Reviewed, UniProtKB/Swiss-Prot Q65D03 (IOLD_BACLD)

Names and origin

Protein names

Recommended name:
    3D-(3,5/4)-trihydroxycyclohexane-1,2-dione hydrolase
      Short name=THcHDO hydrolase
    EC=3.7.1.n2

Gene names

Name:	iolD
Ordered Locus Names:	BLi04248, BL00243

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	637 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Involved in the cleavage of the C1-C2 bond of 3D-(3,5/4)-trihydroxycyclohexane-1,2-dione (THcHDO) to yield 5-deoxy-glucuronate (5DG) By similarity.
Catalytic activity	3,5/4-trihydroxycyclohexa-1,2-dione + H2O = 5-deoxy-glucuronic acid. HAMAP MF_01669
Cofactor	Binds 1 magnesium ion per subunit By similarity. Binds 1 thiamine pyrophosphate per subunit By similarity.
Pathway	Polyol metabolism; myo-inositol degradation into acetyl-CoA; acetyl-CoA from myo-inositol: step 3/7. HAMAP MF_01669
Sequence similarities	Belongs to the TPP enzyme family.

Ontologies

Keywords
Ligand	Magnesium Metal-binding NAD Thiamine pyrophosphate
Molecular function	Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	inositol catabolic process Inferred from electronic annotation. Source: HAMAP
Molecular function	hydrolase activity, acting on acid carbon-carbon bonds, in ketonic substances Inferred from electronic annotation. Source: EC magnesium ion binding Inferred from electronic annotation. Source: HAMAP thiamin pyrophosphate binding Inferred from electronic annotation. Source: HAMAP transferase activity 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 – 637	637	3D-(3,5/4)-trihydroxycyclohexane-1,2-dione hydrolase HAMAP MF_01669		PRO_0000352534
Regions
	Region	442 – 522	81	Thiamine pyrophosphate binding By similarity
Sites
	Metal binding	493	1	Magnesium By similarity
	Metal binding	520	1	Magnesium By similarity
	Binding site	66	1	Thiamine pyrophosphate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q65D03-1 [UniParc]. Last modified October 25, 2004. Version 1. Checksum: BE3E35148FC49F10	FASTA	637	70,180
	10 20 30 40 50 60 MGKKIRLTTA QALIKFLNQQ YIHVDGEETP FVEGIFTIFG HGNVVGIGQA LEQDAGHLKV 70 80 90 100 110 120 FQGKNEQGMA HAAMAYSKQM LRRKIYAVST SVGPGAANLV AAAGTALANN IPVLLIPADT 130 140 150 160 170 180 FATRQPDPVL QQVEQEYSAA ITTNDALKPV SRYWDRITRP EQLMSSLIRA FEVMTDPAKA 190 200 210 220 230 240 GPATICISQD VEGEAYDFDE SFFEKRVHYV DRKEPSEREL KGAAELIKSS KKPLILVGGG 250 260 270 280 290 300 AKYSGARDEL IAMSEAYNIP LVETQAGKST VEADFANNLG GMGITGTLAA NKAARGADLI 310 320 330 340 350 360 IGIGTRYTDF ATSSKTAFDF DNAKFLNINV SRMQAYKLDA FQVVADAKVT LGKLHGLLEG 370 380 390 400 410 420 YKSEFGSTIK ELKDEWLAER DRLSKVTFKR ENFTPEIKDH FSQDILNEYA DVLQTELPQT 430 440 450 460 470 480 TALLAINETV DPDSVVICSA GSLPGDLQRL WHSNVPNTYH LEYGYSCMGY EVSGTLGLKL 490 500 510 520 530 540 AHPDREVYSL VGDGSFLMLH SELITAIQYN KKINVLLFDN SGFGCINNLQ MDHGNGSYYC 550 560 570 580 590 600 EFRTADNQIL NVDYAKVAEG YGAKTYKANT IEELKAALED AKKQDVSTLI EMKVLPKTMT 610 620 630 DGYDSWWHVG VAEVSEQESV QKAYKAKEKM LESAKQY

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].

[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:RESEARCH077.1-RESEARCH077.12(2004) [PubMed: 15461803] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000002 Genomic DNA. Translation: AAU25682.1. AE017333 Genomic DNA. Translation: AAU43061.1.
RefSeq	YP_081320.1. YP_093754.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	3030847. 3098106.
GenomeReviews	Gene locus BLi04248 in contig AE017333_GR. Gene locus BL00243 in contig CP000002_GR.
KEGG	bld:BLi04248. bli:BL00243.
NMPDR	fig|279010.5.peg.4027.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q65D03.
OMA	Q65D03. WRIERER.
Family and domain databases
HAMAP	MF_01669. [Tree]
InterPro	IPR000399. TPP_bd_CS. IPR012001. TPP_bd_enzyme_N. IPR011766. TPP_enzyme_bd_C. IPR012000. TPP_enzyme_M. [Graphical view]
Pfam	PF02775. TPP_enzyme_C. 1 hit. PF00205. TPP_enzyme_M. 1 hit. PF02776. TPP_enzyme_N. 1 hit. [Graphical view]
PROSITE	PS00187. TPP_ENZYMES. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

IOLD_BACLD

Accession

Primary (citable) accession number: Q65D03
Secondary accession number(s): Q62NH9

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 14, 2008
Last sequence update:	October 25, 2004
Last modified:	June 16, 2009
This is version 36 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)