ID B1W219_STRGG Unreviewed; 120 AA. AC B1W219; DT 20-MAY-2008, integrated into UniProtKB/TrEMBL. DT 20-MAY-2008, sequence version 1. DT 27-MAR-2024, entry version 71. DE RecName: Full=chorismate mutase {ECO:0000256|PROSITE-ProRule:PRU00514}; DE EC=5.4.99.5 {ECO:0000256|PROSITE-ProRule:PRU00514}; GN OrderedLocusNames=SGR_5737 {ECO:0000313|EMBL:BAG22566.1}; OS Streptomyces griseus subsp. griseus (strain JCM 4626 / NBRC 13350). OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales; OC Streptomycetaceae; Streptomyces. OX NCBI_TaxID=455632 {ECO:0000313|EMBL:BAG22566.1, ECO:0000313|Proteomes:UP000001685}; RN [1] {ECO:0000313|EMBL:BAG22566.1, ECO:0000313|Proteomes:UP000001685} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCM 4626 / NBRC 13350 {ECO:0000313|Proteomes:UP000001685}; RX PubMed=18375553; DOI=10.1128/JB.00204-08; RA Ohnishi Y., Ishikawa J., Hara H., Suzuki H., Ikenoya M., Ikeda H., RA Yamashita A., Hattori M., Horinouchi S.; RT "Genome sequence of the streptomycin-producing microorganism Streptomyces RT griseus IFO 13350."; RL J. Bacteriol. 190:4050-4060(2008). CC -!- CATALYTIC ACTIVITY: CC Reaction=chorismate = prephenate; Xref=Rhea:RHEA:13897, CC ChEBI:CHEBI:29748, ChEBI:CHEBI:29934; EC=5.4.99.5; CC Evidence={ECO:0000256|PROSITE-ProRule:PRU00514}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AP009493; BAG22566.1; -; Genomic_DNA. DR RefSeq; WP_003970042.1; NC_010572.1. DR AlphaFoldDB; B1W219; -. DR GeneID; 6210318; -. DR KEGG; sgr:SGR_5737; -. DR PATRIC; fig|455632.4.peg.5876; -. DR eggNOG; COG4401; Bacteria. DR HOGENOM; CLU_133236_1_0_11; -. DR Proteomes; UP000001685; Chromosome. DR GO; GO:0004106; F:chorismate mutase activity; IEA:UniProtKB-EC. DR GO; GO:0008652; P:amino acid biosynthetic process; IEA:UniProtKB-UniRule. DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-UniRule. DR CDD; cd02185; AroH; 1. DR Gene3D; 3.30.1330.40; RutC-like; 1. DR InterPro; IPR008243; Chorismate_mutase_AroH. DR InterPro; IPR035959; RutC-like_sf. DR NCBIfam; TIGR01796; CM_mono_aroH; 1. DR PANTHER; PTHR21164; CHORISMATE MUTASE; 1. DR PANTHER; PTHR21164:SF0; CHORISMATE MUTASE AROH; 1. DR Pfam; PF07736; CM_1; 1. DR PIRSF; PIRSF005965; Chor_mut_AroH; 1. DR SUPFAM; SSF55298; YjgF-like; 1. DR PROSITE; PS51167; CHORISMATE_MUT_1; 1. PE 4: Predicted; KW Amino-acid biosynthesis {ECO:0000256|PIRSR:PIRSR005965-1, KW ECO:0000256|PROSITE-ProRule:PRU00514}; KW Aromatic amino acid biosynthesis {ECO:0000256|PIRSR:PIRSR005965-1, KW ECO:0000256|PROSITE-ProRule:PRU00514}; KW Isomerase {ECO:0000256|PROSITE-ProRule:PRU00514}. FT BINDING 7 FT /ligand="prephenate" FT /ligand_id="ChEBI:CHEBI:29934" FT /evidence="ECO:0000256|PIRSR:PIRSR005965-1" FT BINDING 89 FT /ligand="prephenate" FT /ligand_id="ChEBI:CHEBI:29934" FT /evidence="ECO:0000256|PIRSR:PIRSR005965-1" FT BINDING 107 FT /ligand="prephenate" FT /ligand_id="ChEBI:CHEBI:29934" FT /evidence="ECO:0000256|PIRSR:PIRSR005965-1" SQ SEQUENCE 120 AA; 13026 MW; 2C6C31101BCE1232 CRC64; MAVRAVRGAV QLDRDEAGHM ARRVGELLTA VLDRNELVAD DLISIWFTAT PDLHSDFPAA AARGLGIVDV PLICAQELDV EGAMPRVVRI LVHVETYLSR AEISHVYLGA TAALRKDIAQ //