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Database: UniProt
Entry: A0A242DCL7_9ENTE
LinkDB: A0A242DCL7_9ENTE
Original site: A0A242DCL7_9ENTE 
ID   A0A242DCL7_9ENTE        Unreviewed;       638 AA.
AC   A0A242DCL7;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
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=A5875_001619 {ECO:0000313|EMBL:OTO20269.1};
OS   Enterococcus sp. 3H8_DIV0648.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=1834178 {ECO:0000313|EMBL:OTO20269.1, ECO:0000313|Proteomes:UP000194623};
RN   [1] {ECO:0000313|EMBL:OTO20269.1, ECO:0000313|Proteomes:UP000194623}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3H8_DIV0648 {ECO:0000313|EMBL:OTO20269.1,
RC   ECO:0000313|Proteomes:UP000194623};
RG   The Broad Institute Genomics Platform;
RG   The Broad Institute Genomic Center for Infectious Diseases;
RA   Earl A., Manson A., Schwartman J., Gilmore M., Abouelleil A., Cao P.,
RA   Chapman S., Cusick C., Shea T., Young S., Neafsey D., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Enterococcus sp. 3H8_DIV0648.";
RL   Submitted (MAY-2017) 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:OTO20269.1}.
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DR   EMBL; NGLG01000001; OTO20269.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A242DCL7; -.
DR   OrthoDB; 4494979at2; -.
DR   UniPathway; UPA00076; UER00145.
DR   Proteomes; UP000194623; 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; 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          10..133
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          223..354
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          440..592
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         66
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   638 AA;  70433 MW;  F3767351C073A849 CRC64;
     MEKTVCLTTA QALLKFLNQQ YISIDGKETP YVEGIFHVYG HGNVLGIGQA LELEPGHLKS
     YSGKNEQGMA HAATAFARQN LRKKIFAVST SAGPGAANLL TAAGTAFANN IPVLFLPADT
     FATRQPDPVL QQLEHAGSVA FSTNDAFQAV SRYWDRINRP EQLMSALLRA FEVMTNPATM
     GPATICLPQD VEAEAYDYPE EFFKKRVHYI DRRIPTAREL AGASQRIKDS KRPVIIVGGG
     CKYSEAGEIL EQISRDCQIP LVETHAGKST VSWKFKNNLG GMGILGTSAA NKAVQQADLI
     IGIGTRYTDF TSASKSIFNF EQAKMMNINV SRQQAAKLEA FQVVGDAKAT LEQLAPMIEG
     YQTAYGEKIN ELKEEWISER NRLKAAHFKR KDFTPEIKDH FSQEILNEYA DALATNLTQT
     EVFIHLNDFV DEDAIVIGSA GSLPGDMQRL WNPVKENTYH LEYGYSCMGY EIAGAMGVRM
     ARPEQEVYAL VGDGSFLMLH SELVSSLQYD KKINIVLFDN SGFGCINNLQ MDNGGASQGT
     EFRNTKDEIM NIDYAKVAEG YGAKTYRVNS IAELQAAVED AKKQTRSTLI EIKVLPKTMT
     DGYDGSWWNV GISEVSGKAA VQEAYKAKQA KLATIRKY
//
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