OTNC_ECOLI
ID OTNC_ECOLI Reviewed; 212 AA.
AC Q46890; Q2MA91;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=3-oxo-tetronate 4-phosphate decarboxylase {ECO:0000250|UniProtKB:A0A0H2VA12};
DE EC=4.1.1.104 {ECO:0000250|UniProtKB:A0A0H2VA12};
GN Name=otnC {ECO:0000250|UniProtKB:A0A0H2VA12}; Synonyms=ygbL;
GN OrderedLocusNames=b2738, JW2708;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=O111:H- / DEC 12e / CDC 3291-86, and O26:NM / DEC 9f / CDC 2666-74;
RX PubMed=10986240; DOI=10.1128/jb.182.19.5381-5390.2000;
RA Herbelin C.J., Chirillo S.C., Melnick K.A., Whittam T.S.;
RT "Gene conservation and loss in the mutS-rpoS genomic region of pathogenic
RT Escherichia coli.";
RL J. Bacteriol. 182:5381-5390(2000).
RN [2]
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 [3]
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 decarboxylation of 3-oxo-tetronate 4-phosphate
CC to dihydroxyacetone phosphate (DHAP) and CO(2).
CC {ECO:0000250|UniProtKB:A0A0H2VA12}.
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:0000250|UniProtKB:A0A0H2VA12};
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:0000250|UniProtKB:A0A0H2VA12};
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}.
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DR EMBL; AF242208; AAG14969.1; -; Genomic_DNA.
DR EMBL; AF242210; AAG14982.1; -; Genomic_DNA.
DR EMBL; U29579; AAA69248.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75780.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76815.1; -; Genomic_DNA.
DR PIR; F65054; F65054.
DR RefSeq; NP_417218.1; NC_000913.3.
DR RefSeq; WP_001278994.1; NZ_STEB01000027.1.
DR PDB; 6VOP; X-ray; 2.65 A; A=1-212.
DR PDBsum; 6VOP; -.
DR AlphaFoldDB; Q46890; -.
DR SMR; Q46890; -.
DR BioGRID; 4261445; 11.
DR DIP; DIP-12113N; -.
DR IntAct; Q46890; 2.
DR STRING; 511145.b2738; -.
DR PaxDb; Q46890; -.
DR PRIDE; Q46890; -.
DR EnsemblBacteria; AAC75780; AAC75780; b2738.
DR EnsemblBacteria; BAE76815; BAE76815; BAE76815.
DR GeneID; 66673392; -.
DR GeneID; 947197; -.
DR KEGG; ecj:JW2708; -.
DR KEGG; eco:b2738; -.
DR PATRIC; fig|1411691.4.peg.4002; -.
DR EchoBASE; EB2909; -.
DR eggNOG; COG0235; Bacteria.
DR HOGENOM; CLU_006033_3_2_6; -.
DR InParanoid; Q46890; -.
DR OMA; ICRYGRS; -.
DR PhylomeDB; Q46890; -.
DR BioCyc; EcoCyc:G7419-MON; -.
DR PRO; PR:Q46890; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0016832; F:aldehyde-lyase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019323; P:pentose catabolic process; IBA:GO_Central.
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 3D-structure; Carbohydrate metabolism; Lyase; Metal-binding;
KW Reference proteome; Zinc.
FT CHAIN 1..212
FT /note="3-oxo-tetronate 4-phosphate decarboxylase"
FT /id="PRO_0000162930"
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"
FT HELIX 7..24
FT /evidence="ECO:0007829|PDB:6VOP"
FT STRAND 27..29
FT /evidence="ECO:0007829|PDB:6VOP"
FT STRAND 32..38
FT /evidence="ECO:0007829|PDB:6VOP"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:6VOP"
FT HELIX 53..55
FT /evidence="ECO:0007829|PDB:6VOP"
FT HELIX 58..60
FT /evidence="ECO:0007829|PDB:6VOP"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:6VOP"
FT STRAND 70..74
FT /evidence="ECO:0007829|PDB:6VOP"
FT HELIX 80..89
FT /evidence="ECO:0007829|PDB:6VOP"
FT STRAND 95..99
FT /evidence="ECO:0007829|PDB:6VOP"
FT HELIX 102..107
FT /evidence="ECO:0007829|PDB:6VOP"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:6VOP"
FT HELIX 125..129
FT /evidence="ECO:0007829|PDB:6VOP"
FT HELIX 144..153
FT /evidence="ECO:0007829|PDB:6VOP"
FT STRAND 158..162
FT /evidence="ECO:0007829|PDB:6VOP"
FT TURN 163..165
FT /evidence="ECO:0007829|PDB:6VOP"
FT STRAND 166..173
FT /evidence="ECO:0007829|PDB:6VOP"
FT HELIX 174..194
FT /evidence="ECO:0007829|PDB:6VOP"
FT HELIX 204..208
FT /evidence="ECO:0007829|PDB:6VOP"
SQ SEQUENCE 212 AA; 23222 MW; 13A2D480BD6BE02F CRC64;
MSDFAKVEQS LREEMTRIAS SFFQRGYATG SAGNLSLLLP DGNLLATPTG SCLGNLDPQR
LSKVAADGEW LSGDKPSKEV LFHLALYRNN PRCKAVVHLH STWSTALSCL QGLDSSNVIR
PFTPYVVMRM GNVPLVPYYR PGDKRIAQDL AELAADNQAF LLANHGPVVC GESLQEAANN
MEELEETAKL IFILGDRPIR YLTAGEIAEL RS
