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Database: UniProt
Entry: A0A0G0LYG1_9BACT
LinkDB: A0A0G0LYG1_9BACT
Original site: A0A0G0LYG1_9BACT 
ID   A0A0G0LYG1_9BACT        Unreviewed;       320 AA.
AC   A0A0G0LYG1;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   03-MAY-2023, entry version 31.
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=UT22_C0041G0001 {ECO:0000313|EMBL:KKQ96082.1};
OS   Parcubacteria group bacterium GW2011_GWC2_39_11.
OC   Bacteria.
OX   NCBI_TaxID=1618921 {ECO:0000313|EMBL:KKQ96082.1, ECO:0000313|Proteomes:UP000034836};
RN   [1] {ECO:0000313|EMBL:KKQ96082.1, ECO:0000313|Proteomes:UP000034836}
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:KKQ96082.1}.
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DR   EMBL; LBVZ01000041; KKQ96082.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G0LYG1; -.
DR   PATRIC; fig|1618921.3.peg.716; -.
DR   Proteomes; UP000034836; 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; 4.
DR   InterPro; IPR001576; Phosphoglycerate_kinase.
DR   InterPro; IPR015911; Phosphoglycerate_kinase_CS.
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; 3.
DR   PRINTS; PR00477; PHGLYCKINASE.
DR   SUPFAM; SSF53748; Phosphoglycerate kinase; 1.
DR   PROSITE; PS00111; PGLYCERATE_KINASE; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   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}.
SQ   SEQUENCE   320 AA;  35317 MW;  1E45A2A9886BB0FC CRC64;
     MKTVKDFNVK NKRVLVRCDF NVPLDKKGNI TDDFRIRQTL PTLRYLQENG AKLVLASHFA
     DGKCLDHVWK IVKEFIGEKD IVFLENLRLN KGEEENSNNF AKELADLADI YINDAFGVCH
     RTHASVVGVP KYLPSGAGFL LKKETSILSR IMQNPDRPFV AIIGGVKFES KAKVIDGFLR
     VADFVLTGGK IGFSHEVKKL NFSKLVLPVD NIDTFDIGPE TIKLFSEKIS KGKTIIWAGP
     MGLFEEPAFE KGTKEIGKAI CGNKKAFKVA GGGDTVLAIN KFGLQDKFDH LSTGGGAMLE
     FIAGEKLPGL EVLGYYSNNS
//
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