ID   OTNC_CUPNH              Reviewed;         217 AA.
AC   Q0KBC9;
DT   10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 81.
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=H16_A1560 {ECO:0000312|EMBL:CAJ92692.1};
OS   Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442
OS   / H16 / Stanier 337) (Ralstonia eutropha).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=381666;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337;
RX   PubMed=16964242; DOI=10.1038/nbt1244;
RA   Pohlmann A., Fricke W.F., Reinecke F., Kusian B., Liesegang H., Cramm R.,
RA   Eitinger T., Ewering C., Poetter M., Schwartz E., Strittmatter A., Voss I.,
RA   Gottschalk G., Steinbuechel A., Friedrich B., Bowien B.;
RT   "Genome sequence of the bioplastic-producing 'Knallgas' bacterium Ralstonia
RT   eutropha H16.";
RL   Nat. Biotechnol. 24:1257-1262(2006).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337;
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   -!- 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 aldolase class II family. AraD/FucA
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AM260479; CAJ92692.1; -; Genomic_DNA.
DR   RefSeq; WP_010810012.1; NZ_CP039287.1.
DR   AlphaFoldDB; Q0KBC9; -.
DR   SMR; Q0KBC9; -.
DR   STRING; 381666.H16_A1560; -.
DR   EnsemblBacteria; CAJ92692; CAJ92692; H16_A1560.
DR   GeneID; 57643659; -.
DR   KEGG; reh:H16_A1560; -.
DR   PATRIC; fig|381666.6.peg.1945; -.
DR   eggNOG; COG0235; Bacteria.
DR   HOGENOM; CLU_006033_3_2_4; -.
DR   OMA; ICRYGRS; -.
DR   OrthoDB; 599627at2; -.
DR   BRENDA; 4.1.1.104; 231.
DR   Proteomes; UP000008210; Chromosome 1.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
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..217
FT                   /note="3-oxo-tetronate 4-phosphate decarboxylase"
FT                   /id="PRO_0000439750"
FT   ACT_SITE        120
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P0AB87"
FT   BINDING         93
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P0AB87"
FT   BINDING         95
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P0AB87"
SQ   SEQUENCE   217 AA;  23584 MW;  0893E7B4871E329E CRC64;
     MSTESKLREE ICRIGASLYQ RGYTVGSAGN ISARLDDGWL ITPTDACLGM MDPAAVAKVA
     TDGSWVSGDK PSKTLMLHRA IYDNNREAHA VVHTHSTHLV ALTLAGVWQP DDVLPPLTPY
     YVMKVGHIPL IPYHRPGDPA VAARVATLAA QVRGVLLERL GPVVWESSVS RAAFALEELE
     ETAKLWMTMK DTPGFAARAA LPDGALTELR DAFQARW