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Database: UniProt
Entry: A0A0G0LPR0_9BACT
LinkDB: A0A0G0LPR0_9BACT
Original site: A0A0G0LPR0_9BACT 
ID   A0A0G0LPR0_9BACT        Unreviewed;       324 AA.
AC   A0A0G0LPR0;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   03-MAY-2023, entry version 23.
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=UT11_C0016G0010 {ECO:0000313|EMBL:KKQ89960.1};
OS   Berkelbacteria bacterium GW2011_GWA2_38_9.
OC   Bacteria; Candidatus Berkelbacteria.
OX   NCBI_TaxID=1618334 {ECO:0000313|EMBL:KKQ89960.1, ECO:0000313|Proteomes:UP000033934};
RN   [1] {ECO:0000313|EMBL:KKQ89960.1, ECO:0000313|Proteomes:UP000033934}
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:KKQ89960.1}.
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DR   EMBL; LBVO01000016; KKQ89960.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G0LPR0; -.
DR   PATRIC; fig|1618334.3.peg.290; -.
DR   Proteomes; UP000033934; 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   324 AA;  35705 MW;  CD7ED0C97CB6C700 CRC64;
     MILSHLGRPD GIYIPGLSLR PVAEYLATVF KHIPLSFTDE LISMQVRQKM AHIRSGEILV
     LGNTRFMREE ENDNERFAAE IARYGEIYIN DAFAVCHREQ ASVHAITQFL PSYPGLMLES
     ELAHLNKLLT EGTNRPYIAI IGGAKIKDKI TALGNLLPKI DKVLVGGAMA NTFLRAAGNK
     VGQSVFDQGQ LYYAERLLNQ FSDKIVLPTD YVSDIDDDEK FRILDIGQET INNYKQIISQ
     AKTVFWTGDM GVAERHEYAR GTQEVAQAIK ASGAYSVLAG GDTISAVRNW QMDAGFDYIS
     SGGGATLAYL AGEKLPGLVA LKLQ
//
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