ID B8EN74_METSB Unreviewed; 443 AA.
AC B8EN74;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 90.
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 OrderedLocusNames=Msil_0615 {ECO:0000313|EMBL:ACK49587.1};
OS Methylocella silvestris (strain DSM 15510 / CIP 108128 / LMG 27833 / NCIMB
OS 13906 / BL2).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Beijerinckiaceae; Methylocella.
OX NCBI_TaxID=395965 {ECO:0000313|EMBL:ACK49587.1, ECO:0000313|Proteomes:UP000002257};
RN [1] {ECO:0000313|EMBL:ACK49587.1, ECO:0000313|Proteomes:UP000002257}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15510 / CIP 108128 / LMG 27833 / NCIMB 13906 / BL2
RC {ECO:0000313|Proteomes:UP000002257};
RX PubMed=20472789; DOI=10.1128/JB.00506-10;
RA Chen Y., Crombie A., Rahman M.T., Dedysh S.N., Liesack W., Stott M.B.,
RA Alam M., Theisen A.R., Murrell J.C., Dunfield P.F.;
RT "Complete genome sequence of the aerobic facultative methanotroph
RT Methylocella silvestris BL2.";
RL J. Bacteriol. 192:3840-3841(2010).
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}.
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DR EMBL; CP001280; ACK49587.1; -; Genomic_DNA.
DR RefSeq; WP_012589657.1; NC_011666.1.
DR AlphaFoldDB; B8EN74; -.
DR STRING; 395965.Msil_0615; -.
DR KEGG; msl:Msil_0615; -.
DR eggNOG; COG0128; Bacteria.
DR HOGENOM; CLU_024321_0_1_5; -.
DR OrthoDB; 9809920at2; -.
DR UniPathway; UPA00053; UER00089.
DR Proteomes; UP000002257; 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 {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 Reference proteome {ECO:0000313|Proteomes:UP000002257};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00210}.
FT DOMAIN 13..434
FT /note="Enolpyruvate transferase"
FT /evidence="ECO:0000259|Pfam:PF00275"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 97..100
FT /note="Phosphoenolpyruvate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00210"
FT ACT_SITE 326
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00210"
FT ACT_SITE 354
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00210"
FT BINDING 26..27
FT /ligand="3-phosphoshikimate"
FT /ligand_id="ChEBI:CHEBI:145989"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00210"
FT BINDING 31
FT /ligand="3-phosphoshikimate"
FT /ligand_id="ChEBI:CHEBI:145989"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00210"
FT BINDING 127
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00210"
FT BINDING 353
FT /ligand="3-phosphoshikimate"
FT /ligand_id="ChEBI:CHEBI:145989"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00210"
FT BINDING 357
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00210"
FT BINDING 400
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00210"
SQ SEQUENCE 443 AA; 46572 MW; 93BCC1A9C65F19F4 CRC64;
MEVATSRLTA ERSGPLAGRI KPPGDKSISH RALILGLLSV GTTEITGLLE GEDVIHTAKV
CGALGARVER LAPGRWRVEG CGIGSLLQPE ETLDFGNSGT GMRLMMGVVA GHPITATLDG
DASLRTRPMR RVLDPLMMMG AQTLSQAEGG RCPIILKGTA EPIPIVYKSP VASAQIKSAV
LLAGLNSPGE TSVIEPEASR DHTEKMLRYF GAALKVEPFG ENGRKITLQG RPELKPAPVA
VPGDPSSAAF ALVAATIVEN SDIVIESMMM NPLRTGLLTT LLEMGADIEI IDRREEGGEE
VADLRVRGAA LKGVDVPAAR APSMIDEYPI LAVAASFARG QTRMRGLGEL RVKESDRLEA
VAAGLRACGV DPQIIGDDLI VEGGAEVSGG GLVATHLDHR IAMSFLILGL AAQKPVAIDD
VGMIATSFPD FRAQMESLGA RFS
//
