ID   Q0RC29_FRAAA            Unreviewed;       275 AA.
AC   Q0RC29;
DT   05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2006, sequence version 1.
DT   27-MAR-2024, entry version 79.
DE   SubName: Full=Putative Phosphoenolpyruvate phosphomutase (Phosphoenolpyruvate mutase) (PEP mutase) (PEP phosphomutase) {ECO:0000313|EMBL:CAJ65000.1};
DE            EC=5.4.2.9 {ECO:0000313|EMBL:CAJ65000.1};
GN   OrderedLocusNames=FRAAL6377 {ECO:0000313|EMBL:CAJ65000.1};
OS   Frankia alni (strain DSM 45986 / CECT 9034 / ACN14a).
OC   Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae; Frankia.
OX   NCBI_TaxID=326424 {ECO:0000313|EMBL:CAJ65000.1, ECO:0000313|Proteomes:UP000000657};
RN   [1] {ECO:0000313|EMBL:CAJ65000.1, ECO:0000313|Proteomes:UP000000657}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ACN14a {ECO:0000313|Proteomes:UP000000657};
RX   PubMed=17151343; DOI=10.1101/gr.5798407;
RA   Normand P., Lapierre P., Tisa L.S., Gogarten J.P., Alloisio N.,
RA   Bagnarol E., Bassi C.A., Berry A.M., Bickhart D.M., Choisne N., Couloux A.,
RA   Cournoyer B., Cruveiller S., Daubin V., Demange N., Francino M.P.,
RA   Goltsman E., Huang Y., Kopp O.R., Labarre L., Lapidus A., Lavire C.,
RA   Marechal J., Martinez M., Mastronunzio J.E., Mullin B.C., Niemann J.,
RA   Pujic P., Rawnsley T., Rouy Z., Schenowitz C., Sellstedt A., Tavares F.,
RA   Tomkins J.P., Vallenet D., Valverde C., Wall L.G., Wang Y., Medigue C.,
RA   Benson D.R.;
RT   "Genome characteristics of facultatively symbiotic Frankia sp. strains
RT   reflect host range and host plant biogeography.";
RL   Genome Res. 17:7-15(2007).
CC   -!- SIMILARITY: Belongs to the isocitrate lyase/PEP mutase superfamily. PEP
CC       mutase family. {ECO:0000256|ARBA:ARBA00038455}.
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DR   EMBL; CT573213; CAJ65000.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q0RC29; -.
DR   STRING; 326424.FRAAL6377; -.
DR   KEGG; fal:FRAAL6377; -.
DR   eggNOG; COG2513; Bacteria.
DR   HOGENOM; CLU_027389_0_0_11; -.
DR   Proteomes; UP000000657; Chromosome.
DR   GO; GO:0050188; F:phosphoenolpyruvate mutase 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   Isomerase {ECO:0000313|EMBL:CAJ65000.1};
KW   Pyruvate {ECO:0000313|EMBL:CAJ65000.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000657}.
SQ   SEQUENCE   275 AA;  29731 MW;  4BFE2C210BCB8C99 CRC64;
     MLAEGQAVRA AGVHDALGAM LAEQAGFAAV WASSLGISAA RCLPDASLLT MTDYLQAAVQ
     MQRRVGIPVV ADCDTGFGNN LNIAYLVHEY EAAGISAVCI EDKHYPKMNS FAPGNHDLLE
     TTAFARKISI AKRVQSGDDF FVIARTEALI SGLSVDEALN RSYAYAEAGA DALLVHSKHR
     TSAEVQAFLE QWDGRKPVVL VPTTYPGWHF DDAVKAGASV IIYANQGLRA TIDALRATFH
     AIITHGSSAD LEADLASLND VFELQRLRQW QELER
//