ID   GLXK_ALKHC              Reviewed;         380 AA.
AC   Q9Z9P2; Q9KFC9;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 2.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=Glycerate kinase;
DE            EC=2.7.1.31;
GN   Name=glxK; OrderedLocusNames=BH0555;
OS   Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS   / JCM 9153 / C-125) (Bacillus halodurans).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX   NCBI_TaxID=272558;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX   PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA   Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA   Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT   "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT   and genomic sequence comparison with Bacillus subtilis.";
RL   Nucleic Acids Res. 28:4317-4331(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-189.
RC   STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX   PubMed=10086841; DOI=10.1007/s007920050095;
RA   Takami H., Nakasone K., Hirama C., Takaki Y., Masui N., Fuji F.,
RA   Nakamura Y., Inoue A.;
RT   "An improved physical and genetic map of the genome of alkaliphilic
RT   Bacillus sp. C-125.";
RL   Extremophiles 3:21-28(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}.
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; BA000004; BAB04274.1; -; Genomic_DNA.
DR   EMBL; AB013375; BAA75390.1; -; Genomic_DNA.
DR   PIR; C83719; C83719.
DR   RefSeq; WP_010896732.1; NC_002570.2.
DR   AlphaFoldDB; Q9Z9P2; -.
DR   SMR; Q9Z9P2; -.
DR   STRING; 272558.10173168; -.
DR   EnsemblBacteria; BAB04274; BAB04274; BAB04274.
DR   KEGG; bha:BH0555; -.
DR   eggNOG; COG1929; Bacteria.
DR   HOGENOM; CLU_028255_0_1_9; -.
DR   OMA; YTAVHEK; -.
DR   OrthoDB; 1292731at2; -.
DR   Proteomes; UP000001258; 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; Reference proteome; Transferase.
FT   CHAIN           1..380
FT                   /note="Glycerate kinase"
FT                   /id="PRO_0000071536"
SQ   SEQUENCE   380 AA;  39956 MW;  0C6E227253B3E46D CRC64;
     MNTIVIAPDS FKESMTALQA ARAIEKGFRR VIPNANYRLI PMADGGEGTV QSIVDALQGE
     RKVVKVEGPL GDTVEAEYGL SGDRKIAVIE MAQASGLHLV PKEKRNPLWT STYGTGQLLI
     DALDEGVEQI ILGIGGSATN DGGAGMAQAV GVRLLKENGE PIGKGGGKLK ELARIDMSKV
     DPRIQQVKLQ VACDVDNPLV GEKGAAVVYG PQKGATRATI RELDEQLLHF ANIIEEELGK
     EVASIPGAGA AGGLGAGLIA FLDAKLIPGV ELVLQATNFH ELVKDADFVI TGEGRIDQQT
     VYGKTPIGVA KAAKQYGVPV IAIAGSLGQG YEAVFEHGID AAFSLVPRIM SLDEAMQQGD
     SLLEQAARNI AVVSSWNKST