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Database: UniProt
Entry: A0A0G1XYN6_9BACT
LinkDB: A0A0G1XYN6_9BACT
Original site: A0A0G1XYN6_9BACT 
ID   A0A0G1XYN6_9BACT        Unreviewed;       378 AA.
AC   A0A0G1XYN6;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   03-MAY-2023, entry version 26.
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=UY83_C0001G0031 {ECO:0000313|EMBL:KKW36000.1};
OS   Candidatus Adlerbacteria bacterium GW2011_GWA1_54_10.
OC   Bacteria; Candidatus Adlerbacteria.
OX   NCBI_TaxID=1618605 {ECO:0000313|EMBL:KKW36000.1, ECO:0000313|Proteomes:UP000034740};
RN   [1] {ECO:0000313|EMBL:KKW36000.1, ECO:0000313|Proteomes:UP000034740}
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:KKW36000.1}.
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DR   EMBL; LCRO01000001; KKW36000.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G1XYN6; -.
DR   PATRIC; fig|1618605.3.peg.32; -.
DR   Proteomes; UP000034740; 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; 1.
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         179
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000724-2"
FT   BINDING         293
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000724-2"
FT   BINDING         318..321
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000724-2"
SQ   SEQUENCE   378 AA;  40864 MW;  B40FA87B3B1D8428 CRC64;
     MPEIRDIKDA DIENKRTLVR VDFDVPIAEG RILDDVRIKA VIPTLELLHE SGAAKITLIA
     HLGRPNGKTV ESLRLVPVEA RLRELTKVPF EMRENLRFDP REEANDENFA KELAALGDIY
     VNEAFADSHR AHASIVGVPK FLPSYAGLRF MKEVDKLREA QTPPVGSVAV IGGAKFETKE
     PLLRNLLSAY SQVLLGGALA DDVLKARGMP VGESLVAEVG VPTELAGSER ILVPADVYLE
     EEDDKGSARA AMTGDVRKEE RIVDIGPSTA ATWAQKISEA PFVLWNGPMG IYEEGYRAGT
     DALAVALIKG GARAIVGGGD TLAALRSIQD STLKQGSSRP DLDEIEKSGR IFFSMGGGAM
     LKYLAEGTLP GLEALTRR
//
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