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Database: UniProt
Entry: G2FN28_9FIRM
LinkDB: G2FN28_9FIRM
Original site: G2FN28_9FIRM 
ID   G2FN28_9FIRM            Unreviewed;       288 AA.
AC   G2FN28;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   SubName: Full=Carboxyvinyl-carboxyphosphonate phosphorylmutase {ECO:0000313|EMBL:EGW40999.1};
DE            EC=2.7.8.23 {ECO:0000313|EMBL:EGW40999.1};
GN   Name=bcpA {ECO:0000313|EMBL:EGW40999.1};
GN   ORFNames=DOT_1103 {ECO:0000313|EMBL:EGW40999.1};
OS   Desulfosporosinus sp. OT.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC   Desulfosporosinus.
OX   NCBI_TaxID=913865 {ECO:0000313|EMBL:EGW40999.1, ECO:0000313|Proteomes:UP000004928};
RN   [1] {ECO:0000313|EMBL:EGW40999.1, ECO:0000313|Proteomes:UP000004928}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OT {ECO:0000313|EMBL:EGW40999.1,
RC   ECO:0000313|Proteomes:UP000004928};
RX   PubMed=21994931; DOI=10.1128/JB.06018-11;
RA   Abicht H.K., Mancini S., Karnachuk O.V., Solioz M.;
RT   "Genome Sequence of Desulfosporosinus sp. OT, an Acidophilic Sulfate-
RT   Reducing Bacterium from Copper Mining Waste in Norilsk, Northern Siberia.";
RL   J. Bacteriol. 193:6104-6105(2011).
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:EGW40999.1}.
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DR   EMBL; AGAF01000053; EGW40999.1; -; Genomic_DNA.
DR   RefSeq; WP_009614881.1; NZ_AGAF01000053.1.
DR   AlphaFoldDB; G2FN28; -.
DR   PATRIC; fig|913865.3.peg.1006; -.
DR   eggNOG; COG2513; Bacteria.
DR   OrthoDB; 8629576at2; -.
DR   Proteomes; UP000004928; Unassembled WGS sequence.
DR   GO; GO:0008807; F:carboxyvinyl-carboxyphosphonate phosphorylmutase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016833; F:oxo-acid-lyase activity; IEA:UniProt.
DR   CDD; cd00377; ICL_PEPM; 1.
DR   Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR   InterPro; IPR039556; ICL/PEPM.
DR   InterPro; IPR018523; Isocitrate_lyase_ph_CS.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR   PANTHER; PTHR42905:SF5; CARBOXYVINYL-CARBOXYPHOSPHONATE PHOSPHORYLMUTASE, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR42905; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1.
DR   Pfam; PF13714; PEP_mutase; 1.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR   PROSITE; PS00161; ISOCITRATE_LYASE; 1.
PE   4: Predicted;
KW   Transferase {ECO:0000313|EMBL:EGW40999.1}.
SQ   SEQUENCE   288 AA;  31430 MW;  760E445ED5474981 CRC64;
     MNKGKVLRDL LADQEILVVP GAHDVLTAKI IEKTGFQAVY MTGYGQAASH LGTADVGLLT
     MSEMLARANN FASAVDVPVI ADGDTGFGNA INVMRTVRQY EMAGVAAIQL EDQVAPKKCG
     HMTGRQVIPM AEMVGKIRAA VEARRNSDFV IIARTDARTI HGIDEAIRRA KAYEEAGADV
     IFVESPESVE EMKRITSGFN VPVLANMVEG GRTPLLSARE LEKLGYDLVI FPTSSTYMVA
     QAMKNLMEEL MKTGTTKNLM SKMIPFPEFN ELIGLMEIRE LEAKYVIG
//
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