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Database: UniProt
Entry: A3LVV4_PICST
LinkDB: A3LVV4_PICST
Original site: A3LVV4_PICST 
ID   A3LVV4_PICST            Unreviewed;       244 AA.
AC   A3LVV4;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   24-JAN-2024, entry version 75.
DE   SubName: Full=Phosphoglycerate mutase {ECO:0000313|EMBL:ABN67184.1};
DE            EC=5.4.2.- {ECO:0000313|EMBL:ABN67184.1};
GN   Name=GPM2 {ECO:0000313|EMBL:ABN67184.1};
GN   ORFNames=PICST_89865 {ECO:0000313|EMBL:ABN67184.1};
OS   Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS   Y-11545) (Yeast) (Pichia stipitis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX   NCBI_TaxID=322104 {ECO:0000313|EMBL:ABN67184.1, ECO:0000313|Proteomes:UP000002258};
RN   [1] {ECO:0000313|EMBL:ABN67184.1, ECO:0000313|Proteomes:UP000002258}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545
RC   {ECO:0000313|Proteomes:UP000002258};
RX   PubMed=17334359; DOI=10.1038/nbt1290;
RA   Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA   Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.S.,
RA   Passoth V., Richardson P.M.;
RT   "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT   yeast Pichia stipitis.";
RL   Nat. Biotechnol. 25:319-326(2007).
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DR   EMBL; CP000499; ABN67184.1; -; Genomic_DNA.
DR   RefSeq; XP_001385213.1; XM_001385176.1.
DR   AlphaFoldDB; A3LVV4; -.
DR   STRING; 322104.A3LVV4; -.
DR   GeneID; 4839651; -.
DR   KEGG; pic:PICST_89865; -.
DR   eggNOG; KOG0235; Eukaryota.
DR   HOGENOM; CLU_033323_13_0_1; -.
DR   InParanoid; A3LVV4; -.
DR   OMA; GWLIWRD; -.
DR   OrthoDB; 156438at2759; -.
DR   Proteomes; UP000002258; Chromosome 5.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
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   PANTHER; PTHR48100; BROAD-SPECIFICITY PHOSPHATASE YOR283W-RELATED; 1.
DR   PANTHER; PTHR48100:SF15; SEDOHEPTULOSE 1,7-BISPHOSPHATASE; 1.
DR   Pfam; PF00300; His_Phos_1; 1.
DR   SMART; SM00855; PGAM; 1.
DR   SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
PE   4: Predicted;
KW   Isomerase {ECO:0000313|EMBL:ABN67184.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002258}.
FT   ACT_SITE        17
FT                   /note="Tele-phosphohistidine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT   ACT_SITE        105
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT   BINDING         75
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT   BINDING         105..108
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
SQ   SEQUENCE   244 AA;  27738 MW;  FC124B91FDE93A09 CRC64;
     MSPAAKTHTP RIIFVRHGQT EWSKSGQHTS VTDLPLTDFG VKQMRNTGKH LIGSSPFQMI
     KPEDISHIFV SPRTRARHTA ELLTEDVDDI QKARIPIIVD EDIREWEYGD YEGLLTKQII
     DLRKKKGLDQ DVDRWIIWRD GCENGETHVE VKSRLDRFIS KIKEIHAEAL RTNSKSDIIV
     VAHGHILRCF AARWVEREIN IDPSFMLDAG GVGVLSYQHH NVNEPALFLA GAFVCPVEEE
     GADL
//
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