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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
 
 
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