ID A0A260XB01_9NOCA Unreviewed; 442 AA.
AC A0A260XB01;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=3-phosphoshikimate 1-carboxyvinyltransferase {ECO:0000256|HAMAP-Rule:MF_00210};
DE EC=2.5.1.19 {ECO:0000256|HAMAP-Rule:MF_00210};
DE AltName: Full=5-enolpyruvylshikimate-3-phosphate synthase {ECO:0000256|HAMAP-Rule:MF_00210};
DE Short=EPSP synthase {ECO:0000256|HAMAP-Rule:MF_00210};
DE Short=EPSPS {ECO:0000256|HAMAP-Rule:MF_00210};
GN Name=aroA {ECO:0000256|HAMAP-Rule:MF_00210,
GN ECO:0000313|EMBL:OZF58267.1};
GN ORFNames=CH292_00510 {ECO:0000313|EMBL:OZF58267.1};
OS Rhodococcus sp. 14-2470-1a.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=2023150 {ECO:0000313|EMBL:OZF58267.1, ECO:0000313|Proteomes:UP000215821};
RN [1] {ECO:0000313|Proteomes:UP000215821}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=14-2470-1a {ECO:0000313|Proteomes:UP000215821};
RA Savory E.A., Fuller S.J., Weisberg A.J., Thomas W.J., Gordon M.I.,
RA Stevens D.M., Creason A.L., Belcher M.S., Wiseman M., Putnam M.L.,
RA Grunwald N.J., Chang J.H.;
RT "Evolutionary transitions between beneficial and phytopathogenic
RT Rhodococcus challenge disease management.";
RL Submitted (JUL-2017) 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:0000256|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;
CC Evidence={ECO:0000256|ARBA:ARBA00001901, ECO:0000256|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:0000256|ARBA:ARBA00004811, ECO:0000256|HAMAP-Rule:MF_00210}.
CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00210}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00210}.
CC -!- SIMILARITY: Belongs to the EPSP synthase family.
CC {ECO:0000256|ARBA:ARBA00009948, ECO:0000256|HAMAP-Rule:MF_00210}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00210}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OZF58267.1}.
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DR EMBL; NPFZ01000001; OZF58267.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A260XB01; -.
DR UniPathway; UPA00053; UER00089.
DR Proteomes; UP000215821; Unassembled WGS sequence.
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 {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW Rule:MF_00210};
KW Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141,
KW ECO:0000256|HAMAP-Rule:MF_00210};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00210};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00210}.
FT DOMAIN 12..417
FT /note="Enolpyruvate transferase"
FT /evidence="ECO:0000259|Pfam:PF00275"
FT REGION 92..95
FT /note="Phosphoenolpyruvate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00210"
FT ACT_SITE 313
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00210"
FT ACT_SITE 341
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00210"
FT BINDING 24..25
FT /ligand="3-phosphoshikimate"
FT /ligand_id="ChEBI:CHEBI:145989"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00210"
FT BINDING 29
FT /ligand="3-phosphoshikimate"
FT /ligand_id="ChEBI:CHEBI:145989"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00210"
FT BINDING 122
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00210"
FT BINDING 165..167
FT /ligand="3-phosphoshikimate"
FT /ligand_id="ChEBI:CHEBI:145989"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00210"
FT BINDING 194
FT /ligand="3-phosphoshikimate"
FT /ligand_id="ChEBI:CHEBI:145989"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00210"
FT BINDING 344
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00210"
FT BINDING 385
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00210"
FT BINDING 410
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00210"
SQ SEQUENCE 442 AA; 45092 MW; F6855716B22491E5 CRC64;
MVTNWTAPLS TAPVDATVTL PGSKSITNRA LIISALAGGQ STVTAALRSR DTDLMIAALQ
QLGVGITIDP ADPTSLTVTP GALRGGSIDC GLAGTVMRFV PPLAALADGV VRFDGDEQAR
TRPLDTILGA LRHLGADVAG DSLPFTVTGS GTLRGGAVDI DASGSSQFVS GLMLSAAAFD
DGITIHHTGK PVPSMPHIDM TVEMLRRAGV QVSTPADSGD ADTWRVHPGP VDAVSWVVEP
DLSNATPFLA AAAVTGGVVR VPNWPSSTTQ PGDAIRGILE SMGATVTLEN GTLEVRGGAT
STGVDIDLHD VGELTPTVAA LAALADRPSH LRGIAHLRGH ETDRLAALVA EIRRLGGNAT
ETDDGLDIAP AALHGGVWRA YADHRMATAG AILGLVVPGV EVDDIGTTAK TLPGFENLWA
SMLGDSPLAG RGTRPTTEGV SS
//
