ID   OTNC_ECOL6              Reviewed;         212 AA.
AC   A0A0H2VA12;
DT   10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT   16-SEP-2015, sequence version 1.
DT   03-AUG-2022, entry version 24.
DE   RecName: Full=3-oxo-tetronate 4-phosphate decarboxylase {ECO:0000303|PubMed:27402745};
DE            EC=4.1.1.104 {ECO:0000269|PubMed:27402745};
GN   Name=otnC {ECO:0000303|PubMed:27402745};
GN   OrderedLocusNames=c3299 {ECO:0000312|EMBL:AAN81748.1};
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
RN   [2]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
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 decarboxylation of 3-oxo-tetronate 4-phosphate
CC       to dihydroxyacetone phosphate (DHAP) and CO(2).
CC       {ECO:0000269|PubMed:27402745}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-dehydro-4-O-phospho-D-erythronate + H(+) = CO2 +
CC         dihydroxyacetone phosphate; Xref=Rhea:RHEA:52416, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:57642, ChEBI:CHEBI:136593;
CC         EC=4.1.1.104; Evidence={ECO:0000269|PubMed:27402745};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-dehydro-4-O-phospho-L-erythronate + H(+) = CO2 +
CC         dihydroxyacetone phosphate; Xref=Rhea:RHEA:52404, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:57642, ChEBI:CHEBI:136592;
CC         EC=4.1.1.104; Evidence={ECO:0000269|PubMed:27402745};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:P0AB87};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P0AB87};
CC   -!- SIMILARITY: Belongs to the aldolase class II family. AraD/FucA
CC       subfamily. {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; AE014075; AAN81748.1; -; Genomic_DNA.
DR   RefSeq; WP_001279001.1; NC_004431.1.
DR   AlphaFoldDB; A0A0H2VA12; -.
DR   SMR; A0A0H2VA12; -.
DR   STRING; 199310.c3299; -.
DR   EnsemblBacteria; AAN81748; AAN81748; c3299.
DR   KEGG; ecc:c3299; -.
DR   eggNOG; COG0235; Bacteria.
DR   HOGENOM; CLU_006033_3_2_6; -.
DR   OMA; ICRYGRS; -.
DR   BRENDA; 4.1.1.104; 2026.
DR   Proteomes; UP000001410; Chromosome.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005996; P:monosaccharide metabolic process; IEA:UniProt.
DR   Gene3D; 3.40.225.10; -; 1.
DR   InterPro; IPR001303; Aldolase_II/adducin_N.
DR   InterPro; IPR036409; Aldolase_II/adducin_N_sf.
DR   Pfam; PF00596; Aldolase_II; 1.
DR   SMART; SM01007; Aldolase_II; 1.
DR   SUPFAM; SSF53639; SSF53639; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Lyase; Metal-binding; Zinc.
FT   CHAIN           1..212
FT                   /note="3-oxo-tetronate 4-phosphate decarboxylase"
FT                   /id="PRO_0000439751"
FT   ACT_SITE        79
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P0AB87"
FT   ACT_SITE        125
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P0AB87"
FT   BINDING         79
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P0AB87"
FT   BINDING         98
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P0AB87"
FT   BINDING         100
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P0AB87"
FT   BINDING         165
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P0AB87"
SQ   SEQUENCE   212 AA;  23281 MW;  120D7165E7791EB3 CRC64;
     MSDFAKVEQS LREEMTRIAS SFFQRGYATG SAGNLSLLLP DGNLLATPTG SCLGNLDPQR
     LSKVTADGEW LSGDKPSKEV LFHLALYRNN PRCKAVVHLH STWSTALSCL EGLDSNNVIR
     PFTPYVVMRM GNVPLVPYYR PGDKRIAQDL AELAADNQAF LLANHGPVVC GESLQEAANN
     MEELEETAKL IFILGDRPIR YLTAGEIAEL RS