OTNK_PECAS
ID OTNK_PECAS Reviewed; 424 AA.
AC Q6CZ25;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 73.
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=ECA4328 {ECO:0000312|EMBL:CAG77225.1};
OS Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) (Erwinia
OS carotovora subsp. atroseptica).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Pectobacterium.
OX NCBI_TaxID=218491;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCRI 1043 / ATCC BAA-672;
RX PubMed=15263089; DOI=10.1073/pnas.0402424101;
RA Bell K.S., Sebaihia M., Pritchard L., Holden M.T.G., Hyman L.J.,
RA Holeva M.C., Thomson N.R., Bentley S.D., Churcher L.J.C., Mungall K.,
RA Atkin R., Bason N., Brooks K., Chillingworth T., Clark K., Doggett J.,
RA Fraser A., Hance Z., Hauser H., Jagels K., Moule S., Norbertczak H.,
RA Ormond D., Price C., Quail M.A., Sanders M., Walker D., Whitehead S.,
RA Salmond G.P.C., Birch P.R.J., Parkhill J., Toth I.K.;
RT "Genome sequence of the enterobacterial phytopathogen Erwinia carotovora
RT subsp. atroseptica and characterization of virulence factors.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:11105-11110(2004).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=SCRI 1043 / ATCC BAA-672;
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; BX950851; CAG77225.1; -; Genomic_DNA.
DR RefSeq; WP_011095792.1; NC_004547.2.
DR AlphaFoldDB; Q6CZ25; -.
DR SMR; Q6CZ25; -.
DR STRING; 218491.ECA4328; -.
DR EnsemblBacteria; CAG77225; CAG77225; ECA4328.
DR KEGG; eca:ECA4328; -.
DR PATRIC; fig|218491.5.peg.4407; -.
DR eggNOG; COG3395; Bacteria.
DR HOGENOM; CLU_029424_1_0_6; -.
DR OMA; CSVMTNK; -.
DR OrthoDB; 771666at2; -.
DR Proteomes; UP000007966; 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_0000439683"
FT BINDING 260
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q0KBC8"
FT BINDING 364..367
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q0KBC8"
FT BINDING 407
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q0KBC8"
SQ SEQUENCE 424 AA; 45525 MW; 91C00DFB42B12560 CRC64;
MIKLGVIADD FTGATDIASF LVNNGLPTVQ LNGVPPSDFK VDTQAVVISL KSRSCSAEQA
VADSLNALAW LQQQGCQQFY FKYCSTFDST AKGNIGPVTD ALLEQLGETQ TIISPALPVN
GRTVYQGHLF VMDQLLSESG MRHHPVTPMT DSNLMRVMEQ QAAGQCGLVP YAVMDQGADA
VKQRLAQLKE QGMRYVVLDT LNEQHLLTQG EALRDMKLVT GGSGLAIGLA RQWADSTKQT
SSATEAGKPQ SGAGVVLSGS CSVMTNKQVA HYLKQAAGRA IDVARCLESD DAQQSYAQEL
ADWVKAHRDD ALAPLLYATS SPDELAQIQQ RWGAEASSHA VEKLFAAVAR QLQEDGFQRF
IIAGGETSSI VVQTLGIHAF HIGPSISPGV PWVRSTTHPL SLALKSGNFG DEDFFARAQK
EFAA
