GLXK1_ECOLI
ID GLXK1_ECOLI Reviewed; 381 AA.
AC P23524; Q2M985;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Glycerate 2-kinase;
DE EC=2.7.1.165 {ECO:0000269|PubMed:9772162};
DE AltName: Full=Glycerate kinase 1;
DE Short=GK1 {ECO:0000303|PubMed:9772162};
GN Name=garK; Synonyms=yhaD; OrderedLocusNames=b3124, JW3093;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=1705543; DOI=10.1128/jb.173.5.1813-1816.1991;
RA Komine Y., Inokuchi H.;
RT "Precise mapping of the rnpB gene encoding the RNA component of RNase P in
RT Escherichia coli K-12.";
RL J. Bacteriol. 173:1813-1816(1991).
RN [2]
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 [3]
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 [4]
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).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND INDUCTION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9772162; DOI=10.1021/bi981124f;
RA Hubbard B.K., Koch M., Palmer D.R., Babbitt P.C., Gerlt J.A.;
RT "Evolution of enzymatic activities in the enolase superfamily:
RT characterization of the (D)-glucarate/galactarate catabolic pathway in
RT Escherichia coli.";
RL Biochemistry 37:14369-14375(1998).
CC -!- FUNCTION: Catalyzes the transfer of the phosphate group from adenosine
CC triphosphate (ATP) to (R)-glycerate to form (2R)-2-phosphoglycerate, an
CC enzymatic step in (L)-glucarate/galactarate catabolic pathway.
CC {ECO:0000269|PubMed:9772162}.
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:9772162};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27378;
CC Evidence={ECO:0000269|PubMed:9772162};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=51 uM for glycerate {ECO:0000269|PubMed:4887503,
CC ECO:0000269|PubMed:9772162};
CC KM=70 uM for glycerate {ECO:0000269|PubMed:4887503,
CC ECO:0000269|PubMed:9772162};
CC KM=61 uM for ATP {ECO:0000269|PubMed:4887503,
CC ECO:0000269|PubMed:9772162};
CC pH dependence:
CC Optimum pH is 7.3-7.9. {ECO:0000269|PubMed:4887503,
CC ECO:0000269|PubMed:9772162};
CC -!- INDUCTION: In glycerate, glucarate and glycolate-grown cells but not in
CC glucose-grown cells (at protein level). {ECO:0000269|PubMed:4887503,
CC ECO:0000269|PubMed:9772162}.
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. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA57927.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA14239.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAE77171.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; D90212; BAA14239.1; ALT_INIT; Genomic_DNA.
DR EMBL; U18997; AAA57927.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC76158.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE77171.1; ALT_INIT; Genomic_DNA.
DR PIR; JQ0614; JQ0614.
DR RefSeq; NP_417593.4; NC_000913.3.
DR RefSeq; WP_001300387.1; NZ_LN832404.1.
DR AlphaFoldDB; P23524; -.
DR SMR; P23524; -.
DR BioGRID; 4261538; 11.
DR DIP; DIP-28063N; -.
DR IntAct; P23524; 7.
DR STRING; 511145.b3124; -.
DR jPOST; P23524; -.
DR PaxDb; P23524; -.
DR PRIDE; P23524; -.
DR EnsemblBacteria; AAC76158; AAC76158; b3124.
DR EnsemblBacteria; BAE77171; BAE77171; BAE77171.
DR GeneID; 947632; -.
DR KEGG; ecj:JW3093; -.
DR KEGG; eco:b3124; -.
DR PATRIC; fig|1411691.4.peg.3608; -.
DR EchoBASE; EB1162; -.
DR eggNOG; COG1929; Bacteria.
DR HOGENOM; CLU_028255_0_1_6; -.
DR InParanoid; P23524; -.
DR OMA; YTAVHEK; -.
DR PhylomeDB; P23524; -.
DR BioCyc; EcoCyc:GKI-MON; -.
DR BioCyc; MetaCyc:GKI-MON; -.
DR BRENDA; 2.7.1.165; 2026.
DR SABIO-RK; P23524; -.
DR PRO; PR:P23524; -.
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:InterPro.
DR GO; GO:0042838; P:D-glucarate catabolic process; IEP:EcoCyc.
DR GO; GO:0046392; P:galactarate catabolic process; IEP: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 2-kinase"
FT /id="PRO_0000071532"
SQ SEQUENCE 381 AA; 39104 MW; 0A048E2E5F9FBE32 CRC64;
MKIVIAPDSY KESLSASEVA QAIEKGFREI FPDAQYVSVP VADGGEGTVE AMIAATQGAE
RHAWVTGPLG EKVNASWGIS GDGKTAFIEM AAASGLELVP AEKRDPLVTT SRGTGELILQ
ALESGATNII IGIGGSATND GGAGMVQALG AKLCDANGNE IGFGGGSLNT LNDIDISGLD
PRLKDCVIRV ACDVTNPLVG DNGASRIFGP QKGASEAMIV ELDNNLSHYA EVIKKALHVD
VKDVPGAGAA GGMGAALMAF LGAELKSGIE IVTTALNLEE HIHDCTLVIT GEGRIDSQSI
HGKVPIGVAN VAKKYHKPVI GIAGSLTDDV GVVHQHGIDA VFSVLTSIGT LDEAFRGAYD
NICRASRNIA ATLAIGMRNA G
