ID   PGK2_PYRAB              Reviewed;         302 AA.
AC   Q9V2C6; G8ZFY3;
DT   26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 94.
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=PYRAB01480;
GN   ORFNames=PAB2253;
OS   Pyrococcus abyssi (strain GE5 / Orsay).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=272844;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GE5 / Orsay;
RX   PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA   Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA   Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA   Weissenbach J., Zivanovic Y., Forterre P.;
RT   "An integrated analysis of the genome of the hyperthermophilic archaeon
RT   Pyrococcus abyssi.";
RL   Mol. Microbiol. 47:1495-1512(2003).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=GE5 / Orsay;
RX   PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA   Gao J., Wang J.;
RT   "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT   Pyrococcus furiosus DSM 3638.";
RL   Curr. Microbiol. 64:118-129(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: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; AJ248283; CAB49072.1; -; Genomic_DNA.
DR   EMBL; HE613800; CCE69524.1; -; Genomic_DNA.
DR   PIR; A75203; A75203.
DR   RefSeq; WP_010867272.1; NC_000868.1.
DR   AlphaFoldDB; Q9V2C6; -.
DR   STRING; 272844.PAB2253; -.
DR   EnsemblBacteria; CAB49072; CAB49072; PAB2253.
DR   GeneID; 1495035; -.
DR   KEGG; pab:PAB2253; -.
DR   PATRIC; fig|272844.11.peg.161; -.
DR   eggNOG; arCOG01967; Archaea.
DR   HOGENOM; CLU_848909_0_0_2; -.
DR   OMA; EMPFSKG; -.
DR   OrthoDB; 57277at2157; -.
DR   PhylomeDB; Q9V2C6; -.
DR   UniPathway; UPA00551; UER00609.
DR   Proteomes; UP000000810; Chromosome.
DR   Proteomes; UP000009139; 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..302
FT                   /note="2-phosphoglycerate kinase"
FT                   /id="PRO_0000156153"
FT   DOMAIN          2..89
FT                   /note="ATP-cone"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00769"
SQ   SEQUENCE   302 AA;  34314 MW;  CB6EF96598CAC2AC CRC64;
     MIRVVEKGSD VALPFSRGIL TRSITSVGID VDLAYSIAIE VQEELTRKGK SIVTKDEIRK
     LTYQKLVEKG FKEEAKRYLF WRRFRKMKVP LLILLGGPTG VGKSTIATEL AFRLGIRSVI
     GTDSIREVLR KVITPELLPT IHTSTFLAWK EIKGTTSGSP IIAGFESQVS AVAVGVNAII
     ERAKREGLNA IIEGIHVVPG FVDVKGEMTF MYMIVARSRE DLEARFYERT RYSKRSANYY
     ISHLDEIMEI QRYLIERARK FGVPVIENIE LEKTIRAIME DIMERTIEAM KKKGLDMLEE
     PK