ID A0A919WF43_9BACI Unreviewed; 121 AA.
AC A0A919WF43;
DT 22-FEB-2023, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2023, sequence version 1.
DT 05-FEB-2025, entry version 8.
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:GIN60745.1};
GN ORFNames=J27TS8_07380 {ECO:0000313|EMBL:GIN60745.1};
OS Robertmurraya siralis.
OC Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
OC Robertmurraya.
OX NCBI_TaxID=77777 {ECO:0000313|EMBL:GIN60745.1, ECO:0000313|Proteomes:UP000682111};
RN [1] {ECO:0000313|EMBL:GIN60745.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=J27TS8 {ECO:0000313|EMBL:GIN60745.1};
RA Okamoto M., Kumagai M., Kanamori H., Takamatsu D.;
RT "Antimicrobial resistance genes in bacteria isolated from Japanese honey,
RT and their potential for conferring macrolide and lincosamide resistance in
RT the American foulbrood pathogen Paenibacillus larvae.";
RL Submitted (MAR-2021) 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:GIN60745.1}.
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DR EMBL; BORC01000001; GIN60745.1; -; Genomic_DNA.
DR OrthoDB; 9802232at2; -.
DR Proteomes; UP000682111; 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:UP000682111}.
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 121 AA; 13791 MW; BEAB475D0D8A7CC6 CRC64;
MIRGVRGATT IEENVEQEIV SATEKLIREM ILQNDIVAEA VASVFISVTE DIDGAFPAKA
LRRITGWTYV PVMCMREIPV ENSLKNCIRI MIHINTEKSQ REIHHVYLEK AISLRPDLKD
E
//
