AROA_MANHA
ID AROA_MANHA Reviewed; 432 AA.
AC P54220; P96968;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 108.
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};
OS Mannheimia haemolytica (Pasteurella haemolytica).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Mannheimia.
OX NCBI_TaxID=75985;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Serotype A1 / NADC-D60;
RX PubMed=8031095; DOI=10.1128/aem.60.6.2011-2016.1994;
RA Tatum F.M., Briggs R.E., Halling S.M.;
RT "Molecular gene cloning and nucleotide sequencing and construction of an
RT aroA mutant of Pasteurella haemolytica serotype A1.";
RL Appl. Environ. Microbiol. 60:2011-2016(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Serotype 2 / NADC-D171;
RA Hellrung D.J., Tatum F.M., Briggs R.E.;
RT "Molecular cloning, nucleotide sequencing, and construction of a
RT Pasteurella haemolytica serotype 2 aroA mutant.";
RL Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases.
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, ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U03068; AAA21529.1; -; Genomic_DNA.
DR EMBL; U89948; AAB86439.1; -; Genomic_DNA.
DR RefSeq; WP_006250709.1; NZ_VAIO01000037.1.
DR AlphaFoldDB; P54220; -.
DR SMR; P54220; -.
DR STRING; 75985.WC39_07780; -.
DR PATRIC; fig|75985.47.peg.1944; -.
DR UniPathway; UPA00053; UER00089.
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: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; IEA:UniProtKB-UniPathway.
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 3: Inferred from homology;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Cytoplasm;
KW Transferase.
FT CHAIN 1..432
FT /note="3-phosphoshikimate 1-carboxyvinyltransferase"
FT /id="PRO_0000088277"
FT REGION 94..97
FT /note="Phosphoenolpyruvate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT ACT_SITE 317
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT ACT_SITE 345
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 127
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT BINDING 173..175
FT /ligand="3-phosphoshikimate"
FT /ligand_id="ChEBI:CHEBI:145989"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT BINDING 201
FT /ligand="3-phosphoshikimate"
FT /ligand_id="ChEBI:CHEBI:145989"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT BINDING 340
FT /ligand="3-phosphoshikimate"
FT /ligand_id="ChEBI:CHEBI:145989"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT BINDING 344
FT /ligand="3-phosphoshikimate"
FT /ligand_id="ChEBI:CHEBI:145989"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT BINDING 348
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT BINDING 392
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT BINDING 417
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT CONFLICT 75
FT /note="V -> L (in Ref. 1; AAA21529)"
FT /evidence="ECO:0000305"
FT CONFLICT 111..114
FT /note="AETA -> EEKS (in Ref. 1; AAA21529)"
FT /evidence="ECO:0000305"
FT CONFLICT 160..162
FT /note="GLQ -> VCR (in Ref. 1; AAA21529)"
FT /evidence="ECO:0000305"
FT CONFLICT 189
FT /note="S -> G (in Ref. 1; AAA21529)"
FT /evidence="ECO:0000305"
FT CONFLICT 262..264
FT /note="GKV -> AG (in Ref. 1; AAA21529)"
FT /evidence="ECO:0000305"
FT CONFLICT 367
FT /note="E -> EEGE (in Ref. 1; AAA21529)"
FT /evidence="ECO:0000305"
FT CONFLICT 425
FT /note="E -> D (in Ref. 1; AAA21529)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 432 AA; 47064 MW; 4C7E62FD4CA76959 CRC64;
MEKLTLTPIS RVEGEINLPG SKSLSNRALL LAALATGTTQ VTNLLDSDDI RHMLNALKAL
GVKYELSDDK TVCVVEGIGG AFKVQNGLSL FLGNAGTAMR PLAAALCLKG AETAQIILTG
EPRMKERPIK HLVDALRQVG AEVQYLENEG YPPLAISNSG LQGGKVQIDG SISSQFLTAL
LMSAPLAESD MEIEIIGDLV SKPYIDITLS MMNDFGITVE NRDYKTFLVK GKQGYVAPQG
NYLVEGDASS ASYFLASGAI KGKVKVTGIG KKSIQGDRLF ADVLEKMGAK ITWGEDFIQA
EQSPLKGVDM DMNHIPDAAM TIATTALFAE GETVIRNIYN WRVKETDRLT AMATELRKVG
AEVEEGEDFI RIQPLALENF QHAEIETYND HRMAMCFSLI ALSNTEVTIL DPNCTAKTFP
TYFRELEKLS VR
