PGK2_THEKO
ID PGK2_THEKO Reviewed; 290 AA.
AC Q5JDW9;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 85.
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=TK1038;
OS Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS (Pyrococcus kodakaraensis (strain KOD1)).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=69014;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX PubMed=15710748; DOI=10.1101/gr.3003105;
RA Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL Genome Res. 15:352-363(2005).
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, ECO:0000305}.
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DR EMBL; AP006878; BAD85227.1; -; Genomic_DNA.
DR RefSeq; WP_011249989.1; NC_006624.1.
DR AlphaFoldDB; Q5JDW9; -.
DR STRING; 69014.TK1038; -.
DR EnsemblBacteria; BAD85227; BAD85227; TK1038.
DR GeneID; 3234388; -.
DR KEGG; tko:TK1038; -.
DR PATRIC; fig|69014.16.peg.1015; -.
DR eggNOG; arCOG01967; Archaea.
DR HOGENOM; CLU_848909_0_0_2; -.
DR InParanoid; Q5JDW9; -.
DR OMA; EMPFSKG; -.
DR OrthoDB; 57277at2157; -.
DR PhylomeDB; Q5JDW9; -.
DR UniPathway; UPA00551; UER00609.
DR Proteomes; UP000000536; 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..290
FT /note="2-phosphoglycerate kinase"
FT /id="PRO_0000156156"
FT DOMAIN 1..89
FT /note="ATP-cone"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00769"
SQ SEQUENCE 290 AA; 33291 MW; 150C48DBDB579446 CRC64;
MIIVTDSERK IRLPFSRGIL TRSITLAGID VGIAYAIATE VQKELEWKGK KSVTTEEIRE
LTYQKLLEKG LREEAKRYLF WRELRRRKVR LTVLLGGATG VGKSTIATEL AFRLGIRSII
GTDTIREVMR KIIAKELLPD IHVSSFLAER VVKAPKNSDP LIYGFETQVK HVSVGIKAVL
ERARREGLNT LIEGIHVVPG FVEPREDEFM YVIAVPKKDY LIAHFYERAR YSQRDAEKYV
KHVDRIMRIQ DYLVERAREH GIPVIENVEL ESTVSTILAD MMKKLEEMGV
