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
//