ID A0A0G1NYX0_9BACT Unreviewed; 376 AA.
AC A0A0G1NYX0;
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=UX39_C0016G0005 {ECO:0000313|EMBL:KKU25884.1};
OS Candidatus Magasanikbacteria bacterium GW2011_GWA2_46_17.
OC Bacteria; Candidatus Magasanikbacteria.
OX NCBI_TaxID=1619042 {ECO:0000313|EMBL:KKU25884.1, ECO:0000313|Proteomes:UP000034175};
RN [1] {ECO:0000313|EMBL:KKU25884.1, ECO:0000313|Proteomes:UP000034175}
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:KKU25884.1}.
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DR EMBL; LCMA01000016; KKU25884.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1NYX0; -.
DR PATRIC; fig|1619042.3.peg.496; -.
DR Proteomes; UP000034175; 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; 1.
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 194
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000724-2"
FT BINDING 306
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000724-2"
FT BINDING 331..334
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000724-2"
SQ SEQUENCE 376 AA; 40987 MW; 36FF777986856FD2 CRC64;
MSFDFKTIDS EAVSPGRTIL LRLDLNLPIV GGRVRDDFRL RRSLPTLEFL KTRGARTVIL
SHIDNKETDS LKLVSEHLKK FVNLEFIQSL KELPERLLAL QPGEFLLLEN LRRNPGEIGN
DPKFAQTLAS FGDIYINDAF SVSHRAHGSI VGIQKFLPSY AGFLFTEEVS HLSRAFNPPK
PFVFVLAGAK FETKFPLVQK FIKLADSVFV GGALANDLFK TKGYEIGLSK HSGADFGFAE
ILHNPKLVLP IDVVTENTGK KTTKMATAVL SDDTIFDAGP KTVAMLAEKF ASAKFILWNG
TLGAYENGFA EGTEALARAI VKSGAESIVG GGDTLACVSK LNILDEFSFV STGGGAMLEF
LANETLPGIE ALKRSV
//
