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Database: UniProt
Entry: A0A0Y0N5W8_9MICO
LinkDB: A0A0Y0N5W8_9MICO
Original site: A0A0Y0N5W8_9MICO 
ID   A0A0Y0N5W8_9MICO        Unreviewed;       453 AA.
AC   A0A0Y0N5W8;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 38.
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   ORFNames=AWU67_02265 {ECO:0000313|EMBL:AMB57883.1};
OS   Microterricola viridarii.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Microterricola.
OX   NCBI_TaxID=412690 {ECO:0000313|EMBL:AMB57883.1, ECO:0000313|Proteomes:UP000058305};
RN   [1] {ECO:0000313|EMBL:AMB57883.1, ECO:0000313|Proteomes:UP000058305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ERGS5:02 {ECO:0000313|EMBL:AMB57883.1,
RC   ECO:0000313|Proteomes:UP000058305};
RX   PubMed=26854947; DOI=10.1016/j.jbiotec.2016.02.011;
RA   Himanshu, Swarnkar M.K., Singh D., Kumar R.;
RT   "First complete genome sequence of a species in the genus Microterricola,
RT   an extremophilic cold active enzyme producing bacterial strain ERGS5:02
RT   isolated from Sikkim Himalaya.";
RL   J. Biotechnol. 222:17-18(2016).
RN   [2] {ECO:0000313|Proteomes:UP000058305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ERGS5:02 {ECO:0000313|Proteomes:UP000058305};
RA   Kumar R., Singh D., Swarnkar M.K.;
RT   "First complete genome sequence of a species in the genus Microterricola,
RT   an extremophilic cold active enzyme producing strain ERGS5:02 isolated from
RT   Sikkim Himalaya.";
RL   Submitted (JAN-2016) 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}.
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DR   EMBL; CP014145; AMB57883.1; -; Genomic_DNA.
DR   RefSeq; WP_067226220.1; NZ_CP014145.1.
DR   AlphaFoldDB; A0A0Y0N5W8; -.
DR   KEGG; mvd:AWU67_02265; -.
DR   OrthoDB; 9809920at2; -.
DR   UniPathway; UPA00053; UER00089.
DR   Proteomes; UP000058305; 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:UP000058305};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00210}.
FT   DOMAIN          32..442
FT                   /note="Enolpyruvate transferase"
FT                   /evidence="ECO:0000259|Pfam:PF00275"
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          118..121
FT                   /note="Phosphoenolpyruvate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00210"
FT   ACT_SITE        338
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00210"
FT   ACT_SITE        366
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00210"
FT   BINDING         45..46
FT                   /ligand="3-phosphoshikimate"
FT                   /ligand_id="ChEBI:CHEBI:145989"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00210"
FT   BINDING         50
FT                   /ligand="3-phosphoshikimate"
FT                   /ligand_id="ChEBI:CHEBI:145989"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00210"
FT   BINDING         148
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00210"
FT   BINDING         194..196
FT                   /ligand="3-phosphoshikimate"
FT                   /ligand_id="ChEBI:CHEBI:145989"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00210"
FT   BINDING         223
FT                   /ligand="3-phosphoshikimate"
FT                   /ligand_id="ChEBI:CHEBI:145989"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00210"
FT   BINDING         369
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"
FT   BINDING         435
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00210"
SQ   SEQUENCE   453 AA;  47079 MW;  C805DF076059A4EC CRC64;
     MLISRYSKPD FDPYGENSPE PEETLWPAPT ATGPTSAVLS LPGSKSLTNR ELVLSALADG
     PSLLRSPLHS RDSELMVEAL RELGTVIEAV PGNGEYGDDL LITPVEELSG STTIDCGLAG
     TVMRFLPPLA GLALGPTTFD GDDAARRRPM ATTISSLRAL GVDINDDGRP VLPFTVHGTG
     HIVGGEVTID ASLSSQFVSG LLLAASRFDN GLSLTHSGER LPSLPHIEMT IATLAARGVT
     VDSPATGQWV VAPGPIAAAD VDIEPDLSNA APFLAAALVT GGTVTITGWP NETTQIGARL
     ADLLPLFGAT VSRDGDRLTV TGGDGIRGVT LDLPEGGELV PNLVALAALA SEPSTITGIG
     HIRHHETDRL AALVTEINKL GGKVTELPDG LHIEPAELHG GTWLSYEDHR MATTGAIIGL
     AVPGVQIENI DTTAKTLPQF TQLWHAMLGG HGA
//
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