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Database: UniProt
Entry: A0A4R6U4Z0_9BACI
LinkDB: A0A4R6U4Z0_9BACI
Original site: A0A4R6U4Z0_9BACI 
ID   A0A4R6U4Z0_9BACI        Unreviewed;       126 AA.
AC   A0A4R6U4Z0;
DT   31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   31-JUL-2019, sequence version 1.
DT   02-APR-2025, entry version 19.
DE   RecName: Full=chorismate mutase {ECO:0000256|NCBIfam:TIGR01796, ECO:0000256|PROSITE-ProRule:PRU00514};
DE            EC=5.4.99.5 {ECO:0000256|NCBIfam:TIGR01796, ECO:0000256|PROSITE-ProRule:PRU00514};
GN   ORFNames=EV213_103106 {ECO:0000313|EMBL:TDQ41528.1};
OS   Aureibacillus halotolerans.
OC   Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
OC   Aureibacillus.
OX   NCBI_TaxID=1508390 {ECO:0000313|EMBL:TDQ41528.1, ECO:0000313|Proteomes:UP000295632};
RN   [1] {ECO:0000313|EMBL:TDQ41528.1, ECO:0000313|Proteomes:UP000295632}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 28697 {ECO:0000313|EMBL:TDQ41528.1,
RC   ECO:0000313|Proteomes:UP000295632};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT   most valuable type-strain genomes for metagenomic binning, comparative
RT   biology and taxonomic classification.";
RL   Submitted (MAR-2019) to the EMBL/GenBank/DDBJ databases.
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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:TDQ41528.1}.
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DR   EMBL; SNYJ01000003; TDQ41528.1; -; Genomic_DNA.
DR   RefSeq; WP_133579398.1; NZ_SNYJ01000003.1.
DR   AlphaFoldDB; A0A4R6U4Z0; -.
DR   OrthoDB; 9802232at2; -.
DR   UniPathway; UPA00120; UER00203.
DR   Proteomes; UP000295632; Unassembled WGS sequence.
DR   GO; GO:0004106; F:chorismate mutase activity; IEA:UniProtKB-UniRule.
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   GO; GO:0046417; P:chorismate metabolic process; IEA:TreeGrafter.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000295632}.
FT   BINDING         6
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   126 AA;  14021 MW;  567FC16DAA17B169 CRC64;
     MIRGIRGATT VKDNNESDIL DNTEALFRAM IHENAIEPDD VASVYVSVTE NLDAVFPAKA
     LRRIEGWTFV PIMCMAEASI VGSLTSCIRV MMHVNTTTSQ DQIRHVYLED AIVLRPDLAL
     TEDNQV
//
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