Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot B2V4K0 (IOLD_CLOBA)

Last modified June 16, 2009. Version 10. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended 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: CLH_1255
OrganismClostridium botulinum (strain Alaska E43 / Type E3) [Complete proteome] [HAMAP]
Taxonomic identifier508767 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length643 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 6436433D-(3,5/4)-trihydroxycyclohexane-1,2-dione hydrolase HAMAP MF_01669
PRO_0000352537

Regions

Region441 – 52181Thiamine pyrophosphate binding By similarity

Sites

Metal binding4921Magnesium By similarity
Metal binding5191Magnesium By similarity
Binding site651Thiamine pyrophosphate By similarity

Sequences

Sequence LengthMass (Da)Tools
B2V4K0-1 [UniParc].

Last modified July 1, 2008. Version 1.
Checksum: 9FBA9241B930D859

FASTA64371,489
        10         20         30         40         50         60 
MKSTKMTTAQ ALVRFLDNQY VSFDGKEEKF VHGIFTIFGH GIVVGLGQAL DENTRDLKVY 

        70         80         90        100        110        120 
QGRNEQGMAH AATAFAKQNN RRKIIACSSS IGPGAANMVT AAATATVNNI PLLLLPGDSF 

       130        140        150        160        170        180 
ATRQPDPVLQ QIEQSYNLGI TTNDVFKPVC KYWDRVNRPE QLMSAMINAM RVLTDPAETG 

       190        200        210        220        230        240 
AVCISLPQDV QGESFEFPEY FFKKRVHKIT RPLAVEEEFY ECLNIIKNKK KPIIICGGGV 

       250        260        270        280        290        300 
RYSEAGDALS KFANKFNIPI GETQAGKSSI KSSDPMNLGG IGVTGNLASN IIAKDADLVI 

       310        320        330        340        350        360 
GVGTRFSDFT TASKSLFKNP DVEFVTINLS KFHASKLDSC KMVGDAKECL EYLHKLLEKE 

       370        380        390        400        410        420 
NYISSYKDEI KDAKIAWKEE MKRLTNIKYE ENFEPIIKFR NKESLEEFKK LTDTTITQTS 

       430        440        450        460        470        480 
ALGLIRECID DDSIIVGASG SLPGDLQRMW ETESLNSYHM EYGYSCMGYE IAAGFGAKLA 

       490        500        510        520        530        540 
DPEKEVYSIL GDGSYLMLHS ELITSIQENK KVNVLLFDNC GFGCINNLQM SNGIGNLATE 

       550        560        570        580        590        600 
FRYRNSETNK LNGKLIPIDF AKAAEGYGLK TYTAKNLEEL KNALIDAKKQ KVSTLIDIKV 

       610        620        630        640 
LPKTMTDGYE SWWHVGLAEV SEKESVNEAF KNSKKILKGA RKY 

« Hide

References

[1]"Complete genome sequence of Clostridium botulinum E3 str. Alaska E43."
Brinkac L.M., Brown J.L., Bruce D., Detter C., Munk C., Smith L.A., Smith T.J., Sutton G., Brettin T.S.
Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP001078 Genomic DNA. Translation: ACD52572.1.
RefSeqYP_001920649.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID6320314.
GenomeReviewsGene locus CLH_1255 in contig CP001078_GR.
KEGGcbt:CLH_1255.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAB2V4K0. KYLSWWR.

Family and domain databases

HAMAPMF_01669.
[Tree]
InterProIPR000399. TPP_bd_CS.
IPR012001. TPP_bd_enzyme_N.
IPR011766. TPP_enzyme_bd_C.
IPR012000. TPP_enzyme_M.
[Graphical view]
PfamPF02775. TPP_enzyme_C. 1 hit.
PF00205. TPP_enzyme_M. 1 hit.
PF02776. TPP_enzyme_N. 1 hit.
[Graphical view]
PROSITEPS00187. TPP_ENZYMES. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameIOLD_CLOBA
AccessionPrimary (citable) accession number: B2V4K0
Entry history
Integrated into UniProtKB/Swiss-Prot: October 14, 2008
Last sequence update: July 1, 2008
Last modified: June 16, 2009
This is version 10 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents