ID   A0A2X0LQJ3_9BASI        Unreviewed;       225 AA.
AC   A0A2X0LQJ3;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=BZ3500_MvSof-1268-A1-R1_Chr10-1g02671 protein {ECO:0000313|EMBL:SDA01443.1};
GN   ORFNames=BZ3500_MVSOF-1268-A1-R1_CHR10-1G02671
GN   {ECO:0000313|EMBL:SDA01443.1};
OS   Microbotryum saponariae.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Microbotryomycetes; Microbotryales; Microbotryaceae; Microbotryum.
OX   NCBI_TaxID=289078 {ECO:0000313|EMBL:SDA01443.1, ECO:0000313|Proteomes:UP000249723};
RN   [1] {ECO:0000313|Proteomes:UP000249723}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Jeantristanb JTB J.-T., Ricardo R.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FMWP01000116; SDA01443.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2X0LQJ3; -.
DR   STRING; 289078.A0A2X0LQJ3; -.
DR   Proteomes; UP000249723; Unassembled WGS sequence.
DR   GO; GO:0016868; F:intramolecular phosphotransferase activity; IEA:InterPro.
DR   GO; GO:0006096; P:glycolytic process; IEA:InterPro.
DR   CDD; cd07067; HP_PGM_like; 1.
DR   Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR   HAMAP; MF_01039; PGAM_GpmA; 1.
DR   InterPro; IPR013078; His_Pase_superF_clade-1.
DR   InterPro; IPR029033; His_PPase_superfam.
DR   InterPro; IPR005952; Phosphogly_mut1.
DR   NCBIfam; TIGR01258; pgm_1; 2.
DR   PANTHER; PTHR11931; PHOSPHOGLYCERATE MUTASE; 1.
DR   PANTHER; PTHR11931:SF0; PHOSPHOGLYCERATE MUTASE; 1.
DR   Pfam; PF00300; His_Phos_1; 1.
DR   SMART; SM00855; PGAM; 1.
DR   SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
PE   3: Inferred from homology;
KW   Glycolysis {ECO:0000256|ARBA:ARBA00023152};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW   Reference proteome {ECO:0000313|Proteomes:UP000249723}.
FT   ACT_SITE        21
FT                   /note="Tele-phosphohistidine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT   ACT_SITE        100
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT   BINDING         33..34
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT   BINDING         73
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT   BINDING         100..103
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT   BINDING         111
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT   BINDING         127..128
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT   BINDING         171..172
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT   SITE            170
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-3"
SQ   SEQUENCE   225 AA;  24807 MW;  A998998D22EE8912 CRC64;
     MRSKPDHVLT SLLADSTGLK HGESEWNKLN LFTGWKNPAL TEVGRSEALA GAQALKKGGH
     SHFDVAFTSV LKRANDTLTI ILKEIGQEDL ETFKSEKLNE RDYGDLTGLN KDDARKKFGE
     EQVHIWRRSF DVPPPGGESL KLTADRVLPY YESEIKPRLA KGEKVLVAAH GNSLRAMIMA
     LEGLSGEEIL KVELSTGVPI VYKLDAEGKV LSKEVLSELN WLASG
//