ID A0A3D8TVX9_9LIST Unreviewed; 125 AA.
AC A0A3D8TVX9;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 02-APR-2025, entry version 22.
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=UR08_02445 {ECO:0000313|EMBL:RDX03019.1};
OS Listeria kieliensis.
OC Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae;
OC Listeria.
OX NCBI_TaxID=1621700 {ECO:0000313|EMBL:RDX03019.1, ECO:0000313|Proteomes:UP000257055};
RN [1] {ECO:0000313|Proteomes:UP000257055}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Kiel-L1 {ECO:0000313|Proteomes:UP000257055};
RA Schardt J., Mueller-Herbst S., Scherer S., Huptas C.;
RL Submitted (APR-2015) 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:RDX03019.1}.
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; LARY01000001; RDX03019.1; -; Genomic_DNA.
DR RefSeq; WP_115752696.1; NZ_LARY01000001.1.
DR AlphaFoldDB; A0A3D8TVX9; -.
DR UniPathway; UPA00120; UER00203.
DR Proteomes; UP000257055; 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:UP000257055}.
FT BINDING 5
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 125 AA; 14083 MW; B7BFD774D1746223 CRC64;
MRAIRGATTV KENRANEIYS ATDELFRQIL RENKLTNPEQ LVSVIITATP DLNAAFPARA
IRECEGFELL PVMGMVETDV PGAPRKCIRL MVHVEIDQQL ADVKHVYLND AAKLRPDLAR
KRDEA
//
