DTNK_PECAS
ID DTNK_PECAS Reviewed; 442 AA.
AC Q6D0N7;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 77.
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=ECA3761 {ECO:0000312|EMBL:CAG76660.1};
OS Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) (Erwinia
OS carotovora subsp. atroseptica).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Pectobacterium.
OX NCBI_TaxID=218491;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCRI 1043 / ATCC BAA-672;
RX PubMed=15263089; DOI=10.1073/pnas.0402424101;
RA Bell K.S., Sebaihia M., Pritchard L., Holden M.T.G., Hyman L.J.,
RA Holeva M.C., Thomson N.R., Bentley S.D., Churcher L.J.C., Mungall K.,
RA Atkin R., Bason N., Brooks K., Chillingworth T., Clark K., Doggett J.,
RA Fraser A., Hance Z., Hauser H., Jagels K., Moule S., Norbertczak H.,
RA Ormond D., Price C., Quail M.A., Sanders M., Walker D., Whitehead S.,
RA Salmond G.P.C., Birch P.R.J., Parkhill J., Toth I.K.;
RT "Genome sequence of the enterobacterial phytopathogen Erwinia carotovora
RT subsp. atroseptica and characterization of virulence factors.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:11105-11110(2004).
RN [2] {ECO:0007744|PDB:4XFM, ECO:0007744|PDB:4XGJ}
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) IN COMPLEX WITH THREONATE ION,
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=SCRI 1043 / ATCC BAA-672;
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=0.13 mM for D-threonate {ECO:0000269|PubMed:27402745};
CC KM=73 mM for 4-hydroxy-L-threonine {ECO:0000269|PubMed:27402745};
CC Note=kcat is 120 sec(-1) with D-threonate as substrate. kcat is 170
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; BX950851; CAG76660.1; -; Genomic_DNA.
DR RefSeq; WP_011095262.1; NC_004547.2.
DR PDB; 4XFM; X-ray; 1.55 A; A=1-442.
DR PDB; 4XGJ; X-ray; 1.90 A; A=1-442.
DR PDBsum; 4XFM; -.
DR PDBsum; 4XGJ; -.
DR AlphaFoldDB; Q6D0N7; -.
DR SMR; Q6D0N7; -.
DR STRING; 218491.ECA3761; -.
DR EnsemblBacteria; CAG76660; CAG76660; ECA3761.
DR KEGG; eca:ECA3761; -.
DR PATRIC; fig|218491.5.peg.3815; -.
DR eggNOG; COG3395; Bacteria.
DR HOGENOM; CLU_029424_0_1_6; -.
DR OMA; IASCVPW; -.
DR OrthoDB; 771666at2; -.
DR Proteomes; UP000007966; 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; Reference proteome; Transferase.
FT CHAIN 1..442
FT /note="D-threonate kinase"
FT /id="PRO_0000439676"
FT BINDING 17
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:27402745,
FT ECO:0007744|PDB:4XFM"
FT BINDING 60
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:27402745,
FT ECO:0007744|PDB:4XFM"
FT BINDING 90..93
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:27402745,
FT ECO:0007744|PDB:4XFM"
FT BINDING 254
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q0KBC8"
FT BINDING 375..378
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q0KBC8"
FT BINDING 421
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q0KBC8"
FT STRAND 10..17
FT /evidence="ECO:0007829|PDB:4XFM"
FT HELIX 18..30
FT /evidence="ECO:0007829|PDB:4XFM"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:4XFM"
FT HELIX 41..43
FT /evidence="ECO:0007829|PDB:4XFM"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:4XFM"
FT STRAND 50..56
FT /evidence="ECO:0007829|PDB:4XFM"
FT HELIX 64..80
FT /evidence="ECO:0007829|PDB:4XFM"
FT STRAND 85..90
FT /evidence="ECO:0007829|PDB:4XFM"
FT HELIX 99..110
FT /evidence="ECO:0007829|PDB:4XFM"
FT STRAND 115..118
FT /evidence="ECO:0007829|PDB:4XFM"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:4XFM"
FT STRAND 126..129
FT /evidence="ECO:0007829|PDB:4XFM"
FT STRAND 132..135
FT /evidence="ECO:0007829|PDB:4XFM"
FT HELIX 140..142
FT /evidence="ECO:0007829|PDB:4XFM"
FT HELIX 144..146
FT /evidence="ECO:0007829|PDB:4XFM"
FT STRAND 149..151
FT /evidence="ECO:0007829|PDB:4XFM"
FT HELIX 158..163
FT /evidence="ECO:0007829|PDB:4XFM"
FT STRAND 170..173
FT /evidence="ECO:0007829|PDB:4XFM"
FT HELIX 175..178
FT /evidence="ECO:0007829|PDB:4XFM"
FT HELIX 183..193
FT /evidence="ECO:0007829|PDB:4XFM"
FT STRAND 197..200
FT /evidence="ECO:0007829|PDB:4XFM"
FT STRAND 202..204
FT /evidence="ECO:0007829|PDB:4XFM"
FT HELIX 205..215
FT /evidence="ECO:0007829|PDB:4XFM"
FT STRAND 218..220
FT /evidence="ECO:0007829|PDB:4XFM"
FT STRAND 223..227
FT /evidence="ECO:0007829|PDB:4XFM"
FT HELIX 228..238
FT /evidence="ECO:0007829|PDB:4XFM"
FT STRAND 248..252
FT /evidence="ECO:0007829|PDB:4XFM"
FT HELIX 257..267
FT /evidence="ECO:0007829|PDB:4XFM"
FT STRAND 272..278
FT /evidence="ECO:0007829|PDB:4XFM"
FT HELIX 279..283
FT /evidence="ECO:0007829|PDB:4XFM"
FT HELIX 287..303
FT /evidence="ECO:0007829|PDB:4XFM"
FT STRAND 307..313
FT /evidence="ECO:0007829|PDB:4XFM"
FT HELIX 335..354
FT /evidence="ECO:0007829|PDB:4XFM"
FT STRAND 369..375
FT /evidence="ECO:0007829|PDB:4XFM"
FT HELIX 376..385
FT /evidence="ECO:0007829|PDB:4XFM"
FT STRAND 390..397
FT /evidence="ECO:0007829|PDB:4XFM"
FT TURN 398..400
FT /evidence="ECO:0007829|PDB:4XFM"
FT STRAND 401..408
FT /evidence="ECO:0007829|PDB:4XFM"
FT TURN 410..413
FT /evidence="ECO:0007829|PDB:4XFM"
FT STRAND 415..419
FT /evidence="ECO:0007829|PDB:4XFM"
FT HELIX 428..438
FT /evidence="ECO:0007829|PDB:4XFM"
SQ SEQUENCE 442 AA; 46672 MW; CF951A6B519C9552 CRC64;
MPNVQQSAGQ VLVVADDFTG ANDAGVGLAQ HGARVSVVFD VNTLHADLLG DAVVINTDSR
AARDDVASQR TAAAVAAWQA VGGKGWIIKK IDSTLRGNLG AEVAAALSAA DVPVALIAAA
SPTLGRVTRQ GEVWVNGRRL TDTEFASDPK TPVTSASIAA RLAEQTALPV AEIHLDEVRQ
ANLAHRLQQL ADEGTRLIIL DTDVQDDLTH IVNAARALPF RPLLVGSAGL SDALATAQDF
TRKTEKPLLA VVGSMSDIAQ KQIAAARLRS DVTLVEIDIN ALFSPDSSTV MASQCEDALK
ALTNGHHCII RTCHNENQRF EIDARCRELG LSRQQLGETI SHYLGELTRS IVQALDSLAA
DGTRRRLPGG LYLSGGDIAI AVATALGATG FQIKGQIASC VPWGYLLNSI VGMTPVMTKA
GGFGNETTLL DVLRFIEEKV SE
