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Database: UniProt
Entry: A5I2T1_CLOBH
LinkDB: A5I2T1_CLOBH
Original site: A5I2T1_CLOBH 
ID   A5I2T1_CLOBH            Unreviewed;       123 AA.
AC   A5I2T1; A7G491;
DT   26-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2007, sequence version 1.
DT   07-SEP-2016, entry version 68.
DE   RecName: Full=Chorismate mutase AroH {ECO:0000256|PIRNR:PIRNR005965};
DE            EC=5.4.99.5 {ECO:0000256|PIRNR:PIRNR005965};
GN   Name=aroH {ECO:0000313|EMBL:CAL83348.1};
GN   OrderedLocusNames=CBO1809 {ECO:0000313|EMBL:CAL83348.1};
OS   Clostridium botulinum (strain Hall / ATCC 3502 / NCTC 13319 / Type A).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=441771 {ECO:0000313|Proteomes:UP000001986};
RN   [1] {ECO:0000313|EMBL:CAL83348.1, ECO:0000313|Proteomes:UP000001986}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hall / ATCC 3502 / NCTC 13319 / Type A [Sanger]
RC   {ECO:0000313|Proteomes:UP000001986};
RX   PubMed=17519437; DOI=10.1101/gr.6282807;
RA   Sebaihia M., Peck M.W., Minton N.P., Thomson N.R., Holden M.T.G.,
RA   Mitchell W.J., Carter A.T., Bentley S.D., Mason D.R., Crossman L.,
RA   Paul C.J., Ivens A., Wells-Bennik M.H.J., Davis I.J.,
RA   Cerdeno-Tarraga A.M., Churcher C., Quail M.A., Chillingworth T.,
RA   Feltwell T., Fraser A., Goodhead I., Hance Z., Jagels K., Larke N.,
RA   Maddison M., Moule S., Mungall K., Norbertczak H., Rabbinowitsch E.,
RA   Sanders M., Simmonds M., White B., Whithead S., Parkhill J.;
RT   "Genome sequence of a proteolytic (Group I) Clostridium botulinum
RT   strain Hall A and comparative analysis of the clostridial genomes.";
RL   Genome Res. 17:1082-1092(2007).
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; AM412317; CAL83348.1; -; Genomic_DNA.
DR   RefSeq; WP_011986385.1; NC_009698.1.
DR   RefSeq; YP_001254309.1; NC_009495.1.
DR   RefSeq; YP_001387606.1; NC_009698.1.
DR   ProteinModelPortal; A5I2T1; -.
DR   GeneID; 5186064; -.
DR   GeneID; 5401300; -.
DR   KEGG; cbh:CLC_1751; -.
DR   KEGG; cbo:CBO1809; -.
DR   PATRIC; 19365675; VBICloBot22612_1780.
DR   HOGENOM; HOG000043606; -.
DR   KO; K06208; -.
DR   OMA; AFLDCQQ; -.
DR   BioCyc; CBOT413999:GJ72-1869-MONOMER; -.
DR   BioCyc; CBOT441771:GIWX-1719-MONOMER; -.
DR   UniPathway; UPA00120; UER00203.
DR   Proteomes; UP000001986; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004106; F:chorismate mutase activity; IBA:GO_Central.
DR   GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0046417; P:chorismate metabolic process; IBA:GO_Central.
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:UP000001986};
KW   Cytoplasm {ECO:0000256|PIRNR:PIRNR005965};
KW   Isomerase {ECO:0000256|PIRNR:PIRNR005965,
KW   ECO:0000313|EMBL:CAL83348.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001986}.
FT   BINDING       5      5       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR005965-1}.
FT   BINDING      88     88       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR005965-1}.
FT   BINDING     108    108       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR005965-1}.
FT   BINDING     116    116       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR005965-1}.
SQ   SEQUENCE   123 AA;  14336 MW;  E7C20EDE8DAF3EA3 CRC64;
     MQSIRGAITI EKNEVKYIKE ASIKLFSEIL SRNNLNIEDI VSIFISCTND IDKGYPGKYI
     RENFNLKNIA IMHFNEMYVE GSMPLCIRIL ILIDKKNKNI EENIEYVYLG RAKTLRKDLF
     SPN
//
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