ID A0A0G1KGR7_9BACT Unreviewed; 357 AA.
AC A0A0G1KGR7;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 03-MAY-2023, entry version 24.
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=UW79_C0002G0007 {ECO:0000313|EMBL:KKT82690.1};
OS Candidatus Yanofskybacteria bacterium GW2011_GWA2_44_9.
OC Bacteria; Candidatus Yanofskybacteria.
OX NCBI_TaxID=1619025 {ECO:0000313|EMBL:KKT82690.1, ECO:0000313|Proteomes:UP000034032};
RN [1] {ECO:0000313|EMBL:KKT82690.1, ECO:0000313|Proteomes:UP000034032}
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:KKT82690.1}.
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DR EMBL; LCJR01000002; KKT82690.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1KGR7; -.
DR PATRIC; fig|1619025.3.peg.68; -.
DR Proteomes; UP000034032; 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; 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 187
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000724-2"
FT BINDING 286
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000724-2"
FT BINDING 312..315
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000724-2"
SQ SEQUENCE 357 AA; 38674 MW; 8623B5F835FA3282 CRC64;
MLRTINNIGT LKGKKVLLRT DFDVPVAKEE VTEPFRIQKQ KKTIDHLLAG GARVAMAAHI
ASLPSFQSVM PQIEKILGRK VRLIGEISDF HNADESLCLL DNVRRYSGEE KNDMKFSKDL
AKRFDIYVNN AFAVCHRNHA SVSGVTEFLK SYAGFIVEEE VRELGKCLDA PMAGKVVIMG
GAKASTKIPV IKNFINKAEK ILVAGVIAND ILKEKGTNVL GSVADSDSKQ LLSGLDMDSS
KLVLPEDFNE FEGRFLDIGP KTISNYVAII NGAKMIIWNG PMGVFEDSRF SGGTEAVAKA
IAGSGAFKVV GGGDSVAAMN KFNILDKFDF VSTGGGAMLE FLAGDRLPGL AKLGYYE
//
