ID A0A0G0ZD69_9BACT Unreviewed; 336 AA.
AC A0A0G0ZD69;
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=UV11_C0027G0008 {ECO:0000313|EMBL:KKS46647.1};
OS Candidatus Giovannonibacteria bacterium GW2011_GWF2_42_19.
OC Bacteria; Candidatus Giovannonibacteria.
OX NCBI_TaxID=1618659 {ECO:0000313|EMBL:KKS46647.1, ECO:0000313|Proteomes:UP000034036};
RN [1] {ECO:0000313|EMBL:KKS46647.1, ECO:0000313|Proteomes:UP000034036}
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:KKS46647.1}.
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DR EMBL; LCDF01000027; KKS46647.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0ZD69; -.
DR STRING; 1618659.UV11_C0027G0008; -.
DR PATRIC; fig|1618659.3.peg.794; -.
DR Proteomes; UP000034036; 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 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 192
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000724-2"
FT BINDING 271
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000724-2"
FT BINDING 296..299
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000724-2"
SQ SEQUENCE 336 AA; 37793 MW; 29B5057DDC206184 CRC64;
MLSLDKADLK NKKVLVRVDF NVMPFTPREP RIINSLETIR FLMRKKARVI LITHLETNEG
KIPSALKLAK WMRERYFRKL IFVPDLIGDK AEAAVSRVKP GEILMLENLR IDPREKACKI
VFAKRLASFA DIYINEAFAA SHRNHASIVL LPKFLPSYFG FRYEQEINVL SQAFKPPHPL
VLILGGGKVD TKLPLLKAML PKIDKALLGG VIANKFLEKP IIKSPKIILP IDVVRVGDKI
WDDGPETFKE WKKIINKAKL VIWNGPLGFV ENGYVKGTKT LVLILAKTRA RVIIGGGDTT
DYLPKKLPKN IFVSTGGGAM LEFLVKKTLP GIEAIK
//
