ID   IOLJ_BACLD              Reviewed;         292 AA.
AC   Q65D09; Q62NI5;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   16-JUN-2009, entry version 38.
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=BLi04242, BL00237;
OS   Bacillus licheniformis (strain DSM 13 / ATCC 14580).
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=279010;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15383718; DOI=10.1159/000079829;
RA   Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H.,
RA   Ehrenreich P., Baeumer S., Henne A., Liesegang H., Merkl R.,
RA   Ehrenreich A., Gottschalk G.;
RT   "The complete genome sequence of Bacillus licheniformis DSM13, an
RT   organism with great industrial potential.";
RL   J. Mol. Microbiol. Biotechnol. 7:204-211(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15461803; DOI=10.1186/gb-2004-5-10-r77;
RA   Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J.,
RA   Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G.,
RA   Olsen P.B., Rasmussen M.D., Andersen J.T., Joergensen P.L.,
RA   Larsen T.S., Sorokin A., Bolotin A., Lapidus A., Galleron N.,
RA   Ehrlich S.D., Berka R.M.;
RT   "Complete genome sequence of the industrial bacterium Bacillus
RT   licheniformis and comparisons with closely related Bacillus species.";
RL   Genome Biol. 5:RESEARCH077.1-RESEARCH077.12(2004).
CC   -!- FUNCTION: Produces dihydroxyacetone phosphate (DHAP or glycerone
CC       phosphate) and malonic semialdehyde (MSA or 3-oxopropanoate) from
CC       6-phospho-5-dehydro-2-deoxy-D-gluconate (DKGP) (By similarity).
CC   -!- CATALYTIC ACTIVITY: 5-dehydro-2-deoxy-D-gluconate 6-phosphate =
CC       glycerone phosphate + malonate semialdehyde.
CC   -!- COFACTOR: Zinc (By similarity).
CC   -!- PATHWAY: Polyol metabolism; myo-inositol degradation into acetyl-
CC       CoA; acetyl-CoA from myo-inositol: step 6/7.
CC   -!- SIMILARITY: Belongs to the class II fructose-bisphosphate aldolase
CC       family. IolJ subfamily.
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DR   EMBL; CP000002; AAU25676.1; -; Genomic_DNA.
DR   EMBL; AE017333; AAU43055.1; -; Genomic_DNA.
DR   RefSeq; YP_081314.1; -.
DR   RefSeq; YP_093748.1; -.
DR   GeneID; 3030964; -.
DR   GeneID; 3100047; -.
DR   GenomeReviews; AE017333_GR; BLi04242.
DR   GenomeReviews; CP000002_GR; BL00237.
DR   KEGG; bld:BLi04242; -.
DR   KEGG; bli:BL00237; -.
DR   NMPDR; fig|279010.5.peg.3950; -.
DR   HOGENOM; Q65D09; -.
DR   OMA; Q65D09; VGGMEDG.
DR   GO; GO:0047441; F:5-dehydro-2-deoxyphosphogluconate aldolase ...; IEA:EC.
DR   GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030388; P:fructose 1,6-bisphosphate metabolic process; IEA:InterPro.
DR   GO; GO:0006096; P:glycolysis; IEA:InterPro.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR011289; Fruc_bis_ald_.
DR   InterPro; IPR000771; Ketose_bisP_aldolase_II.
DR   Gene3D; G3DSA:3.20.20.70; Aldolase_TIM; 1.
DR   Pfam; PF01116; F_bP_aldolase; 1.
DR   PIRSF; PIRSF001359; F_bP_aldolase_II; 1.
DR   ProDom; PD002376; K_bP_aldolase; 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   Complete proteome; Lyase; Metal-binding; Phosphoprotein; Zinc.
FT   CHAIN         1    292       6-phospho-5-dehydro-2-deoxy-D-gluconate
FT                                aldolase.
FT                                /FTId=PRO_0000352283.
FT   REGION      209    211       Dihydroxyacetone phosphate binding (By
FT                                similarity).
FT   REGION      230    233       Dihydroxyacetone phosphate binding (By
FT                                similarity).
FT   ACT_SITE     85     85       Proton donor (By similarity).
FT   METAL        86     86       Zinc; catalytic (By similarity).
FT   METAL       180    180       Zinc; catalytic (By similarity).
FT   METAL       208    208       Zinc; catalytic (By similarity).
FT   BINDING     181    181       Dihydroxyacetone phosphate; via amide
FT                                nitrogen (By similarity).
FT   MOD_RES     233    233       Phosphothreonine (By similarity).
SQ   SEQUENCE   292 AA;  31615 MW;  38BD8CF7A956FFCA CRC64;
     MAFVSMKELL QEAKEHHYAI GQFNINGLQW TKAILEAAEE ERSPVIAAAS DRLIDYLGGF
     KTVSAMVAAL IEEMSISVPV VLHLDHGKSP ERCKQAIDAG FSSVMIDGSH SPIDENIAMT
     KEVVSYAGVR NVSVEAEVGT VGGMEDGLIG GVQYADIGEC ERIVKETGID ALAAALGSVH
     GKYQGEPNLG FKEMEEISRV TDIPLVLHGA SGIPADQIAR TIRLGHAKIN INTECMVAWT
     EKTRSIFKDN PDLYEPRAYM TPGISAVKET VKHKMREFGS SGKAVCTQKI EI
//