ID A0A3B0CD23_9FLAO Unreviewed; 619 AA.
AC A0A3B0CD23;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=3D-(3,5/4)-trihydroxycyclohexane-1,2-dione acylhydrolase (Decyclizing) {ECO:0000313|EMBL:RKN82508.1};
DE EC=3.7.1.22 {ECO:0000313|EMBL:RKN82508.1};
GN Name=iolD {ECO:0000313|EMBL:RKN82508.1};
GN ORFNames=D7Z94_01275 {ECO:0000313|EMBL:RKN82508.1};
OS Ulvibacterium marinum.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Ulvibacterium.
OX NCBI_TaxID=2419782 {ECO:0000313|EMBL:RKN82508.1, ECO:0000313|Proteomes:UP000276603};
RN [1] {ECO:0000313|EMBL:RKN82508.1, ECO:0000313|Proteomes:UP000276603}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMM003 {ECO:0000313|EMBL:RKN82508.1,
RC ECO:0000313|Proteomes:UP000276603};
RA Zhang Z.;
RT "Ulvibacterium marinum gen. nov., sp. nov., a novel marine bacterium of the
RT family Flavobacteriaceae, isolated from a culture of the green alga Ulva
RT prolifera.";
RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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:RKN82508.1}.
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DR EMBL; RBCJ01000001; RKN82508.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3B0CD23; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000276603; 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:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR GO; GO:0019310; P:inositol catabolic process; IEA:InterPro.
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 InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR InterPro; IPR030817; Myo_inos_IolD.
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:0000313|EMBL:RKN82508.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000276603};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 7..129
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 218..351
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 415..572
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 619 AA; 67834 MW; 24D124A8C6E8E63C CRC64;
MEVKRLTVAQ ATIEYLKNQY VERDGIQNKF FAGCFGILGH GNVAGIGQAL HQNPDFPFYV
ARNEQAMVHT AAAFAKVKDR LQTFVCTSSI GPGATNMITG AAAATINRIP VLLIPGDIFA
TRHVAPVLQQ LESAVTQDIS VNDCFKPVSK YWDRINRPEQ LITALPEVMR VLTSQAETGA
VTLSIPQDVQ AEAYDFPVTL FQKKVWHIGR TMPDQTFLAK AIERIKESKR PLIVSGGGTI
YSGATEILKK LANRTGIPVT ETFAGKGSLD YNEPQNLGAV GVTGTPGAIE IAKEADLVIG
LGTRYSDFTT ISKSAFQNPE VQFVNINITE FDSFKHGALP LIGDAKAILE EMDQQLSDYE
VSKDYREKVE NFNTSWDEFV SGIYLEKNET PAFQGEVIGA VNTFSDASDI MICAAGSLPG
DLHKLWRTRN PKGFHLEYGY SCMGYEIAGG LGAKMANPES EVYVLVGDGS YLMMSQEIIT
SIQERQKLTI VLLNNDGYSS IGGLSASLGS DGFGTYYRYR NEETNQLDGG LLPIDYAANA
ASMGAHVIKT SNVEELKAAL KKAKTIDHTT LIYIEVDRKK GVPGFAWWDV AVAEVSEKVA
VSESHKTYQK NKKTQKYYL
//
