ID   IOLJ_ALKHC              Reviewed;         288 AA.
AC   Q9KAH3;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 105.
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=BH2314;
OS   Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS   / JCM 9153 / C-125) (Bacillus halodurans).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX   NCBI_TaxID=272558;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX   PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA   Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA   Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT   "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT   and genomic sequence comparison with Bacillus subtilis.";
RL   Nucleic Acids Res. 28:4317-4331(2000).
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}.
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; BA000004; BAB06033.1; -; Genomic_DNA.
DR   PIR; B83939; B83939.
DR   RefSeq; WP_010898470.1; NC_002570.2.
DR   AlphaFoldDB; Q9KAH3; -.
DR   SMR; Q9KAH3; -.
DR   STRING; 272558.10174934; -.
DR   EnsemblBacteria; BAB06033; BAB06033; BAB06033.
DR   KEGG; bha:BH2314; -.
DR   eggNOG; COG0191; Bacteria.
DR   HOGENOM; CLU_040088_0_1_9; -.
DR   OMA; TVGGMED; -.
DR   OrthoDB; 827430at2; -.
DR   UniPathway; UPA00076; UER00147.
DR   Proteomes; UP000001258; 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; PS00602; ALDOLASE_CLASS_II_1; 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..288
FT                   /note="6-phospho-5-dehydro-2-deoxy-D-gluconate aldolase"
FT                   /id="PRO_0000352282"
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   288 AA;  31175 MW;  B9F1668378B762AF CRC64;
     MALVSMKEML KKAKAGHYAV GQFNLNNLQW AQAILQAAEE EQAPVIVAAS DRLVDFLGGF
     QTITSMVNSL LIEMKITVPV ALHLDHGMTI DRCKQAIDAG FTSVMIDGSH SPIEDNIAMT
     KEVVAYAQPR NVSVEAEVGT VGGMEDGLIG GVKYADLDEC VRVVEEANID ALAAALGSVH
     GPYQGEPKLG FEEMKVISER TGVPLVLHGG SGIPDYQIRK AILLGHAKIN VNTECLQAWA
     HAVRTILTND QDIYDYRAIT TPGTEAIVET VKTKMREFQT SGKAKERV