(data stored in ACNUC7421 zone)

SWISSPROT: AROC_RUEPO

ID   AROC_RUEPO              Reviewed;         366 AA.
AC   Q5LX60;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   08-MAY-2019, entry version 84.
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=SPO0267;
OS   Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3)
OS   (Silicibacter pomeroyi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Ruegeria.
OX   NCBI_TaxID=246200;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3;
RX   PubMed=15602564; DOI=10.1038/nature03170;
RA   Moran M.A., Buchan A., Gonzalez J.M., Heidelberg J.F., Whitman W.B.,
RA   Kiene R.P., Henriksen J.R., King G.M., Belas R., Fuqua C.,
RA   Brinkac L.M., Lewis M., Johri S., Weaver B., Pai G., Eisen J.A.,
RA   Rahe E., Sheldon W.M., Ye W., Miller T.R., Carlton J., Rasko D.A.,
RA   Paulsen I.T., Ren Q., Daugherty S.C., DeBoy R.T., Dodson R.J.,
RA   Durkin A.S., Madupu R., Nelson W.C., Sullivan S.A., Rosovitz M.J.,
RA   Haft D.H., Selengut J., Ward N.;
RT   "Genome sequence of Silicibacter pomeroyi reveals adaptations to the
RT   marine environment.";
RL   Nature 432:910-913(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3;
RX   PubMed=25780504; DOI=10.1186/1944-3277-9-11;
RA   Rivers A.R., Smith C.B., Moran M.A.;
RT   "An updated genome annotation for the model marine bacterium Ruegeria
RT   pomeroyi DSS-3.";
RL   Stand. Genomic Sci. 9:11-11(2014).
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; CP000031; AAV93587.1; -; Genomic_DNA.
DR   RefSeq; WP_011046029.1; NC_003911.12.
DR   SMR; Q5LX60; -.
DR   STRING; 246200.SPO0267; -.
DR   EnsemblBacteria; AAV93587; AAV93587; SPO0267.
DR   KEGG; sil:SPO0267; -.
DR   eggNOG; ENOG4105D10; Bacteria.
DR   eggNOG; COG0082; LUCA.
DR   HOGENOM; HOG000060335; -.
DR   KO; K01736; -.
DR   OMA; MLSINAV; -.
DR   OrthoDB; 981870at2; -.
DR   BioCyc; RPOM246200:G1G48-272-MONOMER; -.
DR   UniPathway; UPA00053; UER00090.
DR   Proteomes; UP000001023; 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; PS00787; CHORISMATE_SYNTHASE_1; 1.
DR   PROSITE; PS00789; CHORISMATE_SYNTHASE_3; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q5LX60.
DR   SWISS-2DPAGE; Q5LX60.
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW   Complete proteome; FAD; Flavoprotein; FMN; Lyase; NADP;
KW   Reference proteome.
FT   CHAIN         1    366       Chorismate synthase.
FT                                /FTId=PRO_0000140640.
FT   NP_BIND     125    127       FMN. {ECO:0000255|HAMAP-Rule:MF_00300}.
FT   NP_BIND     241    242       FMN. {ECO:0000255|HAMAP-Rule:MF_00300}.
FT   NP_BIND     300    304       FMN. {ECO:0000255|HAMAP-Rule:MF_00300}.
FT   BINDING      48     48       NADP. {ECO:0000255|HAMAP-Rule:MF_00300}.
FT   BINDING     285    285       FMN; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00300}.
FT   BINDING     326    326       FMN. {ECO:0000255|HAMAP-Rule:MF_00300}.
SQ   SEQUENCE   366 AA;  39268 MW;  759206F135A865E1 CRC64;
     MSMNSFGHLF RVTTWGESHG PALGATVDGC PPGVPIEEAM IQHWLDRRKP GQNKYTTQRR
     EADEVKILSG VFEGQTTGTP VQLMIENTDQ RSKDYGDIKD KFRPGHADIT YFQKYGIRDY
     RGGGRSSARE TAARVAAGGL AREAIRALAP NAQITGYMVQ MGPHRIDRAR FDWAQIEQNP
     FWVPDAQAAS DWADYLDGLR KSGSSVGAVI EVVARGVPAG LGAPVYGKLD TDLAAAMMSI
     NAVKGVEIGE GMAAAELTGE ANADEIFMGQ NGPQYSSNHA GGILGGISTG QDIVVRFAVK
     PTSSILTTRK TITKSGEETE IITKGRHDPC VGIRAVPVGE AMMACVILDH LLLHRGQIGA
     NRGHIG
//

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