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Database: UniProt
Entry: A0A0G0SXE5_9BACT
LinkDB: A0A0G0SXE5_9BACT
Original site: A0A0G0SXE5_9BACT 
ID   A0A0G0SXE5_9BACT        Unreviewed;       320 AA.
AC   A0A0G0SXE5;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   03-MAY-2023, entry version 23.
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=UT62_C0017G0007 {ECO:0000313|EMBL:KKR30267.1};
OS   Parcubacteria group bacterium GW2011_GWC1_39_8.
OC   Bacteria.
OX   NCBI_TaxID=1618901 {ECO:0000313|EMBL:KKR30267.1, ECO:0000313|Proteomes:UP000034632};
RN   [1] {ECO:0000313|EMBL:KKR30267.1, ECO:0000313|Proteomes:UP000034632}
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:KKR30267.1}.
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DR   EMBL; LBXM01000017; KKR30267.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G0SXE5; -.
DR   PATRIC; fig|1618901.3.peg.299; -.
DR   Proteomes; UP000034632; 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; 3.
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   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   320 AA;  35400 MW;  1369C9D49B5F179E CRC64;
     MKSIKEIGDV KGKRVLVRLD WSVPTQDGKV VSDYQIKKSF PTIEYLQKAG AKIILLSHAE
     KDEDSLLPIF KYVKNFLPLT FIEPSDLVLL ENLRRDKREK ENSEEFSRKL ADLGDVFINE
     AFPVSHRKHA SVVGIPKFLP SFAGFQFLEE VKNLSTAFHP EHPFFFILGG AKPETKLPLI
     EKFMGIADYI FIGGTLAKSA KEMDLTGDSK IIFPVGDIAA PDINKDTLNL FEEKISQSKF
     IIWNGPLGDY EKGFKGGTLS LAKILADSGK RVIVGGGDTL TIIEELDILD KFSFVSTGGG
     AMLDFLAKGT LPGIEALNTE
//
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