AROC_ECOLI
ID AROC_ECOLI Reviewed; 361 AA.
AC P12008; P78193;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Chorismate synthase {ECO:0000255|HAMAP-Rule:MF_00300, ECO:0000303|PubMed:2969724};
DE Short=CS {ECO:0000255|HAMAP-Rule:MF_00300};
DE EC=4.2.3.5 {ECO:0000255|HAMAP-Rule:MF_00300, ECO:0000269|PubMed:10956653, ECO:0000269|PubMed:11034781, ECO:0000269|PubMed:7848266, ECO:0000269|PubMed:7978236, ECO:0000269|PubMed:8703965};
DE AltName: Full=5-enolpyruvylshikimate-3-phosphate phospholyase {ECO:0000255|HAMAP-Rule:MF_00300, ECO:0000303|PubMed:2969724};
DE Short=EPSP phospholyase {ECO:0000303|PubMed:7848266};
GN Name=aroC {ECO:0000255|HAMAP-Rule:MF_00300, ECO:0000303|PubMed:2969724};
GN OrderedLocusNames=b2329, JW2326;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2182772; DOI=10.1099/00221287-136-2-353;
RA Charles I.G., Lamb H.K., Pickard D., Dougan G., Hawkins A.R.;
RT "Isolation, characterization and nucleotide sequences of the aroC genes
RT encoding chorismate synthase from Salmonella typhi and Escherichia coli.";
RL J. Gen. Microbiol. 136:353-358(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-30, FUNCTION,
RP COFACTOR, AND SUBUNIT.
RC STRAIN=K12;
RX PubMed=2969724; DOI=10.1042/bj2510313;
RA White P.J., Millar G., Coggins J.R.;
RT "The overexpression, purification and complete amino acid sequence of
RT chorismate synthase from Escherichia coli K12 and its comparison with the
RT enzyme from Neurospora crassa.";
RL Biochem. J. 251:313-322(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=7978236; DOI=10.1006/abio.1994.1309;
RA Ramjee M.K., Coggins J.R., Thorneley R.N.;
RT "A continuous, anaerobic spectrophotometric assay for chorismate synthase
RT activity that utilizes photoreduced flavin mononucleotide.";
RL Anal. Biochem. 220:137-141(1994).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY
RP REGULATION.
RX PubMed=7848266; DOI=10.1042/bj3050707;
RA Bornemann S., Balasubramanian S., Coggins J.R., Abell C., Lowe D.J.,
RA Thorneley R.N.;
RT "Escherichia coli chorismate synthase: a deuterium kinetic-isotope effect
RT under single-turnover and steady-state conditions shows that a flavin
RT intermediate forms before the C-(6proR)-H bond is cleaved.";
RL Biochem. J. 305:707-710(1995).
RN [8]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=8703965; DOI=10.1021/bi952958q;
RA Bornemann S., Lowe D.J., Thorneley R.N.;
RT "The transient kinetics of Escherichia coli chorismate synthase: substrate
RT consumption, product formation, phosphate dissociation, and
RT characterization of a flavin intermediate.";
RL Biochemistry 35:9907-9916(1996).
RN [9]
RP COFACTOR.
RX PubMed=8824216; DOI=10.1074/jbc.271.42.25850;
RA Macheroux P., Bornemann S., Ghisla S., Thorneley R.N.;
RT "Studies with flavin analogs provide evidence that a protonated reduced FMN
RT is the substrate-induced transient intermediate in the reaction of
RT Escherichia coli chorismate synthase.";
RL J. Biol. Chem. 271:25850-25858(1996).
RN [10]
RP COFACTOR, AND SUBUNIT.
RX PubMed=9761730; DOI=10.1042/bj3350319;
RA Macheroux P., Schoenbrunn E., Svergun D.I., Volkov V.V., Koch M.H.,
RA Bornemann S., Thorneley R.N.;
RT "Evidence for a major structural change in Escherichia coli chorismate
RT synthase induced by flavin and substrate binding.";
RL Biochem. J. 335:319-327(1998).
RN [11]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND REACTION MECHANISM.
RX PubMed=11034781; DOI=10.1006/bioo.2000.1174;
RA Bornemann S., Theoclitou M.E., Brune M., Webb M.R., Thorneley R.N.,
RA Abell C.;
RT "A secondary beta deuterium kinetic isotope effect in the chorismate
RT synthase reaction.";
RL Bioorg. Chem. 28:191-204(2000).
RN [12]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, AND REACTION
RP MECHANISM.
RX PubMed=10956653; DOI=10.1074/jbc.m005796200;
RA Osborne A., Thorneley R.N., Abell C., Bornemann S.;
RT "Studies with substrate and cofactor analogues provide evidence for a
RT radical mechanism in the chorismate synthase reaction.";
RL J. Biol. Chem. 275:35825-35830(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. It uses NADPH to reduce FMN.
CC {ECO:0000255|HAMAP-Rule:MF_00300, ECO:0000269|PubMed:10956653,
CC ECO:0000269|PubMed:11034781, ECO:0000269|PubMed:2969724,
CC ECO:0000269|PubMed:7848266, ECO:0000269|PubMed:7978236,
CC ECO:0000269|PubMed:8703965}.
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:10956653, ECO:0000269|PubMed:11034781,
CC ECO:0000269|PubMed:7848266, ECO:0000269|PubMed:7978236,
CC ECO:0000269|PubMed:8703965};
CC -!- COFACTOR:
CC Name=FMNH2; Xref=ChEBI:CHEBI:57618;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00300,
CC ECO:0000269|PubMed:10956653, ECO:0000269|PubMed:11034781,
CC ECO:0000269|PubMed:2969724, ECO:0000269|PubMed:7978236,
CC ECO:0000269|PubMed:8824216, ECO:0000269|PubMed:9761730};
CC Note=Reduced FMN (FMNH(2)). It can also use FAD, however FMN is the
CC preferred cofactor. {ECO:0000255|HAMAP-Rule:MF_00300,
CC ECO:0000269|PubMed:10956653, ECO:0000269|PubMed:11034781,
CC ECO:0000269|PubMed:2969724, ECO:0000269|PubMed:7978236,
CC ECO:0000269|PubMed:8824216, ECO:0000269|PubMed:9761730};
CC -!- ACTIVITY REGULATION: Competitively inhibited by 6R-6-fluoro-EPSP.
CC {ECO:0000269|PubMed:10956653, ECO:0000269|PubMed:7848266}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.3 uM for EPSP {ECO:0000269|PubMed:7978236};
CC Vmax=25 umol/min/mg enzyme {ECO:0000269|PubMed:7978236};
CC Note=kcat is 16.5 sec(-1) for phospholyase activity with EPSP as
CC substrate. kcat is 27 sec(-1) for phospholyase activity with EPSP as
CC substrate. {ECO:0000269|PubMed:7848266, ECO:0000269|PubMed:7978236};
CC pH dependence:
CC Optimum pH is between 7.5 and 8. {ECO:0000269|PubMed:7978236};
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:2969724, ECO:0000269|PubMed:9761730}.
CC -!- SIMILARITY: Belongs to the chorismate synthase family.
CC {ECO:0000255|HAMAP-Rule:MF_00300, ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA23488.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; M27714; AAA23487.1; -; Genomic_DNA.
DR EMBL; Y00720; CAA68707.1; ALT_FRAME; Genomic_DNA.
DR EMBL; M33021; AAA23488.1; ALT_FRAME; Genomic_DNA.
DR EMBL; U00096; AAC75389.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16185.1; -; Genomic_DNA.
DR PIR; G65005; SYECKR.
DR RefSeq; NP_416832.1; NC_000913.3.
DR RefSeq; WP_001333535.1; NZ_LN832404.1.
DR AlphaFoldDB; P12008; -.
DR SMR; P12008; -.
DR BioGRID; 4263044; 43.
DR IntAct; P12008; 5.
DR STRING; 511145.b2329; -.
DR jPOST; P12008; -.
DR PaxDb; P12008; -.
DR PRIDE; P12008; -.
DR EnsemblBacteria; AAC75389; AAC75389; b2329.
DR EnsemblBacteria; BAA16185; BAA16185; BAA16185.
DR GeneID; 946814; -.
DR KEGG; ecj:JW2326; -.
DR KEGG; eco:b2329; -.
DR PATRIC; fig|511145.12.peg.2425; -.
DR EchoBASE; EB0073; -.
DR eggNOG; COG0082; Bacteria.
DR InParanoid; P12008; -.
DR OMA; MLSINAV; -.
DR PhylomeDB; P12008; -.
DR BioCyc; EcoCyc:AROC-MON; -.
DR BioCyc; MetaCyc:AROC-MON; -.
DR UniPathway; UPA00053; UER00090.
DR PRO; PR:P12008; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0004107; F:chorismate synthase activity; IDA:EcoCyc.
DR GO; GO:0010181; F:FMN binding; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IBA:GO_Central.
DR GO; GO:0008652; P:cellular amino acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009423; P:chorismate biosynthetic process; IDA:EcoCyc.
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;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2969724"
FT CHAIN 2..361
FT /note="Chorismate synthase"
FT /id="PRO_0000140584"
FT BINDING 48
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00300"
FT BINDING 54
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00300"
FT BINDING 125..127
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"
SQ SEQUENCE 361 AA; 39137 MW; 47C85F91B87DF093 CRC64;
MAGNTIGQLF RVTTFGESHG LALGCIVDGV PPGIPLTEAD LQHDLDRRRP GTSRYTTQRR
EPDQVKILSG VFEGVTTGTS IGLLIENTDQ RSQDYSAIKD VFRPGHADYT YEQKYGLRDY
RGGGRSSARE TAMRVAAGAI AKKYLAEKFG IEIRGCLTQM GDIPLDIKDW SQVEQNPFFC
PDPDKIDALD ELMRALKKEG DSIGAKVTVV ASGVPAGLGE PVFDRLDADI AHALMSINAV
KGVEIGDGFD VVALRGSQNR DEITKDGFQS NHAGGILGGI SSGQQIIAHM ALKPTSSITV
PGRTINRFGE EVEMITKGRH DPCVGIRAVP IAEAMLAIVL MDHLLRQRAQ NADVKTDIPR
W
