Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

3D-(3,5/4)-trihydroxycyclohexane-1,2-dione hydrolase

Gene

iolD

Organism
Bacillus clausii (strain KSM-K16)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

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).UniRule annotation

Catalytic activityi

3D-3,5/4-trihydroxycyclohexa-1,2-dione + H2O = 5-deoxy-D-glucuronate.UniRule annotation

Cofactori

Protein has several cofactor binding sites:
  • Mg2+UniRule annotationNote: Binds 1 Mg2+ ion per subunit.UniRule annotation
  • thiamine diphosphateUniRule annotationNote: Binds 1 thiamine pyrophosphate per subunit.UniRule annotation

Pathwayi: myo-inositol degradation into acetyl-CoA

This protein is involved in step 3 of the subpathway that synthesizes acetyl-CoA from myo-inositol.UniRule annotation
Proteins known to be involved in the 7 steps of the subpathway in this organism are:
  1. Inositol 2-dehydrogenase/D-chiro-inositol 3-dehydrogenase (iolG)
  2. Inosose dehydratase (iolE)
  3. 3D-(3,5/4)-trihydroxycyclohexane-1,2-dione hydrolase (iolD)
  4. 5-deoxy-glucuronate isomerase (iolB)
  5. 5-dehydro-2-deoxygluconokinase (iolC)
  6. 6-phospho-5-dehydro-2-deoxy-D-gluconate aldolase (iolJ)
  7. Methylmalonate semialdehyde dehydrogenase [acylating] 1 (iolA1), Methylmalonate semialdehyde dehydrogenase [acylating] 2 (iolA2)
This subpathway is part of the pathway myo-inositol degradation into acetyl-CoA, which is itself part of Polyol metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes acetyl-CoA from myo-inositol, the pathway myo-inositol degradation into acetyl-CoA and in Polyol metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei66 – 661Thiamine pyrophosphateUniRule annotation
Metal bindingi493 – 4931MagnesiumUniRule annotation
Metal bindingi520 – 5201MagnesiumUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Magnesium, Metal-binding, NAD, Thiamine pyrophosphate

Enzyme and pathway databases

BioCyciBCLA66692:GHMP-458-MONOMER.
UniPathwayiUPA00076; UER00145.

Names & Taxonomyi

Protein namesi
Recommended name:
3D-(3,5/4)-trihydroxycyclohexane-1,2-dione hydrolaseUniRule annotation (EC:3.7.1.22UniRule annotation)
Short name:
THcHDO hydrolaseUniRule annotation
Gene namesi
Name:iolDUniRule annotation
Ordered Locus Names:ABC0425
OrganismiBacillus clausii (strain KSM-K16)
Taxonomic identifieri66692 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001168 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 6376373D-(3,5/4)-trihydroxycyclohexane-1,2-dione hydrolasePRO_0000352532Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi66692.ABC0425.

Structurei

3D structure databases

ProteinModelPortaliQ5WKY8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni442 – 52281Thiamine pyrophosphate bindingUniRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the TPP enzyme family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4107QK6. Bacteria.
COG3962. LUCA.
HOGENOMiHOG000239708.
KOiK03336.
OMAiPNTYHLE.
OrthoDBiPOG091H02KO.

Family and domain databases

Gene3Di3.40.50.1220. 1 hit.
3.40.50.970. 2 hits.
HAMAPiMF_01669. IolD. 1 hit.
InterProiIPR029035. DHS-like_NAD/FAD-binding_dom.
IPR030817. Myo_inos_iolD.
IPR023757. THcHDO_hydrolase_firmi.
IPR029061. THDP-binding.
IPR012000. Thiamin_PyroP_enz_cen_dom.
IPR012001. Thiamin_PyroP_enz_TPP-bd_dom.
IPR000399. TPP-bd_CS.
IPR011766. TPP_enzyme-bd_C.
[Graphical view]
PANTHERiPTHR18968:SF9. PTHR18968:SF9. 1 hit.
PfamiPF02775. TPP_enzyme_C. 1 hit.
PF00205. TPP_enzyme_M. 1 hit.
PF02776. TPP_enzyme_N. 1 hit.
[Graphical view]
SUPFAMiSSF52467. SSF52467. 1 hit.
SSF52518. SSF52518. 2 hits.
TIGRFAMsiTIGR04377. myo_inos_iolD. 1 hit.
PROSITEiPS00187. TPP_ENZYMES. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q5WKY8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKTIRLTTA QALVKFLNAQ YLHADGKEEP FVEGIFTIFG HGNVLGIGQA
60 70 80 90 100
LEQDAGRLNV WQGKNEQGMA HAAMAFSKQM LRKKIYAVTT SVGPGAANLV
110 120 130 140 150
AAAGTALANN IPVLLLPADT FATRQPDPVL QQFEQEYSQA VTTNDALKPV
160 170 180 190 200
SRYWDRITRP EQLMSSLIRA FEVMTDPGKA GPATICIAQD VEGEAYEYPE
210 220 230 240 250
EFFRKRIHYL ERRKPTEREI EEALERIRRS KRPLLVVGGG AKYSEAKEEL
260 270 280 290 300
VALSEQCGIP LVETQAGKAT VAADFANNLG GLGVTGTLAA NKAAREADLV
310 320 330 340 350
IGVGTRYTDF ATSSKTAFDF EHTTFLNINV SRMQTYKLDA YQVVADAKET
360 370 380 390 400
LSLLISRLKT YRSAFGDRIA ALKEEWLAER NRLKSVVFNR KTFVPEVKEH
410 420 430 440 450
FSQEKLNEYA DALGTELPQT TALLAINETI DEDSTIICSS GSLPGDLQRL
460 470 480 490 500
WHANEPNTYH LEYGYSCMGY EISGALGIKL AEPEREVYSI VGDGSFLMLH
510 520 530 540 550
SELITAIQYN KKINILLFDN AGFGCISNLQ MDHGGGSYYC EFLTADNQVM
560 570 580 590 600
NIDYAKVAEG YGAKTYRANT VEQLKAALKD AKKQETSTLI EMKVLPKTMT
610 620 630
DGYESWWNVG VAEVAASQSI QDAYQARQAK LKEAKHY
Length:637
Mass (Da):70,485
Last modified:November 23, 2004 - v1
Checksum:i09450A760DB392A6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP006627 Genomic DNA. Translation: BAD62967.1.
RefSeqiWP_011245286.1. NC_006582.1.

Genome annotation databases

EnsemblBacteriaiBAD62967; BAD62967; ABC0425.
KEGGibcl:ABC0425.
PATRICi18920078. VBIBacCla58185_0444.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP006627 Genomic DNA. Translation: BAD62967.1.
RefSeqiWP_011245286.1. NC_006582.1.

3D structure databases

ProteinModelPortaliQ5WKY8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi66692.ABC0425.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAD62967; BAD62967; ABC0425.
KEGGibcl:ABC0425.
PATRICi18920078. VBIBacCla58185_0444.

Phylogenomic databases

eggNOGiENOG4107QK6. Bacteria.
COG3962. LUCA.
HOGENOMiHOG000239708.
KOiK03336.
OMAiPNTYHLE.
OrthoDBiPOG091H02KO.

Enzyme and pathway databases

UniPathwayiUPA00076; UER00145.
BioCyciBCLA66692:GHMP-458-MONOMER.

Family and domain databases

Gene3Di3.40.50.1220. 1 hit.
3.40.50.970. 2 hits.
HAMAPiMF_01669. IolD. 1 hit.
InterProiIPR029035. DHS-like_NAD/FAD-binding_dom.
IPR030817. Myo_inos_iolD.
IPR023757. THcHDO_hydrolase_firmi.
IPR029061. THDP-binding.
IPR012000. Thiamin_PyroP_enz_cen_dom.
IPR012001. Thiamin_PyroP_enz_TPP-bd_dom.
IPR000399. TPP-bd_CS.
IPR011766. TPP_enzyme-bd_C.
[Graphical view]
PANTHERiPTHR18968:SF9. PTHR18968:SF9. 1 hit.
PfamiPF02775. TPP_enzyme_C. 1 hit.
PF00205. TPP_enzyme_M. 1 hit.
PF02776. TPP_enzyme_N. 1 hit.
[Graphical view]
SUPFAMiSSF52467. SSF52467. 1 hit.
SSF52518. SSF52518. 2 hits.
TIGRFAMsiTIGR04377. myo_inos_iolD. 1 hit.
PROSITEiPS00187. TPP_ENZYMES. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiIOLD_BACSK
AccessioniPrimary (citable) accession number: Q5WKY8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 14, 2008
Last sequence update: November 23, 2004
Last modified: September 7, 2016
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.