ID   V9W6M3_9BACL            Unreviewed;       297 AA.
AC   V9W6M3;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   SubName: Full=Phosphonopyruvate hydrolase PphA {ECO:0000313|EMBL:AHD05768.1};
DE            EC=3.11.1.3 {ECO:0000313|EMBL:AHD05768.1};
GN   Name=pphA {ECO:0000313|EMBL:AHD05768.1};
GN   ORFNames=ERIC2_c19750 {ECO:0000313|EMBL:AHD05768.1};
OS   Paenibacillus larvae subsp. larvae DSM 25430.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=697284 {ECO:0000313|EMBL:AHD05768.1, ECO:0000313|Proteomes:UP000029431};
RN   [1] {ECO:0000313|EMBL:AHD05768.1, ECO:0000313|Proteomes:UP000029431}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 25430 {ECO:0000313|EMBL:AHD05768.1,
RC   ECO:0000313|Proteomes:UP000029431};
RX   PubMed=24599066;
RA   Djukic M., Brzuszkiewicz E., Funfhaus A., Voss J., Gollnow K., Poppinga L.,
RA   Liesegang H., Garcia-Gonzalez E., Genersch E., Daniel R.;
RT   "How to Kill the Honey Bee Larva: Genomic Potential and Virulence
RT   Mechanisms of Paenibacillus larvae.";
RL   PLoS ONE 9:E90914-E90914(2014).
CC   -!- SIMILARITY: Belongs to the isocitrate lyase/PEP mutase superfamily. PEP
CC       mutase family. {ECO:0000256|ARBA:ARBA00038455}.
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DR   EMBL; CP003355; AHD05768.1; -; Genomic_DNA.
DR   RefSeq; WP_024094158.1; NZ_CP019652.1.
DR   AlphaFoldDB; V9W6M3; -.
DR   KEGG; plv:ERIC2_c19750; -.
DR   PATRIC; fig|697284.3.peg.1896; -.
DR   eggNOG; COG2513; Bacteria.
DR   HOGENOM; CLU_027389_0_0_9; -.
DR   Proteomes; UP000029431; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0033978; F:phosphonopyruvate hydrolase 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   Hydrolase {ECO:0000313|EMBL:AHD05768.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Pyruvate {ECO:0000313|EMBL:AHD05768.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029431}.
SQ   SEQUENCE   297 AA;  32488 MW;  F4A8740717AA0CB3 CRC64;
     MVKETKASQL RKMLNGTKLI LVAGAHDGLT AKLAERNGFH AVWASGLGIS AIQTVPDASI
     LTMTELLQAA IVMNDACNLP IIADCDSGFG NIHNVVRMVE KYEGAGIAGV CIEDKVYPKI
     NSFDNGQQKL VSIEDFCAKI RAAKATQKDS DFVLLARVEA LIAGLGQDEA YNRACAYAQA
     GADAILIHSK QKTVDEIAEF MSRWNLDVPI VLVPTKYPDI TFNELEFLGV RMSIYANQAL
     RGSVSAIDSI LKRIMEKGST RDIEGEIASI EDIFELQDIP KMKQKELKFH KPKNATT
//