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Database: UniProt
Entry: A0A398BCT3_9BACI
LinkDB: A0A398BCT3_9BACI
Original site: A0A398BCT3_9BACI 
ID   A0A398BCT3_9BACI        Unreviewed;       256 AA.
AC   A0A398BCT3;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   SubName: Full=Isocitrate lyase/phosphoenolpyruvate mutase family protein {ECO:0000313|EMBL:RID86628.1};
GN   ORFNames=D1970_06765 {ECO:0000313|EMBL:RID86628.1};
OS   Mesobacillus zeae.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Mesobacillus.
OX   NCBI_TaxID=1917180 {ECO:0000313|EMBL:RID86628.1, ECO:0000313|Proteomes:UP000265816};
RN   [1] {ECO:0000313|EMBL:RID86628.1, ECO:0000313|Proteomes:UP000265816}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JJ-247 {ECO:0000313|EMBL:RID86628.1,
RC   ECO:0000313|Proteomes:UP000265816};
RA   Seuylemezian A., Vaishampayan P.;
RT   "Bacillus jemisoniae sp. nov., Bacillus chryseoplanitiae sp. nov., Bacillus
RT   resnikiae sp. nov., and Bacillus frankliniae sp. nov., isolated from Viking
RT   spacecraft and associated surfaces.";
RL   Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
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:RID86628.1}.
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DR   EMBL; QWVT01000012; RID86628.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A398BCT3; -.
DR   OrthoDB; 9780430at2; -.
DR   Proteomes; UP000265816; Unassembled WGS sequence.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
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   Lyase {ECO:0000313|EMBL:RID86628.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Pyruvate {ECO:0000313|EMBL:RID86628.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000265816}.
SQ   SEQUENCE   256 AA;  28451 MW;  A18606737758D8AF CRC64;
     MNKIQKFNEL HSSKEILFLG NAWNLLSALT LEKAGFKAIG TTSWGIANSL GYADGELIDF
     DRHLEIIKTI AGNVKIPVSA DIEAGYGEDI QTIVDHVLKT ADVGVAGINI EDSFKKQKGL
     KEITWHCELL TNIRAALDHN GYKDFYINAR IDTYLQKQNP LFETIERAKA YVESGASGIF
     VPGLIEHDEI KEITMDVSAP LNVLSLRGLT NCTKLKELGV RRFSFGNALS DKVIAYLEKN
     VGELVEFMDT SHLYVD
//
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