ID E1U886_LACCA Unreviewed; 651 AA.
AC E1U886;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 54.
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:ADD13509.1};
GN Synonyms=IolD {ECO:0000313|EMBL:ADD13496.1};
OS Lacticaseibacillus casei (Lactobacillus casei).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lacticaseibacillus.
OX NCBI_TaxID=1582 {ECO:0000313|EMBL:ADD13509.1};
RN [1] {ECO:0000313|EMBL:ADD13496.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=AG9-5 {ECO:0000313|EMBL:ADD13496.1};
RA Zhang W.Y., Sun Z.H.;
RT "Comparative analysis of iol clusters in Lactobacillus casei strains.";
RL Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADD13509.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=XM7-1 {ECO:0000313|EMBL:ADD13509.1};
RA Zhang W., Sun Z.;
RL Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:ADD13509.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=XM7-1 {ECO:0000313|EMBL:ADD13509.1};
RX AGRICOLA=IND44437107; DOI=10.1007/s11274-010-0375-x;
RA Zhang W.Y., Sun Z.H., Yu D.L., Airideng C., Chen W., Meng H., Zhang H.P.;
RT "Comparative analysis of iol clusters in Lactobacillus casei strains.";
RL World J. Microbiol. Biotechnol. 26:1949-1955(2010).
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}.
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DR EMBL; FJ967835; ADD13496.1; -; Genomic_DNA.
DR EMBL; FJ967836; ADD13509.1; -; Genomic_DNA.
DR AlphaFoldDB; E1U886; -.
DR UniPathway; UPA00076; UER00145.
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; 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 Thiamine pyrophosphate {ECO:0000256|HAMAP-Rule:MF_01669}.
FT DOMAIN 22..147
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 235..368
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 453..605
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT REGION 455..535
FT /note="Thiamine pyrophosphate binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01669"
FT BINDING 80
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01669"
FT BINDING 506
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01669"
FT BINDING 533
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01669"
SQ SEQUENCE 651 AA; 71074 MW; 5ED7145AE15F0A6B CRC64;
MTATELNAQV AADAKKETIR LTTAQALVRF LNQQYIDVDG QVTSFVEGLF AIFGHGNVLG
LGEALQEDPG HLKVYQGHNE QGMASTAIAY SRQLYRHKIF AVTASAGPGS ANFVTAAGNA
YVNSIPILFL PADTFATRQP DPVLQQIEVD YSADTTTNDV LKPVYKYWDR IERPEQLMSA
LLKAFEVLTN PATAGPVTIA LPQDVEGQAY DYPLSFFKKR VHVVKRVQPS SAELAGAVEL
IQASQTPVLI VGGGAKFSDA GAAIETFSER FNIPIVETPT GKSAISSDFP NNMGGTGILG
TAAANAVITK ADLIIGAGTR YTDFTTASKT AIHPGKTQLI NINLNRMQSY KFDAFPIVAD
VRDTLSQLTE SLSDYRSQFT DLATIKEAWQ KERQRLAHTN YDAPAYVPEV KNQFDAKTMA
AYAEKLQTHL TQTEAVIAVN NTIDPTSIIV AAAGSLPGDV QRIWDPVVPN TYHMEYGYSM
MGYEVPAALG IKLAQPDQES YALVGDGSFM MLHSELVTAL QYHKKINILV FDNSGFASIN
NLQMAQGSNS YLTEFRTADN DIMKTDFAKI AEGYGAKAYR ANDRKSLIAA IEDAKKQTVS
TLIDIKVLPK TMTQGYGQSW WRVGVSEISN NPKVQKAYQD IQTGIDKAFK Y
//
