ID F0LJG2_THEBM Unreviewed; 299 AA.
AC F0LJG2;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=2-phosphoglycerate kinase {ECO:0000256|HAMAP-Rule:MF_00769};
DE Short=2PGK {ECO:0000256|HAMAP-Rule:MF_00769};
DE EC=2.7.2.16 {ECO:0000256|HAMAP-Rule:MF_00769};
GN Name=pgk2 {ECO:0000256|HAMAP-Rule:MF_00769};
GN OrderedLocusNames=TERMP_00451 {ECO:0000313|EMBL:ADT83428.1};
OS Thermococcus barophilus (strain DSM 11836 / MP).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=391623 {ECO:0000313|EMBL:ADT83428.1, ECO:0000313|Proteomes:UP000007478};
RN [1] {ECO:0000313|EMBL:ADT83428.1, ECO:0000313|Proteomes:UP000007478}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11836 / MP {ECO:0000313|Proteomes:UP000007478};
RX PubMed=21217005; DOI=10.1128/JB.01490-10;
RA Vannier P., Marteinsson V.T., Fridjonsson O.H., Oger P., Jebbar M.;
RT "Complete genome sequence of the hyperthermophilic, piezophilic,
RT heterotrophic, and carboxydotrophic archaeon Thermococcus barophilus MP.";
RL J. Bacteriol. 193:1481-1482(2011).
CC -!- FUNCTION: Catalyzes the phosphorylation of 2-phosphoglycerate to 2,3-
CC diphosphoglycerate. Involved in the biosynthesis of cyclic 2,3-
CC bisphosphoglycerate, a thermoprotectant. {ECO:0000256|HAMAP-
CC Rule:MF_00769}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-2-phosphoglycerate + ATP = (2R)-2,3-bisphosphoglycerate +
CC ADP + H(+); Xref=Rhea:RHEA:42408, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58248, ChEBI:CHEBI:58289,
CC ChEBI:CHEBI:456216; EC=2.7.2.16; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_00769};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00769};
CC -!- PATHWAY: Thermoadapter biosynthesis; cyclic 2,3-diphosphoglycerate
CC biosynthesis; cyclic 2,3-diphosphoglycerate from 2-phospho-D-glycerate:
CC step 1/2. {ECO:0000256|HAMAP-Rule:MF_00769}.
CC -!- SIMILARITY: Belongs to the 2-phosphoglycerate kinase family.
CC {ECO:0000256|HAMAP-Rule:MF_00769}.
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DR EMBL; CP002372; ADT83428.1; -; Genomic_DNA.
DR RefSeq; WP_013466726.1; NC_014804.1.
DR AlphaFoldDB; F0LJG2; -.
DR GeneID; 10040769; -.
DR KEGG; tba:TERMP_00451; -.
DR PATRIC; fig|391623.17.peg.451; -.
DR eggNOG; arCOG01967; Archaea.
DR HOGENOM; CLU_848909_0_0_2; -.
DR OrthoDB; 358692at2157; -.
DR UniPathway; UPA00551; UER00609.
DR Proteomes; UP000007478; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016774; F:phosphotransferase activity, carboxyl group as acceptor; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_00769; 2PGK; 1.
DR InterPro; IPR020872; 2PKG.
DR InterPro; IPR005144; ATP-cone_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR33477; P-LOOP NTPASE DOMAIN-CONTAINING PROTEIN LPA1 HOMOLOG 1; 1.
DR PANTHER; PTHR33477:SF3; P-LOOP NTPASE DOMAIN-CONTAINING PROTEIN LPA1 HOMOLOG 2; 1.
DR Pfam; PF03477; ATP-cone; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51161; ATP_CONE; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00769};
KW Kinase {ECO:0000256|HAMAP-Rule:MF_00769, ECO:0000313|EMBL:ADT83428.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00769}; Reference proteome {ECO:0000313|Proteomes:UP000007478};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00769}.
FT DOMAIN 2..89
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
SQ SEQUENCE 299 AA; 34689 MW; 625028DBB1EF4A72 CRC64;
MIIVIDKERK TELPFSRGIL TRSITSAGVE VGIAYSIATE VMKHFMEMRK KKVTKDDIRE
ITYEKLVEHG LKEEAKRYLF WRRLKKLKFP MIILIGGTTG VGKSTISTEL AFRLGMRTII
GTDTVREVMR KIIAKELIPA IHTSSFLAWK EIENFPKGVS PLIYGFETQV RHVAVGVNAV
IERSYTEGFN TIIEGIHLVP GYIKLNDRSF MYLIVVKDKD SLKARFYERT RYSLRPAEYY
LKNLDEIMEI QEFLIEKAKE HGIPIIENVE LEKTVNAIME RLMEEVLGRL KERGIEIWE
//
