AROC_CAMJE
ID AROC_CAMJE Reviewed; 362 AA.
AC Q9PM41; Q0P7Z4;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 125.
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=Cj1634c;
OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS 11168).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=192222;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=10688204; DOI=10.1038/35001088;
RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA Barrell B.G.;
RT "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT reveals hypervariable sequences.";
RL Nature 403:665-668(2000).
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; AL111168; CAL35731.1; -; Genomic_DNA.
DR PIR; H81259; H81259.
DR RefSeq; WP_002851463.1; NC_002163.1.
DR RefSeq; YP_002345003.1; NC_002163.1.
DR PDB; 1SQ1; X-ray; 2.80 A; A=1-362.
DR PDBsum; 1SQ1; -.
DR AlphaFoldDB; Q9PM41; -.
DR SMR; Q9PM41; -.
DR IntAct; Q9PM41; 92.
DR STRING; 192222.Cj1634c; -.
DR PaxDb; Q9PM41; -.
DR PRIDE; Q9PM41; -.
DR EnsemblBacteria; CAL35731; CAL35731; Cj1634c.
DR GeneID; 905907; -.
DR KEGG; cje:Cj1634c; -.
DR PATRIC; fig|192222.6.peg.1610; -.
DR eggNOG; COG0082; Bacteria.
DR HOGENOM; CLU_034547_0_2_7; -.
DR OMA; MLSINAV; -.
DR UniPathway; UPA00053; UER00090.
DR EvolutionaryTrace; Q9PM41; -.
DR Proteomes; UP000000799; 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.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW FAD; Flavoprotein; FMN; Lyase; NADP; Reference proteome.
FT CHAIN 1..362
FT /note="Chorismate synthase"
FT /id="PRO_0000140568"
FT BINDING 46
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00300"
FT BINDING 122..124
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00300"
FT BINDING 238..239
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00300"
FT BINDING 278
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00300"
FT BINDING 293..297
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00300"
FT BINDING 319
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00300"
FT STRAND 6..13
FT /evidence="ECO:0007829|PDB:1SQ1"
FT HELIX 16..18
FT /evidence="ECO:0007829|PDB:1SQ1"
FT STRAND 21..26
FT /evidence="ECO:0007829|PDB:1SQ1"
FT HELIX 36..45
FT /evidence="ECO:0007829|PDB:1SQ1"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:1SQ1"
FT STRAND 66..69
FT /evidence="ECO:0007829|PDB:1SQ1"
FT STRAND 78..82
FT /evidence="ECO:0007829|PDB:1SQ1"
FT HELIX 128..143
FT /evidence="ECO:0007829|PDB:1SQ1"
FT TURN 144..146
FT /evidence="ECO:0007829|PDB:1SQ1"
FT STRAND 148..156
FT /evidence="ECO:0007829|PDB:1SQ1"
FT HELIX 165..167
FT /evidence="ECO:0007829|PDB:1SQ1"
FT HELIX 170..175
FT /evidence="ECO:0007829|PDB:1SQ1"
FT TURN 183..185
FT /evidence="ECO:0007829|PDB:1SQ1"
FT HELIX 186..198
FT /evidence="ECO:0007829|PDB:1SQ1"
FT STRAND 205..213
FT /evidence="ECO:0007829|PDB:1SQ1"
FT TURN 221..223
FT /evidence="ECO:0007829|PDB:1SQ1"
FT HELIX 226..235
FT /evidence="ECO:0007829|PDB:1SQ1"
FT STRAND 240..245
FT /evidence="ECO:0007829|PDB:1SQ1"
FT HELIX 248..253
FT /evidence="ECO:0007829|PDB:1SQ1"
FT HELIX 256..259
FT /evidence="ECO:0007829|PDB:1SQ1"
FT STRAND 264..267
FT /evidence="ECO:0007829|PDB:1SQ1"
FT STRAND 275..277
FT /evidence="ECO:0007829|PDB:1SQ1"
FT STRAND 280..284
FT /evidence="ECO:0007829|PDB:1SQ1"
FT STRAND 286..292
FT /evidence="ECO:0007829|PDB:1SQ1"
FT HELIX 325..346
FT /evidence="ECO:0007829|PDB:1SQ1"
FT HELIX 348..350
FT /evidence="ECO:0007829|PDB:1SQ1"
FT HELIX 352..358
FT /evidence="ECO:0007829|PDB:1SQ1"
SQ SEQUENCE 362 AA; 39252 MW; 7A9EDAE23F59AA75 CRC64;
MNTFGTRLKF TSFGESHGVA VGCIIDGMPA GVKFDEEFLQ NELDKRKGGS KFATPRKESD
KAQVLSGVFE GYTTGHPIAI VVFNENAHSK DYDNLKDLFR PAHADFTYFY KYGIRDHRGG
GRSSARESVA RVAGGAVAAM LLREFDICVQ SGVFGVGTFV SNLKEEEFDF EFAKKSEIFC
LDPKLESDFK NEILNARNSK DSVGAAVFTK VSGMLIGLGE VLYDKLDSKL AHALMGINAV
KAVEIGEGIN ASKMRGSCNN DALKDGKFLS NHSGGILGGI SNGENLILKT YFKPTPSIFA
KQESIDKFGN NLKFELKGRH DPCVGVRGSV VASAMVRLVL ADCLLLNASA NLNNLKNAYG
LK
