ID AROC_PROMA Reviewed; 362 AA.
AC P46894;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 26-SEP-2003, sequence version 2.
DT 27-MAR-2024, entry version 129.
DE RecName: Full=Chorismate synthase {ECO:0000255|HAMAP-Rule:MF_00300};
DE Short=CS {ECO:0000255|HAMAP-Rule:MF_00300};
DE EC=4.2.3.5 {ECO:0000255|HAMAP-Rule:MF_00300};
DE AltName: Full=5-enolpyruvylshikimate-3-phosphate phospholyase {ECO:0000255|HAMAP-Rule:MF_00300};
GN Name=aroC {ECO:0000255|HAMAP-Rule:MF_00300}; OrderedLocusNames=Pro_0253;
OS Prochlorococcus marinus (strain SARG / CCMP1375 / SS120).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC Prochlorococcaceae; Prochlorococcus.
OX NCBI_TaxID=167539;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SARG / CCMP1375 / SS120;
RX PubMed=12917486; DOI=10.1073/pnas.1733211100;
RA Dufresne A., Salanoubat M., Partensky F., Artiguenave F., Axmann I.M.,
RA Barbe V., Duprat S., Galperin M.Y., Koonin E.V., Le Gall F., Makarova K.S.,
RA Ostrowski M., Oztas S., Robert C., Rogozin I.B., Scanlan D.J.,
RA Tandeau de Marsac N., Weissenbach J., Wincker P., Wolf Y.I., Hess W.R.;
RT "Genome sequence of the cyanobacterium Prochlorococcus marinus SS120, a
RT nearly minimal oxyphototrophic genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:10020-10025(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-52.
RC STRAIN=SARG / CCMP1375 / SS120;
RX PubMed=7766900; DOI=10.1007/bf00020892;
RA Hess W.R., Weihe A., Loiseaux-De Goer S., Partensky F., Vaulot D.;
RT "Characterization of the single psbA gene of Prochlorococcus marinus CCMP
RT 1375 (Prochlorophyta).";
RL Plant Mol. Biol. 27:1189-1196(1995).
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 -!- 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 -!- 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 -!- 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 -!- SIMILARITY: Belongs to the chorismate synthase family.
CC {ECO:0000255|HAMAP-Rule:MF_00300}.
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DR EMBL; AE017126; AAP99299.1; -; Genomic_DNA.
DR EMBL; Z49201; CAA89063.1; -; Genomic_DNA.
DR RefSeq; NP_874647.1; NC_005042.1.
DR RefSeq; WP_011124408.1; NC_005042.1.
DR AlphaFoldDB; P46894; -.
DR SMR; P46894; -.
DR STRING; 167539.Pro_0253; -.
DR EnsemblBacteria; AAP99299; AAP99299; Pro_0253.
DR KEGG; pma:Pro_0253; -.
DR PATRIC; fig|167539.5.peg.261; -.
DR eggNOG; COG0082; Bacteria.
DR HOGENOM; CLU_034547_0_1_3; -.
DR OrthoDB; 9771806at2; -.
DR UniPathway; UPA00053; UER00090.
DR Proteomes; UP000001420; Chromosome.
DR GO; GO:0004107; F:chorismate synthase 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; cd07304; Chorismate_synthase; 1.
DR Gene3D; 3.60.150.10; Chorismate synthase AroC; 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 NCBIfam; TIGR00033; aroC; 1.
DR PANTHER; PTHR21085; CHORISMATE SYNTHASE; 1.
DR PANTHER; PTHR21085:SF0; CHORISMATE SYNTHASE; 1.
DR Pfam; PF01264; Chorismate_synt; 1.
DR PIRSF; PIRSF001456; Chorismate_synth; 1.
DR SUPFAM; SSF103263; Chorismate synthase, AroC; 1.
DR PROSITE; PS00787; CHORISMATE_SYNTHASE_1; 1.
DR PROSITE; PS00788; CHORISMATE_SYNTHASE_2; 1.
DR PROSITE; PS00789; CHORISMATE_SYNTHASE_3; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; FAD;
KW Flavoprotein; FMN; Lyase; NADP; Reference proteome.
FT CHAIN 1..362
FT /note="Chorismate synthase"
FT /id="PRO_0000140628"
FT BINDING 47
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00300"
FT BINDING 124..126
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00300"
FT BINDING 286
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00300"
FT BINDING 301..305
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00300"
FT BINDING 327
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00300"
FT CONFLICT 49..52
FT /note="PGQS -> RQQR (in Ref. 2; CAA89063)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 362 AA; 39429 MW; 4D761D46A694506C CRC64;
MGSSFGDLFR VSTFGESHGG SVGVIVEGCP PRLEIDLEKI QEELDRRRPG QSKITTPRKE
LDQVEILSGI ANRETLGTPI AMIVRNRDQR PSDYKEMKNI FRPSHADGTY HLKYGIQAPS
GGGRASARET IGRVAAGAIA KQLLQKVQNT QILAWVKRIH NIEAEIDINT IGFADIESNI
VRCPNQDVAK LMIQRIEEIS RDGDSCGGLI ECVVRNVPAG LGMPVFDKLE ADLSKALMSL
PATKGFEVGS GFRGTFLKGS EHNDAFIAGD KNRLRTATNN SGGIQGGISN GEPIILRVGF
KPTATIRKDQ QTIDSEGKQI TLASKGRHDP CVLPRAVPMV EAMVSIVLAD HLLRQRGQCS
LW
//
