ID   PGK2_PYRHO              Reviewed;         301 AA.
AC   O57882;
DT   26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=2-phosphoglycerate kinase {ECO:0000255|HAMAP-Rule:MF_00769};
DE            Short=2PGK {ECO:0000255|HAMAP-Rule:MF_00769};
DE            EC=2.7.2.16 {ECO:0000255|HAMAP-Rule:MF_00769};
GN   Name=pgk2 {ECO:0000255|HAMAP-Rule:MF_00769}; OrderedLocusNames=PH0149;
OS   Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS   100139 / OT-3).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=70601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX   PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA   Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA   Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA   Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA   Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA   Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT   "Complete sequence and gene organization of the genome of a hyper-
RT   thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL   DNA Res. 5:55-76(1998).
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:0000255|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:0000255|HAMAP-
CC         Rule:MF_00769};
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000255|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:0000255|HAMAP-Rule:MF_00769}.
CC   -!- SIMILARITY: Belongs to the 2-phosphoglycerate kinase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00769}.
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DR   EMBL; BA000001; BAA29218.1; -; Genomic_DNA.
DR   PIR; C71236; C71236.
DR   RefSeq; WP_010884260.1; NC_000961.1.
DR   AlphaFoldDB; O57882; -.
DR   STRING; 70601.3256535; -.
DR   PRIDE; O57882; -.
DR   EnsemblBacteria; BAA29218; BAA29218; BAA29218.
DR   GeneID; 1444042; -.
DR   KEGG; pho:PH0149; -.
DR   eggNOG; arCOG01967; Archaea.
DR   OMA; EMPFSKG; -.
DR   OrthoDB; 57277at2157; -.
DR   UniPathway; UPA00551; UER00609.
DR   Proteomes; UP000000752; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; -; 1.
DR   HAMAP; MF_00769; 2PGK; 1.
DR   InterPro; IPR020872; 2PKG.
DR   InterPro; IPR005144; ATP-cone_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF03477; ATP-cone; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS51161; ATP_CONE; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Kinase; Nucleotide-binding; Transferase.
FT   CHAIN           1..301
FT                   /note="2-phosphoglycerate kinase"
FT                   /id="PRO_0000156155"
FT   DOMAIN          2..89
FT                   /note="ATP-cone"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00769"
SQ   SEQUENCE   301 AA;  34261 MW;  F0E270E39A160654 CRC64;
     MIRVIEKGDK VSLPFSRGIL TRSITSVGID VDLAYSIAIE VQEELVKKGK TIVTKDEIRK
     LTYQKLIEKG FKEEAKRYIF WRRFRKMKVP LIILLGGPTG VGKSTIATEL AFRLGIRSVI
     GTDSIREVLR KIITPELLPT IHTSTFLAWK ELKGTVTDSP IVAGFESQVS AVTVGINAII
     ERAVREGLNA IIEGIHVVPG FVKVEGEMTF MYMLIARSRE DLEARFYERT RYSKRPADYY
     ISHLDEILEI QDYLIRRAKK FNVPVIENVE LEETVSKIME DIMQKTIEIM KGKGLDLLEE
     P