQVPTTLLAMVDSSIGGKTAIDTP 156
Cdd:pfam01761    4 IPDGEKSKTLETLERIYDALLEAGLDRSSLLIALGGGVIGDLAGFVAATYMRGIRFIQVPTTLLAQVDSSVGGKTGINHP 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  157 LGKNLIGAIWQPHRIYIDIDFIDTLPEREFINGMAEVIKTAAISDEKEFAALEQHADAILkaarskpgkgrfDLVRQVVK 236
Cdd:pfam01761   84 LGKNLIGAFYQPKAVLIDLDFLKTLPDREFRAGLAEVIKYGLIADAEFFEWLEENAEALL------------NLDPDALE 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  237 DRIVASARHKAFVVTADEREGGLRNLLNLGHSIGHAIEAILSP-QVLHGECVAIGMVKELDLARYLGILKPVAVSRMVKC 315
Cdd:pfam01761  152 EAIARSCEVKADVVAQDEKESGLRALLNLGHTFGHAIEALSGYgALLHGEAVAIGMVLAARLSERLGLLDEADVERIRAL 231
                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 2459786690  316 LSKYGLPTSLKDSrvrkhtagkhcSLEQMMANMALDKKN 354
Cdd:pfam01761  232 LKKYGLPTSLPDL-----------DVEQLLAAMARDKKV 259
EPSP_synthase pfam00275
EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);
398-832 4.81e-114

EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase);


Pssm-ID: 395213  Cd Length: 415  Bit Score: 366.62  E-value: 4.81e-114
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  398 PKDLNVVCAPPGSKSISNRALVLAALGSGTVRVKNLLHSDDTEVMLNALERLGAATFAWEDEGEVLVVNGNGGKMQASP- 476
Cdd:pfam00275    3 GSRLSGEVKIPGSKSNSHRALILAALAAGESTITNLLDSDDTLTMLEALRALGAEIIKLDDEKSVVIVEGLGGSFEAPEd 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  477 TELYLGNAGTASRFLTSVATLSGKGSVdyniLTGNNRMKQRPIGDLVDALTINGAQVEYLEKAGSLPLKIAasgGFKGGR 556
Cdd:pfam00275   83 LVLDMGNSGTALRPLTGRLALQSGEVV----LPGDCSIGKRPMDRLLDALRQLGAEIEGREGYNYAPLKVR---GLRLGG 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  557 INLAAKVSSQYVSSLLMCAP-YAKEPVTLKlvggRPISLSYIEMTTAMMRSFGIDVQKSTTEE-WTYHIPQGSYnnPPEY 634
Cdd:pfam00275  156 IHIDGDVSSQFVTSLLMLAAlLAEGTTTIE----NLASEPYIDDTENMLKKFGAKIEGSGTELsITVKGGEKLP--GQEY 229
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  635 VIESDASSATYPLAIAAVTGTTCTVPNIGSASLQGDaRFAVEVLRPMGCKVEQTATSTTVTGPadGVLRPLPnVDMEPMT 714
Cdd:pfam00275  230 RVEGDRSSAAYFLVAAAITGGTVTVENVGINSLQGD-EALLEILEKMGAEITQEEDADIVVGP--PGLRGKA-VDIRTAP 305
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  715 DAFLGASVLAAIAQGEggnhaTRIYGIANQRVKECNRIEAMRVELAKFGVVCREHPDGLEIDGIDrSTLRHpaGGVFCYD 794
Cdd:pfam00275  306 DPAPTTAVLAAFAEGT-----TRIEGISELRVKETDRLFAMATELRRLGADVEELPDGLIIIPAV-KELKG--AEVDSYG 377
                          410       420       430
                   ....*....|....*....|....*....|....*...
gi 2459786690  795 DHRVAFSFSILSLVAPTPTLILEKECVGKTWPTYWDAL 832
Cdd:pfam00275  378 DHRIAMALALAGLVAEGETIIDDIECTDRSFPDFEEKL 415
aroB TIGR01357
3-dehydroquinate synthase; This model represents 3-dehydroquinate synthase, the enzyme ...
40-387 2.24e-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: 2.24e-112
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690   40 VLVTDTNLGSIYREKFAkifnEAAAALSPAPRLLTkeIPPGENSKSRQGKADIEDWMLQQTCGRDTVIIALGGGVIGDLL 119
Cdd:TIGR01357   24 VIITDETVADLYGDKLL----EALQALGYNVLKLT--VPDGEESKSLETVQRLYDQLLEAGLDRSSTIIALGGGVVGDLA 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  120 GFVAATYMRGIRFVQVPTTLLAMVDSSIGGKTAIDTPLGKNLIGAIWQPHRIYIDIDFIDTLPEREFINGMAEVIKTAAI 199
Cdd:TIGR01357   98 GFVAATYMRGIRFIQVPTTLLAMVDSSVGGKTGINFPGGKNLIGTFYQPKAVLIDPDFLKTLPDRELRSGMAEVIKHGLI 177
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  200 SDEKEFAALEQHADAILkaaRSKPGKGRFDLVRQVVKDrivasarhKAFVVTADEREGGLRNLLNLGHSIGHAIEAILSP 279
Cdd:TIGR01357  178 ADAELFDELESNDKLRL---NLQELEHLEELIKRSIEV--------KASIVAEDEKESGLRAILNFGHTIGHAIEAEAGY 246
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  280 -QVLHGECVAIGMVKELDLARYLGILKPVAVSRMVKCLSKYGLPTSLKdsrvrkhtagKHCSLEQMMANMALDKKNDGPR 358
Cdd:TIGR01357  247 gKIPHGEAVAIGMVCEAKLSERLGLLPAELIERLVQLLKRYGLPTDLP----------KDLDVDELLNAMLNDKKNSGGK 316
                          330       340
                   ....*....|....*....|....*....
gi 2459786690  359 KKVVLLSAIGQTYEpkASVVSNEDIRAVL 387
Cdd:TIGR01357  317 IRFVLLEEIGKAAL--AREVPDEMVLELL 343
PRK11860 PRK11860
bifunctional 3-phosphoshikimate 1-carboxyvinyltransferase/cytidylate kinase;
408-889 5.65e-101

bifunctional 3-phosphoshikimate 1-carboxyvinyltransferase/cytidylate kinase;


Pssm-ID: 237003 [Multi-domain]  Cd Length: 661  Bit Score: 338.95  E-value: 5.65e-101
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  408 PGSKSISNRALVLAALGSGTVRVKNLLHSDDTEVMLNALERLGAatfAWEDEGEVLVVNGNGGKMQASPTELYLGNAGTA 487
Cdd:PRK11860    22 PGSKSISNRVLLLAALSEGTTTVRDLLDSDDTRVMLDALRALGC---GVEQLGDTYRITGLGGQFPVKQADLFLGNAGTA 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  488 SRFLTSVATLSGKgsvDYNiLTGNNRMKQRPIGDLVDALTINGAQVEYLEKAGSLPLKIAASGGFKGGRINLAAKVSSQY 567
Cdd:PRK11860    99 MRPLTAALALLGG---EYE-LSGVPRMHERPIGDLVDALRQLGCDIDYLGNEGFPPLRIGPAPLRLDAPIRVRGDVSSQF 174
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  568 VSSLLMCAPY-AKEPVTLKLVgGRPISLSYIEMTTAMMRSFGIDVQKsttEEWT-YHIPQGS-YNNPPEYVIESDASSAT 644
Cdd:PRK11860   175 LTALLMALPLvARRDITIEVV-GELISKPYIEITLNLLARFGIAVQR---EGWQrFTIPAGSrYRSPGEIHVEGDASSAS 250
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  645 YPLAIAAV-TGTTCTVPNIGSASLQGDARFAvEVLRPMGCKVEQTATSTTVTGPAdGVLRPLpNVDMEPMTDAFLGASVL 723
Cdd:PRK11860   251 YFIAAGAIaGGAPVRIEGVGRDSIQGDIRFA-EAARAMGAQVTSGPNWLEVRRGA-WPLKAI-DLDCNHIPDAAMTLAVM 327
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  724 AAIAQGeggnhATRIYGIANQRVKECNRIEAMRVELAKFGVVCREHPDGLEIDGIDRSTLRHPAgGVFCYDDHRVAFSFS 803
Cdd:PRK11860   328 ALYADG-----TTTLRNIASWRVKETDRIAAMATELRKLGATVEEGADYIRVTPPAQAADWKAA-AIHTYDDHRMAMCFS 401
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  804 ILSL-VAPTPTLILEKECVGKTWPTYWDALkqkFGVslkgkelAESEITHGPAdrsdasIVIIGMRGAGKTTTGRWAAKA 882
Cdd:PRK11860   402 LAAFnPAGLPVRINDPKCVAKTFPDYFEAL---FSV-------AQADADRVPV------ICIDGPTASGKGTVAARVAEA 465

                   ....*..
gi 2459786690  883 LNRKFID 889
Cdd:PRK11860   466 LGYHYLD 472
PLN02338 PLN02338
3-phosphoshikimate 1-carboxyvinyltransferase
408-833 1.03e-98

3-phosphoshikimate 1-carboxyvinyltransferase


Pssm-ID: 177972 [Multi-domain]  Cd Length: 443  Bit Score: 325.16  E-value: 1.03e-98
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  408 PGSKSISNRALVLAALGSGTVRVKNLLHSDDTEVMLNALERLGAaTFAWEDEGEVLVVNGNGGKMQAS-----PTELYLG 482
Cdd:PLN02338    19 PGSKSLSNRILLLAALSEGTTVVDNLLDSDDIRYMLGALKTLGL-NVEEDSENNRAVVEGCGGKFPVSgdskeDVELFLG 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  483 NAGTASRFLTSVATLSGkGSVDYnILTGNNRMKQRPIGDLVDALTINGAQVEYLEKAGSLPLKIAASGGFKGGRINLAAK 562
Cdd:PLN02338    98 NAGTAMRPLTAAVTAAG-GNASY-VLDGVPRMRERPIGDLVDGLKQLGADVECTLGTNCPPVRVNAAGGLPGGKVKLSGS 175
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  563 VSSQYVSSLLMCAPYAKEPVTLKLVgGRPISLSYIEMTTAMMRSFGIDVQKSTTEEwTYHIPQG-SYNNPPEYVIESDAS 641
Cdd:PLN02338   176 ISSQYLTALLMAAPLALGDVEIEIV-DKLISVPYVEMTLKLMERFGVSVEHSDSWD-RFFIKGGqKYKSPGNAYVEGDAS 253
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  642 SATYPLAIAAVTGTTCTVPNIGSASLQGDARFAvEVLRPMGCKVEQTATSTTVTGPADGVL--RPLP--NVDMEPMTDAF 717
Cdd:PLN02338   254 SASYFLAGAAITGGTVTVEGCGTTSLQGDVKFA-EVLEKMGAKVEWTENSVTVTGPPRDAFggKHLKaiDVNMNKMPDVA 332
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  718 LGASVLAAIAQGeggnhATRIYGIANQRVKECNRIEAMRVELAKFGVVCREHPD--------GLEIDGIDrstlrhpagg 789
Cdd:PLN02338   333 MTLAVVALFADG-----PTAIRDVASWRVKETERMIAICTELRKLGATVEEGPDyciitppkKLKPAEID---------- 397
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....
gi 2459786690  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 1.24e-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: 1.24e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690 1282 GEIPAKKFAIFGKPVSVSRSPAMHNTLFEQNGLPYVYTRLETDQAQDVKEFIRS--PDFGGASATIPLKLDIIPLIDEVL 1359
Cdd:TIGR01809    1 GNKGPKKAFIIGKPIAHSRSPHLHNAGYEILGLPDKTYEFETCSAEELKEVLSGfgPQFGGASVTIPLKFAILRFADEHT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690 1360 NEAEIIGAVNTIIPVegkdGSTRLIGRNTDWSGIVRCLREAGAHSNEGESSALVIGGGGTARAAIYALHNMGFSTVYVLG 1439
Cdd:TIGR01809   81 DRASLIGSVNTLLRT----QNGIWKGDNTDWDGIAGALANIGKFEPLAGFRGLVIGAGGTSRAAVYALASLGVTDITVIN 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690 1440 RSPEKIQNMASTFPTGFDIRVLENASDIENIP---RVAVGTIPGDRPIEANMREILCTIFERSGRAADGksaaVLLEMAY 1516
Cdd:TIGR01809  157 RNPDKLSRLVDLGVQVGVITRLEGDSGGLAIEkaaEVLVSTVPADVPADYVDLFATVPFLLLKRKSSEG----IFLDAAY 232
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 2459786690 1517 KPSVTPLMQLASDSGWTTIPGLEALVGQGVYQFEYWTGITPVYEVARNAV 1566
Cdd:TIGR01809  233 DPWPTPLVAIVSAAGWRVISGLQMLLHQGFAQFEQWTGMPAPREAMACAL 282
PLN02834 PLN02834
3-dehydroquinate synthase
30-364 6.21e-74

3-dehydroquinate synthase


Pssm-ID: 215448  Cd Length: 433  Bit Score: 253.54  E-value: 6.21e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690   30 LLTNLPSTTYVLVTDTNLGSIYREKFAKIFneaaAALSPAPRLLTKEIPPGENSKSRQGKADIEDWMLQQTCGRDTVIIA 109
Cdd:PLN02834    94 LQRHVHGKRVLVVTNETVAPLYLEKVVEAL----TAKGPELTVESVILPDGEKYKDMETLMKVFDKALESRLDRRCTFVA 169
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  110 LGGGVIGDLLGFVAATYMRGIRFVQVPTTLLAMVDSSIGGKTAIDTPLGKNLIGAIWQPHRIYIDIDFIDTLPEREFING 189
Cdd:PLN02834   170 LGGGVIGDMCGFAAASYQRGVNFVQIPTTVMAQVDSSVGGKTGVNHPLGKNMIGAFYQPQCVLIDTDTLATLPDRELASG 249
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  190 MAEVIKTAAISDEKEFAALEQHADAILkaARsKPGKGRFDLVRqvvkdrivaSARHKAFVVTADEREGGLRNLLNLGHSI 269
Cdd:PLN02834   250 IAEVVKYGLIRDAEFFEWQEANMEKLL--AR-DPGALAYAIKR---------SCENKAEVVSLDEKESGLRATLNLGHTF 317
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  270 GHAIEAILSP-QVLHGECVAIGMVKELDLARYLGILKPVAVSRMVKCLSKYGLPTSLKDSrvrkhtagkhCSLEQMMANM 348
Cdd:PLN02834   318 GHAIETGPGYgEWLHGEAVAAGTVMAADMSYRLGWIDMSLVNRIFALLKRAKLPTNPPEK----------MTVEMFKSLM 387
                          330
                   ....*....|....*.
gi 2459786690  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 5.73e-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: 5.73e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690 1051 SLTLTDLRDSGDLLRTVASGSDAVELRVDLLKDPSSgngipSAEYVAEQISFYRSRVSLPIVFTIRTVSQGGKfPNDAHD 1130
Cdd:pfam01487    3 PLTGKTLEEILEELESGKEGADLVELRVDLLEEPVE-----DAEDVSEQLALLRRVGDLPLIFTFRTKSEGGE-PDGSEE 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690 1131 AALELIMLAIRSGCEFIDLEITFPEDLLRKVAESK--AHAKIIASHHDPQGKLNWAngSWIQYYNKALQYG-DIIKLVGV 1207
Cdd:pfam01487   77 EYLELLRLALRLGVDYVDVELFLPEEILKELIEAKheGGTKVIGSYHDFEGTPSWE--ELISRYEKMQALGaDIVKIAVM 154
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2459786690 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 3.67e-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: 3.67e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690   23 GTYIVQDLLTNLPST---TYVLVTDTNLGSIYREKFAKIFNEAAAalsPAPRLLtkeIPPGENSKSRQGKADIEDWMLQQ 99
Cdd:cd08197      7 GRGILESLLSILEELkadRHFLVTDSNVNDLYGDRLLEGLKKAGI---PVELLV---VPAGESNKTLSTLTELAERLIAA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  100 TCGRDTVIIALGGGVIGDLLGFVAATYMRGIRFVQVPTTLLAMVDSSIGGKTAIDTPLGKNLIGAIWQPHRIYIDIDFID 179
Cdd:cd08197     81 GITRRSVIIALGGGVVGNIAGLLAGLLYRGIRLVHVPTTLLAQSDSVLSLKQAVNGKSGKNLVGSYYAPLFVFVDTEFLK 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  180 TLPEREFINGMAEVIKTAAISDEKEFAALEQHADAILKAArskpgkgrFDLVRQVVKDrivaSARHKAFVVTAD--EREG 257
Cdd:cd08197    161 TLPPRQIRSGLCEAIKNALIQDPEFLDYLEDYLNSDLDYD--------PEFLEKVIDL----SIEAKLEVLSNDpyEKKE 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  258 GLrnLLNLGHSIGHAIEAILSPQVLHGECVAIGMVKELDLARYLGILKPVAVSRMVKCLSKYGLPTSLKDsrvrkhtagk 337
Cdd:cd08197    229 GL--ILEYGHTVGHAIELLSGGELSHGEAVAIGMCVAAEISHLLGLLSEEDVDKHYELLEKIGLPTIIPD---------- 296
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2459786690  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 8.86e-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: 8.86e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690 1047 SFFMSLTLTDLRDSGDLLRTVAS-GSDAVELRVDLLKDPSSGNgipSAEYVAEQISFyrSRVSLPIVFTIRTVSQGGKFP 1125
Cdd:TIGR01093    1 KIFVPLTAPDLEEALAEAEKICEkGADIVELRVDLLKDVSSNN---DVDALSEQLSE--LRVDKPLIFTIRTQSEGGKFP 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690 1126 NDAHDAALELIMLAIRSGCEFIDLEITFPEDLLRKVAES--KAHAKIIASHHDPQGKLNWANgsWIQYYNKALQY-GDII 1202
Cdd:TIGR01093   76 GNEEEYFEELKRAAESLGPDFVDIELFLPDDAVKELINIakKGGTKIIMSNHDFQKTPSWEE--IVERLRKALSYgADIV 153
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2459786690 1203 KLVGVAETLKDNTALREFKDWAeQAHPDVPVIAINMGDKGQLSRMLNGFLTPVSHP-ALPFKAAPGQLSAAEIRKGL 1278
Cdd:TIGR01093  154 KIAVMANSKEDVLTLLSATNKV-DTHYDVPLITMSMGDRGKISRVLGAVFGSVLTFgSLGKASAPGQISVDDLRELL 229
PRK11861 PRK11861
bifunctional prephenate dehydrogenase/3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
408-830 3.75e-67

bifunctional prephenate dehydrogenase/3-phosphoshikimate 1-carboxyvinyltransferase; Provisional


Pssm-ID: 183343 [Multi-domain]  Cd Length: 673  Bit Score: 241.15  E-value: 3.75e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  408 PGSKSISNRALVLAALGSGTVRVKNLLHSDDTEVMLNALERLGAATfawEDEGEVLVVNGNGGKMQASPTELYLGNAGTA 487
Cdd:PRK11861   258 PGSKSISNRVLLLAALAEGETTVTNLLDSDDTRVMLDALTKLGVKL---SRDGGTCVVGGTRGAFTAKTADLFLGNAGTA 334
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  488 SRFLTSVATLSGKgsvDYNIlTGNNRMKQRPIGDLVDALTINGAQVEYLEKAGSLPLKIAASGGFKGGRINLAAKVSSQY 567
Cdd:PRK11861   335 VRPLTAALAVNGG---EYRI-HGVPRMHERPIGDLVDGLRQIGARIDYEGNEGFPPLRIRPATISVDAPIRVRGDVSSQF 410
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  568 VSSLLMCAPY--AKEPVTLKLVGGRPISLSYIEMTTAMMRSFGIDVQKSTTEEWTyhIPQG-SYNNPPEYVIESDASSAT 644
Cdd:PRK11861   411 LTALLMTLPLvkAKDGASVVEIDGELISKPYIEITIKLMARFGVTVERDGWQRFT--VPAGvRYRSPGTIMVEGDASSAS 488
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  645 YPLAIAAVTGTTCTVPNIGSASLQGDARFAvEVLRPMGCKVEQTATSTTVTGPA--DGVLRPLpNVDMEPMTDAFLGASV 722
Cdd:PRK11861   489 YFLAAGALGGGPLRVEGVGRASIQGDVGFA-NALMQMGANVTMGDDWIEVRGIGhdHGRLAPI-DMDFNLIPDAAMTIAV 566
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  723 LAAIAQGeggnhATRIYGIANQRVKECNRIEAMRVELAKFGVVCREHPDGLEIDGIDRSTlrhPAGGVFCYDDHRVAFSF 802
Cdd:PRK11861   567 AALFADG-----PSTLRNIGSWRVKETDRIAAMATELRKVGATVEEGADYLVVTPPAQLT---PNASIDTYDDHRMAMCF 638
                          410       420
                   ....*....|....*....|....*...
gi 2459786690  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 2459786690 1287 KKFAIFGKPVSVSRSPAMHNTLFEQNGLPYVYTRLETDqAQDVKEFI---RSPDFGGASATIPLKLDIIPLIDEVLNEAE 1363
Cdd:COG0169      5 RLYGVIGDPIAHSLSPAIHNAAFAALGLDAVYVAFDVP-PEDLAAAVaglRALGIRGLNVTIPHKEAAIPLLDELDPRAR 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690 1364 IIGAVNTIIPVEGkdgstRLIGRNTDWSGIVRCLREAGAhsNEGESSALVIGGGGTARAAIYALHNMGFSTVYVLGRSPE 1443
Cdd:COG0169     84 LIGAVNTVVFEDG-----RLIGDNTDGIGFVRALREAGV--DLAGKRVLVLGAGGAARAVAAALAEAGAAEITIVNRTPE 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690 1444 KIQNMASTFPtgfdIRVLENAsDIENIPRVA--------VGTIPGDR-PIEAnmrEILctifersgraadgKSAAVLLEM 1514
Cdd:COG0169    157 RAEALAARLG----VRAVPLD-DLAAALAGAdlvinatpLGMAGGDAlPLPA---SLL-------------APGAVVYDL 215
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2459786690 1515 AYKPSVTPLMQLASDSGWTTIPGLEALVGQGVYQFEYWTGITPVYEVARNAVL 1567
Cdd:COG0169    216 VYNPLETPLLRAARARGARVIDGLGMLVHQAAEAFELWTGVRPPVEAMRAALR 268
DHQ-like cd08169
Dehydroquinate synthase-like which includes dehydroquinate synthase, 2-deoxy-scyllo-inosose ...
39-368 4.35e-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: 4.35e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690   39 YVLVTDTNLGSIYREKFAKIFnEAAAALSPAPrlltkeIPPGENSKSRQGKADIEDWMLQQTCGRDTVIIALGGGVIGDL 118
Cdd:cd08169     26 CLIIVDSGVPDLIVNYLAEYF-GYYLEVHVFI------IQGGEAYKTFQTVVEELERAAALHLNRHSAVVAVGGGATGDV 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  119 LGFVAATYMRGIRFVQVPTTLLAMVDSSIGGKTAIDTPLGKNLIGAIWQPHRIYIDIDFIDTLPEREFINGMAEVIKTAA 198
Cdd:cd08169     99 VGFAAATYFRGIAFIRVPTTLLAQSDSSVGIKVGINTRGGKNLLGAFYPPRAVFADFSFLKTLPFRQVRAGMAELVKMAL 178
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  199 ISDEKEFAALEQHADAIlkaarskpgkgRFDLVRQVvkDRIVASARH-KAFVVTADEREGGLRNLLNLGHSIGHAIEAIL 277
Cdd:cd08169    179 IADNDFFEFLEDKANSA-----------TVYSPEQL--EKLINKCISlKLDVVVADEDEQGKRRGLNYGHTFGHALELAS 245
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  278 SPQVLHGECVAIGMVKELDLARYLGILKPVAVSRMVKCLSKYGLPTSLKDSRvrkhtagkhcSLEQMMANMALDKKNDGP 357
Cdd:cd08169    246 GYKIPHGEAVAVGMAYAAKIANRLGLLPEHDVSRIIWLLNKLGLPLDHPLAL----------DPDSLYEYLESDKKSLYG 315
                          330
                   ....*....|.
gi 2459786690  358 RKKVVLLSAIG 368
Cdd:cd08169    316 NLGMILLSGVG 326
EPT-like cd01554
Enol pyruvate transferases family includes EPSP synthases and UDP-N-acetylglucosamine ...
408-833 2.76e-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: 2.76e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  408 PGSKSISNRALVLAALGSGTVRVKNLLHSDDTEVMLNALERLGAatfAWEDEGEVLVVNGNGGKMQASPT-ELYLGNAGT 486
Cdd:cd01554      8 PGDKSISHRSLIFASLAEGETKVYNILRGEDVLSTMQVLRDLGV---EIEDKDGVITIQGVGMAGLKAPQnALNLGNSGT 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  487 ASRFLTSVATLsGKGSVdynILTGNNRMKQRPIGDLVDALTINGAQVEYLEKAGSLPLKIaaSGGFKGGRINLAAKVSSQ 566
Cdd:cd01554     85 AIRLISGVLAG-ADFEV---ELFGDDSLSKRPMDRVTLPLKKMGASISGQEERDLPPLLK--GGKNLGPIHYEDPIASAQ 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  567 YVSSLLMCAPYAKEPVTLKLVGGRPislsYIEMTTAMMRSFGIDVQKSTTEEWTYHIPQgSYNNpPEYVIESDASSATYP 646
Cdd:cd01554    159 VKSALMFAALLAKGETVIIEAAKEP----TINHTENMLQTFGGHISVQGTKKIVVQGPQ-KLTG-QKYVVPGDISSAAFF 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  647 LAIAAVTGTTCTVPNIGSASlqGDARFAvEVLRPMGCKVEQTATSTTVT-GPADGVlrplpNVDMEP---MTDAFLGASV 722
Cdd:cd01554    233 LVAAAIAPGRLVLQNVGINE--TRTGII-DVLRAMGAKIEIGEDTISVEsSDLKAT-----EICGALiprLIDELPIIAL 304
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  723 LAAIAQGeggnhATRIYGIANQRVKECNRIEAMRVELAKFGVVCREHPDGLEIDGIDRSTlrhpAGGVFCYDDHRVAFSF 802
Cdd:cd01554    305 LALQAQG-----TTVIKDAEELKVKETDRIFVVADELNSMGADIEPTADGMIIKGKEKLH----GARVNTFGDHRIGMMT 375
                          410       420       430
                   ....*....|....*....|....*....|.
gi 2459786690  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 1.81e-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: 1.81e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690 1047 SFFMSLTLTDLRDSGDLLRTVASGSDAVELRVDLLKDPSsgngipsAEYVAEQISFYRSRVSLPIVFTIRTVSQGGKFPn 1126
Cdd:cd00502      1 KICVPLTGPDLLEEALSLLELLLGADAVELRVDLLEDPS-------IDDVAEQLSLLRELTPLPIIFTVRTKSEGGNFE- 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690 1127 DAHDAALELIMLAIRSGCEFIDLEITF--PEDLLRKVAesKAHAKIIASHHDPQGKLNwaNGSWIQYYNKALQYG-DIIK 1203
Cdd:cd00502     73 GSEEEYLELLEEALKLGPDYVDIELDSalLEELINSRK--KGNTKIIGSYHDFSGTPS--DEELVSRLEKMAALGaDIVK 148
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2459786690 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 2459786690 1287 KKFAIFGKPVSVSRSPAMHNTLFEQNGLPYVYTRLETDqAQDVKEFIRS---PDFGGASATIPLKLDIIPLIDEVLNEAE 1363
Cdd:PRK00258     6 RLYAVIGNPIAHSKSPLIHNAAFKQLGLDGVYLAILVP-PEDLEDAVKGffaLGGRGANVTVPFKEAAFALADELSERAR 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690 1364 IIGAVNTIIPVEGkdgstRLIGRNTDWSGIVRCLREAGAHSNEGESsALVIGGGGTARAAIYALHNMGFSTVYVLGRSPE 1443
Cdd:PRK00258    85 LIGAVNTLVLEDG-----RLIGDNTDGIGFVRALEERLGVDLKGKR-ILILGAGGAARAVILPLLDLGVAEITIVNRTVE 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690 1444 KIQNMASTFPTGFDIRVLENASDIENIPRVAVGTIP----GDRPIEANMREILctifersgraadgKSAAVLLEMAYKPS 1519
Cdd:PRK00258   159 RAEELAKLFGALGKAELDLELQEELADFDLIINATSagmsGELPLPPLPLSLL-------------RPGTIVYDMIYGPL 225
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 2459786690 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 2459786690   77 IPPGENSKSRQGKADIEDWMLQQTCGRDTVIIALGGGVIGDLLGFVAATYMRGIRFVQVPTTLLAMVDSSIGGKTAIDTP 156
Cdd:PRK14021   243 IPDAEAGKTIEVANGIWQRLGNEGFTRSDAIVGLGGGAATDLAGFVAATWMRGIRYVNCPTSLLAMVDASTGGKTGINTP 322
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  157 LGKNLIGAIWQPHRIYIDIDFIDTLPEREFINGMAEVIKTAAISDEKEFAALEQHADAIlkaaRSKPGKGRFDL-VRQVV 235
Cdd:PRK14021   323 QGKNLVGSFYTPAGVLADTKTLATLPNDIFIEGLGEVAKSGFIRDPEILRILEDHAAEL----RAFDGSTFLGSpLEDVV 398
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  236 KDRIVASARHKAFVVTADEREGGLRNLLNLGHSIGHAIEAILSPQVLHGECVAIGMVKELDLARYLGILKPVAVSRMVKC 315
Cdd:PRK14021   399 AELIERTVKVKAYHVSSDLKEAGLREFLNYGHTLGHAIEKLEHFRWRHGNAVAVGMVYAAELAHLLGYIDQDLVDYHRSL 478
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2459786690  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 8.72e-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: 8.72e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690   40 VLVTDTNLGSIYREKFAKIFNEAAAALspapRLLTkeIPPGENSKSRQGKADIEDWMLQQTCGRDTVIIALGGGVIGDLL 119
Cdd:cd08199     30 LVVVDENVDRLYGARIRAYFAAHGIEA----TILV--LPGGEANKTMETVLRIVDALDDFGLDRREPVIAIGGGVLLDVV 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  120 GFVAATYMRGIRFVQVPTTLLAMVDSSIGGKTAIDTPLGKNLIGAIWQPHRIYIDIDFIDTLPEREFINGMAEVIKTAAI 199
Cdd:cd08199    104 GFAASLYRRGVPYIRVPTTLLGLVDAGVGIKTGVNFGGHKNRLGAYYPPVATLLDRSFLKTLPRRHIRNGLAEIIKMALV 183
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  200 SDEKEFAALEQHADAILKAarskpgkgRFDLvrQVVKDRIVasarHKAFVVTADE-----REGGLRNLLNLGHSIGHAIE 274
Cdd:cd08199    184 KDAELFELLEEHGAALVET--------RFFQ--DEVADEII----RRAIQGMLEElapnlWEHDLERLVDFGHTFSPILE 249
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  275 AILSPQVLHGECVAIGMVKELDLARYLGILKPVAVSRMVKCLSKYGLPTSlkdsrvrkHTagkHCSLEQMM-ANMALDKK 353
Cdd:cd08199    250 MAAAPELLHGEAVAIDMALSAVLAYRRGLLSEEELDRILRLMRRLGLPVW--------HP---LCTPDLLWrALEDIVKH 318
                          330
                   ....*....|....*.
gi 2459786690  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 8.81e-49

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: 170.81  E-value: 8.81e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  861 SIVIIGMRGAGKTTTGRWAAKALNRKFIDLDVELEQTEGKTIPDLIKERGWQGFRDAELSLFKRALTerPTGHVFACGGG 940
Cdd:cd00464      1 NIVLIGMMGAGKTTVGRLLAKALGLPFVDLDELIEQRAGMSIPEIFAEEGEEGFRELEREVLLLLLT--KENAVIATGGG 78
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2459786690  941 IVEIAEARNilidYHKNKGNVLLVMRDIKKVMEFLNIDKTRPAY----IEDMMSVWLRRKPWYQECSNV 1005
Cdd:cd00464     79 AVLREENRR----LLLENGIVVWLDASPEELLERLARDKTRPLLqdedPERLRELLEEREPLYREVADL 143
SKI pfam01202
Shikimate kinase;
868-1031 2.33e-45

Shikimate kinase;


Pssm-ID: 426122 [Multi-domain]  Cd Length: 159  Bit Score: 161.21  E-value: 2.33e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  868 RGAGKTTTGRWAAKALNRKFIDLDVELEQTEGKTIPDLIKERGWQGFRDAELSLFKRALTERptGHVFACGGGIVEIAEA 947
Cdd:pfam01202    1 MGAGKSTIGRLLAKALGLPFIDTDEEIEKRTGMSIAEIFEEEGEEGFRRLESEVLKELLAEH--GLVIATGGGAVLSEEN 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  948 RNILidyhKNKGNVLLVMRDIKKVMEFLNIDKTRPAYIEDMMSVWLRRKPWYQECSNVQYYSRHSSSPELALAMDDFDRF 1027
Cdd:pfam01202   79 RDLL----KERGIVIYLDAPLEVLLERLKRDKTRPLLQNKDPEEELLELLFEERDPLYEEAADIVIDTDESSPEEVATEI 154

                   ....
gi 2459786690 1028 IQFV 1031
Cdd:pfam01202  155 LEAL 158
PLN02520 PLN02520
bifunctional 3-dehydroquinate dehydratase/shikimate dehydrogenase
1061-1555 3.90e-43

bifunctional 3-dehydroquinate dehydratase/shikimate dehydrogenase


Pssm-ID: 178135 [Multi-domain]  Cd Length: 529  Bit Score: 166.48  E-value: 3.90e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690 1061 GDLLRTVASGSDAVELRVDLLKDPSSGNGIPsaeyvaeqisFYRSRVSLPIVFTIRTVSQGGKFPNDaHDAALELIMLAI 1140
Cdd:PLN02520    39 IEMAKAKELGADLVEIRLDFLKNFNPREDLK----------TLIKQSPLPTLVTYRPKWEGGQYEGD-ENKRQDALRLAM 107
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690 1141 RSGCEFIDLEITFPEDLLRKVAESK-AHAKIIASHHDPQgklNWANGSWIQYYNKALQY--GDIIKLVGVAETLKDNTal 1217
Cdd:PLN02520   108 ELGADYVDVELKVAHEFINSISGKKpEKCKVIVSSHNYE---NTPSVEELGNLVARIQAtgADIVKIATTALDITDVA-- 182
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690 1218 REFKdwaEQAHPDVPVIAINMGDKGQLSRML----NGFLTPVSHPAlPFKAAPGQLSAAEIRKGLSIMGEIP-AKKFAIF 1292
Cdd:PLN02520   183 RMFQ---ITVHSQVPTIGLVMGERGLISRILcpkfGGYLTFGTLEA-GKVSAPGQPTIKDLLDLYNFRQIGPdTKVYGII 258
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690 1293 GKPVSVSRSPAMHNTLFEQNGLPYVYTRLETDqaqDVKEFIR---SPDFGGASATIPLKLDIIPLIDEVLNEAEIIGAVN 1369
Cdd:PLN02520   259 GKPVGHSKSPILHNEAFKSVGFNGVYVHLLVD---DLAKFLQtysSPDFAGFSCTIPHKEDALKCCDEVDPIAKSIGAIN 335
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690 1370 TII--PVEGKdgstrLIGRNTDWSGIVRCLREA--GAHSNEGESSAL------VIGGGGTARAAIYALHNMGfSTVYVLG 1439
Cdd:PLN02520   336 TIIrrPSDGK-----LVGYNTDYIGAISAIEDGlrASGSSPASGSPLagklfvVIGAGGAGKALAYGAKEKG-ARVVIAN 409
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690 1440 RSPEKIQNMASTFpTGFDIR-------------VLENASDIENIPRVAVGTIPgdrpieanmREILctifersgraadgK 1506
Cdd:PLN02520   410 RTYERAKELADAV-GGQALTladlenfhpeegmILANTTSVGMQPNVDETPIS---------KHAL-------------K 466
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*....
gi 2459786690 1507 SAAVLLEMAYKPSVTPLMQLASDSGWTTIPGLEALVGQGVYQFEYWTGI 1555
Cdd:PLN02520   467 HYSLVFDAVYTPKITRLLREAEESGAIIVSGTEMFIRQAYEQFERFTGL 515
aroE TIGR00507
shikimate dehydrogenase; This model finds proteins from prokaryotes and functionally ...
1287-1568 1.91e-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: 1.91e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690 1287 KKFAIFGKPVSVSRSPAMHNTLFEQNGLPYVYTRLET--DQAQDVKEFIRSPDFGGASATIPLKLDIIPLIDEVLNEAEI 1364
Cdd:TIGR00507    1 KLYGVIGNPIAHSKSPLIHNAFFKQLGLEGPYIAFLVppDDLEDALSGFFALGFKGANVTSPFKERAFQFLDEIDGRAKL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690 1365 IGAVNTIIPVEGKdgstrLIGRNTDWSGIVRCLREAGAHSNegESSALVIGGGGTARAAIYALHNMGfSTVYVLGRSPEK 1444
Cdd:TIGR00507   81 AGAVNTLVLEDGK-----LVGYNTDGIGLVSDLEQLIPLRP--NQNVLIIGAGGAAKAVALELLKAD-CNVIIANRTVSK 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690 1445 IQNMASTFP-TGFDIRVLENASDIENIPRVAVGTIPGDRPieanmreilcTIFERSGRAADGKSAAVLLEMAYKPSVTPL 1523
Cdd:TIGR00507  153 AEELAERFQrYGEIQAFSMDELPLHRVDLIINATSAGMSG----------NIDEPPVPAEYLKEGKLVYDLVYNPLETPF 222
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 2459786690 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 9.31e-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: 9.31e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690 1388 TDWSGIVRCLREAGAHSNEGesSALVIGGGGTARAAIYALHNMGFSTVYVLGRSPEKIQNMASTFPTGFDIRVLENASDI 1467
Cdd:cd01065      1 TDGLGFVRALEEAGIELKGK--KVLILGAGGAARAVAYALAELGAAKIVIVNRTLEKAKALAERFGELGIAIAYLDLEEL 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690 1468 ENIPRVAVGTIPGDrpieanMREILCTIFErsgrAADGKSAAVLLEMAYKPSVTPLMQLASDSGWTTIPGLEALVGQGVY 1547
Cdd:cd01065     79 LAEADLIINTTPVG------MKPGDELPLP----PSLLKPGGVVYDVVYNPLETPLLKEARALGAKTIDGLEMLVYQAAE 148

                   ....*..
gi 2459786690 1548 QFEYWTG 1554
Cdd:cd01065    149 AFELWTG 155
aroB PRK06203
3-dehydroquinate synthase; Reviewed
59-372 9.68e-36

3-dehydroquinate synthase; Reviewed


Pssm-ID: 235740  Cd Length: 389  Bit Score: 141.19  E-value: 9.68e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690   59 FNEAAAALSPAPRLltkeIPPGENSK-SRQGKADIEDWMLQQTCGRDTVIIALGGGVIGDLLGFVAATYMRGIRFVQVPT 137
Cdd:PRK06203    70 AHADVLELVAEPLV----VPGGEAAKnDPALVEALHAAINRHGIDRHSYVLAIGGGAVLDMVGYAAATAHRGVRLIRIPT 145
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  138 TLLAMVDSSIGGKTAIDTPLGKNLIGAIWQPHRIYIDIDFIDTLPEREFINGMAEVIKTAAISDEKEFAALEQHADAIlk 217
Cdd:PRK06203   146 TVLAQNDSGVGVKNGINAFGKKNFLGTFAPPYAVINDFAFLTTLPDRDWRAGLAEAVKVALIKDAAFFDWLEAHAAAL-- 223
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  218 aarskpgkGRFDLvrQVVKDRIVASAR-HKAFVVTA-DEREGGLRNLLNLGHSIGHAIEAILSPQVLHGECVAIGMVkeL 295
Cdd:PRK06203   224 --------AARDP--EAMEELIYRCAElHLEHIAGGgDPFEFGSSRPLDFGHWSAHKLEQLTNYALRHGEAVAIGIA--L 291
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  296 DlARY---LGILKPVAVSRMVKCLSKYGLPTSlkdsrvrkH-----TAGKHCSLEQmmanmALD--KKNDGPRKKVVLLS 365
Cdd:PRK06203   292 D-SLYsylLGLLSEAEAQRILALLRALGFPLY--------HpalatRDSKGRELLK-----GLEefREHLGGRLTITLLT 357

                   ....*..
gi 2459786690  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 2.12e-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: 2.12e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  103 RDTVIIALGGGVIGDLLGFVAATYMRGIRFVQVPTTLLAMVDSSIGGKTAIDTPLGKNLIGAIWQPHRIYIDIDFIDTLP 182
Cdd:cd08198     99 RHSYVVVIGGGAVLDAVGFAAAIAHRGIRLIRVPTTVLAQNDSGVGVKNGINFFGKKNFLGTFAPPFAVINDFDFLETLP 178
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  183 EREFINGMAEVIKTAAISDEKEFAALEQHADAILkaarskpgKGRFDLVRQVVK-------DRIVASarhkafvvtADER 255
Cdd:cd08198    179 DRDWRSGIAEAVKVALIKDASFFEWLERNAAALR--------QRDPDAMEKLIRrcaelhlDHIAAS---------GDPF 241
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2459786690  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 3.02e-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: 3.02e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  862 IVIIGMRGAGKTTTGRWAAKALNRKFIDLDVELEQTEGKTIPDLIKERGWQGFRDAELSLFKRALTERPTghVFACGGGI 941
Cdd:COG0703      1 IVLIGMMGAGKSTVGRLLAKRLGLPFVDTDAEIEERAGMSIPEIFAEEGEAGFRELEREVLAELLEEENA--VIATGGGA 78
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2459786690  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 2459786690  408 PGSKSISNRALVLAALGSGTVRVKNLLHSDDTEVMLNALERLGaATFAWEDEGEVlVVNGNGGK-MQASPTELYLGNAGT 486
Cdd:PRK14806   319 PGDKSISHRSIMLGSLAEGVTEVEGFLEGEDALATLQAFRDMG-VVIEGPHNGRV-TIHGVGLHgLKAPPGPLYMGNSGT 396
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  487 ASRFLTSVatLSGKgSVDyNILTGNNRMKQRPIGDLVDALTINGAQVEYLEKaGSLPLKIAASGGFKGGRINLAAkVSSQ 566
Cdd:PRK14806   397 SMRLLSGL--LAAQ-SFD-SVLTGDASLSKRPMERVAKPLREMGAVIETGEE-GRPPLSIRGGQRLKGIHYDLPM-ASAQ 470
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  567 YVSSLLMCAPYAK------EPVTlklvggrpiSLSYIEMttaMMRSFGIDVQkstTEEWTYHIPQGSYNNPPEYVIESDA 640
Cdd:PRK14806   471 VKSCLLLAGLYAEgetsvtEPAP---------TRDHTER---MLRGFGYPVK---VEGNTISVEGGGKLTATDIEVPADI 535
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  641 SSATYPLAIAAVT-GTTCTVPNIGSASlqgdARFAV-EVLRPMGCKVEqTATSTTVTGP--ADGVLR--PLPNVDMEP-- 712
Cdd:PRK14806   536 SSAAFFLVAASIAeGSELTLEHVGINP----TRTGViDILKLMGADIT-LENEREVGGEpvADIRVRgaRLKGIDIPEdq 610
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  713 ---MTDAFLGASVLAAIAQGEggnhaTRIYGIANQRVKECNRIEAMRVELAKFGVVCREHPDGLEIDGidrstlRHPAGG 789
Cdd:PRK14806   611 vplAIDEFPVLFVAAACAEGR-----TVLTGAEELRVKESDRIQVMADGLKTLGIDCEPTPDGIIIEG------GIFGGG 679
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2459786690  790 -VFCYDDHRVAFSFSILSLVAPTPTLILEKECVGKTWPTYwDALKQKFGVSL 840
Cdd:PRK14806   680 eVESHGDHRIAMSFSVASLRASGPITIHDCANVATSFPNF-LELANQVGIRI 730
AroD COG0710
3-dehydroquinate dehydratase [Amino acid transport and metabolism]; 3-dehydroquinate ...
1058-1283 3.82e-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: 3.82e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690 1058 RDSGDLLRTVA----SGSDAVELRVDLLKDPSsgngipsAEYVAEQISFYRSRVSLPIVFTIRTVSQGGKFPNDaHDAAL 1133
Cdd:COG0710     13 ATPEDLLAEAEaaarAGADLVELRLDYLEDPD-------LEELKELLEALREYGGLPLIFTFRTAEEGGEFEGS-EEERL 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690 1134 ELIMLAIRS-GCEFIDLEITFPEDLLRKVAES--KAHAKIIASHHD-----PQGKLnwangswIQYYNKALQYG-DIIKL 1204
Cdd:COG0710     85 ELLRAAADSaGVDLVDVELDTLEDDVDDLIEAarEAGVKVIVSYHDfektpSAEEL-------VEILEKMQELGaDIVKI 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690 1205 VGVAETLKDNTALREFKDWAEQaHPDVPVIAINMGDKGQLSR----MLNGFLT--PVSHPalpfkAAPGQLSAAEIRKGL 1278
Cdd:COG0710    158 AVMAKSPEDVLRLLEATLEAKE-ELDRPVITMAMGELGKISRilgpLFGSALTyaSVGEA-----SAPGQIDVEELRELL 231

                   ....*
gi 2459786690 1279 SIMGE 1283
Cdd:COG0710    232 ELLEA 236
PRK13951 PRK13951
bifunctional shikimate kinase AroK/3-dehydroquinate synthase AroB;
53-304 2.04e-31

bifunctional shikimate kinase AroK/3-dehydroquinate synthase AroB;


Pssm-ID: 172457 [Multi-domain]  Cd Length: 488  Bit Score: 130.41  E-value: 2.04e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690   53 EKFAKIFNEAAaalsPAPRLLtkeIPPGENSKSRQGKADIEDWMLQQTCGRDTVIIALGGGVIGDLLGFVAATYMRGIRF 132
Cdd:PRK13951   194 ERVEKIYGRYL----PENRLL---FPDGEEVKTLEHVSRAYYELVRMDFPRGKTIAGVGGGALTDFTGFVASTFKRGVGL 266
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  133 VQVPTTLLAMVDSSIGGKTAIDTPLGKNLIGAIWQPHRIYIDIDFIDTLPEREFINGMAEVIKTAAIS--DEKEFAALEQ 210
Cdd:PRK13951   267 SFYPTTLLAQVDASVGGKNAIDFAGVKNVVGTFRMPDYVIIDPTVTLSMDEGRFEEGVVEAFKMTILSgrGVELFDEPEK 346
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  211 hadaILKAarskpgkgRFDLVRQVVKdrivASARHKAFVVTADEREGGLRNLLNLGHSIGHAIEAILSpqVLHGECVAIG 290
Cdd:PRK13951   347 ----IEKR--------NLRVLSEMVK----ISVEEKARIVMEDPYDMGLRHALNLGHTLGHVYEMLEG--VPHGIAVAWG 408
                          250
                   ....*....|....
gi 2459786690  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 2459786690 1291 IFGKPVSVSRSPAMHNTLFEQNGLPYVYTRLET--DQAQDVKEFIRSPDFGGASATIPLKLDIIPLIDEVLNEAEIIGAV 1368
Cdd:pfam08501    1 VIGNPISHSLSPAIHNAAFKALGLNGVYVAFEVppDNLPDFVEGLRALGFRGLNVTIPHKEAAIPLLDELSPEAKAIGAV 80

                   ...
gi 2459786690 1369 NTI 1371
Cdd:pfam08501   81 NTI 83
aroK PRK00131
shikimate kinase; Reviewed
861-1004 4.54e-26

shikimate kinase; Reviewed


Pssm-ID: 234654 [Multi-domain]  Cd Length: 175  Bit Score: 106.43  E-value: 4.54e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  861 SIVIIGMRGAGKTTTGRWAAKALNRKFIDLDVELEQTEGKTIPDLIKERGWQGFRDAElslfKRALTE--RPTGHVFACG 938
Cdd:PRK00131     6 NIVLIGFMGAGKSTIGRLLAKRLGYDFIDTDHLIEARAGKSIPEIFEEEGEAAFRELE----EEVLAEllARHNLVISTG 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2459786690  939 GGIVEIAEARNILIDYHKnkgNVLLVMrDIKKVMEFLNIDKTRP--------AYIEDMMSVwlrRKPWYQECSN 1004
Cdd:PRK00131    82 GGAVLREENRALLRERGT---VVYLDA-SFEELLRRLRRDRNRPllqtndpkEKLRDLYEE---RDPLYEEVAD 148
PRK12548 PRK12548
shikimate dehydrogenase;
1289-1561 4.61e-24

shikimate dehydrogenase;


Pssm-ID: 183585 [Multi-domain]  Cd Length: 289  Bit Score: 104.05  E-value: 4.61e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690 1289 FAIFGKPVSVSRSPAMHNTLFEQNGLPYVYTRLET--DQAQDVKEFIRSPDFGGASATIPLKLDIIPLIDEVLNEAEIIG 1366
Cdd:PRK12548    12 LGLIGSPVGHSGSPAMYNYSFQKAGLDYAYLAFDIpvDKVPDAIKAIKTFNMRGANVTMPCKSEAAKYMDELSPAARIIG 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690 1367 AVNTIIPVEGKdgstrLIGRNTDWSGIVRCLREAGAhsnEGESSALVIGGGGTARAAIY---ALHnmGFSTVYVLGRSPE 1443
Cdd:PRK12548    92 AVNTIVNDDGK-----LTGHITDGLGFVRNLREHGV---DVKGKKLTVIGAGGAATAIQvqcALD--GAKEITIFNIKDD 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690 1444 KIQNMASTFPTgfdIR-----VLENASDIENIPRV----------AVGTIPGDRPIEaNMREILCTIFERSGraadgksa 1508
Cdd:PRK12548   162 FYERAEQTAEK---IKqevpeCIVNVYDLNDTEKLkaeiassdilVNATLVGMKPND-GETNIKDTSVFRKD-------- 229
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2459786690 1509 AVLLEMAYKPSVTPLMQLASDSGWTTIPGLEALVGQGVYQFEYWTGI-TPVYEV 1561
Cdd:PRK12548   230 LVVADTVYNPKKTKLLEDAEAAGCKTVGGLGMLLWQGAEAYKLYTGKdMPVEEV 283
PRK12550 PRK12550
shikimate 5-dehydrogenase; Reviewed
1305-1566 5.93e-24

shikimate 5-dehydrogenase; Reviewed


Pssm-ID: 183587 [Multi-domain]  Cd Length: 272  Bit Score: 103.50  E-value: 5.93e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690 1305 HNTLFEQNGLPYVYTRLET-DQAQDVKEfIRSPDFGGASATIPLKLDIIPLIDEVLNEAEIIGAVNTIIPVEGkdgstRL 1383
Cdd:PRK12550    27 HNYLYEALGLNFLYKAFTTtDLTAAIGG-VRALGIRGCAVSMPFKEAVIPLVDELDPSAQAIESVNTIVNTDG-----HL 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690 1384 IGRNTDWSGIVRCLREagaHSNEGESSALVIGGGGTARAAIYALHNMGFSTVYVLGRSPEKIQNMASTFptGFDIRvlen 1463
Cdd:PRK12550   101 KAYNTDYIAIAKLLAS---YQVPPDLVVALRGSGGMAKAVAAALRDAGFTDGTIVARNEKTGKALAELY--GYEWR---- 171
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690 1464 aSDIENI-PRVAVGTIPgdrpieanmreilctIFERSGRAADGKS--------AAVLLEMAYKPSVTPLMQLASDSGWTT 1534
Cdd:PRK12550   172 -PDLGGIeADILVNVTP---------------IGMAGGPEADKLAfpeaeidaASVVFDVVALPAETPLIRYARARGKTV 235
                          250       260       270
                   ....*....|....*....|....*....|..
gi 2459786690 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 2459786690 1072 DAVELRVDLLKDPSSgngipsaeyvaEQISFYRSRVSLPIVfTIRtvsqggKFPNDAHDAALELIMLAIRSGCEFIDLEI 1151
Cdd:PRK09310    26 DCIELRVDLLLSLSD-----------LELKKLIELAPIPIL-TWK------KHESCSQAAWIDKMQSLAKLNPNYLDIDK 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690 1152 TFPEDLLRKVAESKAHAKIIASHHDPQgklnwaNGSWIQYYNKAL-QYGDIIKLVGVAETLKDntALREFKdwaEQAHPD 1230
Cdd:PRK09310    88 DFPKEALIRIRKLHPKIKIILSYHTSE------HEDIIQLYNEMLaSAADYYKIAVSSSSSTD--LLNIIH---QKRSLP 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690 1231 VPVIAINMGDKGQLSRMLNGFLTPVSHPALPFKA---APGQLSAAEIR----KGLSIMGEIpakkFAIFGKPVSVSRSPA 1303
Cdd:PRK09310   157 ENTTVLCMGGMGRPSRILSPLLQNAFNYAAGIGAppvAPGQLSLEHLLfynyANLSAQSPI----YGLIGDPVDRSISHL 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690 1304 MHNTLFEQNGLPYVYTRLETDqAQDVKEF---IRSPDFGGASATIPLKLDIIPLIDEVLNEAEIIGAVNTIIPVEGKdgs 1380
Cdd:PRK09310   233 SHNPLFSQLSLNCPYIKLPLT-PQELPKFfstIRDLPFLGLSVTMPLKTAVLDFLDKLDPSVKLCGSCNTLVFRNGK--- 308
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690 1381 trLIGRNTDWSGIVRCLREAGAHSNEGESSalVIGGGGTARaAIYALHNMGFSTVYVLGRSPEKIQNMASTFP-TGFDIR 1459
Cdd:PRK09310   309 --IEGYNTDGEGLFSLLKQKNIPLNNQHVA--IVGAGGAAK-AIATTLARAGAELLIFNRTKAHAEALASRCQgKAFPLE 383
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690 1460 VLENASDIENIprvaVGTIPGDrpieanmreilCTIFERsgraadgkSAAVLLEMAYKPSVTPLMQLASDSGWTTIPGLE 1539
Cdd:PRK09310   384 SLPELHRIDII----INCLPPS-----------VTIPKA--------FPPCVVDINTLPKHSPYTQYARSQGSSIIYGYE 440
                          490
                   ....*....|...
gi 2459786690 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 2459786690 1295 PVSVSRSPAMHNTLFEQNGLPYVYTRLETDQAQ--DVKEFIRSPDFGGASATIPLKLDIIPLIDEVLNEAEIIGAVNTII 1372
Cdd:PRK12749    16 PIRHSLSPEMQNKALEKAGLPFTYMAFEVDNDSfpGAIEGLKALKMRGTGVSMPNKQLACEYVDELTPAAKLVGAINTIV 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690 1373 pveGKDGSTRliGRNTDWSGIVRCLREAGaHSNEGESSALV-IGGGGTARAAIYALHnmGFSTVYVLGRSPEKIQNMASt 1451
Cdd:PRK12749    96 ---NDDGYLR--GYNTDGTGHIRAIKESG-FDIKGKTMVLLgAGGASTAIGAQGAIE--GLKEIKLFNRRDEFFDKALA- 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690 1452 fptgFDIRVLENASDIENIPRVA----------------VGTIPGDRPIEaNMREILCTIFERSGraadgksaAVLLEMA 1515
Cdd:PRK12749   167 ----FAQRVNENTDCVVTVTDLAdqqafaealasadiltNGTKVGMKPLE-NESLVNDISLLHPG--------LLVTECV 233
                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 2459786690 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 4.07e-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: 4.07e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  103 RDTVIIALGGGVIGDLLGFVAATYMRGIRFVQVPTTLLAmvDSSIGGKTAIDTPLGKNL-IGAIWQPHRIYIDIDFIDTL 181
Cdd:cd07766     77 EADAVIAVGGGSTLDTAKAVAALLNRGIPFIIVPTTAST--DSEVSPKSVITDKGGKNKqVGPHYNPDVVFVDTDITKGL 154
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  182 PEREFINGMAEVIKTAAISdEKEFAALEQHADAILkaarSKPGkgrfdlvrqvvkdrivasarhkafvvtaderegglrn 261
Cdd:cd07766    155 PPRQVASGGVDALAHAVEL-EKVVEAATLAGMGLF----ESPG------------------------------------- 192
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2459786690  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 2459786690 1293 GKPVSVSRSPAMHNTLFEQNGLPYVYTRLETDQ----AQDVKEFIRSP---DFGGASATIPLKLDIIPLIDEVLNEAEII 1365
Cdd:PRK12549    12 GAGIQASLSPAMHEAEGDAQGLRYVYRLIDLDAlgltADALPELLDAAermGFAGLNITHPCKQAVIPHLDELSDDARAL 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690 1366 GAVNTIIPvegKDGstRLIGRNTDWSGIVRCLRE--AGAhsneGESSALVIGGGGTARAAIYALHNMGFSTVYVLGRSPE 1443
Cdd:PRK12549    92 GAVNTVVF---RDG--RRIGHNTDWSGFAESFRRglPDA----SLERVVQLGAGGAGAAVAHALLTLGVERLTIFDVDPA 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690 1444 K----IQNMASTFPTGfdirvlenasdienipRVAVGTipgdrPIEANMREilctifersgraADGKSAAVLLEMA---- 1515
Cdd:PRK12549   163 RaaalADELNARFPAA----------------RATAGS-----DLAAALAA------------ADGLVHATPTGMAkhpg 209
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690 1516 ------------------YKPSVTPLMQLASDSGWTTIPGLEALVGQGVYQFEYWTGITP 1557
Cdd:PRK12549   210 lplpaellrpglwvadivYFPLETELLRAARALGCRTLDGGGMAVFQAVDAFELFTGREP 269
PRK14027 PRK14027
quinate/shikimate dehydrogenase (NAD+);
1289-1567 7.32e-21

quinate/shikimate dehydrogenase (NAD+);


Pssm-ID: 172521 [Multi-domain]  Cd Length: 283  Bit Score: 94.72  E-value: 7.32e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690 1289 FAIFGKPVSVSRSPAMHNTLFEQNGLPYVYTRLET--DQA--QDVKEFI---RSPDFGGASATIPLKLDIIPLIDEVLNE 1361
Cdd:PRK14027     7 LGLIGQGLDLSRTPAMHEAEGLAQGRATVYRRIDTlgSRAsgQDLKTLLdaaLYLGFNGLNITHPYKQAVLPLLDEVSEQ 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690 1362 AEIIGAVNTIipVEGKDGSTRliGRNTDWSGIVRCLREagAHSNEGESSALVIGGGGTARAAIYALHNMGFSTVYVLGRS 1441
Cdd:PRK14027    87 ATQLGAVNTV--VIDATGHTT--GHNTDVSGFGRGMEE--GLPNAKLDSVVQVGAGGVGNAVAYALVTHGVQKLQVADLD 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690 1442 PEKIQNMASTF--PTGFDIRVLENASDIENIPRVAVGTIpgdRPIEANMREILCTIFERSGRAADGKSAAVLlemaYKPS 1519
Cdd:PRK14027   161 TSRAQALADVInnAVGREAVVGVDARGIEDVIAAADGVV---NATPMGMPAHPGTAFDVSCLTKDHWVGDVV----YMPI 233
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 2459786690 1520 VTPLMQLASDSGWTTIPGLEALVGQGVYQFEYWTGITPVYEVARNAVL 1567
Cdd:PRK14027   234 ETELLKAARALGCETLDGTRMAIHQAVDAFRLFTGLEPDVSRMRETFL 281
aroL PRK03731
shikimate kinase AroL;
862-1016 2.38e-18

shikimate kinase AroL;


Pssm-ID: 235153 [Multi-domain]  Cd Length: 171  Bit Score: 84.22  E-value: 2.38e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  862 IVIIGMRGAGKTTTGRWAAKALNRKFIDLDVELEQTEGKTIPDLIKERGWQGFRDAElSLFKRALTErpTGHVFACGGGI 941
Cdd:PRK03731     5 LFLVGARGCGKTTVGMALAQALGYRFVDTDQWLQSTSNMTVAEIVEREGWAGFRARE-SAALEAVTA--PSTVIATGGGI 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  942 VEIAEARniliDYHKNKGNVL--------LVMRdikkVMEFLNIDKtRP-----AYIEDMMSVWLRRKPWYQECSNvqYY 1008
Cdd:PRK03731    82 ILTEENR----HFMRNNGIVIylcapvsvLANR----LEANPEEDQ-RPtltgkPISEEVAEVLAEREALYREVAH--HI 150

                   ....*...
gi 2459786690 1009 SRHSSSPE 1016
Cdd:PRK03731   151 IDATQPPS 158
PRK14021 PRK14021
bifunctional shikimate kinase/3-dehydroquinate synthase; Provisional
863-1035 3.82e-18

bifunctional shikimate kinase/3-dehydroquinate synthase; Provisional


Pssm-ID: 184458 [Multi-domain]  Cd Length: 542  Bit Score: 89.92  E-value: 3.82e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  863 VIIGMRGAGKTTTGRWAAKALNRKFIDLDVELEQTEGKTIPDLIKERGWQGFRDAELSLFKRALTErpTGHVFACGGGIV 942
Cdd:PRK14021    10 VIIGMMGAGKTRVGKEVAQMMRLPFADADVEIEREIGMSIPSYFEEYGEPAFREVEADVVADMLED--FDGIFSLGGGAP 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  943 EIAEARNILIDYHKNKGNVLLVMRDIKKVMEFLNIDKTRPAYIEDMMSVWLR----RKPWYQECSNVQYYSrHSSSPELA 1018
Cdd:PRK14021    88 MTPSTQHALASYIAHGGRVVYLDADPKEAMERANRGGGRPMLNGDANKRWKKlfkqRDPVFRQVANVHVHT-RGLTPQAA 166
                          170
                   ....*....|....*....
gi 2459786690 1019 L--AMDDFDRFIQFVSGKT 1035
Cdd:PRK14021   167 AkkLIDMVAERTVHVTGAG 185
aroD PRK02412
type I 3-dehydroquinate dehydratase;
1068-1283 5.27e-18

type I 3-dehydroquinate dehydratase;


Pssm-ID: 235036  Cd Length: 253  Bit Score: 85.33  E-value: 5.27e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690 1068 ASGSDAVELRVDLLKDPSSGNGIPSaeyVAEQIsfYRSRVSLPIVFTIRTVSQGGKFP-NDahDAALELIMLAIRSGC-E 1145
Cdd:PRK02412    39 KYDADIIEWRADFLEKISDVESVLA---AAPAI--REKFAGKPLLFTFRTAKEGGEIAlSD--EEYLALIKAVIKSGLpD 111
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690 1146 FIDLEITFPEDLLRK-VAESKAH-AKIIASHHD-----PQGKLnwangswIQYYNKALQYG-DIIKLVGVAETLKDN--- 1214
Cdd:PRK02412   112 YIDVELFSGKDVVKEmVAFAHEHgVKVVLSYHDfektpPKEEI-------VERLRKMESLGaDIVKIAVMPQSEQDVltl 184
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2459786690 1215 -TALREFKdwaeQAHPDVPVIAINMGDKGQLSRmLNG--FLTPVSHPALPFKAAPGQLSAAEIRKGLSIMGE 1283
Cdd:PRK02412   185 lNATREMK----ELYADQPLITMSMGKLGRISR-LAGevFGSSWTFASLDKASAPGQISVEDLRRILEILHK 251
PRK13947 PRK13947
shikimate kinase; Provisional
862-942 4.79e-15

shikimate kinase; Provisional


Pssm-ID: 184412 [Multi-domain]  Cd Length: 171  Bit Score: 74.74  E-value: 4.79e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  862 IVIIGMRGAGKTTTGRWAAKALNRKFIDLDVELEQTEGKTIPDLIKERGWQGFRDAELSLFKRAltERPTGHVFACGGGI 941
Cdd:PRK13947     4 IVLIGFMGTGKTTVGKRVATTLSFGFIDTDKEIEKMTGMTVAEIFEKDGEVRFRSEEKLLVKKL--ARLKNLVIATGGGV 81

                   .
gi 2459786690  942 V 942
Cdd:PRK13947    82 V 82
PRK13946 PRK13946
shikimate kinase; Provisional
861-940 5.91e-15

shikimate kinase; Provisional


Pssm-ID: 184411 [Multi-domain]  Cd Length: 184  Bit Score: 74.58  E-value: 5.91e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  861 SIVIIGMRGAGKTTTGRWAAKALNRKFIDLDVELEQTEGKTIPDLIKERGWQGFRDAELSLFKRALTERPtgHVFACGGG 940
Cdd:PRK13946    12 TVVLVGLMGAGKSTVGRRLATMLGLPFLDADTEIERAARMTIAEIFAAYGEPEFRDLERRVIARLLKGGP--LVLATGGG 89
PRK13951 PRK13951
bifunctional shikimate kinase AroK/3-dehydroquinate synthase AroB;
862-1001 9.89e-15

bifunctional shikimate kinase AroK/3-dehydroquinate synthase AroB;


Pssm-ID: 172457 [Multi-domain]  Cd Length: 488  Bit Score: 78.79  E-value: 9.89e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  862 IVIIGMRGAGKTTTGRWAAKALNRKFIDLDVELEQTEGKTIPDLIKERGWQGFRDAELSLFkRALTERpTGHVFACGGGI 941
Cdd:PRK13951     3 IFLVGMMGSGKSTIGKRVSEVLDLQFIDMDEEIERREGRSVRRIFEEDGEEYFRLKEKELL-RELVER-DNVVVATGGGV 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2459786690  942 VEIAEARNILidyhkNKGNVLLVMRDIKKVMEFLNIDkTRPAYI---EDMMSVWLRRKPWYQE 1001
Cdd:PRK13951    81 VIDPENRELL-----KKEKTLFLYAPPEVLMERVTTE-NRPLLRegkERIREIWERRKQFYTE 137
aroK PRK05057
shikimate kinase AroK;
862-1005 2.78e-14

shikimate kinase AroK;


Pssm-ID: 235335 [Multi-domain]  Cd Length: 172  Bit Score: 72.44  E-value: 2.78e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  862 IVIIGMRGAGKTTTGRWAAKALNRKFIDLDVELEQTEGKTIPDLIKERGWQGFRDAELSLFKRaLTERpTGHVFACGGGI 941
Cdd:PRK05057     7 IFLVGPMGAGKSTIGRQLAQQLNMEFYDSDQEIEKRTGADIGWVFDVEGEEGFRDREEKVINE-LTEK-QGIVLATGGGS 84
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2459786690  942 VEIAEARNILidyhKNKGNVLLVMRDIKKVMEFLNIDKTRP--------AYIEDMMSVwlrRKPWYQECSNV 1005
Cdd:PRK05057    85 VKSRETRNRL----SARGVVVYLETTIEKQLARTQRDKKRPllqvddprEVLEALANE---RNPLYEEIADV 149
PRK08154 PRK08154
anaerobic benzoate catabolism transcriptional regulator; Reviewed
825-942 7.73e-11

anaerobic benzoate catabolism transcriptional regulator; Reviewed


Pssm-ID: 236167 [Multi-domain]  Cd Length: 309  Bit Score: 64.98  E-value: 7.73e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  825 WPTYWDALKQKFGVSL-KGKELAESEITHGPADRSDASIVIIGMRGAGKTTTGRWAAKALNRKFIDLDVELEQTEGKTIP 903
Cdd:PRK08154    98 WLLIRELLEQASPAQLaRVRDALSGMLGAGRRAARRRRIALIGLRGAGKSTLGRMLAARLGVPFVELNREIEREAGLSVS 177
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2459786690  904 DLIKERGWQGFRDAELSLFKRALTERPTGhVFACGGGIV 942
Cdd:PRK08154   178 EIFALYGQEGYRRLERRALERLIAEHEEM-VLATGGGIV 215
PRK13949 PRK13949
shikimate kinase; Provisional
860-918 8.36e-10

shikimate kinase; Provisional


Pssm-ID: 140006 [Multi-domain]  Cd Length: 169  Bit Score: 59.36  E-value: 8.36e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2459786690  860 ASIVIIGMRGAGKTTTGRWAAKALNRKFIDLDVELEQTEGKTIPDLIKERGWQGFRDAE 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 1.84e-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: 1.84e-07
                           10        20        30
                   ....*....|....*....|....*....|.
gi 2459786690 1537 GLEALVGQGVYQFEYWTGITPVYEVARNAVL 1567
Cdd:pfam18317    1 GLGMLVEQGAEQFELWTGREPPVEVMREALL 31
PRK13948 PRK13948
shikimate kinase; Provisional
856-952 6.89e-07

shikimate kinase; Provisional


Pssm-ID: 184413 [Multi-domain]  Cd Length: 182  Bit Score: 51.33  E-value: 6.89e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  856 DRSDASIVIIGMRGAGKTTTGRWAAKALNRKFIDLDVELEQTEGKTIPDLIKERGWQGFRDAELSLFKRALteRPTGHVF 935
Cdd:PRK13948     7 ERPVTWVALAGFMGTGKSRIGWELSRALMLHFIDTDRYIERVTGKSIPEIFRHLGEAYFRRCEAEVVRRLT--RLDYAVI 84
                           90
                   ....*....|....*..
gi 2459786690  936 ACGGGIVEIAEARNILI 952
Cdd:PRK13948    85 SLGGGTFMHEENRRKLL 101
Fe-ADH_2 pfam13685
Iron-containing alcohol dehydrogenase;
29-288 8.26e-07

Iron-containing alcohol dehydrogenase;


Pssm-ID: 404557 [Multi-domain]  Cd Length: 251  Bit Score: 52.30  E-value: 8.26e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690   29 DLLTNLPSTTYVLVTDTNLGSIYREKFAKIFNEAAaalspaprlLTKEIPPGENsksrqGKADIEDWMLQQTCGRDT--- 105
Cdd:pfam13685   12 EYLAELGFRRVALVADANTYAAAGRKVAESLKRAG---------IEVETRLEVA-----GNADMETAEKLVGALRERdad 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  106 VIIALGGGVIGDLLGFVAATymRGIRFVQVPTTllAMVD------SSI---GGKTAIDT--PLGknligaiwqphrIYID 174
Cdd:pfam13685   78 AVVGVGGGTVIDLAKYAAFK--LGKPFISVPTA--ASNDgfaspgASLtvdGKKRSIPAaaPFG------------VIAD 141
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  175 IDFIDTLPEREFINGMAEVI-KTAAISDEK--------EFAALEQHADAILKAARSKPGKGRFDLVRQVVKDRIVASArh 245
Cdd:pfam13685  142 TDVIAAAPRRLLASGVGDLLaKITAVADWElahaeevaAPLALLSAAMVMNFADRPLRDPGDIEALAELLSALAMGGA-- 219
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 2459786690  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 2.91e-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: 2.91e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690   23 GTYIVQ-DLLTNLPS------TTYVLVTDTNLGSIYREKFAKIFNEAAAALspaprllTKEIPPGENSKS---------R 86
Cdd:COG0371      7 RRYVQGeGALDELGEyladlgKRALIITGPTALKAAGDRLEESLEDAGIEV-------EVEVFGGECSEEeierlaeeaK 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690   87 QGKADiedwmlqqtcgrdtVIIALGGGVIGDLLGFVAatYMRGIRFVQVPTTllAMVD------SSI---GGKTAIDTPL 157
Cdd:COG0371     80 EQGAD--------------VIIGVGGGKALDTAKAVA--YRLGLPVVSVPTI--ASTDapasplSVIyteDGAFDGYSFL 141
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  158 GKNligaiwqPHRIYIDIDFIDTLPEREFINGMAEVI--KTAA----ISDEK-------EFAA---------LEQHADAI 215
Cdd:COG0371    142 AKN-------PDLVLVDTDIIAKAPVRLLAAGIGDALakWYEArdwsLAHRDlageyytEAAValarlcaetLLEYGEAA 214
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  216 LKAARSKpgkGRFDLVRQVVKDRIVASArhkafVVTADEREGGlrnllNLG--HSIGHAIEAIL-SPQVLHGECVAIG-M 291
Cdd:COG0371    215 IKAVEAG---VVTPALERVVEANLLLSG-----LAMGIGSSRP-----GSGaaHAIHNGLTALPeTHHALHGEKVAFGtL 281
                          330       340       350
                   ....*....|....*....|....*....|....*.
gi 2459786690  292 VkeldLARYLGilKPVAVSRMVKCLSKYGLPTSLKD 327
Cdd:COG0371    282 V----QLVLEG--RPEEIEELLDFLRSVGLPTTLAD 311
PLN02199 PLN02199
shikimate kinase
861-942 1.32e-05

shikimate kinase


Pssm-ID: 177850 [Multi-domain]  Cd Length: 303  Bit Score: 48.93  E-value: 1.32e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  861 SIVIIGMRGAGKTTTGRWAAKALNRKFIDLDVELEQT-EGKTIPDLIKERGWQGFRDAELSLFKRALTERPTghVFACGG 939
Cdd:PLN02199   104 SMYLVGMMGSGKTTVGKLMSKVLGYTFFDCDTLIEQAmNGTSVAEIFVHHGENFFRGKETDALKKLSSRYQV--VVSTGG 181

                   ...
gi 2459786690  940 GIV 942
Cdd:PLN02199   182 GAV 184
Gro1PDH cd08173
Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) catalyzes the reversible conversion between ...
103-327 1.56e-04

Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) catalyzes the reversible conversion between dihydroxyacetone phosphate and glycerol-1-phosphate using either NADH or NADPH as a coenzyme; Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH, EC 1.1.1.261) plays an important role in the formation of the enantiomeric configuration of the glycerophosphate backbone (sn-glycerol-1-phosphate) of archaeal ether lipids. It catalyzes the reversible conversion between dihydroxyacetone phosphate and glycerol-1-phosphate using either NADH or NADPH as a coenzyme. The activity is zinc-dependent. One characteristic feature of archaea is that their cellular membrane has an ether linkage between the glycerol backbone and the hydrocarbon residues. The polar lipids of the members of Archaea consist of di- and tetra-ethers of glycerol with isoprenoid alcohols bound at the sn-2 and sn-3 positions of the glycerol moiety. The archaeal polar lipids have the enantiomeric configuration of a glycerophosphate backbone [sn-glycerol-1-phosphate (G-1-P)] that is the mirror image structure of the bacterial or eukaryal counterpart [sn-glycerol- 3-phosphate (G-3-P)]. The absolute stereochemistry of the glycerol moiety in all archaeal polar lipids is opposite to that of glycerol ester lipids in bacteria and eukarya.


Pssm-ID: 341452  Cd Length: 343  Bit Score: 45.62  E-value: 1.56e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  103 RDTVIIALGGGVIGDllgfVA--ATYMRGIRFVQVPTTL-----------LAMVDSSIGGKTaiDTPLGknligaiwqph 169
Cdd:cd08173     80 KADFIIGVGGGKVID----VAkyAAYKLNLPFISIPTSAshdgiaspfasIKGGDKPYSIKA--KAPIA----------- 142
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  170 rIYIDIDFIDTLPEREFINGMAEVI-KTAAISD---------EK--EFAA-LEQHADAILKAARSKPGKGRFDLVRQVVK 236
Cdd:cd08173    143 -IIADTEIISKAPKRLLAAGCGDLIsNITAVKDwrlahrlkgEYysEYAAsLALMSAKLIIENADLIKPGLEEGVRTVVK 221
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  237 DRI---VA-----SARhkafVVTADEregglrnllnlgHSIGHAIEAILSPQVLHGECVAIGMVkeldLARYL--GILKp 306
Cdd:cd08173    222 ALIssgVAmsiagSSR----PASGSE------------HLFSHALDKLAPGPALHGEQCGVGTI----MMAYLhgGDWK- 280
                          250       260
                   ....*....|....*....|.
gi 2459786690  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 2459786690  637 ESDASSATYPLAIAAVTGTTCTVPNIGSAS-----LQGDARFaVEVLRPMG----CKVEQTATSTTVT-GPADGVlrplp 706
Cdd:cd01553      7 KGGGQILRSFLVLAAISGGPITVTGIRPDRakpglLRQHLTF-LKALEKICgatvEGGELGSDRISFRpGTVRGG----- 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  707 NVDMEPMTDAFLG---ASVLAAIAQGEGGNHATRIYGI-ANQRVKECNRIEAMRVELAKFGVVCREhpdgleidGIDRST 782
Cdd:cd01553     81 DVRFAIGSAGSCTdvlQTILPLLLFAKGPTRLTVTGGTdNPSAPPADFIRFVLEPELAKIGAHQEE--------TLLRHG 152
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2459786690  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 2459786690 1410 SALVIGGGGTARAAIYALHNMGFSTVYVLGRSPEKIQNMASTFP 1453
Cdd:PRK00045   184 KVLVIGAGEMGELVAKHLAEKGVRKITVANRTLERAEELAEEFG 227
G1PDH cd08175
Glycerol-1-phosphate dehydrogenase (G1PDH) catalyzes the reversible reduction of ...
30-327 2.51e-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: 42.11  E-value: 2.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690   30 LLTNLPSTTYVLVTDTNlgsIYR---EKFAKIFNEAAAALSPAPRLLTKEIPPGEnsksrqgkADIEDWMLQqTCGRDTV 106
Cdd:cd08175     18 LKELFGGKKVLVVADEN---TYAaagEEVEAALEEAGVTVCLLIFPGEGDLIADE--------AAVGKVLLE-LEKDTDL 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  107 IIALGGGVIGDLLGFVAatYMRGIRFVQVPTTllAMVD------SSI---GGKTAIDTPLgknligaiwqPHRIYIDIDF 177
Cdd:cd08175     86 IIAVGSGTINDLTKYAA--YKLGIPYISVPTA--PSMDgytssgAPIivdGVKKTFPAHA----------PKAIFADLDV 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  178 IDTLPEREFINGMAEVI-KTAAISDEK--EFAALEQHADAIlkaarskpgkgrFDLVRQVVKDRIVASARhkafvVTADE 254
Cdd:cd08175    152 LANAPQRMIAAGFGDLLgKYTALADWKlsHLLGGEYYCPEV------------ADLVQEALEKCLDNAEG-----IAARD 214
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459786690  255 REgGLRNLLN-----------LGHS---------IGHAIE--AILS--PQVLHGECVAIGMVKELDLarYLGILKPvAVS 310
Cdd:cd08175    215 PE-AIEALMEalilsglamqlVGNSrpasgaehhLSHYWEmeFLRLgkPPVLHGEKVGVGTLLIAAL--YILEQLP-PPE 290
                          330
                   ....*....|....*..
gi 2459786690  311 RMVKCLSKYGLPTSLKD 327
Cdd:cd08175    291 ELRELLRKAGAPTTPED 307
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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