ID   F2JT41_CELLD            Unreviewed;       431 AA.
AC   F2JT41;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   RecName: Full=phosphoenolpyruvate mutase {ECO:0000256|ARBA:ARBA00024063};
DE            EC=5.4.2.9 {ECO:0000256|ARBA:ARBA00024063};
GN   OrderedLocusNames=Clole_3577 {ECO:0000313|EMBL:ADZ85260.1};
OS   Cellulosilyticum lentocellum (strain ATCC 49066 / DSM 5427 / NCIMB 11756 /
OS   RHM5) (Clostridium lentocellum).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Cellulosilyticaceae;
OC   Cellulosilyticum.
OX   NCBI_TaxID=642492 {ECO:0000313|EMBL:ADZ85260.1, ECO:0000313|Proteomes:UP000008467};
RN   [1] {ECO:0000313|EMBL:ADZ85260.1, ECO:0000313|Proteomes:UP000008467}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49066 / DSM 5427 / NCIMB 11756 / RHM5
RC   {ECO:0000313|Proteomes:UP000008467};
RX   PubMed=21398547; DOI=10.1128/JB.00239-11;
RG   US DOE Joint Genome Institute;
RA   Miller D.A., Suen G., Bruce D., Copeland A., Cheng J.F., Detter C.,
RA   Goodwin L.A., Han C.S., Hauser L.J., Land M.L., Lapidus A., Lucas S.,
RA   Meincke L., Pitluck S., Tapia R., Teshima H., Woyke T., Fox B.G.,
RA   Angert E.R., Currie C.R.;
RT   "Complete genome sequence of the cellulose-degrading bacterium
RT   Cellulosilyticum lentocellum.";
RL   J. Bacteriol. 193:2357-2358(2011).
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP002582; ADZ85260.1; -; Genomic_DNA.
DR   RefSeq; WP_013658536.1; NC_015275.1.
DR   AlphaFoldDB; F2JT41; -.
DR   STRING; 642492.Clole_3577; -.
DR   KEGG; cle:Clole_3577; -.
DR   eggNOG; COG0615; Bacteria.
DR   eggNOG; COG2513; Bacteria.
DR   HOGENOM; CLU_027389_0_1_9; -.
DR   Proteomes; UP000008467; 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, ECO:0000313|EMBL:ADZ85260.1};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW   Pyruvate {ECO:0000313|EMBL:ADZ85260.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008467};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          11..96
FT                   /note="Cytidyltransferase-like"
FT                   /evidence="ECO:0000259|Pfam:PF01467"
SQ   SEQUENCE   431 AA;  49424 MW;  11E4FB7B4A97140D CRC64;
     MKKVYMCFGT DVIHNGHIEI LRKAAELGEV TVGVLTDEVM ASYKRYPIIN LEQRLQIIES
     IKYVSKVIVQ EELDYTNNLR KVKPDYVVHG DDWRTGYQAS IRSKVIDILK EWDGELVEFP
     YTEDNNIKCL ENTMRERLSM PEFRRARLRK LLKMNRTIRV LEVHSGITGL IAENTKLEKD
     GKINEFDAMW LSSLCDSTVK GKPDIELVDM SSRLKTIEEI LEVTTKPIIL DGDTGGLVEH
     FNFNIRTLER MGVSAIIIED KEGLKKNSLF GTEVHQDQAS IESFCEKIRV GKAALKTKEF
     MLIARIESLI LEKGMEDALA RAQAYVNAGA DGIMIHSRKK EPDEIFAFCD AFRLQNKQTP
     IIVVPTTFNK VYEEELYNHG INIVIYANQL IRSAFPAMQN TARVILENER AYEVDKLCMP
     VKEILTLIKE R
//