ID A0A161Y5H6_9CLOT Unreviewed; 644 AA.
AC A0A161Y5H6;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=3D-(3,5/4)-trihydroxycyclohexane-1,2-dione hydrolase {ECO:0000256|HAMAP-Rule:MF_01669};
DE Short=THcHDO hydrolase {ECO:0000256|HAMAP-Rule:MF_01669};
DE EC=3.7.1.22 {ECO:0000256|HAMAP-Rule:MF_01669};
GN Name=iolD {ECO:0000256|HAMAP-Rule:MF_01669,
GN ECO:0000313|EMBL:KZL93469.1};
GN ORFNames=CLMAG_05150 {ECO:0000313|EMBL:KZL93469.1};
OS Clostridium magnum DSM 2767.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1121326 {ECO:0000313|EMBL:KZL93469.1, ECO:0000313|Proteomes:UP000076603};
RN [1] {ECO:0000313|EMBL:KZL93469.1, ECO:0000313|Proteomes:UP000076603}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2767 {ECO:0000313|EMBL:KZL93469.1,
RC ECO:0000313|Proteomes:UP000076603};
RA Poehlein A., Uhlig R., Fischer R., Bahl H., Daniel R.;
RT "Genome sequence of Clostridium magnum DSM 2767.";
RL Submitted (APR-2016) 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:0000256|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:0000256|HAMAP-Rule:MF_01669};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01669};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01669};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01669};
CC Note=Binds 1 thiamine pyrophosphate per subunit. {ECO:0000256|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:0000256|HAMAP-
CC Rule:MF_01669}.
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|HAMAP-Rule:MF_01669}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KZL93469.1}.
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DR EMBL; LWAE01000001; KZL93469.1; -; Genomic_DNA.
DR RefSeq; WP_066617507.1; NZ_LWAE01000001.1.
DR AlphaFoldDB; A0A161Y5H6; -.
DR STRING; 1121326.CLMAG_05150; -.
DR PATRIC; fig|1121326.3.peg.471; -.
DR OrthoDB; 4494979at2; -.
DR UniPathway; UPA00076; UER00145.
DR Proteomes; UP000076603; Unassembled WGS sequence.
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 CDD; cd02003; TPP_IolD; 1.
DR CDD; cd07035; TPP_PYR_POX_like; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR Gene3D; 3.40.50.1220; TPP-binding domain; 1.
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_TPP-bd.
DR NCBIfam; TIGR04377; myo_inos_iolD; 1.
DR PANTHER; PTHR18968:SF9; 3D-(3,5_4)-TRIHYDROXYCYCLOHEXANE-1,2-DIONE HYDROLASE; 1.
DR PANTHER; PTHR18968; THIAMINE PYROPHOSPHATE ENZYMES; 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; DHS-like NAD/FAD-binding domain; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR PROSITE; PS00187; TPP_ENZYMES; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01669};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01669};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01669};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_01669};
KW Reference proteome {ECO:0000313|Proteomes:UP000076603};
KW Thiamine pyrophosphate {ECO:0000256|HAMAP-Rule:MF_01669}.
FT DOMAIN 7..134
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 219..352
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 441..599
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT REGION 442..522
FT /note="Thiamine pyrophosphate binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01669"
FT BINDING 65
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01669"
FT BINDING 493
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01669"
FT BINDING 520
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01669"
SQ SEQUENCE 644 AA; 71277 MW; 0EA089EB83E67423 CRC64;
MKTIRLTVAQ ALVKFLDNQY VEFDGTVNKF VKGVFTIFGH GNVLGLGQAL EQHPGELVVH
QGRNEQGMAH AAMGFAKQMH RKQIYACTSS VGPGAANMVT AAATATANRI PVLFLPGDVY
ATRQPDPVLQ QIEQFHNLSI STNDTFKAVS KYWDRITRPE QLMSAAISAM RVLTNPADTG
AVTLALPQDV QGEAYDYPEY FFKKRIHRIE RRPATQEMIK DAVELISKKK KPILICGGGV
RYSEAAEAFK NFAEKFNIPF GETQAGKSAI VWNHELNLGG IGTTGNLTAN IIAKEADLVI
GVGTRYTDFT TSSKWLFQNS EVEFLNINVA EFDSYKLDAV KVVADGKAAL EAIGNELEKI
EYKSAYAGEI KEAKSKWEAE LDRLFKLEYT GEEFKPEVAG HLDHVLGEFG KQTGAYLTQT
RALGILDEML DHNAIVVGAS GSLPGDLQRV WRPKEANTYH MEYGYSCMGY EVNAALGAKL
AAPDREVYTL LGDGSYMMLH SELPTSIQER KKINVLVFDN MAFGCINNLQ MGNGMGSFGT
EFRFRNEETG KLDGGLVPID FAMSAAAYGC KTYTVKTVEE LKAAIEDSKK QSVSTLIDIK
ILPKTMTHDY ESWWRVGLAE ISDKESIKEA HKELKENIAK AREY
//
