IOLD_ALKCK
ID IOLD_ALKCK Reviewed; 637 AA.
AC Q5WKY8;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=3D-(3,5/4)-trihydroxycyclohexane-1,2-dione hydrolase {ECO:0000255|HAMAP-Rule:MF_01669};
DE Short=THcHDO hydrolase {ECO:0000255|HAMAP-Rule:MF_01669};
DE EC=3.7.1.22 {ECO:0000255|HAMAP-Rule:MF_01669};
GN Name=iolD {ECO:0000255|HAMAP-Rule:MF_01669}; OrderedLocusNames=ABC0425;
OS Alkalihalobacillus clausii (strain KSM-K16) (Bacillus clausii).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX NCBI_TaxID=66692;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KSM-K16;
RA Takaki Y., Kageyama Y., Shimamura S., Suzuki H., Nishi S., Hatada Y.,
RA Kawai S., Ito S., Horikoshi K.;
RT "The complete genome sequence of the alkaliphilic Bacillus clausii KSM-
RT K16.";
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in the cleavage of the C1-C2 bond of 3D-(3,5/4)-
CC trihydroxycyclohexane-1,2-dione (THcHDO) to yield 5-deoxy-glucuronate
CC (5DG). {ECO:0000255|HAMAP-Rule:MF_01669}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3D-3,5/4-trihydroxycyclohexane-1,2-dione + H2O = 5-deoxy-D-
CC glucuronate + H(+); Xref=Rhea:RHEA:25836, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:28446, ChEBI:CHEBI:58852; EC=3.7.1.22;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01669};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01669};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01669};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01669};
CC Note=Binds 1 thiamine pyrophosphate per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_01669};
CC -!- PATHWAY: Polyol metabolism; myo-inositol degradation into acetyl-CoA;
CC acetyl-CoA from myo-inositol: step 3/7. {ECO:0000255|HAMAP-
CC Rule:MF_01669}.
CC -!- SIMILARITY: Belongs to the TPP enzyme family. {ECO:0000255|HAMAP-
CC Rule:MF_01669}.
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DR EMBL; AP006627; BAD62967.1; -; Genomic_DNA.
DR RefSeq; WP_011245286.1; NC_006582.1.
DR AlphaFoldDB; Q5WKY8; -.
DR SMR; Q5WKY8; -.
DR STRING; 66692.ABC0425; -.
DR EnsemblBacteria; BAD62967; BAD62967; ABC0425.
DR KEGG; bcl:ABC0425; -.
DR eggNOG; COG3962; Bacteria.
DR HOGENOM; CLU_013748_6_0_9; -.
DR OMA; PNTYHLE; -.
DR OrthoDB; 391134at2; -.
DR UniPathway; UPA00076; UER00145.
DR Proteomes; UP000001168; Chromosome.
DR GO; GO:0102481; F:3D-(3,5/4)-trihydroxycyclohexane-1,2-dione hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:UniProtKB-UniRule.
DR GO; GO:0019310; P:inositol catabolic process; IEA:UniProtKB-UniRule.
DR HAMAP; MF_01669; IolD; 1.
DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR InterPro; IPR030817; Myo_inos_IolD.
DR InterPro; IPR023757; THcHDO_hydrolase_firmi.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR InterPro; IPR000399; TPP-bd_CS.
DR InterPro; IPR045229; TPP_enz.
DR InterPro; IPR011766; TPP_enzyme-bd_C.
DR PANTHER; PTHR18968; PTHR18968; 1.
DR PANTHER; PTHR18968:SF9; PTHR18968:SF9; 1.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR Pfam; PF00205; TPP_enzyme_M; 1.
DR Pfam; PF02776; TPP_enzyme_N; 1.
DR SUPFAM; SSF52467; SSF52467; 1.
DR SUPFAM; SSF52518; SSF52518; 2.
DR TIGRFAMs; TIGR04377; myo_inos_iolD; 1.
DR PROSITE; PS00187; TPP_ENZYMES; 1.
PE 3: Inferred from homology;
KW Hydrolase; Magnesium; Metal-binding; NAD; Reference proteome;
KW Thiamine pyrophosphate.
FT CHAIN 1..637
FT /note="3D-(3,5/4)-trihydroxycyclohexane-1,2-dione
FT hydrolase"
FT /id="PRO_0000352532"
FT REGION 442..522
FT /note="Thiamine pyrophosphate binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01669"
FT BINDING 66
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01669"
FT BINDING 493
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01669"
FT BINDING 520
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01669"
SQ SEQUENCE 637 AA; 70485 MW; 09450A760DB392A6 CRC64;
MAKTIRLTTA QALVKFLNAQ YLHADGKEEP FVEGIFTIFG HGNVLGIGQA LEQDAGRLNV
WQGKNEQGMA HAAMAFSKQM LRKKIYAVTT SVGPGAANLV AAAGTALANN IPVLLLPADT
FATRQPDPVL QQFEQEYSQA VTTNDALKPV SRYWDRITRP EQLMSSLIRA FEVMTDPGKA
GPATICIAQD VEGEAYEYPE EFFRKRIHYL ERRKPTEREI EEALERIRRS KRPLLVVGGG
AKYSEAKEEL VALSEQCGIP LVETQAGKAT VAADFANNLG GLGVTGTLAA NKAAREADLV
IGVGTRYTDF ATSSKTAFDF EHTTFLNINV SRMQTYKLDA YQVVADAKET LSLLISRLKT
YRSAFGDRIA ALKEEWLAER NRLKSVVFNR KTFVPEVKEH FSQEKLNEYA DALGTELPQT
TALLAINETI DEDSTIICSS GSLPGDLQRL WHANEPNTYH LEYGYSCMGY EISGALGIKL
AEPEREVYSI VGDGSFLMLH SELITAIQYN KKINILLFDN AGFGCISNLQ MDHGGGSYYC
EFLTADNQVM NIDYAKVAEG YGAKTYRANT VEQLKAALKD AKKQETSTLI EMKVLPKTMT
DGYESWWNVG VAEVAASQSI QDAYQARQAK LKEAKHY
