ID A0A0G0RQ59_9BACT Unreviewed; 369 AA.
AC A0A0G0RQ59;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 03-MAY-2023, entry version 27.
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=UT56_C0011G0017 {ECO:0000313|EMBL:KKR24660.1};
OS Candidatus Levybacteria bacterium GW2011_GWB1_39_7.
OC Bacteria; Candidatus Levybacteria.
OX NCBI_TaxID=1618464 {ECO:0000313|EMBL:KKR24660.1, ECO:0000313|Proteomes:UP000034882};
RN [1] {ECO:0000313|EMBL:KKR24660.1, ECO:0000313|Proteomes:UP000034882}
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:KKR24660.1}.
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DR EMBL; LBXG01000011; KKR24660.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0RQ59; -.
DR STRING; 1618464.UT56_C0011G0017; -.
DR PATRIC; fig|1618464.3.peg.432; -.
DR Proteomes; UP000034882; 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 369 AA; 40767 MW; 8A715E1153AADA69 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 DQGSKIKDQR
SGNTERGTME LAEFIVRTKA YKVVGGGDTV SFLRRMNLLN KFDFVSTGGG AMLEFLSGHK
LPGLQALEA
//
