PGK2_PYRFU
ID PGK2_PYRFU Reviewed; 302 AA.
AC Q8U4K7; O73953;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 81.
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=PF0078;
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 168-302.
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10368153; DOI=10.1128/jb.181.12.3777-3783.1999;
RA Voorhorst W.G., Gueguen Y., Geerling A.C.M., Schut G., Dahlke I., Thomm M.,
RA van der Oost J., de Vos W.M.;
RT "Transcriptional regulation in the hyperthermophilic archaeon Pyrococcus
RT furiosus: coordinated expression of divergently oriented genes in response
RT to beta-linked glucose polymers.";
RL J. Bacteriol. 181:3777-3783(1999).
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; AE009950; AAL80202.1; -; Genomic_DNA.
DR EMBL; AF013169; AAC25559.1; -; Genomic_DNA.
DR RefSeq; WP_011011190.1; NZ_CP023154.1.
DR AlphaFoldDB; Q8U4K7; -.
DR STRING; 186497.PF0078; -.
DR EnsemblBacteria; AAL80202; AAL80202; PF0078.
DR GeneID; 41711866; -.
DR KEGG; pfu:PF0078; -.
DR PATRIC; fig|186497.12.peg.82; -.
DR eggNOG; arCOG01967; Archaea.
DR HOGENOM; CLU_848909_0_0_2; -.
DR OMA; EMPFSKG; -.
DR OrthoDB; 57277at2157; -.
DR PhylomeDB; Q8U4K7; -.
DR UniPathway; UPA00551; UER00609.
DR Proteomes; UP000001013; 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; Reference proteome; Transferase.
FT CHAIN 1..302
FT /note="2-phosphoglycerate kinase"
FT /id="PRO_0000156154"
FT DOMAIN 2..89
FT /note="ATP-cone"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00769"
SQ SEQUENCE 302 AA; 34670 MW; 3D22D6970E9F4617 CRC64;
MIKVIERDGK VRLPFSRGIL TRSITSVGVD VDLAYAIATE VQEELIRQGK KVVTKEEIRN
ITYQKLVEKG FKEEAKRYLF WRRFRKLKIP LIILLGGPTG VGKSTIATEL AFRLGIRSVI
GTDTIREVMR KIITPELLPT IHTSTFLAWK ELRGTVTGSP IIAGFESQVN AVAVGVNAVI
QRAIKEGLNA IIEGIHLVPG FIKIDYEMAF MYMIVARSRE ELEARFYERT RYSKRSAQYY
ISHLDEIMEI QEYLIKKARE YRVPIIENVE LEKTISTIME DIMEKTVEIM KKKGLDMLEE
PK
