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Database: UniProt
Entry: Q3AV33_SYNS9
LinkDB: Q3AV33_SYNS9
Original site: Q3AV33_SYNS9 
ID   Q3AV33_SYNS9            Unreviewed;       127 AA.
AC   Q3AV33;
DT   22-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2005, sequence version 1.
DT   11-MAY-2016, entry version 61.
DE   SubName: Full=Chorismate mutase {ECO:0000313|EMBL:ABB26739.1};
DE            EC=5.4.99.5 {ECO:0000313|EMBL:ABB26739.1};
GN   OrderedLocusNames=Syncc9902_1782 {ECO:0000313|EMBL:ABB26739.1};
OS   Synechococcus sp. (strain CC9902).
OC   Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales;
OC   Synechococcus.
OX   NCBI_TaxID=316279 {ECO:0000313|EMBL:ABB26739.1, ECO:0000313|Proteomes:UP000002712};
RN   [1] {ECO:0000313|Proteomes:UP000002712}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CC9902 {ECO:0000313|Proteomes:UP000002712};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Martinez M., Schmutz J., Larimer F.,
RA   Land M., Kyrpides N., Ivanova N., Richardson P.;
RT   "Complete sequence of Synechococcus sp. CC9902.";
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the Claisen rearrangement of chorismate to
CC       prephenate. Probably involved in the aromatic amino acid
CC       biosynthesis. {ECO:0000256|PIRNR:PIRNR005965}.
CC   -!- CATALYTIC ACTIVITY: Chorismate = prephenate.
CC       {ECO:0000256|PIRNR:PIRNR005965}.
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; prephenate
CC       biosynthesis; prephenate from chorismate: step 1/1.
CC       {ECO:0000256|PIRNR:PIRNR005965}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR005965}.
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DR   EMBL; CP000097; ABB26739.1; -; Genomic_DNA.
DR   RefSeq; WP_011360546.1; NC_007513.1.
DR   ProteinModelPortal; Q3AV33; -.
DR   STRING; 316279.Syncc9902_1782; -.
DR   EnsemblBacteria; ABB26739; ABB26739; Syncc9902_1782.
DR   KEGG; sye:Syncc9902_1782; -.
DR   PATRIC; 23801053; VBISynSp76179_1975.
DR   eggNOG; ENOG4105KHN; Bacteria.
DR   eggNOG; COG4401; LUCA.
DR   HOGENOM; HOG000043606; -.
DR   KO; K06208; -.
DR   OMA; RGAVCCE; -.
DR   OrthoDB; EOG6WT8J3; -.
DR   BioCyc; SSP316279:GJCI-1800-MONOMER; -.
DR   UniPathway; UPA00120; UER00203.
DR   Proteomes; UP000002712; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0004106; F:chorismate mutase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0046417; P:chorismate metabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.1330.40; -; 1.
DR   InterPro; IPR008243; Chorismate_mutase_AroH.
DR   InterPro; IPR013813; Endoribo_LPSP/chorism_mut-like.
DR   PANTHER; PTHR21164; PTHR21164; 1.
DR   Pfam; PF07736; CM_1; 1.
DR   PIRSF; PIRSF005965; Chor_mut_AroH; 1.
DR   ProDom; PD031888; Chorismate_mutase_AroH; 1.
DR   SUPFAM; SSF55298; SSF55298; 1.
DR   TIGRFAMs; TIGR01796; CM_mono_aroH; 1.
DR   PROSITE; PS51167; CHORISMATE_MUT_1; 1.
PE   4: Predicted;
KW   Amino-acid biosynthesis {ECO:0000256|PIRNR:PIRNR005965};
KW   Aromatic amino acid biosynthesis {ECO:0000256|PIRNR:PIRNR005965};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002712};
KW   Cytoplasm {ECO:0000256|PIRNR:PIRNR005965};
KW   Isomerase {ECO:0000256|PIRNR:PIRNR005965,
KW   ECO:0000313|EMBL:ABB26739.1}.
FT   BINDING      12     12       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR005965-1}.
FT   BINDING      95     95       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR005965-1}.
FT   BINDING     112    112       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR005965-1}.
FT   BINDING     120    120       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR005965-1}.
SQ   SEQUENCE   127 AA;  14005 MW;  6C02B7C2ECCFAC45 CRC64;
     MSDTTLKLVG LRGATTSAAN TTAAIQSAVR DLIDALVEEN DLSPEQIVSV TFSVTADLDA
     CFPAAIARQR PGWDGVALLD CQQMAVQGDL ERCIRVLAHA WMPPTREPRH PYRSEAQRLR
     PDRSRYN
//
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