ID   A0A0B5QKD2_CLOBE        Unreviewed;       432 AA.
AC   A0A0B5QKD2;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=phosphoenolpyruvate mutase {ECO:0000256|ARBA:ARBA00024063};
DE            EC=5.4.2.9 {ECO:0000256|ARBA:ARBA00024063};
GN   ORFNames=LF65_04862 {ECO:0000313|EMBL:AJH01391.1};
OS   Clostridium beijerinckii (Clostridium MP).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1520 {ECO:0000313|EMBL:AJH01391.1, ECO:0000313|Proteomes:UP000031866};
RN   [1] {ECO:0000313|Proteomes:UP000031866}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=59B {ECO:0000313|Proteomes:UP000031866};
RA   Little G.T., Minton N.P.;
RT   "Genome sequence of Clostridium beijerinckii strain 59B.";
RL   Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP010086; AJH01391.1; -; Genomic_DNA.
DR   RefSeq; WP_041899817.1; NZ_MBAF01000076.1.
DR   STRING; 1520.LF65_04862; -.
DR   KEGG; cbei:LF65_04862; -.
DR   OrthoDB; 9802794at2; -.
DR   Proteomes; UP000031866; Chromosome.
DR   GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0050188; F:phosphoenolpyruvate mutase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   CDD; cd00377; ICL_PEPM; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR   InterPro; IPR004821; Cyt_trans-like.
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   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   NCBIfam; TIGR00125; cyt_tran_rel; 1.
DR   NCBIfam; TIGR02320; PEP_mutase; 1.
DR   PANTHER; PTHR43793; FAD SYNTHASE; 1.
DR   PANTHER; PTHR43793:SF1; FAD SYNTHASE; 1.
DR   Pfam; PF01467; CTP_transf_like; 1.
DR   Pfam; PF13714; PEP_mutase; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
PE   4: Predicted;
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW   Pyruvate {ECO:0000313|EMBL:AJH01391.1};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          10..105
FT                   /note="Cytidyltransferase-like"
FT                   /evidence="ECO:0000259|Pfam:PF01467"
SQ   SEQUENCE   432 AA;  48712 MW;  B2D405B559716425 CRC64;
     MKIVYVAMSA DIIHQGHLNV LNEARKFGNI IVGLHTDEVI RGYWRNPIMK YDERKEVISN
     IKGVISVVPQ ESLDQVPNLL KIKPNYVLHG DDWKEGSQKE LREKVIEVLK QWEGELMEVP
     YTKGVSISKL DEELAKIGIT PQMRMKGLKE LIYSKKPLRI LEAHNGLTGL IVEKTKVQRD
     GKIKEFDGMW ISSLCDSTAK GKPDIELVDL TSRLNTINDI LEVTTKPIIV DGDTGGQIEH
     FVYTVKTLER LGVSAIIIED KTGLKKNSLF GTEVKQTQDT IEHFCDKIRA GREARVTSDF
     MIISRIESLI AGAGMDDAIK RAKAYIEAGT DGIMIHSKEK DGREIIEFCR RYNEFENRVP
     LVVVPTSYNF MKEEELMELG VNVIIYANHL IRSAYPAMVN TAKSILENGR SKEASINCMP
     IKEILTLIPG GM
//