ID A0A0G0F7C2_9BACT Unreviewed; 350 AA.
AC A0A0G0F7C2;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 03-MAY-2023, entry version 22.
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=US27_C0008G0010 {ECO:0000313|EMBL:KKQ13827.1};
OS Candidatus Moranbacteria bacterium GW2011_GWF1_36_78.
OC Bacteria; Candidatus Moranbacteria.
OX NCBI_TaxID=1618718 {ECO:0000313|EMBL:KKQ13827.1, ECO:0000313|Proteomes:UP000034485};
RN [1] {ECO:0000313|EMBL:KKQ13827.1, ECO:0000313|Proteomes:UP000034485}
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:KKQ13827.1}.
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DR EMBL; LBSI01000008; KKQ13827.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0F7C2; -.
DR PATRIC; fig|1618718.3.peg.599; -.
DR Proteomes; UP000034485; 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 199
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000724-2"
FT BINDING 275
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000724-2"
SQ SEQUENCE 350 AA; 39032 MW; 27343BB08FDDC0AF CRC64;
MKKIQDANLE NKKVLLRVDF NVALKNGRIK EKFKIEACKE TVKFLLEKNC QVALISHLGR
PEGKINPEFS LRQITDDVES ILGLKVRFIS DCISEEIRNN LENLSDGEII LLENVRFYEG
DEDNDIEFSK KLAKGFDIFV NDAFSASHRD HASVSGVAKL IPSFAGLRLQ KEIHEMERVK
NDFARPAVAI IGGAKIETKL PVIKFFEEKY DNILVGGKIA NEALDQKKEF SEKVILPFDF
IDDRLDIGPK TLEKFKEIIS NAKTIVWNGP TGKFEDEKYA VSSNEIMKAV LNSGAYTVVG
GGETLEILEK NNATDRIDFV STGGGAMLDY LGGGEMPGIE VLSEPLIITD
//
