ID   Q64T51_BACFR            Unreviewed;       435 AA.
AC   Q64T51;
DT   25-OCT-2004, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2004, sequence version 1.
DT   27-MAR-2024, entry version 88.
DE   RecName: Full=phosphoenolpyruvate mutase {ECO:0000256|ARBA:ARBA00024063};
DE            EC=5.4.2.9 {ECO:0000256|ARBA:ARBA00024063};
GN   OrderedLocusNames=BF2578 {ECO:0000313|EMBL:BAD49328.1};
OS   Bacteroides fragilis (strain YCH46).
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=295405 {ECO:0000313|EMBL:BAD49328.1, ECO:0000313|Proteomes:UP000002197};
RN   [1] {ECO:0000313|EMBL:BAD49328.1, ECO:0000313|Proteomes:UP000002197}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YCH46 {ECO:0000313|EMBL:BAD49328.1,
RC   ECO:0000313|Proteomes:UP000002197};
RX   PubMed=15466707; DOI=10.1073/pnas.0404172101;
RA   Kuwahara T., Yamashita A., Hirakawa H., Nakayama H., Toh H., Okada N.,
RA   Kuhara S., Hattori M., Hayashi T., Ohnishi Y.;
RT   "Genomic analysis of Bacteroides fragilis reveals extensive DNA inversions
RT   regulating cell surface adaptation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:14919-14924(2004).
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DR   EMBL; AP006841; BAD49328.1; -; Genomic_DNA.
DR   RefSeq; WP_011202933.1; NC_006347.1.
DR   RefSeq; YP_099862.1; NC_006347.1.
DR   AlphaFoldDB; Q64T51; -.
DR   STRING; 295405.BF2578; -.
DR   KEGG; bfr:BF2578; -.
DR   PATRIC; fig|295405.11.peg.2488; -.
DR   HOGENOM; CLU_027389_0_1_10; -.
DR   OrthoDB; 9795543at2; -.
DR   Proteomes; UP000002197; 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; cd02170; cytidylyltransferase; 1.
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:BAD49328.1};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          12..133
FT                   /note="Cytidyltransferase-like"
FT                   /evidence="ECO:0000259|Pfam:PF01467"
SQ   SEQUENCE   435 AA;  48449 MW;  40FC777B2BB85414 CRC64;
     MIDRKKVYVG MSADIIHPGH LNIIHEAQKL GYVTVGVLTD AAISSYKRLP YLNYEQRSLI
     VKNLKGVEEV IPQSTLDYVP NLELLRPDFV VHGDDWKEGV QKETRQRVID TISKWGGKVI
     DVPYTKGISS TQLNSKLKEI GTTPEIRLKR LRRLIEAKSI VRICESHSGL TGLIIENTSV
     EVNGIRREFD GMWSSSLTDS TSKGKPDIEA VDLTTRLHDL NDALECTTKP IIFDGDTGGK
     IEHFVFTVRT LERLGISAVI IEDKIGLKKN SLFGTDAIQT QDTIDGFCNK IRAGKRAQIT
     DDFMIIARIE SFIAGKGQED AMERALAYIE AGADGIMIHS KDKSGEDIRL FCKALRLANQ
     SVPIVVVPTT YNHVTEEELS LWGANIVIYA NHMLRSAYPA MLNTAKSILS HGRSYEANEL
     CMPVKEILEL IPGTK
//