OTNK_SALTY
ID OTNK_SALTY Reviewed; 420 AA.
AC Q8ZMG5;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 93.
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:0000303|PubMed:27402745};
GN Synonyms=ygbK {ECO:0000312|EMBL:AAL21797.1};
GN OrderedLocusNames=STM2917 {ECO:0000312|EMBL:AAL21797.1};
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [2]
RP DISRUPTION PHENOTYPE.
RC STRAIN=LT2;
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).
RN [3] {ECO:0007744|PDB:3DQQ}
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS).
RC STRAIN=LT2;
RA Zhang R., Gu M., Zhou M., Anderson W., Joachimiak A.;
RT "The crystal structure of the putative tRNA synthase from Salmonella
RT typhimurium LT2.";
RL Submitted (JUL-2008) to the PDB data bank.
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 -!- DISRUPTION PHENOTYPE: Deletion mutant is unable to use L-threonate or
CC D-erythronate as a carbon source. {ECO:0000269|PubMed:27402745}.
CC -!- SIMILARITY: Belongs to the four-carbon acid sugar kinase family.
CC {ECO:0000305}.
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DR EMBL; AE006468; AAL21797.1; -; Genomic_DNA.
DR RefSeq; NP_461838.1; NC_003197.2.
DR RefSeq; WP_000912488.1; NC_003197.2.
DR PDB; 3DQQ; X-ray; 2.70 A; A/B=1-420.
DR PDBsum; 3DQQ; -.
DR AlphaFoldDB; Q8ZMG5; -.
DR SMR; Q8ZMG5; -.
DR STRING; 99287.STM2917; -.
DR PaxDb; Q8ZMG5; -.
DR EnsemblBacteria; AAL21797; AAL21797; STM2917.
DR GeneID; 1254440; -.
DR KEGG; stm:STM2917; -.
DR PATRIC; fig|99287.12.peg.3071; -.
DR HOGENOM; CLU_029424_1_0_6; -.
DR OMA; CSVMTNK; -.
DR PhylomeDB; Q8ZMG5; -.
DR BioCyc; SENT99287:STM2917-MON; -.
DR BRENDA; 2.7.1.217; 5542.
DR EvolutionaryTrace; Q8ZMG5; -.
DR Proteomes; UP000001014; 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..420
FT /note="3-oxo-tetronate kinase"
FT /id="PRO_0000439686"
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"
FT BINDING 403
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q0KBC8"
FT STRAND 4..10
FT /evidence="ECO:0007829|PDB:3DQQ"
FT HELIX 11..23
FT /evidence="ECO:0007829|PDB:3DQQ"
FT STRAND 28..34
FT /evidence="ECO:0007829|PDB:3DQQ"
FT STRAND 44..49
FT /evidence="ECO:0007829|PDB:3DQQ"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:3DQQ"
FT HELIX 57..73
FT /evidence="ECO:0007829|PDB:3DQQ"
FT STRAND 77..82
FT /evidence="ECO:0007829|PDB:3DQQ"
FT HELIX 95..105
FT /evidence="ECO:0007829|PDB:3DQQ"
FT STRAND 111..114
FT /evidence="ECO:0007829|PDB:3DQQ"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:3DQQ"
FT STRAND 122..125
FT /evidence="ECO:0007829|PDB:3DQQ"
FT STRAND 128..131
FT /evidence="ECO:0007829|PDB:3DQQ"
FT HELIX 136..138
FT /evidence="ECO:0007829|PDB:3DQQ"
FT HELIX 140..143
FT /evidence="ECO:0007829|PDB:3DQQ"
FT STRAND 145..147
FT /evidence="ECO:0007829|PDB:3DQQ"
FT HELIX 154..159
FT /evidence="ECO:0007829|PDB:3DQQ"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:3DQQ"
FT STRAND 166..169
FT /evidence="ECO:0007829|PDB:3DQQ"
FT HELIX 171..176
FT /evidence="ECO:0007829|PDB:3DQQ"
FT HELIX 178..190
FT /evidence="ECO:0007829|PDB:3DQQ"
FT STRAND 194..198
FT /evidence="ECO:0007829|PDB:3DQQ"
FT STRAND 200..202
FT /evidence="ECO:0007829|PDB:3DQQ"
FT HELIX 203..213
FT /evidence="ECO:0007829|PDB:3DQQ"
FT STRAND 217..222
FT /evidence="ECO:0007829|PDB:3DQQ"
FT HELIX 223..234
FT /evidence="ECO:0007829|PDB:3DQQ"
FT HELIX 243..245
FT /evidence="ECO:0007829|PDB:3DQQ"
FT STRAND 252..256
FT /evidence="ECO:0007829|PDB:3DQQ"
FT HELIX 261..270
FT /evidence="ECO:0007829|PDB:3DQQ"
FT TURN 271..273
FT /evidence="ECO:0007829|PDB:3DQQ"
FT STRAND 276..278
FT /evidence="ECO:0007829|PDB:3DQQ"
FT HELIX 281..283
FT /evidence="ECO:0007829|PDB:3DQQ"
FT STRAND 284..286
FT /evidence="ECO:0007829|PDB:3DQQ"
FT HELIX 287..303
FT /evidence="ECO:0007829|PDB:3DQQ"
FT STRAND 311..313
FT /evidence="ECO:0007829|PDB:3DQQ"
FT HELIX 317..319
FT /evidence="ECO:0007829|PDB:3DQQ"
FT HELIX 320..324
FT /evidence="ECO:0007829|PDB:3DQQ"
FT HELIX 335..350
FT /evidence="ECO:0007829|PDB:3DQQ"
FT STRAND 355..360
FT /evidence="ECO:0007829|PDB:3DQQ"
FT HELIX 361..370
FT /evidence="ECO:0007829|PDB:3DQQ"
FT STRAND 375..383
FT /evidence="ECO:0007829|PDB:3DQQ"
FT STRAND 386..395
FT /evidence="ECO:0007829|PDB:3DQQ"
FT STRAND 397..401
FT /evidence="ECO:0007829|PDB:3DQQ"
FT HELIX 410..416
FT /evidence="ECO:0007829|PDB:3DQQ"
SQ SEQUENCE 420 AA; 44791 MW; C90E6ED8DF9E34B4 CRC64;
MLKIGVIADD FTGATDIASF LVENGMPTVQ INDVPTGTQP EGCDAVVISL KTRSCPAQEA
IKQSLAALVW LKKQGCQQVY FKYCSTFDST AEGNIGPVTD ALMVALDTSF TVISPALPVN
GRTVYQGYLF VMNHLLAESG MRHHPINPMT DSYLPRLMEA QAQGRCGVIP AQTLDEGVAA
TRAALSRLQQ EGYRYAVLDA LNERHLEIQG EVLRDAPLVT GGSGLAMGLA RQWAKHGVSQ
ARSAGYPLSG RAVVLSGSCS QMTNQQVAFY RQHAPTRDVD VARCLSSETR EAYAEALAQW
VLSQDSELAP MISATASTQA LAAIQQQYGA TEASHAVEAL FSLLAARLAE GGITRFIVAG
GETSGVVTQS LGITGFHIGP CISPGVPWVN ALHAPVSLAL KSGNFGDESF FIRAQREFQV
