ID   I2C242_BACAY            Unreviewed;       296 AA.
AC   I2C242;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2012, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   SubName: Full=Putative phosphoenolpyruvate phosphomutase (Phosphoenolpyruvate mutase) (PEP mutase) (PEP phosphomutase) {ECO:0000313|EMBL:AFJ60716.1};
DE            EC=5.4.2.9 {ECO:0000313|EMBL:AFJ60716.1};
GN   ORFNames=MUS_0647 {ECO:0000313|EMBL:AFJ60716.1};
OS   Bacillus amyloliquefaciens (strain Y2) (Bacillus amyloliquefaciens subsp.
OS   plantarum (strain B9601-Y2)).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus amyloliquefaciens group.
OX   NCBI_TaxID=1155777 {ECO:0000313|EMBL:AFJ60716.1, ECO:0000313|Proteomes:UP000002878};
RN   [1] {ECO:0000313|EMBL:AFJ60716.1, ECO:0000313|Proteomes:UP000002878}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y2 {ECO:0000313|EMBL:AFJ60716.1};
RX   PubMed=23357245; DOI=10.1016/j.jbiotec.2012.12.014;
RA   He P., Hao K., Blom J., Ruckert C., Vater J., Mao Z., Wu Y., Hou M., He P.,
RA   He Y., Borriss R.;
RT   "Genome sequence of the plant growth promoting strain Bacillus
RT   amyloliquefaciens subsp. plantarum B9601-Y2 and expression of mersacidin
RT   and other secondary metabolites.";
RL   J. Biotechnol. 164:281-291(2012).
CC   -!- SIMILARITY: Belongs to the isocitrate lyase/PEP mutase superfamily. PEP
CC       mutase family. {ECO:0000256|ARBA:ARBA00038455}.
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DR   EMBL; CP003332; AFJ60716.1; -; Genomic_DNA.
DR   RefSeq; WP_014417091.1; NC_017912.1.
DR   AlphaFoldDB; I2C242; -.
DR   GeneID; 66320960; -.
DR   KEGG; bqy:MUS_0647; -.
DR   KEGG; bya:BANAU_0589; -.
DR   PATRIC; fig|1126211.3.peg.625; -.
DR   HOGENOM; CLU_027389_0_0_9; -.
DR   Proteomes; UP000002878; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
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:0000313|EMBL:AFJ60716.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Pyruvate {ECO:0000313|EMBL:AFJ60716.1}.
SQ   SEQUENCE   296 AA;  32496 MW;  7C66D9F4003EE195 CRC64;
     MMVKNRKSSI FRDALNSKGL VKVAGAHDGL SAKLAEKNGF NAVWASGLGI SAVQTVPDAS
     ILTMTEFLEA AVIMNESCNL PVIADCDSGY GNIHNVTRMI KKYEAAGIAG VCIEDKVYPK
     LNSFDDRQQI LVSTEEFCAK IRAAKMAQQN DDFVLIARVE ALIAKLGQEE AYTRAKAYVH
     AGADAILIHS KEQSPDEIIE FVNNWDVDAP LVVVPTKYPT LSMEQLEKLG VKVSIYANQA
     LRASVKAIND TFESIINNKS SLQIENDIVS VNEIFDIQDV PGMKQLERLI HRQPAN
//