Reviewed, UniProtKB/Swiss-Prot P42415 (IOLD_BACSU)

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
Synonyms:	yxdD
Ordered Locus Names:	BSU39730
ORF Names:	E83D

Organism

Bacillus subtilis [Complete proteome] [HAMAP]

Taxonomic identifier

1423 [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	Evidence at protein level.

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). Ref.3
Catalytic activity	3,5/4-trihydroxycyclohexa-1,2-dione + H2O = 5-deoxy-glucuronic acid. Ref.3
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_0000090815
Regions
	Region	442 – 522	81	Thiamine pyrophosphate binding HAMAP MF_01669
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)
	P42415-1 [UniParc]. Last modified October 14, 2008. Version 2. Checksum: BB8633F2B9358971	FASTA	637	70,380
	10 20 30 40 50 60 MGKKIRLTTA QALIKFLNQQ YIHVDGKEEP FVEGIFTIFG HGNVLGIGQA LEQDAGHLKV 70 80 90 100 110 120 YQGKNEQGMA HAAMAYSKQM LRRKIYAVST SVGPGAANLV AAAGTALANN IPVLLIPADT 130 140 150 160 170 180 FATRQPDPVL QQMEQEYSAA ITTNDALKPV SRYWDRITRP EQLMSSLLRA FEVMTDPAKA 190 200 210 220 230 240 GPATICISQD VEGEAYDFDE SFFVKRVHYI DRMQPSEREL QGAAELIKSS KKPVILVGGG 250 260 270 280 290 300 AKYSGARDEL VAISEAYNIP LVETQAGKST VEADFANNLG GMGITGTLAA NKAARQADLI 310 320 330 340 350 360 IGIGTRYTDF ATSSKTAFDF DKAKFLNINV SRMQAYKLDA FQVVADAKVT LGKLHGLLEG 370 380 390 400 410 420 YESEFGTTIR ELKDEWLAER ERLSKVTFKR EAFDPEIKNH FSQEVLNEYA DALNTELPQT 430 440 450 460 470 480 TALLTINETI PEDSVIICSA GSLPGDLQRL WHSNVPNTYH LEYGYSCMGY EVSGTLGLKL 490 500 510 520 530 540 AHPDREVYSI VGDGSFLMLH SELITAIQYN KKINVLLFDN SGFGCINNLQ MDHGSGSYYC 550 560 570 580 590 600 EFRTDDNQIL NVDYAKVAEG YGAKTYRANT VEELKAALED AKKQDVSTLI EMKVLPKTMT 610 620 630 DGYDSWWHVG VAEVSEQESV QKAYEAKEKK LESAKQY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and nucleotide sequencing of a 15 kb region of the Bacillus subtilis genome containing the iol operon." Yoshida K., Sano H., Miwa Y., Ogasawara N., Fujita Y. Microbiology 140:2289-2298(1994) [PubMed: 7952181] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168 / BGSC1A1.
[2]	"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A. Nature 390:249-256(1997) [PubMed: 9384377] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168.
[3]	"Myo-inositol catabolism in Bacillus subtilis." Yoshida K., Yamaguchi M., Morinaga T., Kinehara M., Ikeuchi M., Ashida H., Fujita Y. J. Biol. Chem. 283:10415-10424(2008) [PubMed: 18310071] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY. Strain: 168 / 60015.

Cross-references

Sequence databases
EMBLGenBankDDBJ	D14399 Genomic DNA. Translation: BAA03293.1. Different initiation. Z99124 Genomic DNA. Translation: CAB16009.1. Different initiation.
PIR	D69645.
RefSeq	NP_391852.1.
3D structure databases
HSSP	HSSP built from PDB template 1JSC based on UniProtKB P07342.
ModBase	Search...
Genome annotation databases
GeneID	937590.
GenomeReviews	Gene locus BSU39730 in contig AL009126_GR.
KEGG	bsu:BSU39730.
NMPDR	fig|224308.1.peg.3978.
Organism-specific databases
SubtiList	BG11120. iolD. [Micado]
CMR	Search...
Phylogenomic databases
HOGENOM	P42415.
Enzyme and pathway databases
BioCyc	BSUB224308:BSU3969-MON.
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_BACSU

Accession

Primary (citable) accession number: P42415

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	October 14, 2008
Last modified:	June 16, 2009
This is version 69 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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