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Database: UniProt
Entry: K8X038_9GAMM
LinkDB: K8X038_9GAMM
Original site: K8X038_9GAMM 
ID   K8X038_9GAMM            Unreviewed;       302 AA.
AC   K8X038;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=phosphoenolpyruvate mutase {ECO:0000256|ARBA:ARBA00024063};
DE            EC=5.4.2.9 {ECO:0000256|ARBA:ARBA00024063};
GN   ORFNames=OOA_05931 {ECO:0000313|EMBL:EKT62992.1};
OS   Providencia burhodogranariea DSM 19968.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Providencia.
OX   NCBI_TaxID=1141662 {ECO:0000313|EMBL:EKT62992.1, ECO:0000313|Proteomes:UP000009336};
RN   [1] {ECO:0000313|EMBL:EKT62992.1, ECO:0000313|Proteomes:UP000009336}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19968 {ECO:0000313|EMBL:EKT62992.1,
RC   ECO:0000313|Proteomes:UP000009336};
RX   PubMed=23145767; DOI=10.1186/1471-2164-13-612;
RA   Galac M.R., Lazzaro B.P.;
RT   "Comparative genomics of bacteria in the genus Providencia isolated from
RT   wild Drosophila melanogaster.";
RL   BMC Genomics 13:612-612(2012).
CC   -!- SIMILARITY: Belongs to the isocitrate lyase/PEP mutase superfamily. PEP
CC       mutase family. {ECO:0000256|ARBA:ARBA00038455}.
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:EKT62992.1}.
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DR   EMBL; AKKL01000016; EKT62992.1; -; Genomic_DNA.
DR   RefSeq; WP_008911218.1; NZ_KB233222.1.
DR   AlphaFoldDB; K8X038; -.
DR   STRING; 1141662.OOA_05931; -.
DR   PATRIC; fig|1141662.3.peg.1203; -.
DR   eggNOG; COG2513; Bacteria.
DR   HOGENOM; CLU_027389_0_1_6; -.
DR   OrthoDB; 9802794at2; -.
DR   Proteomes; UP000009336; Unassembled WGS sequence.
DR   GO; GO:0016833; F:oxo-acid-lyase activity; IEA:UniProt.
DR   GO; GO:0050188; F:phosphoenolpyruvate mutase activity; IEA:UniProtKB-EC.
DR   CDD; cd00377; ICL_PEPM; 1.
DR   Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR   InterPro; IPR039556; ICL/PEPM.
DR   InterPro; IPR012698; PEnolPyrv_PMutase_core.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR   NCBIfam; TIGR02320; PEP_mutase; 1.
DR   PANTHER; PTHR42905; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1.
DR   PANTHER; PTHR42905:SF7; PHOSPHOENOLPYRUVATE PHOSPHOMUTASE-RELATED; 1.
DR   Pfam; PF13714; PEP_mutase; 1.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW   Pyruvate {ECO:0000313|EMBL:EKT62992.1}.
SQ   SEQUENCE   302 AA;  33560 MW;  718C2B5370090433 CRC64;
     MSKVILSNNN IGNRIASLRD KLETKNGLRI METHSPLSAM LVENIKFENK KEIVEYDGFW
     SSSLTDSAIR GKPDIELIDI AHRLSAVSEI FDVTSKPLIF DADTGGKIEH IVYSISTAER
     LGISAVIIED KEGLKKNSLL GNDVYQKQAK PEEFAEKVSA AAKAAKTDEF MLIARIESLI
     LDAGMEDALL RANLYVEAGA KGIMIHSRKT DPTEIFVFAK RFKNSHPTIT LVCVPTSFNQ
     VKFDDLVNHG YNIVIYANHL LRAAYPAMKY VAEMILKNGR TQEVEGICMS INDILELIPG
     TK
//
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