GCK_SULTO
ID GCK_SULTO Reviewed; 399 AA.
AC Q96YZ3;
DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Glycerate 2-kinase;
DE Short=GCK;
DE EC=2.7.1.165 {ECO:0000269|PubMed:19690808};
DE AltName: Full=2-phosphoglycerate forming glycerate kinase;
GN Name=gck; OrderedLocusNames=STK_20370;
OS Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
OS (Sulfolobus tokodaii).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfurisphaera.
OX NCBI_TaxID=273063;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16993 / JCM 10545 / NBRC 100140 / 7;
RX PubMed=11572479; DOI=10.1093/dnares/8.4.123;
RA Kawarabayasi Y., Hino Y., Horikawa H., Jin-no K., Takahashi M., Sekine M.,
RA Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y.,
RA Nishijima K., Otsuka R., Nakazawa H., Takamiya M., Kato Y., Yoshizawa T.,
RA Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K.,
RA Masuda S., Yanagii M., Nishimura M., Yamagishi A., Oshima T., Kikuchi H.;
RT "Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon,
RT Sulfolobus tokodaii strain7.";
RL DNA Res. 8:123-140(2001).
RN [2]
RP FUNCTION AS A GLYCERATE KINASE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, COFACTOR, SUBSTRATE SPECIFICITY, AND SUBUNIT.
RX PubMed=19690808; DOI=10.1007/s10529-009-0089-z;
RA Liu B., Wu L., Liu T., Hong Y., Shen Y., Ni J.;
RT "A MOFRL family glycerate kinase from the thermophilic crenarchaeon,
RT Sulfolobus tokodaii, with unique enzymatic properties.";
RL Biotechnol. Lett. 31:1937-1941(2009).
CC -!- FUNCTION: Catalyzes the ATP-dependent phosphorylation of D-glycerate to
CC 2-phosphoglycerate. It can also utilize GTP, CTP, UTP, ADP, AMP or
CC pyrophosphate as phosphate donor. {ECO:0000269|PubMed:19690808}.
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:19690808};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:19690808};
CC Name=Ni(2+); Xref=ChEBI:CHEBI:49786;
CC Evidence={ECO:0000269|PubMed:19690808};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:19690808};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000269|PubMed:19690808};
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:19690808};
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:19690808};
CC Name=Sr(2+); Xref=ChEBI:CHEBI:35104;
CC Evidence={ECO:0000269|PubMed:19690808};
CC Note=Magnesium. It could be replaced to some extent by nickel,
CC manganese, cobalt, calcium, zinc or strontium.
CC {ECO:0000269|PubMed:19690808};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 4.5. More than 70% of the optimum activity remains at
CC pH between 3 and 7. {ECO:0000269|PubMed:19690808};
CC Temperature dependence:
CC Optimum temperature is 90 degrees Celsius. It exhibits more than half
CC of the maximum activity at temperatures ranging from 70 to 100
CC degrees Celsius. {ECO:0000269|PubMed:19690808};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:19690808}.
CC -!- SIMILARITY: Belongs to the glycerate kinase type-1 family.
CC {ECO:0000305}.
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DR EMBL; BA000023; BAB67133.1; -; Genomic_DNA.
DR RefSeq; WP_010980109.1; NC_003106.2.
DR AlphaFoldDB; Q96YZ3; -.
DR SMR; Q96YZ3; -.
DR STRING; 273063.STK_20370; -.
DR EnsemblBacteria; BAB67133; BAB67133; STK_20370.
DR GeneID; 1460098; -.
DR KEGG; sto:STK_20370; -.
DR PATRIC; fig|273063.9.peg.2323; -.
DR eggNOG; arCOG04170; Archaea.
DR OMA; GKAAWRM; -.
DR OrthoDB; 53827at2157; -.
DR BioCyc; MetaCyc:MON-15370; -.
DR BRENDA; 2.7.1.165; 15396.
DR Proteomes; UP000001015; 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..399
FT /note="Glycerate 2-kinase"
FT /id="PRO_0000415148"
FT BINDING 48
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 399 AA; 44010 MW; 7568CB6061212B67 CRC64;
MDKIIEKILT FSDPYIALDE RVVIKKNEII VDGNHFPYTK PAIIAVGKAS YKMAKFFIDK
LKDVKGLVIL PKGSYISLPK VEVIESTHPD ISELSFKAGT EVIKFLKNED YDLLIFLLSG
GASALMEYSN VPYEILRDIN EKLVKSGLSV NEINIVRKHL SLIKGGKLTE FSKAPILTLI
VSDVPGGDLS AVGSGPTLPD SSTVDDAKLI LNKVGLGEYS KYLIETKKEV HNSFNFLILD
INIVLRKLRD IVQNPIILSS EIRGDAYSFG QNLAGIVNTS FSNLGLKPPY TLLAGGEPDV
KIEGKAGKGG RNGEVCLGFL KWVKRNSNHR FKLYAIATDG IDGNSEYAGC IVDENTIVDN
IEYYIYSHSS YEALEKVGRV IKTGYTFTNV NNVYVLEVT
