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Database: UniProt
Entry: Q636R0_BACCZ
LinkDB: Q636R0_BACCZ
Original site: Q636R0_BACCZ 
ID   Q636R0_BACCZ            Unreviewed;       274 AA.
AC   Q636R0;
DT   25-OCT-2004, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2004, sequence version 1.
DT   27-MAR-2024, entry version 90.
DE   RecName: Full=Isocitrate lyase/phosphoenolpyruvate mutase family protein {ECO:0008006|Google:ProtNLM};
GN   OrderedLocusNames=BCE33L3525 {ECO:0000313|EMBL:AAU16741.1};
OS   Bacillus cereus (strain ZK / E33L).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=288681 {ECO:0000313|EMBL:AAU16741.1, ECO:0000313|Proteomes:UP000002612};
RN   [1] {ECO:0000313|Proteomes:UP000002612}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ZK / E33L {ECO:0000313|Proteomes:UP000002612};
RX   PubMed=16621833; DOI=10.1128/JB.188.9.3382-3390.2006;
RA   Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S., Brown N.,
RA   Bruce D., Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C.,
RA   Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A.,
RA   Green L.D., Hill K.K., Hitchcock P., Jackson P.J., Keim P.,
RA   Kewalramani A.R., Longmire J., Lucas S., Malfatti S., McMurry K.,
RA   Meincke L.J., Misra M., Moseman B.L., Mundt M., Munk A.C., Okinaka R.T.,
RA   Parson-Quintana B., Reilly L.P., Richardson P., Robinson D.L., Rubin E.,
RA   Saunders E., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA   Ticknor L.O., Wills P.L., Brettin T.S., Gilna P.;
RT   "Pathogenomic sequence analysis of Bacillus cereus and Bacillus
RT   thuringiensis isolates closely related to Bacillus anthracis.";
RL   J. Bacteriol. 188:3382-3390(2006).
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DR   EMBL; CP000001; AAU16741.1; -; Genomic_DNA.
DR   RefSeq; WP_000997901.1; NZ_CP009968.1.
DR   AlphaFoldDB; Q636R0; -.
DR   KEGG; bcz:BCE33L3525; -.
DR   PATRIC; fig|288681.22.peg.1885; -.
DR   Proteomes; UP000002612; Chromosome.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:SF16; CARBOXYPHOSPHONOENOLPYRUVATE PHOSPHONOMUTASE-LIKE PROTEIN (AFU_ORTHOLOGUE AFUA_5G07230); 1.
DR   PANTHER; PTHR42905; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1.
DR   Pfam; PF13714; PEP_mutase; 1.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
PE   4: Predicted;
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
SQ   SEQUENCE   274 AA;  30593 MW;  18419D026FFF8948 CRC64;
     MNDILMKSKI FNDYHHDSSI LILPNAWDVM SAKIYEDLNY RAIGTTSAGI AASLGYSDGE
     QLPFESMLDV IEKITQSVNI PVSADIESGY GETIEEVLEN VRKIIASGVV GINLEDSKKN
     HVYSLYDTAY QQKKIESIKN VSISEGVPLF INARTDAYLL NNNRFEETMK RAQAYKDAGA
     DGIFIPGLAK KEHIHMFTEK INLPLNVLVN NSTPSILDLE YLNVSRISFG SGAYRATIST
     LRKLASEVIT KGQYETMTNE VMSYENMVGF LHKN
//
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