DTNK_BORBR
ID DTNK_BORBR Reviewed; 405 AA.
AC A0A0H3LX82;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 16-SEP-2015, sequence version 1.
DT 03-AUG-2022, entry version 33.
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=BB3215 {ECO:0000312|EMBL:CAE33707.1};
OS Bordetella bronchiseptica (strain ATCC BAA-588 / NCTC 13252 / RB50)
OS (Alcaligenes bronchisepticus).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=257310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-588 / NCTC 13252 / RB50;
RX PubMed=12910271; DOI=10.1038/ng1227;
RA Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
RA Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T.,
RA Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S.,
RA Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E.,
RA Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M.,
RA Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S.,
RA Barrell B.G., Maskell D.J.;
RT "Comparative analysis of the genome sequences of Bordetella pertussis,
RT Bordetella parapertussis and Bordetella bronchiseptica.";
RL Nat. Genet. 35:32-40(2003).
RN [2] {ECO:0007744|PDB:4XFR, ECO:0007744|PDB:4XG0}
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC BAA-588 / NCTC 13252 / RB50;
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=0.16 mM for D-threonate {ECO:0000269|PubMed:27402745};
CC KM=33 mM for 4-hydroxy-L-threonine {ECO:0000269|PubMed:27402745};
CC Note=kcat is 41 sec(-1) with D-threonate as substrate. kcat is 28
CC sec(-1) with 4-hydroxy-L-threonine as substrate.
CC {ECO:0000269|PubMed:27402745};
CC -!- SIMILARITY: Belongs to the four-carbon acid sugar kinase family.
CC {ECO:0000305}.
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DR EMBL; BX640446; CAE33707.1; -; Genomic_DNA.
DR RefSeq; WP_003810609.1; NC_002927.3.
DR PDB; 4XFR; X-ray; 2.00 A; A/B=1-405.
DR PDB; 4XG0; X-ray; 1.70 A; A=1-405.
DR PDBsum; 4XFR; -.
DR PDBsum; 4XG0; -.
DR AlphaFoldDB; A0A0H3LX82; -.
DR SMR; A0A0H3LX82; -.
DR STRING; 257310.BB3215; -.
DR EnsemblBacteria; CAE33707; CAE33707; BB3215.
DR KEGG; bbr:BB3215; -.
DR eggNOG; COG3395; Bacteria.
DR HOGENOM; CLU_029424_0_1_4; -.
DR OMA; TIYCPAF; -.
DR OrthoDB; 771666at2; -.
DR Proteomes; UP000001027; 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 3D-structure; ATP-binding; Carbohydrate metabolism; Kinase;
KW Nucleotide-binding; Transferase.
FT CHAIN 1..405
FT /note="D-threonate kinase"
FT /id="PRO_0000439674"
FT BINDING 12
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q6D0N7"
FT BINDING 59
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q6D0N7"
FT BINDING 88..91
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q6D0N7"
FT BINDING 243
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q0KBC8"
FT BINDING 337..340
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q0KBC8"
FT BINDING 383
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q0KBC8"
FT STRAND 6..12
FT /evidence="ECO:0007829|PDB:4XG0"
FT HELIX 13..25
FT /evidence="ECO:0007829|PDB:4XG0"
FT STRAND 30..32
FT /evidence="ECO:0007829|PDB:4XG0"
FT HELIX 37..42
FT /evidence="ECO:0007829|PDB:4XG0"
FT HELIX 44..46
FT /evidence="ECO:0007829|PDB:4XG0"
FT STRAND 50..55
FT /evidence="ECO:0007829|PDB:4XG0"
FT HELIX 63..79
FT /evidence="ECO:0007829|PDB:4XG0"
FT STRAND 84..88
FT /evidence="ECO:0007829|PDB:4XG0"
FT HELIX 97..108
FT /evidence="ECO:0007829|PDB:4XG0"
FT STRAND 113..117
FT /evidence="ECO:0007829|PDB:4XG0"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:4XG0"
FT STRAND 125..128
FT /evidence="ECO:0007829|PDB:4XG0"
FT STRAND 131..134
FT /evidence="ECO:0007829|PDB:4XG0"
FT HELIX 139..141
FT /evidence="ECO:0007829|PDB:4XG0"
FT HELIX 143..146
FT /evidence="ECO:0007829|PDB:4XG0"
FT STRAND 148..150
FT /evidence="ECO:0007829|PDB:4XG0"
FT HELIX 157..161
FT /evidence="ECO:0007829|PDB:4XG0"
FT STRAND 164..166
FT /evidence="ECO:0007829|PDB:4XG0"
FT HELIX 174..183
FT /evidence="ECO:0007829|PDB:4XG0"
FT TURN 184..186
FT /evidence="ECO:0007829|PDB:4XG0"
FT STRAND 187..190
FT /evidence="ECO:0007829|PDB:4XG0"
FT STRAND 192..194
FT /evidence="ECO:0007829|PDB:4XG0"
FT HELIX 195..208
FT /evidence="ECO:0007829|PDB:4XG0"
FT HELIX 209..211
FT /evidence="ECO:0007829|PDB:4XG0"
FT STRAND 212..216
FT /evidence="ECO:0007829|PDB:4XG0"
FT HELIX 218..230
FT /evidence="ECO:0007829|PDB:4XG0"
FT STRAND 237..241
FT /evidence="ECO:0007829|PDB:4XG0"
FT HELIX 246..257
FT /evidence="ECO:0007829|PDB:4XG0"
FT STRAND 261..263
FT /evidence="ECO:0007829|PDB:4XG0"
FT HELIX 267..270
FT /evidence="ECO:0007829|PDB:4XG0"
FT HELIX 273..282
FT /evidence="ECO:0007829|PDB:4XG0"
FT STRAND 295..299
FT /evidence="ECO:0007829|PDB:4XG0"
FT HELIX 312..327
FT /evidence="ECO:0007829|PDB:4XG0"
FT STRAND 331..337
FT /evidence="ECO:0007829|PDB:4XG0"
FT HELIX 338..347
FT /evidence="ECO:0007829|PDB:4XG0"
FT STRAND 352..360
FT /evidence="ECO:0007829|PDB:4XG0"
FT STRAND 363..371
FT /evidence="ECO:0007829|PDB:4XG0"
FT TURN 372..375
FT /evidence="ECO:0007829|PDB:4XG0"
FT STRAND 377..381
FT /evidence="ECO:0007829|PDB:4XG0"
FT HELIX 390..399
FT /evidence="ECO:0007829|PDB:4XG0"
SQ SEQUENCE 405 AA; 40922 MW; 571AD6144AFD24CD CRC64;
MGGPYIGIVA DDLTGSGDTA VQFVRAGWAT QLSVGGAEQA LADPAVRQAE VLAVTTHSRP
LAAADAAAVV RGEVERLRAA GVQRLYKKVD STLRGAFKAE IDAARLAWGE DAIAVVCPAF
PVTGRTVRQG VLYVGDRPVT ETSAATDPVT PVTESHIPTL LGCAQLAAQA GETPAELARR
IAAAAPVVVV DALDDADVQR LARAIGVLGQ RAVPVGSGGL AAPLARVWAG GQAAGPVLVV
VTSQHSAARQ QAAALQQAGA RTWAPTLAQL ADDRNWAAWT AEVEAAEHGM PAVDALMLLA
PEGRLAGLDA DSVARRLGEL AARLVLAHGA AGVVATGGDG ASAVLAALQA SGIALVDEVT
GGVPLGTLTG GQAAGLPVVT KAGGFGEQDV LIRAAQAIRE RRFTK
