AROA_VIBCH
ID AROA_VIBCH Reviewed; 426 AA.
AC Q9KRB0;
DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 126.
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=VC_1732;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.02 ANGSTROMS) IN COMPLEX WITH
RP SHIKIMATE-3-PHOSPHATE AND PHOSPHOENOLPYRUVATE ANALOGS, AND ACTIVE SITE.
RG Center for Structural Genomics of Infectious Diseases (CSGID);
RA Minasov G., Light S.H., Halavaty A., Shuvalova G., Papazisi L.,
RA Anderson W.F.;
RT "1.02 Angstrom resolution crystal structure of 3-phosphoshikimate 1-
RT carboxyvinyltransferase from Vibrio cholerae in complex with shikimate-3-
RT phosphate (partially hotolyzed) and glyphosate.";
RL Submitted (JUL-2010) to the PDB data bank.
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 16-243, AND SUBUNIT.
RG Center for Structural Genomics of Infectious Diseases (CSGID);
RA Light S.H., Minasov G., Halavaty A.S., Shuvalova L., Papazisi L.,
RA Anderson W.F.;
RT "1.90 Angstrom resolution crystal structure of N-terminal domain 3-
RT phosphoshikimate 1-carboxyvinyltransferase from Vibrio cholerae.";
RL Submitted (AUG-2011) 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: Homotetramer. {ECO:0000269|Ref.3}.
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; AE003852; AAF94882.1; -; Genomic_DNA.
DR PIR; D82163; D82163.
DR RefSeq; NP_231368.1; NC_002505.1.
DR RefSeq; WP_000445261.1; NZ_LT906614.1.
DR PDB; 3NVS; X-ray; 1.02 A; A=1-426.
DR PDB; 3TI2; X-ray; 1.90 A; A/B/C/D=16-243.
DR PDBsum; 3NVS; -.
DR PDBsum; 3TI2; -.
DR AlphaFoldDB; Q9KRB0; -.
DR SMR; Q9KRB0; -.
DR STRING; 243277.VC_1732; -.
DR PRIDE; Q9KRB0; -.
DR DNASU; 2613737; -.
DR EnsemblBacteria; AAF94882; AAF94882; VC_1732.
DR GeneID; 66939576; -.
DR KEGG; vch:VC_1732; -.
DR PATRIC; fig|243277.26.peg.1657; -.
DR eggNOG; COG0128; Bacteria.
DR HOGENOM; CLU_024321_0_0_6; -.
DR OMA; YEDHRMA; -.
DR BioCyc; VCHO:VC1732-MON; -.
DR BRENDA; 2.5.1.19; 15862.
DR UniPathway; UPA00053; UER00089.
DR EvolutionaryTrace; Q9KRB0; -.
DR Proteomes; UP000000584; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003866; F:3-phosphoshikimate 1-carboxyvinyltransferase activity; IBA:GO_Central.
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..426
FT /note="3-phosphoshikimate 1-carboxyvinyltransferase"
FT /id="PRO_0000088314"
FT REGION 94..97
FT /note="Phosphoenolpyruvate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210,
FT ECO:0000269|Ref.2"
FT ACT_SITE 314
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210,
FT ECO:0000305|Ref.2"
FT ACT_SITE 342
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210,
FT ECO:0000305|Ref.2"
FT BINDING 22..23
FT /ligand="3-phosphoshikimate"
FT /ligand_id="ChEBI:CHEBI:145989"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210,
FT ECO:0000269|Ref.2"
FT BINDING 27
FT /ligand="3-phosphoshikimate"
FT /ligand_id="ChEBI:CHEBI:145989"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210,
FT ECO:0000269|Ref.2"
FT BINDING 124
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210,
FT ECO:0000269|Ref.2"
FT BINDING 170..172
FT /ligand="3-phosphoshikimate"
FT /ligand_id="ChEBI:CHEBI:145989"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210,
FT ECO:0000269|Ref.2"
FT BINDING 198
FT /ligand="3-phosphoshikimate"
FT /ligand_id="ChEBI:CHEBI:145989"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210,
FT ECO:0000269|Ref.2"
FT BINDING 337
FT /ligand="3-phosphoshikimate"
FT /ligand_id="ChEBI:CHEBI:145989"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210,
FT ECO:0000269|Ref.2"
FT BINDING 341
FT /ligand="3-phosphoshikimate"
FT /ligand_id="ChEBI:CHEBI:145989"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210,
FT ECO:0000269|Ref.2"
FT BINDING 345
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210,
FT ECO:0000269|Ref.2"
FT BINDING 387
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210,
FT ECO:0000269|Ref.2"
FT BINDING 412
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT STRAND 3..6
FT /evidence="ECO:0007829|PDB:3NVS"
FT STRAND 14..17
FT /evidence="ECO:0007829|PDB:3NVS"
FT HELIX 22..34
FT /evidence="ECO:0007829|PDB:3NVS"
FT STRAND 35..43
FT /evidence="ECO:0007829|PDB:3NVS"
FT HELIX 48..59
FT /evidence="ECO:0007829|PDB:3NVS"
FT STRAND 63..66
FT /evidence="ECO:0007829|PDB:3NVS"
FT STRAND 73..76
FT /evidence="ECO:0007829|PDB:3NVS"
FT STRAND 88..91
FT /evidence="ECO:0007829|PDB:3NVS"
FT HELIX 96..105
FT /evidence="ECO:0007829|PDB:3NVS"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:3NVS"
FT STRAND 112..116
FT /evidence="ECO:0007829|PDB:3NVS"
FT HELIX 119..123
FT /evidence="ECO:0007829|PDB:3NVS"
FT HELIX 127..135
FT /evidence="ECO:0007829|PDB:3NVS"
FT STRAND 139..145
FT /evidence="ECO:0007829|PDB:3NVS"
FT STRAND 151..154
FT /evidence="ECO:0007829|PDB:3NVS"
FT STRAND 160..165
FT /evidence="ECO:0007829|PDB:3NVS"
FT HELIX 172..180
FT /evidence="ECO:0007829|PDB:3NVS"
FT HELIX 181..183
FT /evidence="ECO:0007829|PDB:3NVS"
FT STRAND 184..186
FT /evidence="ECO:0007829|PDB:3NVS"
FT STRAND 188..194
FT /evidence="ECO:0007829|PDB:3NVS"
FT HELIX 199..211
FT /evidence="ECO:0007829|PDB:3NVS"
FT STRAND 217..219
FT /evidence="ECO:0007829|PDB:3NVS"
FT TURN 220..222
FT /evidence="ECO:0007829|PDB:3NVS"
FT STRAND 223..226
FT /evidence="ECO:0007829|PDB:3NVS"
FT STRAND 236..239
FT /evidence="ECO:0007829|PDB:3NVS"
FT HELIX 244..257
FT /evidence="ECO:0007829|PDB:3NVS"
FT STRAND 259..265
FT /evidence="ECO:0007829|PDB:3NVS"
FT HELIX 273..276
FT /evidence="ECO:0007829|PDB:3NVS"
FT HELIX 277..284
FT /evidence="ECO:0007829|PDB:3NVS"
FT STRAND 287..290
FT /evidence="ECO:0007829|PDB:3NVS"
FT STRAND 292..298
FT /evidence="ECO:0007829|PDB:3NVS"
FT STRAND 306..308
FT /evidence="ECO:0007829|PDB:3NVS"
FT TURN 313..315
FT /evidence="ECO:0007829|PDB:3NVS"
FT HELIX 316..322
FT /evidence="ECO:0007829|PDB:3NVS"
FT HELIX 323..325
FT /evidence="ECO:0007829|PDB:3NVS"
FT STRAND 326..328
FT /evidence="ECO:0007829|PDB:3NVS"
FT STRAND 330..334
FT /evidence="ECO:0007829|PDB:3NVS"
FT HELIX 336..340
FT /evidence="ECO:0007829|PDB:3NVS"
FT STRAND 341..343
FT /evidence="ECO:0007829|PDB:3NVS"
FT HELIX 345..355
FT /evidence="ECO:0007829|PDB:3NVS"
FT STRAND 359..362
FT /evidence="ECO:0007829|PDB:3NVS"
FT STRAND 364..370
FT /evidence="ECO:0007829|PDB:3NVS"
FT HELIX 386..393
FT /evidence="ECO:0007829|PDB:3NVS"
FT HELIX 394..397
FT /evidence="ECO:0007829|PDB:3NVS"
FT STRAND 398..400
FT /evidence="ECO:0007829|PDB:3NVS"
FT STRAND 402..406
FT /evidence="ECO:0007829|PDB:3NVS"
FT HELIX 407..412
FT /evidence="ECO:0007829|PDB:3NVS"
FT HELIX 417..424
FT /evidence="ECO:0007829|PDB:3NVS"
SQ SEQUENCE 426 AA; 46102 MW; 38852D6483BFE1C3 CRC64;
MESLTLQPIE LISGEVNLPG SKSVSNRALL LAALASGTTR LTNLLDSDDI RHMLNALTKL
GVNYRLSADK TTCEVEGLGQ AFHTTQPLEL FLGNAGTAMR PLAAALCLGQ GDYVLTGEPR
MKERPIGHLV DALRQAGAQI EYLEQENFPP LRIQGTGLQA GTVTIDGSIS SQFLTAFLMS
APLAQGKVTI KIVGELVSKP YIDITLHIME QFGVQVINHD YQEFVIPAGQ SYVSPGQFLV
EGDASSASYF LAAAAIKGGE VKVTGIGKNS IQGDIQFADA LEKMGAQIEW GDDYVIARRG
ELNAVDLDFN HIPDAAMTIA TTALFAKGTT AIRNVYNWRV KETDRLAAMA TELRKVGATV
EEGEDFIVIT PPTKLIHAAI DTYDDHRMAM CFSLVALSDT PVTINDPKCT SKTFPDYFDK
FAQLSR
