DTNK_SALTY
ID DTNK_SALTY Reviewed; 423 AA.
AC Q8ZRS5;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 83.
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=STM0162 {ECO:0000312|EMBL:AAL19126.1};
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [2]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF GLY-401.
RX PubMed=27294475; DOI=10.1021/acschembio.6b00279;
RA Thiaville J.J., Flood J., Yurgel S., Prunetti L., Elbadawi-Sidhu M.,
RA Hutinet G., Forouhar F., Zhang X., Ganesan V., Reddy P., Fiehn O.,
RA Gerlt J.A., Hunt J.F., Copley S.D., de Crecy-Lagard V.;
RT "Members of a novel kinase family (DUF1537) can recycle toxic intermediates
RT into an essential metabolite.";
RL ACS Chem. Biol. 11:2304-2311(2016).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
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 (PubMed:27402745). Can also phosphorylate 4-
CC hydroxy-L-threonine, with lower efficiency. This side reaction may
CC serve to deal with the toxicity of 4-hydroxy-L-threonine by converting
CC it into 4-hydroxy-L-threonine 4-phosphate, a useful product that can be
CC used by PdxA2 (PubMed:27402745, PubMed:27294475).
CC {ECO:0000269|PubMed:27294475, 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=0.29 mM for D-threonate {ECO:0000269|PubMed:27294475,
CC ECO:0000269|PubMed:27402745};
CC KM=3.8 mM for 4-hydroxy-L-threonine {ECO:0000269|PubMed:27294475,
CC ECO:0000269|PubMed:27402745};
CC Note=kcat is 22 sec(-1) with D-threonate as substrate. kcat is 4.0
CC sec(-1) with 4-hydroxy-L-threonine as substrate.
CC {ECO:0000269|PubMed:27294475, 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; AE006468; AAL19126.1; -; Genomic_DNA.
DR RefSeq; NP_459167.1; NC_003197.2.
DR RefSeq; WP_000782192.1; NC_003197.2.
DR AlphaFoldDB; Q8ZRS5; -.
DR SMR; Q8ZRS5; -.
DR STRING; 99287.STM0162; -.
DR PaxDb; Q8ZRS5; -.
DR EnsemblBacteria; AAL19126; AAL19126; STM0162.
DR GeneID; 1251680; -.
DR KEGG; stm:STM0162; -.
DR PATRIC; fig|99287.12.peg.172; -.
DR HOGENOM; CLU_029424_0_1_6; -.
DR OMA; IASCVPW; -.
DR PhylomeDB; Q8ZRS5; -.
DR BioCyc; MetaCyc:STM0162-MON; -.
DR BioCyc; SENT99287:STM0162-MON; -.
DR BRENDA; 2.7.1.219; 5542.
DR Proteomes; UP000001014; Chromosome.
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..423
FT /note="D-threonate kinase"
FT /id="PRO_0000439677"
FT BINDING 9
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q6D0N7"
FT BINDING 51
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q6D0N7"
FT BINDING 81..84
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q6D0N7"
FT BINDING 245
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q0KBC8"
FT BINDING 355..358
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q0KBC8"
FT BINDING 401
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q0KBC8"
FT MUTAGEN 401
FT /note="G->A: Lack of activity."
FT /evidence="ECO:0000269|PubMed:27294475"
SQ SEQUENCE 423 AA; 44986 MW; E6AF54C3BB43AD37 CRC64;
MKMIVIADDF TGSNDTGVQL AKKGARTEVM LSASQKPSRR ADVLVINTES RAMPADQAAS
AVYAALSPWC ETSPAPLVYK KIDSTFRGNI GAEVTAAMRA SQRKLAVIAA AIPAAGRTTL
EGKCLVNGVP LLETEFASDP KTPIVSSRIA EIVALQSEIP VYEVFLQDVR RGGLSALLTA
YAAEGEGIIV VDAVEERDLT LIAQAACEQP SMPLLVGAAG LANALPVELF MQDRQRLPVL
VVAGSMSEAT RRQVDNALCR GRAEVVDIDA ARMVSDSAEQ EIASVVEQAC ALLSQHRHTI
LRTSRRAEDR QLIDALCEKS AMSRQQLGER LSQRLGVVTL NIIEQARIGG LFLTGGDIAT
AVAGALGAEG YRIQSEVAPC IPCGTFVNSE IDDLPVITKA GGFGSDSTLC DALYYIEEMY
CGD
