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Database: UniProt
Entry: A0A0G0MR15_9BACT
LinkDB: A0A0G0MR15_9BACT
Original site: A0A0G0MR15_9BACT 
ID   A0A0G0MR15_9BACT        Unreviewed;       332 AA.
AC   A0A0G0MR15;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   03-MAY-2023, entry version 19.
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=UT26_C0016G0006 {ECO:0000313|EMBL:KKR02881.1};
OS   Microgenomates group bacterium GW2011_GWC1_39_12.
OC   Bacteria.
OX   NCBI_TaxID=1618514 {ECO:0000313|EMBL:KKR02881.1, ECO:0000313|Proteomes:UP000034167};
RN   [1] {ECO:0000313|EMBL:KKR02881.1, ECO:0000313|Proteomes:UP000034167}
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:KKR02881.1}.
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DR   EMBL; LBWD01000016; KKR02881.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G0MR15; -.
DR   Proteomes; UP000034167; 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   PRINTS; PR00477; PHGLYCKINASE.
DR   SUPFAM; SSF53748; Phosphoglycerate 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   332 AA;  37054 MW;  79CBBF00C2F15E57 CRC64;
     MKLRSVNEVP ENSKVILRMD LDVPMYEGKI EDPDRLKKSL PTIKLLLDKH CKICVIGHLG
     RPKGNDQSLS LHPVYEALIS LIEEYQKMSV SHQFIKDIEN YELCDVSVLE NIRFWSGEES
     NDAEFLKVLI KISNCYVNDA LTVAHRKHRS VMLFKELPAY YGVAFISEVE KILTVTQNPQ
     KPITIILGGA KEDKLSYLPS LIPIADYICI GGKLPLFISQ KQGDKIYVAK LREDKLDLSD
     DDIQEFKKYI ALSKTIIWSG ALGFFEKEDA RKGTLAIARA IAESSAYTII AGGDTKASVS
     HIGVEDKINL IASGGGMLLE LLTKGTLPAW EA
//
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