OTNC_PECAS
ID OTNC_PECAS Reviewed; 218 AA.
AC Q6CZ24;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 76.
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=ECA4329 {ECO:0000312|EMBL:CAG77226.1};
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 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}.
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DR EMBL; BX950851; CAG77226.1; -; Genomic_DNA.
DR RefSeq; WP_011095793.1; NC_004547.2.
DR AlphaFoldDB; Q6CZ24; -.
DR SMR; Q6CZ24; -.
DR STRING; 218491.ECA4329; -.
DR EnsemblBacteria; CAG77226; CAG77226; ECA4329.
DR GeneID; 57211022; -.
DR KEGG; eca:ECA4329; -.
DR PATRIC; fig|218491.5.peg.4408; -.
DR eggNOG; COG0235; Bacteria.
DR HOGENOM; CLU_006033_3_2_6; -.
DR OMA; ICRYGRS; -.
DR OrthoDB; 599627at2; -.
DR BRENDA; 4.1.1.104; 9330.
DR Proteomes; UP000007966; 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; Reference proteome; Zinc.
FT CHAIN 1..218
FT /note="3-oxo-tetronate 4-phosphate decarboxylase"
FT /id="PRO_0000439752"
FT ACT_SITE 86
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P0AB87"
FT ACT_SITE 132
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P0AB87"
FT BINDING 86
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P0AB87"
FT BINDING 105
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P0AB87"
FT BINDING 107
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P0AB87"
FT BINDING 172
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P0AB87"
SQ SEQUENCE 218 AA; 23745 MW; 6DEB30FBCF85C05D CRC64;
MSEHHNGTEA SLSSEQRARA EMVKLGASFF QRGYATGSAG NLSLLLDDGT LLATPTGSCL
GELDAERLSK VSLSGEWISG DKPSKEVSFH LSIYRNDPEC KAIVHLHSTY LTALSCLEGL
DTQDAIKPFT PYVVMRVGKV PVVPYYRPGD ARLGEDLAKL ASRYKAFLLA NHGPVVTGKN
LRAAADNMEE LEETAKLIFI LGDRKIRYLT ADDIAELS
