ID A0A060LS55_9BACI Unreviewed; 636 AA.
AC A0A060LS55;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
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 ORFNames=BleG1_0257 {ECO:0000313|EMBL:AIC92865.1};
OS Shouchella lehensis G1.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Shouchella.
OX NCBI_TaxID=1246626 {ECO:0000313|EMBL:AIC92865.1, ECO:0000313|Proteomes:UP000027142};
RN [1] {ECO:0000313|EMBL:AIC92865.1, ECO:0000313|Proteomes:UP000027142}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G1 {ECO:0000313|EMBL:AIC92865.1,
RC ECO:0000313|Proteomes:UP000027142};
RX PubMed=24811681; DOI=10.1016/j.gene.2014.05.012;
RA Noor Y.M., Samsulrizal N.H., Jema'on N.A., Low K.O., Ramli A.N.,
RA Alias N.I., Damis S.I., Fuzi S.F., Isa M.N., Murad A.M., Raih M.F.,
RA Bakar F.D., Najimudin N., Mahadi N.M., Illias R.M.;
RT "A comparative genomic analysis of the alkalitolerant soil bacterium
RT Bacillus lehensis G1.";
RL Gene 545:253-261(2014).
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; CP003923; AIC92865.1; -; Genomic_DNA.
DR RefSeq; WP_038476231.1; NZ_CP003923.1.
DR AlphaFoldDB; A0A060LS55; -.
DR STRING; 1246626.BleG1_0257; -.
DR KEGG; ble:BleG1_0257; -.
DR PATRIC; fig|1246626.3.peg.240; -.
DR eggNOG; COG3962; Bacteria.
DR HOGENOM; CLU_013748_6_0_9; -.
DR OrthoDB; 4494979at2; -.
DR UniPathway; UPA00076; UER00145.
DR Proteomes; UP000027142; 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 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:UP000027142};
KW Thiamine pyrophosphate {ECO:0000256|HAMAP-Rule:MF_01669}.
FT DOMAIN 29..135
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 220..352
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 439..591
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT REGION 441..521
FT /note="Thiamine pyrophosphate binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01669"
FT BINDING 66
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01669"
FT BINDING 492
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01669"
FT BINDING 519
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01669"
SQ SEQUENCE 636 AA; 70093 MW; 94F9A96519800ADA CRC64;
MAETIRLTTG QALVKFLNNQ FISVDGKEEH FVEGMFNIFG HGNVLGIGQA LEQDAGHLKV
IQGKNEQGMA HAAIAYSKQM LRKKIYAVTT SVGPGAANLV AAAGTALANN IPVLLLPADT
FATRQPDPVL QQFEQEYSAA ITTNDALKPV SRYWDRVVRP EQLMSSLLRA FEVMTDPAKA
GPVTICIAQD VEGEAYDYPM TFFGKRVHYV DRSEPTSREI DQAIQAIRKS KKPLIIVGGG
AKYSEARDEL VTFSETYRVP MVETQAGKST VESHHPLNLG GVGVTGTKAA NLAAKEADLV
IGVGTRYTDF TSSSKTAFSY DKASFVNINV SRMHAYKMDA VQVVADARVT LSILFEKLKG
YRSHHGSIDS WKKEWIQERE RLSAISFDRN RFKPEIEGQF SQQVLNEYAD TLNTEFPQTT
ALIALNKAIA KDAVIVCAAG SLPGDLQRLW DTETPNTYHL EYGYSCMGYE IAGGFGAKLA
EPEKEVYSFV GDGSFLMMHS ELVTAIQYGY KLNVVLFDNA GFGCISNLQM DHGSGSHGCE
FRTHTGDIMN IDYAKIAEAY GAKVYRVSSV EQLQKAVKDA MCQEVSTLIE IKVLPKTMTD
GYESWWNVGV AETSNVTSVQ RAYQQHQTKL NTAKLY
//
