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Database: UniProt
Entry: A0A149Q2Y3_9PROT
LinkDB: A0A149Q2Y3_9PROT
Original site: A0A149Q2Y3_9PROT 
ID   A0A149Q2Y3_9PROT        Unreviewed;       108 AA.
AC   A0A149Q2Y3;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=chorismate mutase {ECO:0000256|ARBA:ARBA00012404};
DE            EC=5.4.99.5 {ECO:0000256|ARBA:ARBA00012404};
GN   ORFNames=AD928_13410 {ECO:0000313|EMBL:KXU91720.1};
OS   Acetobacter cerevisiae.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Acetobacter.
OX   NCBI_TaxID=178900 {ECO:0000313|EMBL:KXU91720.1, ECO:0000313|Proteomes:UP000075473};
RN   [1] {ECO:0000313|EMBL:KXU91720.1, ECO:0000313|Proteomes:UP000075473}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 1625 {ECO:0000313|EMBL:KXU91720.1,
RC   ECO:0000313|Proteomes:UP000075473};
RA   Li L., Cleenwerck I., De Vuyst L., Vandamme P.;
RT   "Improved classification and identification of acetic acid bacteria using
RT   matrix-assisted laser desorption/ionization time-of-flight mass
RT   spectrometry; Gluconobacter nephelii and Gluconobacter uchimurae are later
RT   heterotypic synonyms of Gluconobacter japonicus and Gluconobacter oxydans,
RT   respectively.";
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
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:KXU91720.1}.
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DR   EMBL; LHZA01000157; KXU91720.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A149Q2Y3; -.
DR   PATRIC; fig|178900.5.peg.432; -.
DR   Proteomes; UP000075473; Unassembled WGS sequence.
DR   GO; GO:0004106; F:chorismate mutase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046417; P:chorismate metabolic process; IEA:InterPro.
DR   Gene3D; 1.20.59.10; Chorismate mutase; 1.
DR   InterPro; IPR036263; Chorismate_II_sf.
DR   InterPro; IPR010951; CM_bact.
DR   InterPro; IPR036979; CM_dom_sf.
DR   InterPro; IPR002701; CM_II_prokaryot.
DR   NCBIfam; TIGR01795; CM_mono_cladeE; 1.
DR   PANTHER; PTHR38041; CHORISMATE MUTASE; 1.
DR   PANTHER; PTHR38041:SF1; CHORISMATE MUTASE; 1.
DR   Pfam; PF01817; CM_2; 1.
DR   SMART; SM00830; CM_2; 1.
DR   SUPFAM; SSF48600; Chorismate mutase II; 1.
DR   PROSITE; PS51168; CHORISMATE_MUT_2; 1.
PE   4: Predicted;
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:KXU91720.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000075473}.
FT   DOMAIN          8..99
FT                   /note="Chorismate mutase"
FT                   /evidence="ECO:0000259|PROSITE:PS51168"
SQ   SEQUENCE   108 AA;  12141 MW;  90FE4067F9090580 CRC64;
     MQTVTDQPTP TDALLDLRRS IDNIDAALVA MLAERFRCTK AVGALKARYG MPPADPARES
     RQITRLRTLA EEAHLDPDFA EKFLNFIIHE VIRHHEAIAK QSSESTTK
//
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