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Database: UniProt
Entry: T0Q5I3_SAPDV
LinkDB: T0Q5I3_SAPDV
Original site: T0Q5I3_SAPDV 
ID   T0Q5I3_SAPDV            Unreviewed;       241 AA.
AC   T0Q5I3;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=Phosphoglycerate mutase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=SDRG_13570 {ECO:0000313|EMBL:EQC28695.1};
OS   Saprolegnia diclina (strain VS20).
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC   Saprolegnia.
OX   NCBI_TaxID=1156394 {ECO:0000313|EMBL:EQC28695.1, ECO:0000313|Proteomes:UP000030762};
RN   [1] {ECO:0000313|EMBL:EQC28695.1, ECO:0000313|Proteomes:UP000030762}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VS20 {ECO:0000313|EMBL:EQC28695.1,
RC   ECO:0000313|Proteomes:UP000030762};
RG   The Broad Institute Genome Sequencing Platform;
RA   Russ C., Nusbaum C., Tyler B., van West P., Dieguez-Uribeondo J.,
RA   de Bruijn I., Tripathy S., Jiang R., Young S.K., Zeng Q., Gargeya S.,
RA   Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA   Berlin A., Chapman S.B., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Larimer J., McCowen C., Montmayeur A., Murphy C.,
RA   Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA   Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Saprolegnia declina VS20.";
RL   Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC       Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   EMBL; JH767192; EQC28695.1; -; Genomic_DNA.
DR   RefSeq; XP_008617887.1; XM_008619665.1.
DR   AlphaFoldDB; T0Q5I3; -.
DR   STRING; 1156394.T0Q5I3; -.
DR   EnsemblProtists; EQC28695; EQC28695; SDRG_13570.
DR   GeneID; 19954297; -.
DR   VEuPathDB; FungiDB:SDRG_13570; -.
DR   eggNOG; KOG0235; Eukaryota.
DR   InParanoid; T0Q5I3; -.
DR   OMA; ISYGDWD; -.
DR   OrthoDB; 45565at2759; -.
DR   Proteomes; UP000030762; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
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:UP000030762}.
FT   ACT_SITE        41
FT                   /note="Tele-phosphohistidine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT   ACT_SITE        116
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT   BINDING         40..47
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT   BINDING         91
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT   BINDING         142..143
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
SQ   SEQUENCE   241 AA;  26776 MW;  54405A69A7F01BEF CRC64;
     MQQQVISTFA GPRTRQLIMR TLSQCLPPLQ EGCTRIYLCR HGETDYNVAG ILQGRGVNMR
     LNKNGHKQAQ QLARSFKDIP LDAVYSSALA RAKETAACIQ HAHPTTKTGA FVDLEEMSFG
     TLEGTPRTQN AVFLQEIYAK WRRGILDANA RFPSGECPLD VKKRGVAMLH ELAAGSDDDH
     IAFVCHGRFN KIILAELLSI PVENPPIPQD NTCVNVLDYN RVKGTYTAVV INHTTHLVDR
     P
//
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