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Database: UniProt
Entry: A0A223D643_9BACL
LinkDB: A0A223D643_9BACL
Original site: A0A223D643_9BACL 
ID   A0A223D643_9BACL        Unreviewed;       311 AA.
AC   A0A223D643;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=phosphoenolpyruvate mutase {ECO:0000256|ARBA:ARBA00024063};
DE            EC=5.4.2.9 {ECO:0000256|ARBA:ARBA00024063};
GN   Name=aepX {ECO:0000313|EMBL:ASS77058.1};
GN   ORFNames=CIG75_00855 {ECO:0000313|EMBL:ASS77058.1};
OS   Tumebacillus algifaecis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Alicyclobacillaceae;
OC   Tumebacillus.
OX   NCBI_TaxID=1214604 {ECO:0000313|EMBL:ASS77058.1, ECO:0000313|Proteomes:UP000214688};
RN   [1] {ECO:0000313|EMBL:ASS77058.1, ECO:0000313|Proteomes:UP000214688}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=THMBR28 {ECO:0000313|EMBL:ASS77058.1,
RC   ECO:0000313|Proteomes:UP000214688};
RX   PubMed=25858243; DOI=10.1099/ijs.0.000240;
RA   Wu Y.F., Zhang B., Xing P., Wu Q.L., Liu S.J.;
RT   "Tumebacillus algifaecis sp. nov., isolated from decomposing algal scum.";
RL   Int. J. Syst. Evol. Microbiol. 65:2194-2198(2015).
CC   -!- SIMILARITY: Belongs to the isocitrate lyase/PEP mutase superfamily. PEP
CC       mutase family. {ECO:0000256|ARBA:ARBA00038455}.
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DR   EMBL; CP022657; ASS77058.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A223D643; -.
DR   KEGG; tab:CIG75_00855; -.
DR   OrthoDB; 8629576at2; -.
DR   Proteomes; UP000214688; 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:ASS77058.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000214688}.
SQ   SEQUENCE   311 AA;  34151 MW;  D1F4BCBCC85AC1D1 CRC64;
     MRKSTKLRQL LQEDRCLKII GANDGMTAIL GEREGFDGLW ASGLAISTSY GVPDASILTM
     TEFLDAASMM NKASSLPIIA DCDTGFGEVN NIIRMIREYE NAGIAAVCIE DKNFPKRNSF
     LEGHDLADMY EFAAKIHIAK AAQTDPDFVV IARLESLIAG MGLEDALTRA QMYADAGADA
     ILVHSKSKEA TEVLAFAARW KKIGRKTPLI IVPTTYYTLT FQQAEMAGFS MVIYANQLLR
     SAVKAMEEAL LVINEHGNTE PLEAQMSTVK EVFSLVKTQE ATAKETSFDQ LVSRLREQEM
     TQDLLSVGES S
//
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