ID   E0U086_BACSH            Unreviewed;       296 AA.
AC   E0U086;
DT   02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   RecName: Full=phosphoenolpyruvate mutase {ECO:0000256|ARBA:ARBA00024063};
DE            EC=5.4.2.9 {ECO:0000256|ARBA:ARBA00024063};
GN   Name=rhiH {ECO:0000313|EMBL:ADM36257.1};
GN   OrderedLocusNames=BSUW23_01000 {ECO:0000313|EMBL:ADM36257.1};
OS   Bacillus spizizenii (strain ATCC 23059 / NRRL B-14472 / W23) (Bacillus
OS   subtilis subsp. spizizenii).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=655816 {ECO:0000313|EMBL:ADM36257.1, ECO:0000313|Proteomes:UP000002233};
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=W23;
RA   Zeigler D.R.;
RL   Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADM36257.1, ECO:0000313|Proteomes:UP000002233}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23059 / NRRL B-14472 / W23
RC   {ECO:0000313|Proteomes:UP000002233};
RX   PubMed=21527469; DOI=10.1099/mic.0.048520-0;
RA   Zeigler D.R.;
RT   "The genome sequence of Bacillus subtilis subsp. spizizenii W23: insights
RT   into speciation within the B. subtilis complex and into the history of B.
RT   subtilis genetics.";
RL   Microbiology 157:2033-2041(2011).
CC   -!- SIMILARITY: Belongs to the isocitrate lyase/PEP mutase superfamily. PEP
CC       mutase family. {ECO:0000256|ARBA:ARBA00038455}.
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DR   EMBL; CP002183; ADM36257.1; -; Genomic_DNA.
DR   RefSeq; WP_003223692.1; NC_014479.1.
DR   AlphaFoldDB; E0U086; -.
DR   GeneID; 64302054; -.
DR   KEGG; bss:BSUW23_01000; -.
DR   HOGENOM; CLU_027389_0_0_9; -.
DR   Proteomes; UP000002233; 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; 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   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Pyruvate {ECO:0000313|EMBL:ADM36257.1}.
SQ   SEQUENCE   296 AA;  32561 MW;  1FA8D450821AE9FE CRC64;
     MKAKKLRELL YSNQVVRVMG AHNGLSAKLA EQAGFHAIWA SGLEISASYA VPDANILTMT
     ENLQAAVVMN ESTSIPIICD CDSGYGSVNN VIRMVKEYER NGIAGICIED KQFPKLNSFV
     KGSQKLADID EFSNKIRAAK DVQKNPDFVV IARIEALIAG QGMDEALNRA YAYEAAGADA
     ILIHSKENQP NEIKEFVKQF TGAVPIVIVP TTYPHITVKE MELLGINMVI YANHGLRSSI
     KAMQETFSQI LLDGNTVGVE DNIVSMKTVF ELQGMYDMRK QEDMYNSGTS VISTIK
//