ID   IOLJ_BACVZ              Reviewed;         290 AA.
AC   A7ZAH2;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 90.
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=RBAM_036690;
OS   Bacillus velezensis (strain DSM 23117 / BGSC 10A6 / LMG 26770 / FZB42)
OS   (Bacillus amyloliquefaciens subsp. plantarum).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus amyloliquefaciens group.
OX   NCBI_TaxID=326423;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 23117 / BGSC 10A6 / LMG 26770 / FZB42;
RX   PubMed=17704766; DOI=10.1038/nbt1325;
RA   Chen X.H., Koumoutsi A., Scholz R., Eisenreich A., Schneider K.,
RA   Heinemeyer I., Morgenstern B., Voss B., Hess W.R., Reva O., Junge H.,
RA   Voigt B., Jungblut P.R., Vater J., Suessmuth R., Liesegang H.,
RA   Strittmatter A., Gottschalk G., Borriss R.;
RT   "Comparative analysis of the complete genome sequence of the plant growth-
RT   promoting bacterium Bacillus amyloliquefaciens FZB42.";
RL   Nat. Biotechnol. 25:1007-1014(2007).
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; CP000560; ABS75998.1; -; Genomic_DNA.
DR   RefSeq; WP_012118840.1; NC_009725.2.
DR   AlphaFoldDB; A7ZAH2; -.
DR   SMR; A7ZAH2; -.
DR   STRING; 326423.RBAM_036690; -.
DR   EnsemblBacteria; ABS75998; ABS75998; RBAM_036690.
DR   KEGG; bay:RBAM_036690; -.
DR   HOGENOM; CLU_040088_0_1_9; -.
DR   OMA; TVGGMED; -.
DR   UniPathway; UPA00076; UER00147.
DR   Proteomes; UP000001120; 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; Zinc.
FT   CHAIN           1..290
FT                   /note="6-phospho-5-dehydro-2-deoxy-D-gluconate aldolase"
FT                   /id="PRO_0000352280"
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   290 AA;  31357 MW;  3047EDBC4B761908 CRC64;
     MAFVTMKHLL AEAKREHYAV GQFNINGLQW TKAILQAAQK EQSPVIAAAS DRLVDYLGGF
     KTISAMVGAL MEEMAITVPV VLHLDHGSSA ERCRQAIDAG FSSVMIDGSH HPIDENIAMT
     KEVADYAAKH GVSVEAEVGT VGGMEDGLVG GVRYADVAEC ERIVKETNID ALAAALGSVH
     GKYQGEPNLG FKEMEAISRM TDIPLVLHGA SGIPQEQIKK AITLGHAKIN INTECMVAWT
     DETRRMFQKN GDLYEPRGYM TPGIEAVEET VRSKMREFGS AGKAVKQQVG