ID   A0A109Q6J5_9BRAD        Unreviewed;       296 AA.
AC   A0A109Q6J5;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=phosphoenolpyruvate mutase {ECO:0000256|ARBA:ARBA00024063};
DE            EC=5.4.2.9 {ECO:0000256|ARBA:ARBA00024063};
GN   ORFNames=BCCGELA001_29045 {ECO:0000313|EMBL:AMA61553.1};
OS   Bradyrhizobium sp. CCGE-LA001.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Bradyrhizobium.
OX   NCBI_TaxID=1223566 {ECO:0000313|EMBL:AMA61553.1, ECO:0000313|Proteomes:UP000019052};
RN   [1] {ECO:0000313|EMBL:AMA61553.1, ECO:0000313|Proteomes:UP000019052}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCGE-LA001 {ECO:0000313|EMBL:AMA61553.1,
RC   ECO:0000313|Proteomes:UP000019052};
RX   PubMed=24952318; DOI=10.1016/j.ympev.2014.06.006;
RA   Servin-Garciduenas L.E., Zayas-Del Moral A., Ormeno-Orrillo E., Rogel M.A.,
RA   Delgado-Salinas A., Sanchez F., Martinez-Romero E.;
RT   "Symbiont shift towards Rhizobium nodulation in a group of phylogenetically
RT   related Phaseolus species.";
RL   Mol. Phylogenet. Evol. 79:1-11(2014).
CC   -!- SIMILARITY: Belongs to the isocitrate lyase/PEP mutase superfamily. PEP
CC       mutase family. {ECO:0000256|ARBA:ARBA00038455}.
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DR   EMBL; CP013949; AMA61553.1; -; Genomic_DNA.
DR   RefSeq; WP_060737913.1; NZ_CP013949.1.
DR   AlphaFoldDB; A0A109Q6J5; -.
DR   STRING; 1223566.BCCGELA001_29045; -.
DR   KEGG; brc:BCCGELA001_29045; -.
DR   Proteomes; UP000019052; 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; IPR012698; PEnolPyrv_PMutase_core.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR   NCBIfam; TIGR02320; PEP_mutase; 1.
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:0000256|ARBA:ARBA00023235};
KW   Pyruvate {ECO:0000313|EMBL:AMA61553.1}.
SQ   SEQUENCE   296 AA;  32277 MW;  FCD0323814A12E25 CRC64;
     MLRAELYDST KLSFFMEAHD GLSAAIAKGA RFKGLWASGL SIACSLGYRD ANEASWSQLV
     AVVERIVDSS ELPVLVDGDS GFGNFNNARL VARKLCQRGA AGVAIQDSCF PKMNSFVGDR
     HPLADTDEFS GRLRAVKDRV ADAFVLVART EAFIAGHGTD EALSRAHAYA EAGADAIIIH
     SRRSTADEIL SFTRAWQNRL PVVIIPTKYY RTPISVFHEA RVSAVIWANQ SMRAATASMR
     EVCHRIMAEQ STAGIEPGIA TLEEVFELFK YDELARAEAE YCGPTLKPAE RIVGTG
//