AROA_COXBU
ID AROA_COXBU Reviewed; 438 AA.
AC Q83E11;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=3-phosphoshikimate 1-carboxyvinyltransferase {ECO:0000255|HAMAP-Rule:MF_00210};
DE EC=2.5.1.19 {ECO:0000255|HAMAP-Rule:MF_00210};
DE AltName: Full=5-enolpyruvylshikimate-3-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00210};
DE Short=EPSP synthase {ECO:0000255|HAMAP-Rule:MF_00210};
DE Short=EPSPS {ECO:0000255|HAMAP-Rule:MF_00210};
GN Name=aroA {ECO:0000255|HAMAP-Rule:MF_00210}; OrderedLocusNames=CBU_0526;
OS Coxiella burnetii (strain RSA 493 / Nine Mile phase I).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC Coxiella.
OX NCBI_TaxID=227377;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RSA 493 / Nine Mile phase I;
RX PubMed=12704232; DOI=10.1073/pnas.0931379100;
RA Seshadri R., Paulsen I.T., Eisen J.A., Read T.D., Nelson K.E., Nelson W.C.,
RA Ward N.L., Tettelin H., Davidsen T.M., Beanan M.J., DeBoy R.T.,
RA Daugherty S.C., Brinkac L.M., Madupu R., Dodson R.J., Khouri H.M.,
RA Lee K.H., Carty H.A., Scanlan D., Heinzen R.A., Thompson H.A., Samuel J.E.,
RA Fraser C.M., Heidelberg J.F.;
RT "Complete genome sequence of the Q-fever pathogen, Coxiella burnetii.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:5455-5460(2003).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS), AND SUBUNIT.
RG Center for Structural Genomics of Infectious Diseases (CSGID);
RA Light S.H., Minasov G., Krishna S.N., Halavaty A.S., Shuvalova L.,
RA Papazisi L., Anderson W.F.;
RT "2.20 Angstrom resolution structure of 3-phosphoshikimate 1-
RT carboxyvinyltransferase (AroA) from Coxiella burnetii.";
RL Submitted (APR-2011) to the PDB data bank.
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH
RP SHIKIMATE-3-PHOSPHATE AND PHOSPHOENOLPYRUVATE ANLOG, ACTIVE SITE, AND
RP SUBUNIT.
RG Center for Structural Genomics of Infectious Diseases (CSGID);
RA Light S.H., Minasov G., Filippova E.V., Krishna S.N., Shuvalova L.,
RA Papazisi L., Anderson W.F.;
RT "1.70 Angstrom resolution structure of 3-phosphoshikimate 1-
RT carboxyvinyltransferase(AroA) from Coxiella burnetii in complex with
RT shikimate-3-phosphate and glyphosate.";
RL Submitted (JUN-2011) to the PDB data bank.
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH PHOSPHATES.
RA Cheung J., Franklin M., Rudolph M., Cassidy M., Gary E., Burshteyn F.,
RA Love J.;
RT "Structure of a 3-phosphoshikimate 1-carboxyvinyltransferase (aroA) from
RT Coxiella burnetii.";
RL Submitted (SEP-2011) to the PDB data bank.
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) IN COMPLEX WITH PHOSPHOENOLPYRUVATE,
RP AND SUBUNIT.
RA Krishna S.N., Light S.H., Minasov G., Shuvalova L., Kwon K., Anderson W.F.;
RT "2.50 angstrom resolution structure of 3-phosphoshikimate 1-
RT carboxyvinyltransferase (AroA) from Coxiella burnetii in complex with
RT phosphoenolpyruvate.";
RL Submitted (MAR-2012) to the PDB data bank.
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS).
RA Light S.H., Minasov G., Krishna S.N., Shuvalova L., Papazisi L.,
RA Anderson W.F.;
RT "2.7 Angstrom resolution structure of 3-phosphoshikimate 1-
RT carboxyvinyltransferase (AroA) from Coxiella burnetii in second
RT conformational state.";
RL Submitted (AUG-2012) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the transfer of the enolpyruvyl moiety of
CC phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate
CC (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic
CC phosphate. {ECO:0000255|HAMAP-Rule:MF_00210}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-
CC carboxyvinyl)-3-phosphoshikimate + phosphate; Xref=Rhea:RHEA:21256,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57701, ChEBI:CHEBI:58702,
CC ChEBI:CHEBI:145989; EC=2.5.1.19; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00210};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC 6/7. {ECO:0000255|HAMAP-Rule:MF_00210}.
CC -!- SUBUNIT: Homodimer or homotetramer. {ECO:0000269|Ref.2,
CC ECO:0000269|Ref.3, ECO:0000269|Ref.5}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00210}.
CC -!- SIMILARITY: Belongs to the EPSP synthase family. {ECO:0000255|HAMAP-
CC Rule:MF_00210}.
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DR EMBL; AE016828; AAO90072.1; -; Genomic_DNA.
DR RefSeq; NP_819558.1; NC_002971.3.
DR RefSeq; WP_010957637.1; NC_002971.4.
DR PDB; 3ROI; X-ray; 2.20 A; A/B=1-438.
DR PDB; 3SLH; X-ray; 1.70 A; A/B/C/D=1-438.
DR PDB; 3TR1; X-ray; 2.00 A; A=1-438.
DR PDB; 4EGR; X-ray; 2.50 A; A/B/C/D/E/F=1-438.
DR PDB; 4GFP; X-ray; 2.70 A; A=1-438.
DR PDB; 4ZND; X-ray; 2.55 A; A=1-438.
DR PDBsum; 3ROI; -.
DR PDBsum; 3SLH; -.
DR PDBsum; 3TR1; -.
DR PDBsum; 4EGR; -.
DR PDBsum; 4GFP; -.
DR PDBsum; 4ZND; -.
DR AlphaFoldDB; Q83E11; -.
DR SMR; Q83E11; -.
DR STRING; 227377.CBU_0526; -.
DR EnsemblBacteria; AAO90072; AAO90072; CBU_0526.
DR GeneID; 1208411; -.
DR KEGG; cbu:CBU_0526; -.
DR PATRIC; fig|227377.7.peg.521; -.
DR eggNOG; COG0128; Bacteria.
DR HOGENOM; CLU_024321_0_1_6; -.
DR OMA; YEDHRMA; -.
DR BRENDA; 2.5.1.19; 1677.
DR UniPathway; UPA00053; UER00089.
DR Proteomes; UP000002671; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003866; F:3-phosphoshikimate 1-carboxyvinyltransferase activity; ISS:UniProtKB.
DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0008652; P:cellular amino acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009423; P:chorismate biosynthetic process; IBA:GO_Central.
DR CDD; cd01556; EPSP_synthase; 1.
DR Gene3D; 3.65.10.10; -; 2.
DR HAMAP; MF_00210; EPSP_synth; 1.
DR InterPro; IPR001986; Enolpyruvate_Tfrase_dom.
DR InterPro; IPR036968; Enolpyruvate_Tfrase_sf.
DR InterPro; IPR006264; EPSP_synthase.
DR InterPro; IPR023193; EPSP_synthase_CS.
DR InterPro; IPR013792; RNA3'P_cycl/enolpyr_Trfase_a/b.
DR Pfam; PF00275; EPSP_synthase; 1.
DR PIRSF; PIRSF000505; EPSPS; 1.
DR SUPFAM; SSF55205; SSF55205; 1.
DR TIGRFAMs; TIGR01356; aroA; 1.
DR PROSITE; PS00104; EPSP_SYNTHASE_1; 1.
DR PROSITE; PS00885; EPSP_SYNTHASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW Cytoplasm; Reference proteome; Transferase.
FT CHAIN 1..438
FT /note="3-phosphoshikimate 1-carboxyvinyltransferase"
FT /id="PRO_1000071737"
FT REGION 93..96
FT /note="Phosphoenolpyruvate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210,
FT ECO:0000269|Ref.3, ECO:0000269|Ref.5"
FT ACT_SITE 315
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210,
FT ECO:0000269|Ref.3"
FT ACT_SITE 343
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT BINDING 21..22
FT /ligand="3-phosphoshikimate"
FT /ligand_id="ChEBI:CHEBI:145989"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210,
FT ECO:0000269|Ref.3"
FT BINDING 26
FT /ligand="3-phosphoshikimate"
FT /ligand_id="ChEBI:CHEBI:145989"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210,
FT ECO:0000269|Ref.3"
FT BINDING 123
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210,
FT ECO:0000269|Ref.5"
FT BINDING 342
FT /ligand="3-phosphoshikimate"
FT /ligand_id="ChEBI:CHEBI:145989"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210,
FT ECO:0000269|Ref.3"
FT BINDING 346
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210,
FT ECO:0000269|Ref.5"
FT BINDING 387
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210,
FT ECO:0000269|Ref.5"
FT STRAND 1..5
FT /evidence="ECO:0007829|PDB:3SLH"
FT STRAND 12..16
FT /evidence="ECO:0007829|PDB:3SLH"
FT HELIX 21..33
FT /evidence="ECO:0007829|PDB:3SLH"
FT STRAND 34..42
FT /evidence="ECO:0007829|PDB:3SLH"
FT HELIX 47..58
FT /evidence="ECO:0007829|PDB:3SLH"
FT STRAND 62..66
FT /evidence="ECO:0007829|PDB:3SLH"
FT HELIX 67..69
FT /evidence="ECO:0007829|PDB:3SLH"
FT STRAND 71..75
FT /evidence="ECO:0007829|PDB:3SLH"
FT HELIX 95..105
FT /evidence="ECO:0007829|PDB:3SLH"
FT STRAND 108..115
FT /evidence="ECO:0007829|PDB:3SLH"
FT HELIX 120..122
FT /evidence="ECO:0007829|PDB:3SLH"
FT HELIX 126..134
FT /evidence="ECO:0007829|PDB:3SLH"
FT STRAND 138..142
FT /evidence="ECO:0007829|PDB:3SLH"
FT STRAND 145..151
FT /evidence="ECO:0007829|PDB:3SLH"
FT STRAND 160..162
FT /evidence="ECO:0007829|PDB:3SLH"
FT STRAND 164..166
FT /evidence="ECO:0007829|PDB:3TR1"
FT HELIX 168..178
FT /evidence="ECO:0007829|PDB:3SLH"
FT STRAND 181..188
FT /evidence="ECO:0007829|PDB:3SLH"
FT HELIX 196..203
FT /evidence="ECO:0007829|PDB:3SLH"
FT STRAND 215..218
FT /evidence="ECO:0007829|PDB:3SLH"
FT HELIX 234..246
FT /evidence="ECO:0007829|PDB:3SLH"
FT STRAND 251..258
FT /evidence="ECO:0007829|PDB:3SLH"
FT HELIX 261..263
FT /evidence="ECO:0007829|PDB:3SLH"
FT HELIX 265..273
FT /evidence="ECO:0007829|PDB:3SLH"
FT STRAND 276..285
FT /evidence="ECO:0007829|PDB:3SLH"
FT STRAND 288..296
FT /evidence="ECO:0007829|PDB:3SLH"
FT HELIX 307..309
FT /evidence="ECO:0007829|PDB:3SLH"
FT HELIX 310..313
FT /evidence="ECO:0007829|PDB:3SLH"
FT HELIX 314..316
FT /evidence="ECO:0007829|PDB:3SLH"
FT HELIX 317..325
FT /evidence="ECO:0007829|PDB:3SLH"
FT STRAND 327..333
FT /evidence="ECO:0007829|PDB:3SLH"
FT HELIX 337..341
FT /evidence="ECO:0007829|PDB:3SLH"
FT STRAND 342..344
FT /evidence="ECO:0007829|PDB:3SLH"
FT HELIX 346..356
FT /evidence="ECO:0007829|PDB:3SLH"
FT STRAND 360..364
FT /evidence="ECO:0007829|PDB:3SLH"
FT STRAND 367..371
FT /evidence="ECO:0007829|PDB:3SLH"
FT STRAND 378..381
FT /evidence="ECO:0007829|PDB:3SLH"
FT HELIX 386..398
FT /evidence="ECO:0007829|PDB:3SLH"
FT STRAND 399..401
FT /evidence="ECO:0007829|PDB:3TR1"
FT STRAND 403..406
FT /evidence="ECO:0007829|PDB:3SLH"
FT HELIX 409..413
FT /evidence="ECO:0007829|PDB:3SLH"
FT HELIX 418..425
FT /evidence="ECO:0007829|PDB:3SLH"
FT STRAND 429..433
FT /evidence="ECO:0007829|PDB:3SLH"
SQ SEQUENCE 438 AA; 46432 MW; EF1C0FEEEBCD4D54 CRC64;
MDYQTIPSQG LSGEICVPGD KSISHRAVLL AAIAEGQTQV DGFLMGADNL AMVSALQQMG
ASIQVIEDEN ILVVEGVGMT GLQAPPEALD CGNSGTAIRL LSGLLAGQPF NTVLTGDSSL
QRRPMKRIID PLTLMGAKID STGNVPPLKI YGNPRLTGIH YQLPMASAQV KSCLLLAGLY
ARGKTCITEP APSRDHTERL LKHFHYTLQK DKQSICVSGG GKLKANDISI PGDISSAAFF
IVAATITPGS AIRLCRVGVN PTRLGVINLL KMMGADIEVT HYTEKNEEPT ADITVRHARL
KGIDIPPDQV PLTIDEFPVL LIAAAVAQGK TVLRDAAELR VKETDRIAAM VDGLQKLGIA
AESLPDGVII QGGTLEGGEV NSYDDHRIAM AFAVAGTLAK GPVRIRNCDN VKTSFPNFVE
LANEVGMNVK GVRGRGGF
