ID   GLXK_NEIMB              Reviewed;         371 AA.
AC   P57099;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 1.
DT   25-MAY-2022, entry version 110.
DE   RecName: Full=Glycerate kinase;
DE            EC=2.7.1.31;
GN   Name=glxK; OrderedLocusNames=NMB1268;
OS   Neisseria meningitidis serogroup B (strain MC58).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=122586;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MC58;
RX   PubMed=10710307; DOI=10.1126/science.287.5459.1809;
RA   Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E.,
RA   Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C.,
RA   Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H.,
RA   Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., Mason T.M.,
RA   Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D.,
RA   Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V.,
RA   Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M.,
RA   Moxon E.R., Rappuoli R., Venter J.C.;
RT   "Complete genome sequence of Neisseria meningitidis serogroup B strain
RT   MC58.";
RL   Science 287:1809-1815(2000).
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; AE002098; AAF41645.1; -; Genomic_DNA.
DR   PIR; F81102; F81102.
DR   RefSeq; NP_274289.1; NC_003112.2.
DR   RefSeq; WP_002222399.1; NC_003112.2.
DR   AlphaFoldDB; P57099; -.
DR   SMR; P57099; -.
DR   STRING; 122586.NMB1268; -.
DR   PaxDb; P57099; -.
DR   EnsemblBacteria; AAF41645; AAF41645; NMB1268.
DR   KEGG; nme:NMB1268; -.
DR   PATRIC; fig|122586.8.peg.1587; -.
DR   HOGENOM; CLU_028255_0_0_4; -.
DR   OMA; YTAVHEK; -.
DR   Proteomes; UP000000425; 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..371
FT                   /note="Glycerate kinase"
FT                   /id="PRO_0000071538"
SQ   SEQUENCE   371 AA;  39537 MW;  779AD64ADA322DDF CRC64;
     MKIVIAPDSF KESLTAQQVA EAIKRGFQQS IADVECLLCP VGDGGEGTVD AIRHSLDLEE
     KCLQVTGPFG QKEVMRYFQK EQLALFEVAD LVGLGKIPLE KRNPLQIQTR GIGELIRHLI
     SQEIKEIYIG VGGTASNDGG IGIAAGLGYQ FYDEDGNALP VCGQSLLNLA SVSTENRYEI
     PEDVHIRILA DVVSPLCGHQ GATYTFGKQK GLDSTMFEAV DQAIQDFYEK VSPATLKLKG
     AGAGGGIAGG LCAFAQASIV SGIDTCLDLI DFDKKVSDVD LVIVGEGRLD RQSLAGKAPI
     GVAKRTPVGV PVVAICGSLV EDLPSLPFEN IQAAFSILEK SEPLEDSLKN ASLYLEHTAS
     NIGHLLNMPK I