Q65D09 (IOLJ_BACLD) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
6-phospho-5-dehydro-2-deoxy-D-gluconate aldolase
Short name=DKGP aldolase
EC=4.1.2.29

Gene names

Name:	iolJ
Ordered Locus Names:	BLi04242, BL00237

Organism

Bacillus licheniformis (strain DSM 13 / ATCC 14580) [Complete proteome] [HAMAP]

Taxonomic identifier

279010 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	292 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Produces dihydroxyacetone phosphate (DHAP or glycerone phosphate) and malonic semialdehyde (MSA or 3-oxopropanoate) from 6-phospho-5-dehydro-2-deoxy-D-gluconate (DKGP) By similarity.
Catalytic activity	5-dehydro-2-deoxy-D-gluconate 6-phosphate = glycerone phosphate + malonate semialdehyde.
Cofactor	Zinc By similarity.
Pathway	Polyol metabolism; myo-inositol degradation into acetyl-CoA; acetyl-CoA from myo-inositol: step 6/7.
Sequence similarities	Belongs to the class II fructose-bisphosphate aldolase family. IolJ subfamily.

Ontologies

Keywords
Ligand	Metal-binding Zinc
Molecular function	Lyase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	fructose 1,6-bisphosphate metabolic process Inferred from electronic annotation. Source: InterPro glycolysis Inferred from electronic annotation. Source: InterPro
Molecular function	5-dehydro-2-deoxyphosphogluconate aldolase activity Inferred from electronic annotation. Source: EC fructose-bisphosphate aldolase activity Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 292	292	6-phospho-5-dehydro-2-deoxy-D-gluconate aldolase		PRO_0000352283
Regions
	Region	209 – 211	3	Dihydroxyacetone phosphate binding By similarity
	Region	230 – 233	4	Dihydroxyacetone phosphate binding By similarity
Sites
	Active site	85	1	Proton donor By similarity
	Metal binding	86	1	Zinc; catalytic By similarity
	Metal binding	180	1	Zinc; catalytic By similarity
	Metal binding	208	1	Zinc; catalytic By similarity
	Binding site	181	1	Dihydroxyacetone phosphate; via amide nitrogen By similarity
Amino acid modifications
	Modified residue	233	1	Phosphothreonine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q65D09 [UniParc]. Last modified October 25, 2004. Version 1. Checksum: 38BD8CF7A956FFCA	FASTA	292	31,615
	10 20 30 40 50 60 MAFVSMKELL QEAKEHHYAI GQFNINGLQW TKAILEAAEE ERSPVIAAAS DRLIDYLGGF 70 80 90 100 110 120 KTVSAMVAAL IEEMSISVPV VLHLDHGKSP ERCKQAIDAG FSSVMIDGSH SPIDENIAMT 130 140 150 160 170 180 KEVVSYAGVR NVSVEAEVGT VGGMEDGLIG GVQYADIGEC ERIVKETGID ALAAALGSVH 190 200 210 220 230 240 GKYQGEPNLG FKEMEEISRV TDIPLVLHGA SGIPADQIAR TIRLGHAKIN INTECMVAWT 250 260 270 280 290 EKTRSIFKDN PDLYEPRAYM TPGISAVKET VKHKMREFGS SGKAVCTQKI EI

References

[1]

"The complete genome sequence of Bacillus licheniformis DSM13, an organism with great industrial potential." Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P., Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G. J. Mol. Microbiol. Biotechnol. 7:204-211(2004) [PubMed: 15383718] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DSM 13 / ATCC 14580.

[2]

"Complete genome sequence of the industrial bacterium Bacillus licheniformis and comparisons with closely related Bacillus species." Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J., Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B., Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A., Bolotin A., Lapidus A. , Galleron N., Ehrlich S.D., Berka R.M. Genome Biol. 5:R77.1-R77.12(2004) [PubMed: 15461803] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DSM 13 / ATCC 14580.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000002 Genomic DNA. Translation: AAU25676.1. AE017333 Genomic DNA. Translation: AAU43055.1.
RefSeq	YP_081314.1. NC_006270.3. YP_093748.1. NC_006322.1.
3D structure databases
ProteinModelPortal	Q65D09.
ModBase	Search...
Protein-protein interaction databases
STRING	Q65D09.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBACT00000054288; EBBACP00000052819; EBBACG00000054279. EBBACT00000061434; EBBACP00000059867; EBBACG00000061425.
GeneID	3030964. 3100047.
GenomeReviews	Gene locus BLi04242 in contig AE017333_GR. Gene locus BL00237 in contig CP000002_GR.
KEGG	bld:BLi04242. bli:BL00237.
NMPDR	fig|279010.5.peg.3950.
PATRIC	18954310. VBIBacLic203714_4330.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0191.
GeneTree	EBGT00050000002241.
HOGENOM	HBG327581.
OMA	IAMTKEV.
ProtClustDB	CLSK888173.
Enzyme and pathway databases
BioCyc	BLIC279010-1:BLI04242-MONOMER. BLIC279010:BL00237-MONOMER.
Family and domain databases
InterPro	IPR013785. Aldolase_TIM. IPR011289. Fruc_bis_ald_class-2. IPR000771. Ketose_bisP_aldolase_II. [Graphical view]
Gene3D	G3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
KO	K03339.
Pfam	PF01116. F_bP_aldolase. 1 hit. [Graphical view]
PIRSF	PIRSF001359. F_bP_aldolase_II. 1 hit.
TIGRFAMs	TIGR00167. CbbA. 1 hit. TIGR01859. Fruc_bis_ald_. 1 hit.
PROSITE	PS00602. ALDOLASE_CLASS_II_1. 1 hit. PS00806. ALDOLASE_CLASS_II_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

IOLJ_BACLD

Accession

Primary (citable) accession number: Q65D09
Secondary accession number(s): Q62NI5

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 14, 2008
Last sequence update:	October 25, 2004
Last modified:	January 25, 2012
This is version 57 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program