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Database: UniProt/TrEMBL
Entry: D0FQT4_ERWPE
LinkDB: D0FQT4_ERWPE
Original site: D0FQT4_ERWPE 
ID   D0FQT4_ERWPE            Unreviewed;       361 AA.
AC   D0FQT4;
DT   24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   24-NOV-2009, sequence version 1.
DT   01-APR-2015, entry version 38.
DE   RecName: Full=Chorismate synthase {ECO:0000256|HAMAP-Rule:MF_00300, ECO:0000256|RuleBase:RU000605};
DE            Short=CS {ECO:0000256|HAMAP-Rule:MF_00300};
DE            EC=4.2.3.5 {ECO:0000256|HAMAP-Rule:MF_00300, ECO:0000256|RuleBase:RU000605};
DE   AltName: Full=5-enolpyruvylshikimate-3-phosphate phospholyase {ECO:0000256|HAMAP-Rule:MF_00300};
GN   Name=aroC {ECO:0000256|HAMAP-Rule:MF_00300,
GN   ECO:0000313|EMBL:CAX54984.1};
GN   OrderedLocusNames=EpC_12050 {ECO:0000313|EMBL:CAX54984.1};
OS   Erwinia pyrifoliae (strain Ep1/96).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Erwinia.
OX   NCBI_TaxID=634499 {ECO:0000313|Proteomes:UP000007061};
RN   [1] {ECO:0000313|EMBL:CAX54984.1, ECO:0000313|Proteomes:UP000007061}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ep1/96 {ECO:0000313|EMBL:CAX54984.1,
RC   ECO:0000313|Proteomes:UP000007061};
RX   PubMed=20565991; DOI=10.1186/1471-2164-11-393;
RA   Kube M., Migdoll A.M., Gehring I., Heitmann K., Mayer Y., Kuhl H.,
RA   Knaust F., Geider K., Reinhardt R.;
RT   "Genome comparison of the epiphytic bacteria Erwinia billingiae and E.
RT   tasmaniensis with the pear pathogen E. pyrifoliae.";
RL   BMC Genomics 11:393-393(2010).
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:0000256|HAMAP-Rule:MF_00300}.
CC   -!- CATALYTIC ACTIVITY: 5-O-(1-carboxyvinyl)-3-phosphoshikimate =
CC       chorismate + phosphate. {ECO:0000256|HAMAP-Rule:MF_00300,
CC       ECO:0000256|RuleBase:RU000605}.
CC   -!- COFACTOR:
CC       Name=FMNH2; Xref=ChEBI:CHEBI:57618;
CC         Evidence={ECO:0000256|RuleBase:RU000605};
CC       Note=Reduced FMN (FMNH(2)). {ECO:0000256|RuleBase:RU000605};
CC   -!- COFACTOR:
CC       Name=FMNH2; Xref=ChEBI:CHEBI:57618; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00300};
CC       Note=Reduced FMN (FMNH(2)). {ECO:0000256|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:0000256|HAMAP-Rule:MF_00300,
CC       ECO:0000256|RuleBase:RU000605}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00300}.
CC   -!- SIMILARITY: Belongs to the chorismate synthase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00300, ECO:0000256|RuleBase:RU000605}.
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DR   EMBL; FP236842; CAX54984.1; -; Genomic_DNA.
DR   RefSeq; YP_002648230.1; NC_012214.1.
DR   ProteinModelPortal; D0FQT4; -.
DR   STRING; 634499.EpC_12050; -.
DR   EnsemblBacteria; CAX54984; CAX54984; EpC_12050.
DR   KEGG; epy:EpC_12050; -.
DR   PATRIC; 20420626; VBIErwPyr67807_1215.
DR   HOGENOM; HOG000060335; -.
DR   KO; K01736; -.
DR   OMA; NNPFFCP; -.
DR   OrthoDB; EOG6WDSHT; -.
DR   BioCyc; EPYR634499:GJIP-1257-MONOMER; -.
DR   UniPathway; UPA00053; UER00090.
DR   Proteomes; UP000007061; Chromosome.
DR   GO; GO:0004107; F:chorismate synthase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-HAMAP.
DR   GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway.
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; PS00788; CHORISMATE_SYNTHASE_2; 1.
DR   PROSITE; PS00789; CHORISMATE_SYNTHASE_3; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00300,
KW   ECO:0000256|RuleBase:RU000605};
KW   Aromatic amino acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00300,
KW   ECO:0000256|RuleBase:RU000605};
KW   Complete proteome {ECO:0000313|Proteomes:UP000007061};
KW   FAD {ECO:0000256|HAMAP-Rule:MF_00300};
KW   Flavoprotein {ECO:0000256|HAMAP-Rule:MF_00300};
KW   FMN {ECO:0000256|HAMAP-Rule:MF_00300};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00300,
KW   ECO:0000256|RuleBase:RU000605};
KW   NADP {ECO:0000256|HAMAP-Rule:MF_00300}.
FT   NP_BIND     125    127       FMN. {ECO:0000256|HAMAP-Rule:MF_00300}.
FT   NP_BIND     238    239       FMN. {ECO:0000256|HAMAP-Rule:MF_00300}.
FT   NP_BIND     293    297       FMN. {ECO:0000256|HAMAP-Rule:MF_00300}.
FT   BINDING      48     48       NADP. {ECO:0000256|HAMAP-Rule:MF_00300}.
FT   BINDING      54     54       NADP. {ECO:0000256|HAMAP-Rule:MF_00300}.
FT   BINDING     278    278       FMN; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00300}.
FT   BINDING     319    319       FMN. {ECO:0000256|HAMAP-Rule:MF_00300}.
SQ   SEQUENCE   361 AA;  39138 MW;  986FE9B58F637944 CRC64;
     MAGNTIGQLF RVTTFGESHG IALGCIVDGV PPGIPLTEDD LQHDLDRRRP GTSRYTTPRR
     EPDRVKILSG VFEGRTTGTS IGLLIENTDQ RSQDYGAIKE LYRPGHADFT YDGKYGFRDY
     RGGGRSSARE TAMRVAAGAI AKKYLAMKHD IKVRGYLAQM GDVVCELKDW QQVEQNPFFS
     PDVDKLDALD ELMRALKKEG DSIGAKVAVM AENVPVGLGE PVFDRLDADL AHALMSINAV
     KGVEIGDGFA VVNQRGSEHR DEIRANGFQS NHAGGILGGI SSGQTITANL AMKPTSSITV
     PGKTINRSGE EVEMITKGRH DPCVGIRAVP IAEAMMAIVL MDHLLRHRGQ NADVNADMPR
     G
//
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