ID   DTNK_CUPNH              Reviewed;         415 AA.
AC   Q0K4F6;
DT   10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=D-threonate kinase {ECO:0000303|PubMed:27402745};
DE            EC=2.7.1.219 {ECO:0000269|PubMed:27402745};
GN   Name=dtnK {ECO:0000303|PubMed:27402745};
GN   OrderedLocusNames=H16_B0318 {ECO:0000312|EMBL:CAJ95118.1};
OS   Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442
OS   / H16 / Stanier 337) (Ralstonia eutropha).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=381666;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337;
RX   PubMed=16964242; DOI=10.1038/nbt1244;
RA   Pohlmann A., Fricke W.F., Reinecke F., Kusian B., Liesegang H., Cramm R.,
RA   Eitinger T., Ewering C., Poetter M., Schwartz E., Strittmatter A., Voss I.,
RA   Gottschalk G., Steinbuechel A., Friedrich B., Bowien B.;
RT   "Genome sequence of the bioplastic-producing 'Knallgas' bacterium Ralstonia
RT   eutropha H16.";
RL   Nat. Biotechnol. 24:1257-1262(2006).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND DISRUPTION
RP   PHENOTYPE.
RC   STRAIN=ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337;
RX   PubMed=27402745; DOI=10.1073/pnas.1605546113;
RA   Zhang X., Carter M.S., Vetting M.W., San Francisco B., Zhao S.,
RA   Al-Obaidi N.F., Solbiati J.O., Thiaville J.J., de Crecy-Lagard V.,
RA   Jacobson M.P., Almo S.C., Gerlt J.A.;
RT   "Assignment of function to a domain of unknown function: DUF1537 is a new
RT   kinase family in catabolic pathways for acid sugars.";
RL   Proc. Natl. Acad. Sci. U.S.A. 113:E4161-E4169(2016).
CC   -!- FUNCTION: Catalyzes the ATP-dependent phosphorylation of D-threonate to
CC       D-threonate 4-phosphate. Can also phosphorylate 4-hydroxy-L-threonine,
CC       with lower efficiency. {ECO:0000269|PubMed:27402745}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + D-threonate = 4-O-phospho-D-threonate + ADP + H(+);
CC         Xref=Rhea:RHEA:52388, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:45912, ChEBI:CHEBI:136590, ChEBI:CHEBI:456216;
CC         EC=2.7.1.219; Evidence={ECO:0000269|PubMed:27402745};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.12 mM for D-threonate {ECO:0000269|PubMed:27402745};
CC         KM=86 mM for 4-hydroxy-L-threonine {ECO:0000269|PubMed:27402745};
CC         Note=kcat is 45 sec(-1) with D-threonate as substrate. kcat is 27
CC         sec(-1) with 4-hydroxy-L-threonine as substrate.
CC         {ECO:0000269|PubMed:27402745};
CC   -!- DISRUPTION PHENOTYPE: Deletion mutant is unable to use D-threonate as a
CC       carbon source. {ECO:0000269|PubMed:27402745}.
CC   -!- SIMILARITY: Belongs to the four-carbon acid sugar kinase family.
CC       {ECO:0000305}.
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DR   EMBL; AM260480; CAJ95118.1; -; Genomic_DNA.
DR   RefSeq; WP_010812612.1; NZ_CP039288.1.
DR   AlphaFoldDB; Q0K4F6; -.
DR   SMR; Q0K4F6; -.
DR   STRING; 381666.H16_B0318; -.
DR   EnsemblBacteria; CAJ95118; CAJ95118; H16_B0318.
DR   GeneID; 57646200; -.
DR   KEGG; reh:H16_B0318; -.
DR   eggNOG; COG3395; Bacteria.
DR   HOGENOM; CLU_029424_1_0_4; -.
DR   OMA; TIADCET; -.
DR   OrthoDB; 771666at2; -.
DR   BRENDA; 2.7.1.219; 231.
DR   Proteomes; UP000008210; Chromosome 2.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.10840; -; 1.
DR   Gene3D; 3.40.980.20; -; 1.
DR   InterPro; IPR037051; 4-carb_acid_sugar_kinase_N_sf.
DR   InterPro; IPR010737; DUF1537.
DR   InterPro; IPR031475; NBD_C.
DR   InterPro; IPR042213; NBD_C_sf.
DR   Pfam; PF17042; NBD_C; 1.
DR   Pfam; PF07005; SBD_N; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Carbohydrate metabolism; Kinase; Nucleotide-binding;
KW   Reference proteome; Transferase.
FT   CHAIN           1..415
FT                   /note="D-threonate kinase"
FT                   /id="PRO_0000439675"
FT   BINDING         9
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q6D0N7"
FT   BINDING         53
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q6D0N7"
FT   BINDING         81..84
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q6D0N7"
FT   BINDING         251
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q0KBC8"
FT   BINDING         345..348
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q0KBC8"
FT   BINDING         392
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q0KBC8"
SQ   SEQUENCE   415 AA;  42589 MW;  44B0FA23C25CCA5E CRC64;
     MSWLIIADDL SGAADCAIGY AMSGARTVVT LEAAPAGADL SQADVVACDV DSRRMAPQEA
     AARNLEAWHR GQGASRRLYK KIDSTLRGNW AAETAALAPL AGLAIVAPAF PATGRTTAGG
     CMFVNGQPLE DSDIWRLEAL TGRADLVALL AARGLRATLL PLDTVRAGDA TLRLTIAGLA
     REGVRAVVCD AQTEQDLAAL AAATAQLDVP AFWVGSGGLA RALAAPCLFE GGAPQPLPAP
     EGGPVLTLVG SLSGISGRQA ACLRERTGMQ SLVVPPRILR EGAGHADWDA AQQSITGCLR
     AGRDLLVSIG RDDAFDPGEG PRLSAALAQL SLPGFQHTRG LIATGGETAR AMLSAAGIGA
     LMLRREVEPG VPLSDTPALP GVPARRVATK AGAFGSEAAL WHAWQAMTES RAPSA