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Database: UniProt
Entry: A0A1G2JGF6_9BACT
LinkDB: A0A1G2JGF6_9BACT
Original site: A0A1G2JGF6_9BACT 
ID   A0A1G2JGF6_9BACT        Unreviewed;       198 AA.
AC   A0A1G2JGF6;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=2,3-bisphosphoglycerate-dependent phosphoglycerate mutase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=A2401_02255 {ECO:0000313|EMBL:OGZ85591.1};
OS   Candidatus Staskawiczbacteria bacterium RIFOXYC1_FULL_38_18.
OC   Bacteria; Candidatus Staskawiczbacteria.
OX   NCBI_TaxID=1802229 {ECO:0000313|EMBL:OGZ85591.1, ECO:0000313|Proteomes:UP000177751};
RN   [1] {ECO:0000313|EMBL:OGZ85591.1, ECO:0000313|Proteomes:UP000177751}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OGZ85591.1}.
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DR   EMBL; MHPP01000001; OGZ85591.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G2JGF6; -.
DR   STRING; 1802229.A2401_02255; -.
DR   Proteomes; UP000177751; 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   InterPro; IPR013078; His_Pase_superF_clade-1.
DR   InterPro; IPR029033; His_PPase_superfam.
DR   InterPro; IPR005952; Phosphogly_mut1.
DR   NCBIfam; TIGR01258; pgm_1; 1.
DR   PANTHER; PTHR11931; PHOSPHOGLYCERATE MUTASE; 1.
DR   PANTHER; PTHR11931:SF0; PHOSPHOGLYCERATE MUTASE; 1.
DR   Pfam; PF00300; His_Phos_1; 1.
DR   PIRSF; PIRSF000709; 6PFK_2-Ptase; 1.
DR   SMART; SM00855; PGAM; 1.
DR   SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
PE   4: Predicted;
FT   BINDING         21..22
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT   BINDING         58
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT   BINDING         85..88
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT   BINDING         96
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT   BINDING         112..113
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
SQ   SEQUENCE   198 AA;  22595 MW;  D33AC3E6723B9905 CRC64;
     MVVASHNSLR AIVWNLENKF TGWTDVPLSQ EGIEGAKDAA VGLRDFKIDK IYTSPLIRNR
     ETVRLILEKL GIKNDSVIYD KSLDERDYGE LTGLDKDEAK KKFGEEQIGL WRRSYNIAPP
     GGESLNDVYD RAVPFFIKYI EKDLKEGKNV LVVASHNSLR AIVKYLENIS DEKIIDLELP
     FGALRKYESN EGRYSLLQ
//
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