(data stored in ACNUC7421 zone)

SWISSPROT: AROC_ANADE

ID   AROC_ANADE              Reviewed;         381 AA.
AC   Q2IMD4;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   08-MAY-2019, entry version 80.
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};
GN   OrderedLocusNames=Adeh_0186;
OS   Anaeromyxobacter dehalogenans (strain 2CP-C).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
OX   NCBI_TaxID=290397;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2CP-C;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C.,
RA   Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S.,
RA   Kirby J.R., Zhulin I.B., Loeffler F.E., Richardson P.;
RT   "Complete sequence of Anaeromyxobacter dehalogenans 2CP-C.";
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the anti-1,4-elimination of the C-3 phosphate
CC       and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate
CC       (EPSP) to yield chorismate, which is the branch point compound
CC       that serves as the starting substrate for the three terminal
CC       pathways of aromatic amino acid biosynthesis. This reaction
CC       introduces a second double bond into the aromatic ring system.
CC       {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
CC       biosynthesis; chorismate from D-erythrose 4-phosphate and
CC       phosphoenolpyruvate: step 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}.
DR   EMBL; CP000251; ABC79963.1; -; Genomic_DNA.
DR   RefSeq; WP_011419246.1; NC_007760.1.
DR   SMR; Q2IMD4; -.
DR   STRING; 290397.Adeh_0186; -.
DR   PRIDE; Q2IMD4; -.
DR   EnsemblBacteria; ABC79963; ABC79963; Adeh_0186.
DR   KEGG; ade:Adeh_0186; -.
DR   eggNOG; ENOG4105D10; Bacteria.
DR   eggNOG; COG0082; LUCA.
DR   HOGENOM; HOG000060334; -.
DR   KO; K01736; -.
DR   OMA; MLSINAV; -.
DR   BioCyc; ADEH290397:G1G5W-192-MONOMER; -.
DR   UniPathway; UPA00053; UER00090.
DR   Proteomes; UP000001935; 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: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; PS00788; CHORISMATE_SYNTHASE_2; 1.
DR   PROSITE; PS00789; CHORISMATE_SYNTHASE_3; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q2IMD4.
DR   SWISS-2DPAGE; Q2IMD4.
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW   Complete proteome; FAD; Flavoprotein; FMN; Lyase; NADP;
KW   Reference proteome.
FT   CHAIN         1    381       Chorismate synthase.
FT                                /FTId=PRO_1000071965.
FT   NP_BIND     127    129       FMN. {ECO:0000255|HAMAP-Rule:MF_00300}.
FT   NP_BIND     247    248       FMN. {ECO:0000255|HAMAP-Rule:MF_00300}.
FT   NP_BIND     306    310       FMN. {ECO:0000255|HAMAP-Rule:MF_00300}.
FT   BINDING      41     41       NADP. {ECO:0000255|HAMAP-Rule:MF_00300}.
FT   BINDING      47     47       NADP. {ECO:0000255|HAMAP-Rule:MF_00300}.
FT   BINDING     291    291       FMN; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00300}.
FT   BINDING     332    332       FMN. {ECO:0000255|HAMAP-Rule:MF_00300}.
SQ   SEQUENCE   381 AA;  40537 MW;  7D7718C9F77BC9A2 CRC64;
     MTLRYLTAGE SHGPALVAIA EGFPAGLPVD FEAVDRDLRR RQKGYGRGGR MKIETDAAQF
     LAGLRGGVTT GAPIALAVWN KDHENWKDLV SPYARGGRKF TQVRPGHADL AGALKYGLDD
     ARDVLERASA RSTAVIVALG ALAKALLSSQ GVEVCSRVVA IGPRDIRPDA PPTPAQRDAI
     EASDLHVDDE ALAAEWRALI DAEKARGGSI GGAFDVYATG LPIGLGSHVH PDRRLDARLA
     GALCGVQAIR AVEIGDGTQV GRPGYEFHDA IHHDPARGFW RETNRAGGLE GGMTDGMPLR
     VRAYMKPIPT MLHPLATVDL ATRAATQARY ERSDVCAVPA AAVVGEAVVA WELANALLEK
     FGGDTVEDVR RAVEAYAARI R
//

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