GLXK_BACC1
ID GLXK_BACC1 Reviewed; 381 AA.
AC Q9XBL1;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2004, sequence version 2.
DT 25-MAY-2022, entry version 113.
DE RecName: Full=Glycerate kinase;
DE EC=2.7.1.31;
GN Name=glxK; OrderedLocusNames=BCE_0153;
OS Bacillus cereus (strain ATCC 10987 / NRS 248).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=222523;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10987 / NRS 248;
RX PubMed=14960714; DOI=10.1093/nar/gkh258;
RA Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L.,
RA Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F.,
RA Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D.;
RT "The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic
RT adaptations and a large plasmid related to Bacillus anthracis pXO1.";
RL Nucleic Acids Res. 32:977-988(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 313-381.
RX PubMed=10217496; DOI=10.1099/13500872-145-3-621;
RA Oekstad O.A., Hegna I.K., Lindbaeck T., Rishovd A.-L., Kolstoe A.-B.;
RT "Genome organization is not conserved between Bacillus cereus and Bacillus
RT subtilis.";
RL Microbiology 145:621-631(1999).
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 -!- SIMILARITY: Belongs to the glycerate kinase type-1 family.
CC {ECO:0000305}.
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DR EMBL; AE017194; AAS39089.1; -; Genomic_DNA.
DR EMBL; AJ010129; CAB40583.1; -; Genomic_DNA.
DR RefSeq; WP_000869571.1; NC_003909.8.
DR AlphaFoldDB; Q9XBL1; -.
DR SMR; Q9XBL1; -.
DR EnsemblBacteria; AAS39089; AAS39089; BCE_0153.
DR GeneID; 59156509; -.
DR KEGG; bca:BCE_0153; -.
DR HOGENOM; CLU_028255_0_0_9; -.
DR OMA; YTAVHEK; -.
DR Proteomes; UP000002527; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008887; F:glycerate kinase activity; IEA:UniProtKB-EC.
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 3: Inferred from homology;
KW ATP-binding; Kinase; Nucleotide-binding; Transferase.
FT CHAIN 1..381
FT /note="Glycerate kinase"
FT /id="PRO_0000071535"
SQ SEQUENCE 381 AA; 40481 MW; 9D20DA7CC57F6ED9 CRC64;
MKVVIASDSY KESLKAIEVC EAIERGFGAI FPKAEYVKIP IGDGGEGTVD SLVDATSGRI
ISFHVTGPLR ESVQAFYGMS KDKKTAFIEM AAASGLQHVP AKKRNPLITT TKGTGELILH
ALDEGAEHII LGLGGSATND GGAGMLSALG VRFINGKGEV IEPSGGTLHS IVSIDFSQMD
SRLKHIKIEA ACDVDNPLVG IRGASFVFGR QKGADEEMMK ELDENLKHYA HILKQYLFCD
VSKIPGAGAA GGMGAAVIAV LKGSLRRGIE IVLDYTNFDK HIEGADLIIT GEGRIDEQTA
YGKAPVGVAE RAKLFHIPVI AIGGSVSPNY SAVHEKGIDA VFSITTSPTT LEEAYKVAEE
NIEMTAKNIA AVWKIASEKH F