Q4V1F5 (IOLD2_BACCZ) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Gene names

Name:	iolD2
Ordered Locus Names:	pE33L466_0302

Encoded on

Plasmid pE33L466

Organism

Bacillus cereus (strain ZK / E33L) [Complete proteome] [HAMAP]

Taxonomic identifier

288681 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group

Protein attributes

Sequence length	644 AA.
Sequence status	Complete.
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. HAMAP MF_01669
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. HAMAP MF_01669 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 Plasmid
Gene Ontology (GO)
Biological process	inositol catabolic process Inferred from electronic annotation. Source: InterPro
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: InterPro thiamine pyrophosphate binding Inferred from electronic annotation. Source: InterPro 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 – 644	644	3D-(3,5/4)-trihydroxycyclohexane-1,2-dione hydrolase 2 HAMAP MF_01669		PRO_0000352531
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	65	1	Thiamine pyrophosphate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q4V1F5 [UniParc]. Last modified July 5, 2005. Version 1. Checksum: B3A6EF58DF3D2F60	FASTA	644	71,017
	10 20 30 40 50 60 MQTVRMTTAQ ALVKFLNQQY IEFDGEQQKF IKGIFTIFGH GNVVGLGQAL EEDAGELEVY 70 80 90 100 110 120 QGRNEQGMAN AAMAFAKQKH RKQIMACTSS VGPGSANMIT SAATASANNI PVLLLPGDVF 130 140 150 160 170 180 ATRQPDPVLQ QIEQTHDLSI STNDAFRAVS KYWDRINRPE QLMTAMIQAM RVLTNPADTG 190 200 210 220 230 240 AVTICLPQDV QGEAWDFPSY FFQKCVHRIE RRLPTRASLA DAVEMIKRKK KPVMICGGGV 250 260 270 280 290 300 RYAEAAEELK QFAEAFRIPF GETQAGKSAI ESSHPYNLGG IGVTGNLAAN TIAKEADLVI 310 320 330 340 350 360 GIGTRFTDFT TASKQLFQNE EVEFVNINIS EFHANKLDAL KVIADAKEAL LALINELQAI 370 380 390 400 410 420 EYRSSYTVEI AAAKEFWETE LARLHNIRFT GQDFKPEVEG HFDDNLNEYV DALGTQLTQT 430 440 450 460 470 480 AVIGEMNTLL DEDAIIVGAA GSLPGDLQRM WTSRKPNTYH MEYGYSCMGY EVAGALGAKL 490 500 510 520 530 540 AEPSKEVYAM VGDGSYQMLH SELVTSLQEN KKINVLLFDN SGFGCINNLQ MGNGMGSFGT 550 560 570 580 590 600 EFRYRNEETR KLNGAIMKID FAASAAGYGV KTYRVTSVEQ LQEALKDAKK QTVSTLIDIK 610 620 630 640 VLPKTMTNGY ESWWHVGVAE VSNSQSVQAA YESKVSNLQK ARSY

References

[1]

"Pathogenomic sequence analysis of Bacillus cereus and Bacillus thuringiensis isolates closely related to Bacillus anthracis." Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S., Bruce D., Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C., Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A., Hill K.K., Hitchcock P. , Jackson P.J., Keim P., Kewalramani A.R., Longmire J., Lucas S., Malfatti S., McMurry K., Meincke L.J., Misra M., Moseman B.L., Mundt M., Munk A.C., Okinaka R.T., Parson-Quintana B., Reilly L.P., Richardson P., Robinson D.L., Rubin E., Saunders E., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Ticknor L.O., Wills P.L., Brettin T.S., Gilna P. J. Bacteriol. 188:3382-3390(2006) [PubMed: 16621833] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ZK / E33L.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000040 Genomic DNA. Translation: AAY60452.1.
RefSeq	YP_245790.1. NC_007103.1.
3D structure databases
HSSP	HSSP built from PDB template 1JSC based on UniProtKB P07342.
ProteinModelPortal	Q4V1F5.
ModBase	Search...
Protein-protein interaction databases
STRING	Q4V1F5.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBACT00000045478; EBBACP00000044239; EBBACG00000045469.
GeneID	3399736.
GenomeReviews	Gene locus pE33L466_0302 in contig CP000040_GR.
KEGG	bcz:pE33L466_0302.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG3962.
GeneTree	EBGT00070000032034.
HOGENOM	HBG294332.
ProtClustDB	CLSK2304880.
Family and domain databases
HAMAP	MF_01669. IolD. [Tree]
InterPro	IPR023110. PH1570-like_domain. IPR023757. THcHDO_hydrolase. IPR012000. Thiamin_PyroP_enz_cen_dom. IPR012001. Thiamin_PyroP_enz_TPP-bd_dom. IPR000399. TPP-bd_CS. IPR011766. TPP_enzyme-bd_C. [Graphical view]
Gene3D	G3DSA:3.40.1600.10. G3DSA:3.40.1600.10. 1 hit.
KO	K03336.
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

IOLD2_BACCZ

Accession

Primary (citable) accession number: Q4V1F5

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 14, 2008
Last sequence update:	July 5, 2005
Last modified:	November 16, 2011
This is version 38 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program