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Protein

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

Gene

iolD

Organism
Bacillus clausii (strain KSM-K16)
Status
Reviewed-Annotation score: -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. Malonate-semialdehyde dehydrogenase 1 (iolA1), Malonate-semialdehyde dehydrogenase 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)DescriptionActionsGraphical viewLength
Binding sitei66Thiamine pyrophosphateUniRule annotation1
Metal bindingi493MagnesiumUniRule annotation1
Metal bindingi520MagnesiumUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHydrolase
LigandMagnesium, Metal-binding, NAD, Thiamine pyrophosphate

Enzyme and pathway databases

BioCyciBCLA66692:G1G25-467-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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003525321 – 6373D-(3,5/4)-trihydroxycyclohexane-1,2-dione hydrolaseAdd BLAST637

Proteomic databases

PRIDEiQ5WKY8

Interactioni

Protein-protein interaction databases

STRINGi66692.ABC0425

Structurei

3D structure databases

ProteinModelPortaliQ5WKY8
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni442 – 522Thiamine pyrophosphate bindingUniRule annotationAdd BLAST81

Sequence similaritiesi

Belongs to the TPP enzyme family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4107QK6 Bacteria
COG3962 LUCA
HOGENOMiHOG000239708
KOiK03336
OMAiLPKTMTH
OrthoDBiPOG091H02KO

Family and domain databases

HAMAPiMF_01669 IolD, 1 hit
InterProiView protein in InterPro
IPR029035 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
PANTHERiPTHR18968:SF9 PTHR18968:SF9, 1 hit
PfamiView protein in Pfam
PF02775 TPP_enzyme_C, 1 hit
PF00205 TPP_enzyme_M, 1 hit
PF02776 TPP_enzyme_N, 1 hit
SUPFAMiSSF52467 SSF52467, 1 hit
SSF52518 SSF52518, 2 hits
TIGRFAMsiTIGR04377 myo_inos_iolD, 1 hit
PROSITEiView protein in PROSITE
PS00187 TPP_ENZYMES, 1 hit

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
GeneIDi34046468
KEGGibcl:ABC0425

Similar proteinsi

Entry informationi

Entry nameiIOLD_BACSK
AccessioniPrimary (citable) accession number: Q5WKY8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 14, 2008
Last sequence update: November 23, 2004
Last modified: May 23, 2018
This is version 86 of the entry and version 1 of the sequence. See 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

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