ID A0A0G1KAE2_9BACT Unreviewed; 374 AA.
AC A0A0G1KAE2;
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=UW75_C0002G0003 {ECO:0000313|EMBL:KKT80575.1};
OS Parcubacteria group bacterium GW2011_GWF2_44_8.
OC Bacteria.
OX NCBI_TaxID=1618971 {ECO:0000313|EMBL:KKT80575.1, ECO:0000313|Proteomes:UP000034896};
RN [1] {ECO:0000313|EMBL:KKT80575.1, ECO:0000313|Proteomes:UP000034896}
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:KKT80575.1}.
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DR EMBL; LCJN01000002; KKT80575.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1KAE2; -.
DR PATRIC; fig|1618971.3.peg.6; -.
DR Proteomes; UP000034896; 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 374 AA; 40669 MW; A299F8F2CF12FBD6 CRC64;
MELKSIVEAG ELRGKVVLVR ASCNVPLIDG KVRNSFRLRR ALPTLKYLKE AGAKVIVISH
IGREVEETLL PVYEELAASI DMQWGGKVTE PLFAEKKAAL EDGDILFCEN LRQDVREEEN
SPELAALLAE GVDIYVNDAF AEAHREHAST YGVAKLLPAY AGLTLLEEVT ELQKVMQPNH
PSLFLLGGAK FETKMPLVEK YLALYDHVLV GGALANDVLK ARGLEVGQSL VSEISLKDAS
FLWSEKMIVP VDVVVEGPRG VVTKPADQVL PDEKIFDMGP QTVELITRYI AEAKTILWNG
PFGNYEAGFE ESTEEVAKLI AASSAFSVLG GGDTVAAVEK LGLNEQFGFI SIGGGSMLTF
MEHGSTPVLD VLKK
//
