IOLJ_BACLD
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 03-AUG-2022, entry version 103.
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 ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 /
OS NBRC 12200 / NCIMB 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=279010;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375
RC / NCTC 10341 / NRRL NRS-1264 / Gibson 46;
RX PubMed=15383718; DOI=10.1159/000079829;
RA Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P.,
RA Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G.;
RT "The complete genome sequence of Bacillus licheniformis DSM13, an organism
RT with great industrial potential.";
RL J. Mol. Microbiol. Biotechnol. 7:204-211(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375
RC / NCTC 10341 / NRRL NRS-1264 / Gibson 46;
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., Olsen P.B.,
RA Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A.,
RA Bolotin A., Lapidus A., Galleron N., 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:R77.1-R77.12(2004).
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; CP000002; AAU25676.1; -; Genomic_DNA.
DR EMBL; AE017333; AAU43055.1; -; Genomic_DNA.
DR RefSeq; WP_003177802.1; NC_006322.1.
DR AlphaFoldDB; Q65D09; -.
DR SMR; Q65D09; -.
DR STRING; 279010.BL00237; -.
DR EnsemblBacteria; AAU25676; AAU25676; BL00237.
DR GeneID; 66213829; -.
DR KEGG; bld:BLi04242; -.
DR KEGG; bli:BL00237; -.
DR eggNOG; COG0191; Bacteria.
DR HOGENOM; CLU_040088_0_1_9; -.
DR OMA; TVGGMED; -.
DR BioCyc; BLIC279010:BLI_RS20860-MON; -.
DR UniPathway; UPA00076; UER00147.
DR Proteomes; UP000000606; 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..292
FT /note="6-phospho-5-dehydro-2-deoxy-D-gluconate aldolase"
FT /id="PRO_0000352283"
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 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
