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Database: UniProt
Entry: A0A0G1TIQ1_9BACT
LinkDB: A0A0G1TIQ1_9BACT
Original site: A0A0G1TIQ1_9BACT 
ID   A0A0G1TIQ1_9BACT        Unreviewed;       318 AA.
AC   A0A0G1TIQ1;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   03-MAY-2023, entry version 20.
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=UY10_C0050G0004 {ECO:0000313|EMBL:KKU81671.1};
OS   Microgenomates group bacterium GW2011_GWA2_47_8.
OC   Bacteria.
OX   NCBI_TaxID=1618503 {ECO:0000313|EMBL:KKU81671.1, ECO:0000313|Proteomes:UP000034016};
RN   [1] {ECO:0000313|EMBL:KKU81671.1, ECO:0000313|Proteomes:UP000034016}
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:KKU81671.1}.
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DR   EMBL; LCOS01000050; KKU81671.1; -; Genomic_DNA.
DR   PATRIC; fig|1618503.3.peg.737; -.
DR   Proteomes; UP000034016; 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   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   318 AA;  34982 MW;  815F26DB8EC44A84 CRC64;
     MPDITEAHVR GKRVVVRADF NVSLTNDNTI ANDTRIREAI PTIEYLLKKG ASVILLSHLG
     RPKGVQPELS LSCVAKRLEE LLKRPVRFAT DYLNGIPKGD VVLCENVRFH EGEEENDPRF
     AKKLAKLGDV FVNDAFGTAH RAHASTVGVA AYLPSYAGLL LSREVRMISR AAFHPKRPLL
     VIIGGGKTPE KIRVIEKLLD VADTIYLGGA VANTFFATWG IGVGVSRVDH EMIEMARNVL
     WKATRVKSQL LLPSDVMVSN ADRTTLPAAL PYNKVPMGLG IYDIGPHARE ELGAMIKKAK
     TIIWNGPMGL YEDXXXXX
//
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