(data stored in ACNUC7421 zone)

SWISSPROT: AROC_SINFN

ID   AROC_SINFN              Reviewed;         365 AA.
AC   C3MHI8;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   07-JUN-2017, entry version 46.
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=NGR_c05200;
OS   Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=394;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234;
RX   PubMed=19376903; DOI=10.1128/AEM.00515-09;
RA   Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA   Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA   Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA   Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT   "Rhizobium sp. strain NGR234 possesses a remarkable number of
RT   secretion systems.";
RL   Appl. Environ. Microbiol. 75:4035-4045(2009).
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: 5-O-(1-carboxyvinyl)-3-phosphoshikimate =
CC       chorismate + phosphate. {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; CP001389; ACP24316.1; -; Genomic_DNA.
DR   RefSeq; WP_012707101.1; NC_012587.1.
DR   RefSeq; YP_002825069.1; NC_012587.1.
DR   ProteinModelPortal; C3MHI8; -.
DR   SMR; C3MHI8; -.
DR   STRING; 394.NGR_c05200; -.
DR   EnsemblBacteria; ACP24316; ACP24316; NGR_c05200.
DR   GeneID; 7791746; -.
DR   KEGG; rhi:NGR_c05200; -.
DR   PATRIC; fig|394.7.peg.3333; -.
DR   eggNOG; ENOG4105D10; Bacteria.
DR   eggNOG; COG0082; LUCA.
DR   HOGENOM; HOG000060335; -.
DR   KO; K01736; -.
DR   OMA; MLSINAV; -.
DR   OrthoDB; POG091H00EG; -.
DR   UniPathway; UPA00053; UER00090.
DR   Proteomes; UP000001054; Chromosome.
DR   GO; GO:0004107; F:chorismate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009073; P:aromatic amino acid family 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; 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; C3MHI8.
DR   SWISS-2DPAGE; C3MHI8.
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW   Complete proteome; FAD; Flavoprotein; FMN; Lyase; NADP;
KW   Reference proteome.
FT   CHAIN         1    365       Chorismate synthase.
FT                                /FTId=PRO_1000132783.
FT   NP_BIND     131    133       FMN. {ECO:0000255|HAMAP-Rule:MF_00300}.
FT   NP_BIND     243    244       FMN. {ECO:0000255|HAMAP-Rule:MF_00300}.
FT   NP_BIND     303    307       FMN. {ECO:0000255|HAMAP-Rule:MF_00300}.
FT   BINDING      48     48       NADP. {ECO:0000255|HAMAP-Rule:MF_00300}.
FT   BINDING      54     54       NADP. {ECO:0000255|HAMAP-Rule:MF_00300}.
FT   BINDING     288    288       FMN; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00300}.
FT   BINDING     329    329       FMN. {ECO:0000255|HAMAP-Rule:MF_00300}.
SQ   SEQUENCE   365 AA;  39339 MW;  7032475DD4B0A6AF CRC64;
     MSHNSFGHLF RVTTWGESHG PALGCVVDGC PPGIRFTLAE IQAWLDKRKP GQSRFVTQRR
     EDDLVKVLSG VMLDDDGETM ISTGTPISMM IENTDQRSKD YSEIAKRYRP GHADYTYDVK
     YGIRDYRGGG RSSARETAAR VAAGGIARKV VPGLVVRAAL VQIGKHRINR ANWDWSEVNN
     NPFFAPDPAI VPVWEEYLDG IRKAGSSIGA VVEVIAEGVP AGIGAPIYGK LDQDIASNLM
     SINAVKGVEI GDGFATAELS GEENADEMRI GSDGKPVFLA NHAGGILGGI ATGQPVVARF
     AIKPTSSILT ERRSIDSDGN EVDVRTKGRH DPCVGIRAVP IGEAMLACTI ADHYLRDRGQ
     TGRLK
//

If you have problems or comments...

PBIL Back to PBIL home page