GLXK2_ECOLI
ID GLXK2_ECOLI Reviewed; 381 AA.
AC P77364; Q2MBR4;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Glycerate 3-kinase;
DE EC=2.7.1.31;
DE AltName: Full=D-Glycerate-3-kinase;
DE AltName: Full=Glycerate kinase 2;
DE Short=GK2;
GN Name=glxK; Synonyms=glxB5, ybbZ; OrderedLocusNames=b0514, JW0502;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / ECL1;
RX PubMed=10601204; DOI=10.1128/jb.181.24.7479-7484.1999;
RA Cusa E., Obradors N., Baldoma L., Badia J., Aguilar J.;
RT "Genetic analysis of a chromosomal region containing genes required for
RT assimilation of allantoin nitrogen and linked glyoxylate metabolism in
RT Escherichia coli.";
RL J. Bacteriol. 181:7479-7484(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP COFACTOR, ACTIVITY REGULATION, AND INDUCTION.
RC STRAIN=Crooks;
RX PubMed=5325263; DOI=10.1016/s0021-9258(18)96874-2;
RA Doughty C.C., Hayashi J.A., Guenther H.L.;
RT "Purification and properties of D-glycerate 3-kinase from Escherichia
RT coli.";
RL J. Biol. Chem. 241:568-572(1966).
RN [6]
RP BIOPHYSICOCHEMICAL PROPERTIES, ENZYME STABILITY, AND INDUCTION.
RC STRAIN=K1, K12, and R4;
RX PubMed=4887503; DOI=10.1128/jb.97.3.1227-1233.1969;
RA Ornston M.K., Ornston L.N.;
RT "Two forms of D-glycerate kinase in Escherichia coli.";
RL J. Bacteriol. 97:1227-1233(1969).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-glycerate + ATP = (2R)-3-phosphoglycerate + ADP + H(+);
CC Xref=Rhea:RHEA:23516, ChEBI:CHEBI:15378, ChEBI:CHEBI:16659,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58272, ChEBI:CHEBI:456216;
CC EC=2.7.1.31;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:5325263};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000269|PubMed:5325263};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:5325263};
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000269|PubMed:5325263};
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:5325263};
CC Note=Divalent metal cations; Mg(2+) and Co(2+) are better than Mn(2+),
CC Fe(2+) or Ca(2+). {ECO:0000269|PubMed:5325263};
CC -!- ACTIVITY REGULATION: Inhibited by EDTA, p-hydroxy-mercuribenzoate and
CC iodoacetate but not by NaF. {ECO:0000269|PubMed:5325263}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.07 mM for glycerate {ECO:0000269|PubMed:4887503};
CC pH dependence:
CC Optimum pH is 7.0-7.6. {ECO:0000269|PubMed:4887503};
CC -!- PATHWAY: Organic acid metabolism; glycolate degradation; 3-phospho-D-
CC glycerate from glycolate: step 4/4.
CC -!- INDUCTION: In glycolate-grown cells but not in glucose-grown cells (at
CC protein level). {ECO:0000269|PubMed:4887503,
CC ECO:0000269|PubMed:5325263}.
CC -!- DISRUPTION PHENOTYPE: Loss of glycerate kinase activity.
CC {ECO:0000269|PubMed:10601204}.
CC -!- MISCELLANEOUS: GK1 has a half-life of 92 minutes while GK2 has a half-
CC life of 11 minutes at 49 degrees Celsius.
CC -!- SIMILARITY: Belongs to the glycerate kinase type-1 family.
CC {ECO:0000305}.
CC -!- CAUTION: E.coli has 2 glycerate kinases, GK1 and GK2; it is not clear
CC which gene encodes which enzyme. PubMed:5325263 may be a mix of GK1 and
CC GK2. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U89279; AAB93855.1; -; Genomic_DNA.
DR EMBL; U82664; AAB40266.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73616.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76292.1; -; Genomic_DNA.
DR PIR; A64783; A64783.
DR RefSeq; NP_415047.1; NC_000913.3.
DR RefSeq; WP_001333621.1; NZ_SSZK01000024.1.
DR AlphaFoldDB; P77364; -.
DR SMR; P77364; -.
DR BioGRID; 4262012; 12.
DR IntAct; P77364; 3.
DR STRING; 511145.b0514; -.
DR ChEMBL; CHEMBL3309014; -.
DR jPOST; P77364; -.
DR PaxDb; P77364; -.
DR PRIDE; P77364; -.
DR EnsemblBacteria; AAC73616; AAC73616; b0514.
DR EnsemblBacteria; BAE76292; BAE76292; BAE76292.
DR GeneID; 945129; -.
DR KEGG; ecj:JW0502; -.
DR KEGG; eco:b0514; -.
DR PATRIC; fig|1411691.4.peg.1764; -.
DR EchoBASE; EB3386; -.
DR eggNOG; COG1929; Bacteria.
DR HOGENOM; CLU_028255_0_1_6; -.
DR InParanoid; P77364; -.
DR OMA; SIEMNEC; -.
DR PhylomeDB; P77364; -.
DR BioCyc; EcoCyc:GLY3KIN-MON; -.
DR BioCyc; MetaCyc:GLY3KIN-MON; -.
DR BRENDA; 2.7.1.165; 2165.
DR UniPathway; UPA00864; UER00833.
DR PRO; PR:P77364; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0043798; F:glycerate 2-kinase activity; IDA:EcoCyc.
DR GO; GO:0008887; F:glycerate kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0046296; P:glycolate catabolic process; IEP:EcoCyc.
DR GO; GO:0009436; P:glyoxylate catabolic process; IMP:EcoCyc.
DR GO; GO:0031388; P:organic acid phosphorylation; IEA:InterPro.
DR Gene3D; 3.40.50.10350; -; 1.
DR Gene3D; 3.90.1510.10; -; 1.
DR InterPro; IPR018193; Glyc_kinase_flavodox-like_fold.
DR InterPro; IPR004381; Glycerate_kinase.
DR InterPro; IPR018197; Glycerate_kinase_RE-like.
DR InterPro; IPR036129; Glycerate_kinase_sf.
DR PANTHER; PTHR21599; PTHR21599; 1.
DR Pfam; PF02595; Gly_kinase; 1.
DR PIRSF; PIRSF006078; GlxK; 1.
DR SUPFAM; SSF110738; SSF110738; 1.
DR TIGRFAMs; TIGR00045; TIGR00045; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Kinase; Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..381
FT /note="Glycerate 3-kinase"
FT /id="PRO_0000071531"
SQ SEQUENCE 381 AA; 38734 MW; 0F902DF27DE63578 CRC64;
MKIVIAPDSF KESLSAEKCC QAIKAGFSTL FPDANYICLP IADGGEGTVD AMVAATGGNI
VTLEVCGPMG EKVNAFYGLT GDGKTAVIEM AAASGLMLVA PEKRNPLLAS SFGTGELIRH
ALDNDIRHII LGIGGSATVD GGMGMAQALG VRFLDADGQA LAANGGNLAR VASIEMDECD
PRLANCHIEV ACDVDNPLVG ARGAAAVFGP QKGATPEMVE ELEQGLQNYA RVLQQQTEIN
VCQMAGGGAA GGMGIAAAVF LNADIKPGIE IVLNAVNLAQ AVQGAALVIT GEGRIDSQTA
GGKAPLGVAS VAKQFNVPVI GIAGVLGDGV EVVHQYGIDA VFSILPRLAP LAEVLASGET
NLFNSARNIA CAIKIGQGIK N
