ID   IOLJ_ALKCK              Reviewed;         293 AA.
AC   Q5WKY5;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=6-phospho-5-dehydro-2-deoxy-D-gluconate aldolase;
DE            Short=DKGP aldolase;
DE            EC=4.1.2.29;
GN   Name=iolJ; OrderedLocusNames=ABC0428;
OS   Alkalihalobacillus clausii (strain KSM-K16) (Bacillus clausii).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX   NCBI_TaxID=66692;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KSM-K16;
RA   Takaki Y., Kageyama Y., Shimamura S., Suzuki H., Nishi S., Hatada Y.,
RA   Kawai S., Ito S., Horikoshi K.;
RT   "The complete genome sequence of the alkaliphilic Bacillus clausii KSM-
RT   K16.";
RL   Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Produces dihydroxyacetone phosphate (DHAP or glycerone
CC       phosphate) and malonic semialdehyde (MSA or 3-oxopropanoate) from 6-
CC       phospho-5-dehydro-2-deoxy-D-gluconate (DKGP). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=6-phospho-5-dehydro-2-deoxy-D-gluconate = 3-oxopropanoate +
CC         dihydroxyacetone phosphate; Xref=Rhea:RHEA:13177, ChEBI:CHEBI:33190,
CC         ChEBI:CHEBI:57642, ChEBI:CHEBI:57949; EC=4.1.2.29;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC   -!- PATHWAY: Polyol metabolism; myo-inositol degradation into acetyl-CoA;
CC       acetyl-CoA from myo-inositol: step 6/7.
CC   -!- SIMILARITY: Belongs to the class II fructose-bisphosphate aldolase
CC       family. IolJ subfamily. {ECO:0000305}.
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DR   EMBL; AP006627; BAD62970.1; -; Genomic_DNA.
DR   RefSeq; WP_011245289.1; NC_006582.1.
DR   AlphaFoldDB; Q5WKY5; -.
DR   SMR; Q5WKY5; -.
DR   STRING; 66692.ABC0428; -.
DR   EnsemblBacteria; BAD62970; BAD62970; ABC0428.
DR   KEGG; bcl:ABC0428; -.
DR   eggNOG; COG0191; Bacteria.
DR   HOGENOM; CLU_040088_0_1_9; -.
DR   OMA; TVGGMED; -.
DR   OrthoDB; 827430at2; -.
DR   UniPathway; UPA00076; UER00147.
DR   Proteomes; UP000001168; Chromosome.
DR   GO; GO:0047441; F:5-dehydro-2-deoxyphosphogluconate aldolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0030388; P:fructose 1,6-bisphosphate metabolic process; IEA:InterPro.
DR   GO; GO:0006096; P:glycolytic process; IEA:InterPro.
DR   CDD; cd00947; TBP_aldolase_IIB; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR000771; FBA_II.
DR   InterPro; IPR011289; Fruc_bis_ald_class-2.
DR   Pfam; PF01116; F_bP_aldolase; 1.
DR   PIRSF; PIRSF001359; F_bP_aldolase_II; 1.
DR   TIGRFAMs; TIGR00167; cbbA; 1.
DR   TIGRFAMs; TIGR01859; fruc_bis_ald; 1.
DR   PROSITE; PS00806; ALDOLASE_CLASS_II_2; 1.
PE   3: Inferred from homology;
KW   Lyase; Metal-binding; Phosphoprotein; Reference proteome; Zinc.
FT   CHAIN           1..293
FT                   /note="6-phospho-5-dehydro-2-deoxy-D-gluconate aldolase"
FT                   /id="PRO_0000352281"
FT   ACT_SITE        85
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         86
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         180
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         181
FT                   /ligand="dihydroxyacetone phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57642"
FT                   /evidence="ECO:0000250"
FT   BINDING         208
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         209..211
FT                   /ligand="dihydroxyacetone phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57642"
FT                   /evidence="ECO:0000250"
FT   BINDING         230..233
FT                   /ligand="dihydroxyacetone phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57642"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         233
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   293 AA;  31239 MW;  532F8E249FBD9BEB CRC64;
     MGFVPMAPLL ADAKKDSYAI GQFNINGLQW AKAILAGAES QQSPVIAAAS DRLIDYLGGF
     QTVVAMMGAL TDELGITVPV VLHLDHGLSI ERCKKAVDAG FSSVMFDGSH YPINENIDMT
     KEVVAYAHAH NVSVEGEVGT VGGMEDGLMA EIKYADVEEC QRFVCETNVD ALAAALGSVH
     GKYKGEPKLG FNEMAAISAS TNVPLVLHGA SGIPDEQLQR AIKLGHAKIN INTECMIAWS
     DACRTTFAEQ ETAFEPRLLL QEGLAMVQAT VEKKIKQFGA ANKAAGSASL QRR