(data stored in SCRATCH9089 zone)

SWISSPROT: AROC_PASMU

ID   AROC_PASMU              Reviewed;         357 AA.
AC   P57840;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   27-APR-2001, sequence version 1.
DT   11-DEC-2019, entry version 107.
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}; OrderedLocusNames=PM0359;
OS   Pasteurella multocida (strain Pm70).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Pasteurella.
OX   NCBI_TaxID=272843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pm70;
RX   PubMed=11248100; DOI=10.1073/pnas.051634598;
RA   May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT   "Complete genomic sequence of Pasteurella multocida Pm70.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
CC   -!- FUNCTION: Catalyzes the anti-1,4-elimination of the C-3 phosphate and
CC       the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to
CC       yield chorismate, which is the branch point compound that serves as the
CC       starting substrate for the three terminal pathways of aromatic amino
CC       acid biosynthesis. This reaction introduces a second double bond into
CC       the aromatic ring system. {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 biosynthesis;
CC       chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC       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; AE004439; AAK02443.1; -; Genomic_DNA.
DR   RefSeq; WP_005721535.1; NC_002663.1.
DR   SMR; P57840; -.
DR   PRIDE; P57840; -.
DR   EnsemblBacteria; AAK02443; AAK02443; PM0359.
DR   KEGG; pmu:PM0359; -.
DR   PATRIC; fig|272843.6.peg.372; -.
DR   eggNOG; ENOG4105D10; Bacteria.
DR   eggNOG; COG0082; LUCA.
DR   HOGENOM; HOG000060335; -.
DR   KO; K01736; -.
DR   OMA; MLSINAV; -.
DR   BioCyc; PMUL272843:G1FZ8-378-MONOMER; -.
DR   UniPathway; UPA00053; UER00090.
DR   Proteomes; UP000000809; 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; PS00788; CHORISMATE_SYNTHASE_2; 1.
DR   PROSITE; PS00789; CHORISMATE_SYNTHASE_3; 1.
PE   3: Inferred from homology;
DR   PRODOM; P57840.
DR   SWISS-2DPAGE; P57840.
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis; FAD;
KW   Flavoprotein; FMN; Lyase; NADP; Reference proteome.
FT   CHAIN           1..357
FT                   /note="Chorismate synthase"
FT                   /id="PRO_0000140623"
FT   NP_BIND         125..127
FT                   /note="FMN"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00300"
FT   NP_BIND         243..244
FT                   /note="FMN"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00300"
FT   NP_BIND         298..302
FT                   /note="FMN"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00300"
FT   BINDING         48
FT                   /note="NADP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00300"
FT   BINDING         54
FT                   /note="NADP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00300"
FT   BINDING         283
FT                   /note="FMN; via amide nitrogen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00300"
FT   BINDING         324
FT                   /note="FMN"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00300"
SQ   SEQUENCE   357 AA;  38425 MW;  8C7BB60C1061C0F7 CRC64;
     MAGNTIGQLF QVTTFGESHG IALGCIVDGV PPGLSLSEAD IQPDLDRRKP GTSRYTTPRR
     EDDEVQILSG VFEGKTTGTS IGMIIKNADQ RSQDYGDIKD RFRPGHADFT YQQKYGIRDY
     RGGGRSSARE TAMRVAAGAI AKKYLREHFG VEVRGFLAQI GDVAIAPQVI EQIDWQQVNS
     NPFFCPDPSA VEKFDELIRQ LKKEGDSIGA KLTVVAENVP VGLGEPVFDR LDADLAHALM
     GINAVKAVEI GDGFAVVNQR GSAHRDEMTP EGFLSNHAGG ILGGISSGQP IVATIALKPT
     SSITIPGRSV NLANEPVEVI TKGRHDPCVG IRAVPIAEAM VAIVLLDHLL RHKAQNR
//

If you have problems or comments...

PBIL Back to PBIL home page