OTNK_PSE14
ID OTNK_PSE14 Reviewed; 429 AA.
AC Q48PB0;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=3-oxo-tetronate kinase {ECO:0000303|PubMed:27402745};
DE EC=2.7.1.217 {ECO:0000269|PubMed:27402745};
DE AltName: Full=3-dehydrotetronate 4-kinase {ECO:0000305};
GN Name=otnK {ECO:0000303|PubMed:27402745};
GN OrderedLocusNames=PSPPH_0456 {ECO:0000312|EMBL:AAZ35071.1};
OS Pseudomonas savastanoi pv. phaseolicola (strain 1448A / Race 6)
OS (Pseudomonas syringae pv. phaseolicola (strain 1448A / Race 6)).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=264730;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1448A / Race 6;
RX PubMed=16159782; DOI=10.1128/jb.187.18.6488-6498.2005;
RA Joardar V., Lindeberg M., Jackson R.W., Selengut J., Dodson R.,
RA Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S., Gwinn Giglio M.,
RA Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S.A., Crabtree J.,
RA Creasy T., Davidsen T.M., Haft D.H., Zafar N., Zhou L., Halpin R.,
RA Holley T., Khouri H.M., Feldblyum T.V., White O., Fraser C.M.,
RA Chatterjee A.K., Cartinhour S., Schneider D., Mansfield J.W., Collmer A.,
RA Buell R.;
RT "Whole-genome sequence analysis of Pseudomonas syringae pv. phaseolicola
RT 1448A reveals divergence among pathovars in genes involved in virulence and
RT transposition.";
RL J. Bacteriol. 187:6488-6498(2005).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=1448A / Race 6;
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 3-oxo-
CC tetronate to 3-oxo-tetronate 4-phosphate.
CC {ECO:0000269|PubMed:27402745}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-dehydro-L-erythronate + ATP = 3-dehydro-4-O-phospho-L-
CC erythronate + ADP + H(+); Xref=Rhea:RHEA:52552, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:136592, ChEBI:CHEBI:136670,
CC ChEBI:CHEBI:456216; EC=2.7.1.217;
CC Evidence={ECO:0000269|PubMed:27402745};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-dehydro-D-erythronate + ATP = 3-dehydro-4-O-phospho-D-
CC erythronate + ADP + H(+); Xref=Rhea:RHEA:52556, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:57958, ChEBI:CHEBI:136593,
CC ChEBI:CHEBI:456216; EC=2.7.1.217;
CC Evidence={ECO:0000269|PubMed:27402745};
CC -!- SIMILARITY: Belongs to the four-carbon acid sugar kinase family.
CC {ECO:0000305}.
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DR EMBL; CP000058; AAZ35071.1; -; Genomic_DNA.
DR RefSeq; WP_004666462.1; NC_005773.3.
DR AlphaFoldDB; Q48PB0; -.
DR SMR; Q48PB0; -.
DR STRING; 264730.PSPPH_0456; -.
DR EnsemblBacteria; AAZ35071; AAZ35071; PSPPH_0456.
DR KEGG; psp:PSPPH_0456; -.
DR eggNOG; COG3395; Bacteria.
DR HOGENOM; CLU_029424_1_0_6; -.
DR OMA; CSVMTNK; -.
DR OrthoDB; 771666at2; -.
DR Proteomes; UP000000551; 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 Transferase.
FT CHAIN 1..429
FT /note="3-oxo-tetronate kinase"
FT /id="PRO_0000439685"
FT BINDING 268
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q0KBC8"
FT BINDING 366..369
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q0KBC8"
FT BINDING 410
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q0KBC8"
SQ SEQUENCE 429 AA; 44521 MW; 5220EBFF93EF21A5 CRC64;
MSLNNARPLL GCIADDFTGA TDLANMLVRG GMRTVQSIGI PSAEMAAGLD ADAIVIALKS
RTTPSADAVA ESLAALEWLR ERGCEQIFFK YCSTFDSTAA GNIGQVSEAL LEQLDSDFTL
ACPAFPENGR TIFRGHLFVQ DQLLSESGMQ NHPLTPMTDA NLVRVLQAQT RHKVGLLRYD
SIAQGVEGVR NRIAELRAEG VSMAIADALS DADLYTLGEA CADLPLLTGG SGLALGLPGN
FRKAGKLRDI DAAKQVAISG GEVVLAGSAS VATNGQVAAW LEDNRPALRI NPLDLAAGKP
VVEQALTFAR DAGQTVLIYA TSTPDEVKAV QKELGVERSG AMVEAALGEI AKGLLNAGVR
RFVVAGGETS GAVVQALGVQ LLQIGAQIDP GVPATVSSGA QPLALALKSG NFGARDFFAK
ALKQLAGAA
