ID   OTNK_METRJ              Reviewed;         424 AA.
AC   B1M1V6;
DT   10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 62.
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=Mrad2831_1132 {ECO:0000312|EMBL:ACB23141.1};
OS   Methylobacterium radiotolerans (strain ATCC 27329 / DSM 1819 / JCM 2831 /
OS   NBRC 15690 / NCIMB 10815 / 0-1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Methylobacteriaceae; Methylobacterium.
OX   NCBI_TaxID=426355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27329 / DSM 1819 / JCM 2831 / NBRC 15690 / NCIMB 10815 / 0-1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T., Detter J.C., Han C.,
RA   Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Marx C.J., Richardson P.;
RT   "Complete sequence of chromosome of Methylobacterium radiotolerans JCM
RT   2831.";
RL   Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=ATCC 27329 / DSM 1819 / JCM 2831 / NBRC 15690 / NCIMB 10815 / 0-1;
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; CP001001; ACB23141.1; -; Genomic_DNA.
DR   RefSeq; WP_012318131.1; NC_010505.1.
DR   AlphaFoldDB; B1M1V6; -.
DR   SMR; B1M1V6; -.
DR   STRING; 426355.Mrad2831_1132; -.
DR   EnsemblBacteria; ACB23141; ACB23141; Mrad2831_1132.
DR   KEGG; mrd:Mrad2831_1132; -.
DR   PATRIC; fig|426355.14.peg.1176; -.
DR   eggNOG; COG3395; Bacteria.
DR   HOGENOM; CLU_029424_1_0_5; -.
DR   OMA; CSVMTNK; -.
DR   OrthoDB; 771666at2; -.
DR   Proteomes; UP000006589; 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..424
FT                   /note="3-oxo-tetronate kinase"
FT                   /id="PRO_0000439682"
FT   BINDING         264
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q0KBC8"
FT   BINDING         363..366
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q0KBC8"
FT   BINDING         408
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q0KBC8"
SQ   SEQUENCE   424 AA;  42893 MW;  B3F1860AD09D326C CRC64;
     MSLALGCVAD DYTGASDLAN TLTKAGLRTI QTIGVPEAGR ALPEADAVVV ALKSRSIPAD
     QAVARSREAE RWLRARGAAH VMFKVCSTFD STDAGNIGPV MDALRADAGE TVALVTPAFP
     ETGRSVYQGN LFVGSVPLNE SPLKDHPLNP MRDANLVRVL GRQSRSPVGL IDTATVARGA
     EAVAARLDAL AQEGKGAAIA DAIFDSDLEV LGRAILDRKF SVGASGLGLG LARALAADGR
     GTRDAAGAAV GEPVGGASAC LAGSCSQATL QQVAAAEAIM PVLRLDPARL LAGDDVVAEA
     LAFAEERLAS GPVLIATSAP PEAVRALQAA HGVDAAGHAI EAALAAIAEG LVARGVRRLV
     VAGGETSGAV VDRLGLTAFL LGPEIAAGVP VLRTAGRPEP MLLALKSGNF GGADFFGRAL
     DMMA