ID AROA_MANSM Reviewed; 433 AA.
AC Q65S78;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 27-MAR-2024, entry version 113.
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=MS1575;
OS Mannheimia succiniciproducens (strain MBEL55E).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Basfia.
OX NCBI_TaxID=221988;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MBEL55E;
RX PubMed=15378067; DOI=10.1038/nbt1010;
RA Hong S.H., Kim J.S., Lee S.Y., In Y.H., Choi S.S., Rih J.-K., Kim C.H.,
RA Jeong H., Hur C.G., Kim J.J.;
RT "The genome sequence of the capnophilic rumen bacterium Mannheimia
RT succiniciproducens.";
RL Nat. Biotechnol. 22:1275-1281(2004).
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: Monomer. {ECO:0000255|HAMAP-Rule:MF_00210}.
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; AE016827; AAU38182.1; -; Genomic_DNA.
DR RefSeq; WP_011200747.1; NC_006300.1.
DR AlphaFoldDB; Q65S78; -.
DR SMR; Q65S78; -.
DR STRING; 221988.MS1575; -.
DR KEGG; msu:MS1575; -.
DR eggNOG; COG0128; Bacteria.
DR HOGENOM; CLU_024321_0_0_6; -.
DR OrthoDB; 9809920at2; -.
DR UniPathway; UPA00053; UER00089.
DR Proteomes; UP000000607; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003866; F:3-phosphoshikimate 1-carboxyvinyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008652; P:amino acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd01556; EPSP_synthase; 1.
DR Gene3D; 3.65.10.10; Enolpyruvate transferase domain; 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 NCBIfam; TIGR01356; aroA; 1.
DR PANTHER; PTHR21090; AROM/DEHYDROQUINATE SYNTHASE; 1.
DR PANTHER; PTHR21090:SF5; PENTAFUNCTIONAL AROM POLYPEPTIDE; 1.
DR Pfam; PF00275; EPSP_synthase; 1.
DR PIRSF; PIRSF000505; EPSPS; 1.
DR SUPFAM; SSF55205; EPT/RTPC-like; 1.
DR PROSITE; PS00104; EPSP_SYNTHASE_1; 1.
DR PROSITE; PS00885; EPSP_SYNTHASE_2; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Cytoplasm;
KW Transferase.
FT CHAIN 1..433
FT /note="3-phosphoshikimate 1-carboxyvinyltransferase"
FT /id="PRO_1000012448"
FT REGION 94..97
FT /note="Phosphoenolpyruvate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT ACT_SITE 318
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT ACT_SITE 346
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT BINDING 22..23
FT /ligand="3-phosphoshikimate"
FT /ligand_id="ChEBI:CHEBI:145989"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT BINDING 27
FT /ligand="3-phosphoshikimate"
FT /ligand_id="ChEBI:CHEBI:145989"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT BINDING 129
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT BINDING 175..177
FT /ligand="3-phosphoshikimate"
FT /ligand_id="ChEBI:CHEBI:145989"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT BINDING 203
FT /ligand="3-phosphoshikimate"
FT /ligand_id="ChEBI:CHEBI:145989"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT BINDING 341
FT /ligand="3-phosphoshikimate"
FT /ligand_id="ChEBI:CHEBI:145989"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT BINDING 345
FT /ligand="3-phosphoshikimate"
FT /ligand_id="ChEBI:CHEBI:145989"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT BINDING 349
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT BINDING 393
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT BINDING 418
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
SQ SEQUENCE 433 AA; 47187 MW; DC89A616A14739AB CRC64;
MEKLTLTPIS HVEGTVNLPG SKSLSNRALL LAALAKGTTR VTNLLDSDDV RHMLNALKQL
GVNYSLSEDK SVCEVQGLGK AFAWQNGLAL FLGNAGTAMR PLTAALCLAN ADSVPAEIIL
TGEPRMKERP IKHLVDALLQ AGADVQYLEQ EGYPPLAIRN TGLKGGKVKI DGSVSSQFLT
ALLMAAPMAE RDTEIEIIGE LVSKPYIDIT LNMMKIFAVD VDNQNYQRFV VKGNQQYQSP
NIFLVEGDAS SASYFLAAGA IKGKVRVTGV GKNSIQGDRL FAEVLEKMGA KITWGEDYIE
AERGELNGID MDMNHIPDAA MTIATTALFA QGETVIRNIY NWRVKETDRL SAMATELRKV
GAEVEEGEDF IRIQPPASDQ FKHAEIETYN DHRMAMCFAL VALSNTAVTI CDPKCTAKTF
PTFFDEFSAI ATV
//
