ID   A0A0D2UF99_CAPO3        Unreviewed;       327 AA.
AC   A0A0D2UF99;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=phosphoenolpyruvate mutase {ECO:0000256|ARBA:ARBA00024063};
DE            EC=5.4.2.9 {ECO:0000256|ARBA:ARBA00024063};
GN   ORFNames=CAOG_004530 {ECO:0000313|EMBL:KJE93786.1};
OS   Capsaspora owczarzaki (strain ATCC 30864).
OC   Eukaryota; Filasterea; Capsaspora.
OX   NCBI_TaxID=595528 {ECO:0000313|EMBL:KJE93786.1, ECO:0000313|Proteomes:UP000008743};
RN   [1] {ECO:0000313|Proteomes:UP000008743}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 30864 {ECO:0000313|Proteomes:UP000008743};
RA   Russ C., Cuomo C., Burger G., Gray M.W., Holland P.W.H., King N.,
RA   Lang F.B.F., Roger A.J., Ruiz-Trillo I., Young S.K., Zeng Q., Gargeya S.,
RA   Alvarado L., Berlin A., Chapman S.B., Chen Z., Freedman E., Gellesch M.,
RA   Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Howarth C.,
RA   Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA   Sisk P., Stolte C., Sykes S., White J., Yandava C., Haas B., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Capsaspora owczarzaki ATCC 30864.";
RL   Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the isocitrate lyase/PEP mutase superfamily. PEP
CC       mutase family. {ECO:0000256|ARBA:ARBA00038455}.
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DR   EMBL; KE346366; KJE93786.1; -; Genomic_DNA.
DR   RefSeq; XP_004347277.1; XM_004347227.2.
DR   AlphaFoldDB; A0A0D2UF99; -.
DR   STRING; 595528.A0A0D2UF99; -.
DR   EnsemblProtists; KJE93786; KJE93786; CAOG_004530.
DR   GeneID; 14897897; -.
DR   eggNOG; KOG1260; Eukaryota.
DR   InParanoid; A0A0D2UF99; -.
DR   OMA; IIHGDDW; -.
DR   OrthoDB; 2678353at2759; -.
DR   PhylomeDB; A0A0D2UF99; -.
DR   Proteomes; UP000008743; Unassembled WGS sequence.
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:KJE93786.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008743};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..327
FT                   /note="phosphoenolpyruvate mutase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002253392"
SQ   SEQUENCE   327 AA;  35997 MW;  7911B2E6E17BDC89 CRC64;
     MLASSALRLV LAPSLCNAVA NNAIRAASTS ASASKPKKTT QLKQMLTSNN LEFLMEAHNG
     LSAKIVEEAG FKGIWGSGLS ISASLGVRDS NEASYTQVLE VLEYMSDATT IPILLDGDTG
     YGNFNNARRL VTKLEQRGVA GVCMEDKTFP KTNSLLDGRA QPLADIEEFS GKIRACKDTQ
     KDADFCVVAR VEAFIAGWPL EEALRRAEAY HKAGADAVLI HSKKKDPSDI EAFMKAWNNR
     APVVIVPTNY YTTPTDRFRE LGISTIIWAN HNMRTAISSM QATTKQIFQD QSLKNVETKI
     ATVKEVFRLQ NDQELTKAED KYLPKEK
//