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Database: UniProt
Entry: A0A3S8RVX7_9BACL
LinkDB: A0A3S8RVX7_9BACL
Original site: A0A3S8RVX7_9BACL 
ID   A0A3S8RVX7_9BACL        Unreviewed;       124 AA.
AC   A0A3S8RVX7;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   02-APR-2025, entry version 21.
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   Name=aroH {ECO:0000313|EMBL:AZK47179.1};
GN   ORFNames=EIM92_14265 {ECO:0000313|EMBL:AZK47179.1};
OS   Paenibacillus lentus.
OC   Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Paenibacillaceae;
OC   Paenibacillus.
OX   NCBI_TaxID=1338368 {ECO:0000313|EMBL:AZK47179.1, ECO:0000313|Proteomes:UP000273145};
RN   [1] {ECO:0000313|EMBL:AZK47179.1, ECO:0000313|Proteomes:UP000273145}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 25539 {ECO:0000313|EMBL:AZK47179.1,
RC   ECO:0000313|Proteomes:UP000273145};
RA   Kook J.-K., Park S.-N., Lim Y.K.;
RT   "Genome sequencing of Paenibacillus lentus DSM25539(T).";
RL   Submitted (NOV-2018) 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};
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DR   EMBL; CP034248; AZK47179.1; -; Genomic_DNA.
DR   RefSeq; WP_125083216.1; NZ_CP034248.1.
DR   AlphaFoldDB; A0A3S8RVX7; -.
DR   KEGG; plen:EIM92_14265; -.
DR   OrthoDB; 9802232at2; -.
DR   UniPathway; UPA00120; UER00203.
DR   Proteomes; UP000273145; Chromosome.
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   ECO:0000313|EMBL:AZK47179.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000273145}.
FT   BINDING         7
FT                   /ligand="prephenate"
FT                   /ligand_id="ChEBI:CHEBI:29934"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005965-1"
FT   BINDING         90
FT                   /ligand="prephenate"
FT                   /ligand_id="ChEBI:CHEBI:29934"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005965-1"
FT   BINDING         108
FT                   /ligand="prephenate"
FT                   /ligand_id="ChEBI:CHEBI:29934"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005965-1"
SQ   SEQUENCE   124 AA;  13926 MW;  F460B7038B752B33 CRC64;
     MYNRGIRGAT TVTRNDEAEI LQETAVLLKE IVARNEIEPE DICSVWITVT ADLDATFPAR
     AIRVLKGWEL VPLMCSTEIP VKGSLPKCIR FLIQVNTNKS QREMKHVYLN EAKSLRPDLA
     ASNS
//
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