AROC_CHLCV
ID AROC_CHLCV Reviewed; 359 AA.
AC Q822F8;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 101.
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=CCA_00725;
OS Chlamydia caviae (strain ATCC VR-813 / DSM 19441 / 03DC25 / GPIC)
OS (Chlamydophila caviae).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=227941;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC VR-813 / DSM 19441 / 03DC25 / GPIC;
RX PubMed=12682364; DOI=10.1093/nar/gkg321;
RA Read T.D., Myers G.S.A., Brunham R.C., Nelson W.C., Paulsen I.T.,
RA Heidelberg J.F., Holtzapple E.K., Khouri H.M., Federova N.B., Carty H.A.,
RA Umayam L.A., Haft D.H., Peterson J.D., Beanan M.J., White O.,
RA Salzberg S.L., Hsia R.-C., McClarty G., Rank R.G., Bavoil P.M.,
RA Fraser C.M.;
RT "Genome sequence of Chlamydophila caviae (Chlamydia psittaci GPIC):
RT examining the role of niche-specific genes in the evolution of the
RT Chlamydiaceae.";
RL Nucleic Acids Res. 31:2134-2147(2003).
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; AE015925; AAP05466.1; -; Genomic_DNA.
DR RefSeq; WP_011006680.1; NC_003361.3.
DR AlphaFoldDB; Q822F8; -.
DR SMR; Q822F8; -.
DR STRING; 227941.CCA_00725; -.
DR EnsemblBacteria; AAP05466; AAP05466; CCA_00725.
DR KEGG; cca:CCA_00725; -.
DR eggNOG; COG0082; Bacteria.
DR HOGENOM; CLU_034547_0_2_0; -.
DR OMA; MLSINAV; -.
DR OrthoDB; 981870at2; -.
DR UniPathway; UPA00053; UER00090.
DR Proteomes; UP000002193; 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.
FT CHAIN 1..359
FT /note="Chorismate synthase"
FT /id="PRO_1000022477"
FT BINDING 47
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00300"
FT BINDING 123..125
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00300"
FT BINDING 283
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00300"
FT BINDING 298..302
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00300"
FT BINDING 326
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00300"
SQ SEQUENCE 359 AA; 38623 MW; 2F70E5C4F760ED79 CRC64;
MRNRFGSLFS LTTWGESHGP SIGVVIDGCP AGLLLDPEDF IPAMSRRSPG RPGTSPRKEA
DIVHILSGVY QGKTTGTPIS LQIFNTDVKS ATYHQQEDRY RPGHGQLAYE KKYGLVDPLG
GGRSSARETA CRVAAGVIAA KILAHYDIYC LAFLSKLGKE SIETYPKLSK EFAQNIYNSP
FLSPLDNDSI LQTLTHLQNE QDSLGGVVSF ITSPIHESLG EPVFNKVQAV LASGLMSIPA
AKGFEIGLGF ASTDSYGSEY IDPFIIENEN ISMGSNNCGG SLGGITVGMP LNGRVAFKPT
SSIRKPFLTV TKTGEPSIYA TQKEGRHDPC VAIRAVAVVE AMVNLVLADL LLQQRCARL
