IOLD_CLOTE
ID IOLD_CLOTE Reviewed; 644 AA.
AC Q898E8;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 2.
DT 03-AUG-2022, entry version 103.
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=CTC_00510;
OS Clostridium tetani (strain Massachusetts / E88).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=212717;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Massachusetts / E88;
RX PubMed=12552129; DOI=10.1073/pnas.0335853100;
RA Brueggemann H., Baeumer S., Fricke W.F., Wiezer A., Liesegang H.,
RA Decker I., Herzberg C., Martinez-Arias R., Merkl R., Henne A.,
RA Gottschalk G.;
RT "The genome sequence of Clostridium tetani, the causative agent of tetanus
RT disease.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:1316-1321(2003).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAO35133.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE015927; AAO35133.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_035124721.1; NC_004557.1.
DR AlphaFoldDB; Q898E8; -.
DR SMR; Q898E8; -.
DR STRING; 212717.CTC_00510; -.
DR PRIDE; Q898E8; -.
DR EnsemblBacteria; AAO35133; AAO35133; CTC_00510.
DR GeneID; 64180364; -.
DR KEGG; ctc:CTC_00510; -.
DR HOGENOM; CLU_013748_6_0_9; -.
DR OMA; PNTYHLE; -.
DR OrthoDB; 391134at2; -.
DR UniPathway; UPA00076; UER00145.
DR Proteomes; UP000001412; 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; 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.
PE 3: Inferred from homology;
KW Hydrolase; Magnesium; Metal-binding; NAD; Reference proteome;
KW Thiamine pyrophosphate.
FT CHAIN 1..644
FT /note="3D-(3,5/4)-trihydroxycyclohexane-1,2-dione
FT hydrolase"
FT /id="PRO_0000352541"
FT REGION 442..522
FT /note="Thiamine pyrophosphate binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01669"
FT BINDING 65
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 644 AA; 71760 MW; BECFCFA9D7751DD4 CRC64;
METIKITTAQ ALIKFLNQQY VELDGQEYRF VQGIFTIFGH GNVLGIGQAL EEDPGHLEVY
QGHNEQGMAQ SAIAFAKQSN RKQIYACTSS VGPGAANMVT AAATATANNI PVLLLPGDTF
STRQPDPVLQ QVEQTYNLSI TTNDAFKAVS KYWDRVNRPE QLMTAMINAM RVLTDPANTG
AVTIALPQDV QGEIYDFPEY FFKKRVHRIE RTPPSKQAIE DAVELIKRKK KPLIICGGGV
RYSEAAESLK RFSEKFNIPF GETQAGKSAI EWSYGLNLGG IGVTGNSAAN SIAKDADLII
GVGTRFTDFT TCSKFLFQND DVEFLTINIS SFHANKLDAL KVISDAKVGL DTIANELERQ
GYSSDYEDEI KKAKNEWEKE LNRLFNIEYT EKEFVPEIAG HCDKVVEEFY KEFDSCLTQT
KVLGELNELL DDDAIVIGAS GSLPGDLHKV WCPKRSNTYH MEYGYSCMGY EVSAALGVKL
AEEDKEVYSL VGDGAYLMLH SELITSIKEG KKINILLFDN AGFGCINNLQ MSNGMGSFAT
EFRHRNSETG KLDGKLLKID FAKSAEGYGV KTYKVNTIDK LRYAIEDSKK QKISTLIDIK
ILPKTMTRGY ESWWHVGVSE KSKNPKINKA YESKINHLAK ARKY
