ID   PEPM_STRHY              Reviewed;         313 AA.
AC   P29247;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   13-SEP-2023, entry version 84.
DE   RecName: Full=Phosphoenolpyruvate phosphomutase;
DE            Short=PEP mutase;
DE            Short=PEP phosphomutase;
DE            Short=Phosphoenolpyruvate mutase;
DE            EC=5.4.2.9;
GN   Name=bcpB;
OS   Streptomyces hygroscopicus.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces; Streptomyces violaceusniger group.
OX   NCBI_TaxID=1912;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 21705 / DSM 41527 / SF-1293;
RX   PubMed=1337066; DOI=10.7164/antibiotics.45.1977;
RA   Hidaka T., Hidaka M., Seto H.;
RT   "Studies on the biosynthesis of bialaphos (SF-1293). 14. Nucleotide
RT   sequence of phosphoenolpyruvate phosphomutase gene isolated from a
RT   bialaphos producing organism, Streptomyces hygroscopicus, and its
RT   expression in Streptomyces lividans.";
RL   J. Antibiot. 45:1977-1980(1992).
CC   -!- FUNCTION: Formation of a carbon-phosphorus bond by converting
CC       phosphoenolpyruvate (PEP) to phosphonopyruvate (P-Pyr).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + phosphoenolpyruvate = 3-phosphonopyruvate;
CC         Xref=Rhea:RHEA:17013, ChEBI:CHEBI:15378, ChEBI:CHEBI:58702,
CC         ChEBI:CHEBI:71402; EC=5.4.2.9;
CC   -!- PATHWAY: Secondary metabolite biosynthesis; bialaphos biosynthesis.
CC   -!- SIMILARITY: Belongs to the isocitrate lyase/PEP mutase superfamily. PEP
CC       mutase family. {ECO:0000305}.
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DR   EMBL; D10016; BAA00905.1; -; Genomic_DNA.
DR   PIR; S27698; S27698.
DR   AlphaFoldDB; P29247; -.
DR   SMR; P29247; -.
DR   UniPathway; UPA00197; -.
DR   GO; GO:0050188; F:phosphoenolpyruvate mutase activity; IEA:UniProtKB-EC.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
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   Antibiotic biosynthesis; Isomerase.
FT   CHAIN           1..313
FT                   /note="Phosphoenolpyruvate phosphomutase"
FT                   /id="PRO_0000068825"
FT   ACT_SITE        69
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   313 AA;  33696 MW;  DB361EB98F3344BA CRC64;
     MNATEQAANG DRGTTRSAGG RLRYLLHAPG ACQLMGVHDG LSARIAVAEG FEALWASGLC
     MSTARGVRDS DEASWTELLT LVGTMTDAVP GVPVLVDGDT GYGNFNTARR FAGRAERVGA
     AGVCFEDKVF PKMNSFFGDG HQLAPVAEFC GKIRACKDAQ RDPDFVVVAR TEALISKLPM
     EEALDRAAAY AEAGADALFI HSRMNTPQQI ATFMERWEGS TPVLIAPTTY HTPSVDDFAA
     LGIAGCIWAN HSMRAAFAAM RDVCQRIRTD RGIYGIEDQV APLKEIFGLF DYEGLEKDEN
     CYTQAPDLAA VQG
//