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Database: UniProt/TrEMBL
Entry: F8FAU9_PAEMK
LinkDB: F8FAU9_PAEMK
Original site: F8FAU9_PAEMK 
ID   F8FAU9_PAEMK            Unreviewed;       122 AA.
AC   F8FAU9;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   08-JUN-2016, entry version 27.
DE   RecName: Full=Chorismate mutase AroH {ECO:0000256|PIRNR:PIRNR005965};
DE            EC=5.4.99.5 {ECO:0000256|PIRNR:PIRNR005965};
GN   OrderedLocusNames=KNP414_02790 {ECO:0000313|EMBL:AEI41350.1};
OS   Paenibacillus mucilaginosus (strain KNP414).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae;
OC   Paenibacillus.
OX   NCBI_TaxID=1036673 {ECO:0000313|EMBL:AEI41350.1, ECO:0000313|Proteomes:UP000006620};
RN   [1] {ECO:0000313|Proteomes:UP000006620}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KNP414 {ECO:0000313|Proteomes:UP000006620};
RA   Wang J., Hu S., Hu X., Zhang B., Dong D., Zhang S., Zhao K., Wu D.;
RT   "Complete genome sequence of Paenibacillus mucilaginosus KNP414.";
RL   Submitted (JUN-2011) 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; CP002869; AEI41350.1; -; Genomic_DNA.
DR   RefSeq; WP_013916511.1; NC_015690.1.
DR   ProteinModelPortal; F8FAU9; -.
DR   STRING; 1036673.KNP414_02790; -.
DR   EnsemblBacteria; AEI41350; AEI41350; KNP414_02790.
DR   KEGG; pms:KNP414_02790; -.
DR   eggNOG; ENOG4105KHN; Bacteria.
DR   eggNOG; COG4401; LUCA.
DR   KO; K06208; -.
DR   OMA; CIRVMMT; -.
DR   BioCyc; PMUC1036673:GJD1-2790-MONOMER; -.
DR   Proteomes; UP000006620; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004106; F:chorismate mutase activity; IEA:UniProtKB-UniRule.
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:UP000006620};
KW   Cytoplasm {ECO:0000256|PIRNR:PIRNR005965};
KW   Isomerase {ECO:0000256|PIRNR:PIRNR005965}.
FT   BINDING       7      7       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR005965-1}.
FT   BINDING      90     90       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   122 AA;  13827 MW;  EA67AA388485689B CRC64;
     MGVRGIRGAI TVEHNEENEI LSATTELLHR IVLENGIVPE EIASVFITVT PDLTATFPAK
     TIRQMKDWEL VPLMCSLEIP VEGALPKCIR FMVMVNTEKK QDEIVHVYLR EAMRLRPDLT
     KS
//
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