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Database: UniProt
Entry: A0A0G0PDR3_9BACT
LinkDB: A0A0G0PDR3_9BACT
Original site: A0A0G0PDR3_9BACT 
ID   A0A0G0PDR3_9BACT        Unreviewed;       378 AA.
AC   A0A0G0PDR3;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   03-MAY-2023, entry version 25.
DE   RecName: Full=Phosphoglycerate kinase {ECO:0000256|ARBA:ARBA00013061, ECO:0000256|RuleBase:RU000532};
DE            EC=2.7.2.3 {ECO:0000256|ARBA:ARBA00013061, ECO:0000256|RuleBase:RU000532};
GN   ORFNames=UT57_C0044G0002 {ECO:0000313|EMBL:KKR26058.1};
OS   Microgenomates group bacterium GW2011_GWC1_39_7.
OC   Bacteria.
OX   NCBI_TaxID=1618515 {ECO:0000313|EMBL:KKR26058.1, ECO:0000313|Proteomes:UP000034535};
RN   [1] {ECO:0000313|EMBL:KKR26058.1, ECO:0000313|Proteomes:UP000034535}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA   Wilkins M.J., Williams K.H., Banfield J.F.;
RT   "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT   radiation of phyla.";
RL   Nature 0:0-0(2015).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl
CC         phosphate + ADP; Xref=Rhea:RHEA:14801, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:57604, ChEBI:CHEBI:58272, ChEBI:CHEBI:456216; EC=2.7.2.3;
CC         Evidence={ECO:0000256|ARBA:ARBA00000642,
CC         ECO:0000256|RuleBase:RU000532};
CC   -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC       {ECO:0000256|RuleBase:RU000532}.
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:KKR26058.1}.
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DR   EMBL; LBXH01000044; KKR26058.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G0PDR3; -.
DR   PATRIC; fig|1618515.3.peg.486; -.
DR   Proteomes; UP000034535; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004618; F:phosphoglycerate kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006096; P:glycolytic process; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1260; Phosphoglycerate kinase, N-terminal domain; 2.
DR   InterPro; IPR001576; Phosphoglycerate_kinase.
DR   InterPro; IPR015824; Phosphoglycerate_kinase_N.
DR   InterPro; IPR036043; Phosphoglycerate_kinase_sf.
DR   PANTHER; PTHR11406; PHOSPHOGLYCERATE KINASE; 1.
DR   PANTHER; PTHR11406:SF23; PHOSPHOGLYCERATE KINASE 1, CHLOROPLASTIC-RELATED; 1.
DR   Pfam; PF00162; PGK; 2.
DR   PIRSF; PIRSF000724; Pgk; 2.
DR   PRINTS; PR00477; PHGLYCKINASE.
DR   SUPFAM; SSF53748; Phosphoglycerate kinase; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRSR:PIRSR000724-
KW   2}; Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU000532};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000532}.
FT   BINDING         209
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000724-2"
FT   BINDING         260
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000724-2"
FT   BINDING         326..329
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000724-2"
SQ   SEQUENCE   378 AA;  41805 MW;  A91CD912D1CAE8E8 CRC64;
     MSKFRTVDSV SSLSGKTALL RIDTDIDIEN GRILDDTRLQ SALPTIELLL KKGADVNIVG
     HLGRPKAQFP ISNFQFPISN ENKEFTLEPI AHWLAKKFDG KVEETKIGEL PGWRITPKII
     LLENIRFSEG EEENDLEFAR ELSLLGDIFV NDAFAVSHRE HASIVGVTKY LPSYAGLHLE
     REIEVLSNVL KNPKRPLAVL IGGAKIETKL PLVEAMHHLA DYVLVGGEIA EQDRVLIKVQ
     HEKIAGKKSA VLVSDSTKDG FDITPHSIEN FKQILAQAKT IVWNGPVGKI DQRSKIKDQG
     SGDTERGTME LAEFIVRTKA YKVVGGGDTV SFLRRMNLLN KFDFVSTGGG AMLEFLSGHK
     LPGLQALEAE KDQTHLGQ
//
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