AROC_STAAU
ID AROC_STAAU Reviewed; 388 AA.
AC Q59803;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Chorismate synthase {ECO:0000255|HAMAP-Rule:MF_00300, ECO:0000303|PubMed:8885411};
DE Short=CS {ECO:0000255|HAMAP-Rule:MF_00300};
DE EC=4.2.3.5 {ECO:0000255|HAMAP-Rule:MF_00300, ECO:0000269|PubMed:8885411};
DE AltName: Full=5-enolpyruvylshikimate-3-phosphate phospholyase {ECO:0000255|HAMAP-Rule:MF_00300};
GN Name=aroC {ECO:0000255|HAMAP-Rule:MF_00300, ECO:0000303|PubMed:8885411};
OS Staphylococcus aureus.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1280;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-28, FUNCTION,
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MASS SPECTROMETRY, AND
RP SUBUNIT.
RC STRAIN=601055;
RX PubMed=8885411; DOI=10.1099/13500872-142-10-2943;
RA Horsburgh M.J., Foster T.J., Barth P.T., Coggins J.R.;
RT "Chorismate synthase from Staphylococcus aureus.";
RL Microbiology 142:2943-2950(1996).
CC -!- FUNCTION: Catalyzes the anti-1,4-elimination of the C-3 phosphate and
CC the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to
CC yield chorismate, which is the branch point compound that serves as the
CC starting substrate for the three terminal pathways of aromatic amino
CC acid biosynthesis. This reaction introduces a second double bond into
CC the aromatic ring system. {ECO:0000255|HAMAP-Rule:MF_00300,
CC ECO:0000269|PubMed:8885411}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate +
CC phosphate; Xref=Rhea:RHEA:21020, ChEBI:CHEBI:29748,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57701; EC=4.2.3.5;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00300,
CC ECO:0000269|PubMed:8885411};
CC -!- COFACTOR:
CC Name=FMNH2; Xref=ChEBI:CHEBI:57618;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00300};
CC Note=Reduced FMN (FMNH(2)). {ECO:0000255|HAMAP-Rule:MF_00300};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=12.7 uM for EPSP (at pH 7 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:8885411};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC 7/7. {ECO:0000255|HAMAP-Rule:MF_00300}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00300,
CC ECO:0000269|PubMed:8885411}.
CC -!- MASS SPECTROMETRY: Mass=43024; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:8885411};
CC -!- SIMILARITY: Belongs to the chorismate synthase family.
CC {ECO:0000255|HAMAP-Rule:MF_00300}.
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DR EMBL; U31979; AAB41907.1; -; Genomic_DNA.
DR AlphaFoldDB; Q59803; -.
DR SMR; Q59803; -.
DR UniPathway; UPA00053; UER00090.
DR GO; GO:0004107; F:chorismate synthase 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; cd07304; Chorismate_synthase; 1.
DR Gene3D; 3.60.150.10; -; 1.
DR HAMAP; MF_00300; Chorismate_synth; 1.
DR InterPro; IPR000453; Chorismate_synth.
DR InterPro; IPR035904; Chorismate_synth_AroC_sf.
DR InterPro; IPR020541; Chorismate_synthase_CS.
DR PANTHER; PTHR21085; PTHR21085; 1.
DR Pfam; PF01264; Chorismate_synt; 1.
DR PIRSF; PIRSF001456; Chorismate_synth; 1.
DR SUPFAM; SSF103263; SSF103263; 1.
DR TIGRFAMs; TIGR00033; aroC; 1.
DR PROSITE; PS00787; CHORISMATE_SYNTHASE_1; 1.
DR PROSITE; PS00788; CHORISMATE_SYNTHASE_2; 1.
DR PROSITE; PS00789; CHORISMATE_SYNTHASE_3; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW Direct protein sequencing; FAD; Flavoprotein; FMN; Lyase; NADP.
FT CHAIN 1..388
FT /note="Chorismate synthase"
FT /id="PRO_0000140646"
FT BINDING 39
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00300"
FT BINDING 45
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00300"
FT BINDING 132..134
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00300"
FT BINDING 251..252
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00300"
FT BINDING 296
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00300"
FT BINDING 311..315
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00300"
FT BINDING 337
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00300"
SQ SEQUENCE 388 AA; 43060 MW; 33F39F901C2B6502 CRC64;
MRYLTSGESH GPQLTVIVEG VPANLEVKVE DINKEMFKRQ GGYGRGRRMQ IEKDTVEIVS
GVRNGYTLGS PITMVVTNDD FTHWRKIMGR APISDEEREN MKRTITKPRP GHADLLGGMK
YNHRDLRNVL ERSSARETAA RVAVGALCKV LLEQLDIEIY SRVVEIGGIK DKDFYDSETF
KANLDRNDVR VIDDGIAQAM RDKIDEAKTD GDSIGGVVQV VVENMPVGVG SYVHYDRKLD
GRIAQGVVSI NAFKGVSFGE GFKAAEKPGS EIQDEILYNT ELGYYRGSNH LGGLEGGMSN
GMPIIVNGVM KPIPTLYKPL NSVDINTKED FKATIERSDS CAVPAASIVC EHVVAFAIAK
ALLEEFQSNH IEQLKQQIIE RRQLNIEF
