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Database: UniProt
Entry: B6JWB1_SCHJY
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ID   B6JWB1_SCHJY            Unreviewed;       210 AA.
AC   B6JWB1;
DT   16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   SubName: Full=Phosphoglycerate mutase family protein {ECO:0000313|EMBL:EEB05662.1};
GN   ORFNames=SJAG_00685 {ECO:0000313|EMBL:EEB05662.1};
OS   Schizosaccharomyces japonicus (strain yFS275 / FY16936) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=402676 {ECO:0000313|EMBL:EEB05662.1, ECO:0000313|Proteomes:UP000001744};
RN   [1] {ECO:0000313|EMBL:EEB05662.1, ECO:0000313|Proteomes:UP000001744}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=yFS275 / FY16936 {ECO:0000313|Proteomes:UP000001744};
RX   PubMed=21511999; DOI=10.1126/science.1203357;
RA   Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA   Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA   Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA   Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA   French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA   Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA   Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA   Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA   Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA   Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT   "Comparative functional genomics of the fission yeasts.";
RL   Science 332:930-936(2011).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC       Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   EMBL; KE651166; EEB05662.1; -; Genomic_DNA.
DR   RefSeq; XP_002171955.1; XM_002171919.2.
DR   AlphaFoldDB; B6JWB1; -.
DR   STRING; 402676.B6JWB1; -.
DR   EnsemblFungi; EEB05662; EEB05662; SJAG_00685.
DR   GeneID; 7050721; -.
DR   JaponicusDB; SJAG_00685; -.
DR   VEuPathDB; FungiDB:SJAG_00685; -.
DR   eggNOG; KOG0235; Eukaryota.
DR   HOGENOM; CLU_033323_9_2_1; -.
DR   OMA; DANNERW; -.
DR   OrthoDB; 9136at2759; -.
DR   Proteomes; UP000001744; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0004331; F:fructose-2,6-bisphosphate 2-phosphatase activity; IBA:GO_Central.
DR   GO; GO:0045820; P:negative regulation of glycolytic process; IBA:GO_Central.
DR   GO; GO:0043456; P:regulation of pentose-phosphate shunt; IBA:GO_Central.
DR   CDD; cd07067; HP_PGM_like; 1.
DR   Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR   InterPro; IPR013078; His_Pase_superF_clade-1.
DR   InterPro; IPR029033; His_PPase_superfam.
DR   InterPro; IPR001345; PG/BPGM_mutase_AS.
DR   PANTHER; PTHR46517; FRUCTOSE-2,6-BISPHOSPHATASE TIGAR; 1.
DR   PANTHER; PTHR46517:SF1; FRUCTOSE-2,6-BISPHOSPHATASE TIGAR; 1.
DR   Pfam; PF00300; His_Phos_1; 1.
DR   SMART; SM00855; PGAM; 1.
DR   SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
DR   PROSITE; PS00175; PG_MUTASE; 1.
PE   4: Predicted;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001744}.
FT   ACT_SITE        8
FT                   /note="Tele-phosphohistidine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT   ACT_SITE        82
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT   BINDING         7..14
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT   BINDING         57
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
SQ   SEQUENCE   210 AA;  23790 MW;  7142DF256E6A8EF4 CRC64;
     MRVFLVRHGE TDRNKAKILQ GSFDAELNAD GKQQAELVAK RLAKLDVDQV FCSTMSRCKQ
     TIAPFVKTRP DVPIEYSDLI RERVFGELEG MPVAEAKKLL AENHPDRFGE GYSSLLKRLL
     KFWDEKIIPL YGQKKCVVVL CHGGVINALR DHFMQEKGFT FEKEKHEKKF ITSNTGVTEI
     ELLSKEGGHI HCFGDTSHLD EAANCAPQEQ
//
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