GCK_PICTO
ID GCK_PICTO Reviewed; 415 AA.
AC Q6KZ25;
DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Glycerate 2-kinase;
DE Short=GCK;
DE EC=2.7.1.165 {ECO:0000269|PubMed:16684110};
DE AltName: Full=2-phosphoglycerate forming glycerate kinase {ECO:0000303|PubMed:16684110};
GN Name=gck; OrderedLocusNames=PTO1442;
OS Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC
OS 100828).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Picrophilaceae; Picrophilus.
OX NCBI_TaxID=263820;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828;
RX PubMed=15184674; DOI=10.1073/pnas.0401356101;
RA Fuetterer O., Angelov A., Liesegang H., Gottschalk G., Schleper C.,
RA Schepers B., Dock C., Antranikian G., Liebl W.;
RT "Genome sequence of Picrophilus torridus and its implications for life
RT around pH 0.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9091-9096(2004).
RN [2]
RP FUNCTION AS A GLYCERATE KINASE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, COFACTOR, SUBSTRATE SPECIFICITY, SUBUNIT, AND NOMENCLATURE.
RX PubMed=16684110; DOI=10.1111/j.1574-6968.2006.00264.x;
RA Reher M., Bott M., Schonheit P.;
RT "Characterization of glycerate kinase (2-phosphoglycerate forming), a key
RT enzyme of the nonphosphorylative Entner-Doudoroff pathway, from the
RT thermoacidophilic euryarchaeon Picrophilus torridus.";
RL FEMS Microbiol. Lett. 259:113-119(2006).
CC -!- FUNCTION: Catalyzes the ATP-dependent phosphorylation of D-glycerate to
CC 2-phosphoglycerate. It can also partially utilize GTP, CTP or UTP as
CC phosphate donor. {ECO:0000269|PubMed:16684110}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-glycerate + ATP = (2R)-2-phosphoglycerate + ADP + H(+);
CC Xref=Rhea:RHEA:27377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16659,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58289, ChEBI:CHEBI:456216;
CC EC=2.7.1.165; Evidence={ECO:0000269|PubMed:16684110};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:16684110};
CC Name=Ni(2+); Xref=ChEBI:CHEBI:49786;
CC Evidence={ECO:0000269|PubMed:16684110};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:16684110};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000269|PubMed:16684110};
CC Note=Magnesium. It could be replaced to some extent by nickel,
CC manganese or cobalt. {ECO:0000269|PubMed:16684110};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=340 uM for glycerate (at 50 degrees Celsius and at pH 7.3)
CC {ECO:0000269|PubMed:16684110};
CC KM=500 uM for ATP (at 50 degrees Celsius and at pH 7.3)
CC {ECO:0000269|PubMed:16684110};
CC Vmax=435 umol/min/mg enzyme (at 50 degrees Celsius and at pH 7.3)
CC {ECO:0000269|PubMed:16684110};
CC pH dependence:
CC Optimum pH is 7.3 and 50% of activity at pH 5.6 and at pH 8.6.
CC {ECO:0000269|PubMed:16684110};
CC Temperature dependence:
CC Optimum temperature is 60 degrees Celsius. It does not lose activity
CC upon incubation at 60 degrees Celsius for 2 h. The half time at 70
CC degrees Celsius is about 5 min. {ECO:0000269|PubMed:16684110};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16684110}.
CC -!- SIMILARITY: Belongs to the glycerate kinase type-1 family.
CC {ECO:0000305}.
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DR EMBL; AE017261; AAT44027.1; -; Genomic_DNA.
DR RefSeq; WP_011178243.1; NC_005877.1.
DR AlphaFoldDB; Q6KZ25; -.
DR SMR; Q6KZ25; -.
DR STRING; 263820.PTO1442; -.
DR EnsemblBacteria; AAT44027; AAT44027; PTO1442.
DR GeneID; 2844855; -.
DR KEGG; pto:PTO1442; -.
DR PATRIC; fig|263820.9.peg.1496; -.
DR eggNOG; arCOG04170; Archaea.
DR HOGENOM; CLU_032279_1_1_2; -.
DR OMA; GKAAWRM; -.
DR OrthoDB; 53827at2157; -.
DR SABIO-RK; Q6KZ25; -.
DR Proteomes; UP000000438; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0043798; F:glycerate 2-kinase activity; IDA:UniProtKB.
DR GO; GO:0008887; F:glycerate kinase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.1480.10; -; 1.
DR Gene3D; 3.40.50.10180; -; 1.
DR InterPro; IPR037035; GK-like_C_sf.
DR InterPro; IPR038614; GK_N_sf.
DR InterPro; IPR007835; MOFRL.
DR InterPro; IPR025286; MOFRL_assoc_dom.
DR InterPro; IPR039760; MOFRL_protein.
DR PANTHER; PTHR12227; PTHR12227; 1.
DR Pfam; PF13660; DUF4147; 1.
DR Pfam; PF05161; MOFRL; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Kinase; Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..415
FT /note="Glycerate 2-kinase"
FT /id="PRO_0000415149"
FT BINDING 57
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 415 AA; 46644 MW; 0AD8284AD879A76C CRC64;
MIENYNDIAI TDTRRKILNI IDKTLIAMDP ENAIKNFIEK NNIKFDSKRI FLIGFGKAAF
KMYSGIRPFI LKDLVYASII VPDDEKTNDY NELRILRGTH PFTGDLSVSS SISMLSGLKN
LNENDLVIVL ISGGGSSLFE IPEDGINIDD IKNISKTMMD KGCDIYELNM VRSMLSKVKG
GKLATMLYPA RVISFIISDV KNDDLSIIAS GPLTRIDYRI EDLMETIKKY LGNDERIKMY
RNIDDIYFNN VKQYIILKNR DFLDYIYSNI NDDAVNLGSN FSGNVEDLSL ILHNILKNIY
SSKRKPFYFM LGGETTVDVK GHGSGGRNQE LVLRFMKNSS NSEVYTIASF GTDGIDGVSP
AAGGIVDSDH EIDNINEYLN RNDSYNLLIK NHGAIITGRT GNNVSDIIIG LYYNK
