ID   OTNK_PSEF5              Reviewed;         430 AA.
AC   Q4KBD3;
DT   10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   03-AUG-2022, entry version 77.
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=PFL_3345 {ECO:0000312|EMBL:AAY92614.1};
OS   Pseudomonas fluorescens (strain ATCC BAA-477 / NRRL B-23932 / Pf-5).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=220664;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-477 / NRRL B-23932 / Pf-5;
RX   PubMed=15980861; DOI=10.1038/nbt1110;
RA   Paulsen I.T., Press C.M., Ravel J., Kobayashi D.Y., Myers G.S.A.,
RA   Mavrodi D.V., DeBoy R.T., Seshadri R., Ren Q., Madupu R., Dodson R.J.,
RA   Durkin A.S., Brinkac L.M., Daugherty S.C., Sullivan S.A., Rosovitz M.J.,
RA   Gwinn M.L., Zhou L., Schneider D.J., Cartinhour S.W., Nelson W.C.,
RA   Weidman J., Watkins K., Tran K., Khouri H., Pierson E.A., Pierson L.S. III,
RA   Thomashow L.S., Loper J.E.;
RT   "Complete genome sequence of the plant commensal Pseudomonas fluorescens
RT   Pf-5.";
RL   Nat. Biotechnol. 23:873-878(2005).
RN   [2]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=ATCC BAA-477 / NRRL B-23932 / Pf-5;
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; CP000076; AAY92614.1; -; Genomic_DNA.
DR   RefSeq; WP_011061627.1; NC_004129.6.
DR   AlphaFoldDB; Q4KBD3; -.
DR   SMR; Q4KBD3; -.
DR   STRING; 220664.PFL_3345; -.
DR   PRIDE; Q4KBD3; -.
DR   EnsemblBacteria; AAY92614; AAY92614; PFL_3345.
DR   GeneID; 57476364; -.
DR   KEGG; pfl:PFL_3345; -.
DR   PATRIC; fig|220664.5.peg.3414; -.
DR   eggNOG; COG3395; Bacteria.
DR   HOGENOM; CLU_029424_1_0_6; -.
DR   OMA; CSVMTNK; -.
DR   OrthoDB; 771666at2; -.
DR   Proteomes; UP000008540; 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..430
FT                   /note="3-oxo-tetronate kinase"
FT                   /id="PRO_0000439684"
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   430 AA;  44568 MW;  AB3365DEBA71DE39 CRC64;
     MTISNPRPLL GCIADDFTGA TDLANMLVRG GMRTVQSIGI PSAEVAAGLD ADAVVIALKS
     RTTAASEAVA ESLAALQWLR DQGCEQIFFK YCSTFDSTAA GNIGQVSEAL LEALGSDFTL
     ACPAFPENGR TIFRGHLFVQ DQLLSESGMQ HHPLTPMTDA NLVRVLQSQT RLPVGLLRYD
     SIAQGVEAVR SRIAELRGQG VALAIADALS DADLYTLGAA CADLPLLTGG SGLALGLPEN
     FRRAGKLRDL DAASLPKVAG GEVVLAGSAS LATNAQVDAW LEAERPAWRI DPLALAAGEA
     VVEQALAFAR EQQGTVLIYA TSTPEEVKAV QRQLGAERAG ALVENALGEI ARGLRDSGVR
     RFVVAGGETS GAVVKALDVR LLQIGAQIDP GVPATVSSGG EPLALALKSG NFGGRDFFSK
     ALGQLAGGQA