OTNK_ECOLI
ID OTNK_ECOLI Reviewed; 388 AA.
AC Q46889; Q2MA92;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=3-oxo-tetronate kinase {ECO:0000250|UniProtKB:P44093};
DE EC=2.7.1.217 {ECO:0000250|UniProtKB:P44093};
DE AltName: Full=3-dehydrotetronate 4-kinase {ECO:0000305};
GN Name=otnK {ECO:0000250|UniProtKB:P44093}; Synonyms=ygbK;
GN OrderedLocusNames=b2737, JW2707;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
CC -!- FUNCTION: Catalyzes the ATP-dependent phosphorylation of 3-oxo-
CC tetronate to 3-oxo-tetronate 4-phosphate.
CC {ECO:0000250|UniProtKB:P44093}.
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:0000250|UniProtKB:P44093};
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:0000250|UniProtKB:P44093};
CC -!- SIMILARITY: Belongs to the four-carbon acid sugar kinase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U29579; AAA69247.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75779.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76814.1; -; Genomic_DNA.
DR PIR; E65054; E65054.
DR RefSeq; NP_417217.1; NC_000913.3.
DR RefSeq; WP_001393459.1; NZ_LN832404.1.
DR AlphaFoldDB; Q46889; -.
DR SMR; Q46889; -.
DR BioGRID; 4261444; 20.
DR DIP; DIP-12112N; -.
DR IntAct; Q46889; 3.
DR STRING; 511145.b2737; -.
DR PaxDb; Q46889; -.
DR PRIDE; Q46889; -.
DR DNASU; 947199; -.
DR EnsemblBacteria; AAC75779; AAC75779; b2737.
DR EnsemblBacteria; BAE76814; BAE76814; BAE76814.
DR GeneID; 947199; -.
DR KEGG; ecj:JW2707; -.
DR KEGG; eco:b2737; -.
DR PATRIC; fig|511145.12.peg.2830; -.
DR EchoBASE; EB2908; -.
DR eggNOG; COG3395; Bacteria.
DR HOGENOM; CLU_029424_1_0_6; -.
DR InParanoid; Q46889; -.
DR OMA; CSVMTNK; -.
DR PhylomeDB; Q46889; -.
DR BioCyc; EcoCyc:G7418-MON; -.
DR PRO; PR:Q46889; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; 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 3: Inferred from homology;
KW ATP-binding; Carbohydrate metabolism; Kinase; Nucleotide-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..388
FT /note="3-oxo-tetronate kinase"
FT /id="PRO_0000169313"
FT BINDING 258
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q0KBC8"
FT BINDING 360..363
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q0KBC8"
SQ SEQUENCE 388 AA; 41339 MW; 5824A120E9393892 CRC64;
MIKIGVIADD FTGATDIASF LVENGLPTVQ INGVPTGKMP EAIDALVISL KTRSCPVVEA
TQQSLAALSW LQQQGCKQIY FKYCSTFDST AKGNIGPVTD ALMDALDTPF TVFSPALPVN
GRTVYQGYLF VMNQLLAESG MRHHPVNPMT DSYLPRLVEA QSTGRCGVVS AHVFEQGVDA
VRQELARLQQ EGYRYAVLDA LTEHHLEIQG EALRDAPLVT GGSGLAIGLA RQWAQENGNQ
ARKAGRPLAG RGVVLSGSCS QMTNRQVAHY RQIAPAREVD VARCLSIETL AAYAHELAEW
VLGQESVLAP LVFATASTDA LAAIQQQYGA QKASQAVETL FSQLAARLAA EGVTRFIVAG
GETSGVVTQS LGIKGFHIGP TISPACRG
