ID I3RC04_9EURY Unreviewed; 301 AA.
AC I3RC04;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 51.
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 ORFNames=Py04_0159 {ECO:0000313|EMBL:AFK21764.1};
OS Pyrococcus sp. ST04.
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=1183377 {ECO:0000313|EMBL:AFK21764.1, ECO:0000313|Proteomes:UP000006467};
RN [1] {ECO:0000313|EMBL:AFK21764.1, ECO:0000313|Proteomes:UP000006467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ST04 {ECO:0000313|EMBL:AFK21764.1,
RC ECO:0000313|Proteomes:UP000006467};
RX PubMed=22843576; DOI=10.1128/JB.00824-12;
RA Jung J.H., Lee J.H., Holden J.F., Seo D.H., Shin H., Kim H.Y., Kim W.,
RA Ryu S., Park C.S.;
RT "Complete Genome Sequence of the Hyperthermophilic Archaeon Pyrococcus sp.
RT Strain ST04, Isolated from a Deep-Sea Hydrothermal Sulfide Chimney on the
RT Juan de Fuca Ridge.";
RL J. Bacteriol. 194:4434-4435(2012).
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; CP003534; AFK21764.1; -; Genomic_DNA.
DR RefSeq; WP_014733290.1; NC_017946.1.
DR AlphaFoldDB; I3RC04; -.
DR STRING; 1183377.Py04_0159; -.
DR GeneID; 13021382; -.
DR KEGG; pys:Py04_0159; -.
DR eggNOG; arCOG01967; Archaea.
DR HOGENOM; CLU_848909_0_0_2; -.
DR OrthoDB; 358692at2157; -.
DR UniPathway; UPA00551; UER00609.
DR Proteomes; UP000006467; 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; 1.
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:AFK21764.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00769};
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 301 AA; 34330 MW; ACDF195EB8C884DE CRC64;
MIRVVEKDGK IALPFSRGIL TRSITSVGID VDLAYAIAIE VQEELKKGGK TIVTKDEIRR
LTYQKLIEKG FKEEARRYLF WRRFRKMKIP LIILLGGPTG VGKSTIATEL AFRLGIRSVI
GTDTIREVMR KIITPELLPT IHTSTFLAWK ELKGTVEGSP IIAGFESQVS AVTVGINAVI
QRARREGLNA IIEGIHVVPG FVDMKHEMTF MYMIVAKSRE DLEARFYERT RYSKRSAEYY
ISHLDSIMEI QEYLIGKARE HNVPIIENIE LESTIAKIMQ DIMEKTLEIM KKKGLDMLEE
P
//
