Reviewed, UniProtKB/Swiss-Prot A5YBJ6 (IOLD_LACCA)

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

Organism

Lactobacillus casei

Taxonomic identifier

1582 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Lactobacillales › Lactobacillaceae › Lactobacillus

Protein attributes

Sequence length	642 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
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 – 642	642	3D-(3,5/4)-trihydroxycyclohexane-1,2-dione hydrolase HAMAP MF_01669		PRO_0000352544
Regions
	Region	446 – 526	81	Thiamine pyrophosphate binding By similarity
Sites
	Metal binding	497	1	Magnesium By similarity
	Metal binding	524	1	Magnesium By similarity
	Binding site	71	1	Thiamine pyrophosphate By similarity

Sequences

	Sequence		Length	Mass (Da)
	A5YBJ6-1 [UniParc]. Last modified October 14, 2008. Version 2. Checksum: 520559671F0022C5	FASTA	642	70,086
	10 20 30 40 50 60 MAADAKKETI RLTTAQALVR FLNQQYIDVD GQVTSFVEGL FAIFGHGNVL GLGEALQEDP 70 80 90 100 110 120 GHLKVYQGHN EQGMASTAIA YSRQLYRHKI FAVTASAGPG SANFVTAAGN AYVNSIPILF 130 140 150 160 170 180 LPADTFATRQ PDPVLQQIEV DYSADTTTND VLKPVSKYWD RIERPEQLMS ALLKAFEVLT 190 200 210 220 230 240 NPATAGPVTI ALPQDVEGQA YDYPLSFFKK RVHVVKRVQP SSAELAGAVE LIQASQTPVL 250 260 270 280 290 300 IVGGGAKFSD AGAAIETFSE RFNIPIVETP TGKSAISSDF PNNMGGTGIL GTAAANAVIT 310 320 330 340 350 360 KADLIIGAGT RYTDFTTASK TAIHPGKTQL ININLNRMQS YKFDAFPIVA DVRDTLSQLT 370 380 390 400 410 420 ESLSDYRSQF TDLATIKEAW QKERQRLAHT NYDAPAYVPE VKNQFDAKTM AAYAEKLQTH 430 440 450 460 470 480 LTQTEAVIAV NNTIDPTSII VAAAGSLPGD VQRIWDPVVP NTYHMEYGYS MMGYEVPAAL 490 500 510 520 530 540 GIKLAQPDQE SYALVGDGSF MMLHSELVTA LQYHKKINIL VFDNSGFASI NNLQMAQGSN 550 560 570 580 590 600 SYLTEFRTSD NDIMKTDFAK IAEGYGAKAY RANDRKSLIA AIEDAKKQTV STLIDIKVLP 610 620 630 640 KTMTQGYGQS WWRVGVSEIS NNPKVQKAYQ DIQTGIDKAF KY

References

[1]

"Identification of a gene cluster allowing Lactobacillus casei BL23 the utilization of myo-inositol." Yebra M.J., Zuniga M., Beaufils S., Perez-Martinez G., Deutscher J., Monedero V. Appl. Environ. Microbiol. 73:3850-3858(2007) [PubMed: 17449687] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: BL23.

Cross-references

Sequence databases
EMBLGenBankDDBJ	EF382358 Genomic DNA. Translation: ABP57765.1. Different initiation.
3D structure databases
ModBase	Search...
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_LACCA

Accession

Primary (citable) accession number: A5YBJ6

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 14, 2008
Last sequence update:	October 14, 2008
Last modified:	December 16, 2008
This is version 14 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)