AROC_STRSV
ID AROC_STRSV Reviewed; 388 AA.
AC A3CNV6;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 90.
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=SSA_1467;
OS Streptococcus sanguinis (strain SK36).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=388919;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK36;
RX PubMed=17277061; DOI=10.1128/jb.01808-06;
RA Xu P., Alves J.M., Kitten T., Brown A., Chen Z., Ozaki L.S., Manque P.,
RA Ge X., Serrano M.G., Puiu D., Hendricks S., Wang Y., Chaplin M.D., Akan D.,
RA Paik S., Peterson D.L., Macrina F.L., Buck G.A.;
RT "Genome of the opportunistic pathogen Streptococcus sanguinis.";
RL J. Bacteriol. 189:3166-3175(2007).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000387; ABN44861.1; -; Genomic_DNA.
DR RefSeq; WP_002920830.1; NC_009009.1.
DR RefSeq; YP_001035411.1; NC_009009.1.
DR AlphaFoldDB; A3CNV6; -.
DR SMR; A3CNV6; -.
DR STRING; 388919.SSA_1467; -.
DR EnsemblBacteria; ABN44861; ABN44861; SSA_1467.
DR KEGG; ssa:SSA_1467; -.
DR PATRIC; fig|388919.9.peg.1392; -.
DR eggNOG; COG0082; Bacteria.
DR HOGENOM; CLU_034547_2_0_9; -.
DR OMA; MLSINAV; -.
DR OrthoDB; 981870at2; -.
DR UniPathway; UPA00053; UER00090.
DR Proteomes; UP000002148; Chromosome.
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 3: Inferred from homology;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; FAD;
KW Flavoprotein; FMN; Lyase; NADP; Reference proteome.
FT CHAIN 1..388
FT /note="Chorismate synthase"
FT /id="PRO_0000322425"
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 130..132
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; 42236 MW; 6452F6D6D73D070E CRC64;
MRYLTAGESH GPRLTAIIEG VPAGLPLTAD YINAELKRRQ GGYGRGARMK IESDQVEITS
GVRHGLTMGG PITLNVTNLD HQKWQEIMSA ADVDEKKKGL RKITKPRPGH ADLVGGMKYR
FDDLRNSLER SSARETTMRV AVGAVAKRLL EEIGVEVASH IVTFGGIDIN VPNNLTVGEI
KERAAQSEVS IVNPDREEEI KAYIDQIKKD GDTIGGVIET VVGGVPVGLG SYVQWDKKLD
AKIAQGVVSI NAFKGVEFGV GFEAGRLKGS QVMDEILWSE EDGFTRRTNN LGGFEGGMTN
GQPIVVRGVM KPIPTLYKPL MSVDIETHEP YKATVERSDP TALPAAGVVM ESVVATVLAT
EVLEKFSSDN LEELKDAVAR HREFVKNF
