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Database: UniProt
Entry: A0A0G1QBB2_9BACT
LinkDB: A0A0G1QBB2_9BACT
Original site: A0A0G1QBB2_9BACT 
ID   A0A0G1QBB2_9BACT        Unreviewed;       269 AA.
AC   A0A0G1QBB2;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   03-MAY-2023, entry version 21.
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=UX21_C0007G0025 {ECO:0000313|EMBL:KKU15023.1};
OS   Microgenomates group bacterium GW2011_GWC2_45_8.
OC   Bacteria.
OX   NCBI_TaxID=1618531 {ECO:0000313|EMBL:KKU15023.1, ECO:0000313|Proteomes:UP000034847};
RN   [1] {ECO:0000313|EMBL:KKU15023.1, ECO:0000313|Proteomes:UP000034847}
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:KKU15023.1}.
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DR   EMBL; LCLI01000007; KKU15023.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G1QBB2; -.
DR   Proteomes; UP000034847; 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; 1.
DR   PRINTS; PR00477; PHGLYCKINASE.
DR   SUPFAM; SSF53748; Phosphoglycerate kinase; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   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}.
SQ   SEQUENCE   269 AA;  30180 MW;  7F97DA93BCD3AF97 CRC64;
     MVNQLRTIKQ ADVRGKRIIV RVDWNVTIGK ALQIVDDTRI VRTLPTIKWV LGHDAKQVIL
     MSHLGKAEER RSLRPISEYA SKLLGEEISF GEESRVMMLE NLRLNAGEDK NDSEFAKQLA
     QYGDVYVNEA FGECHRESAS IVGITKYLPS YAGLWLREEV ETILKVRENP EHPYVVVMGG
     AKVEDKIKLI EVLSEQADTI LLGGKLANPS SLSELRRGTV SMGKARILTP LEKGELLDIG
     EETQKLFAGE IAKAKTVVWN ISNRDRSNL
//
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