ID A0A370B4K3_9ACTN Unreviewed; 714 AA.
AC A0A370B4K3;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=3D-(3,5/4)-trihydroxycyclohexane-1,2-dione acylhydrolase (Decyclizing) {ECO:0000313|EMBL:RDG36767.1};
DE EC=3.7.1.22 {ECO:0000313|EMBL:RDG36767.1};
GN Name=iolD {ECO:0000313|EMBL:RDG36767.1};
GN ORFNames=DVH02_18405 {ECO:0000313|EMBL:RDG36767.1};
OS Streptomyces corynorhini.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2282652 {ECO:0000313|EMBL:RDG36767.1, ECO:0000313|Proteomes:UP000253741};
RN [1] {ECO:0000313|EMBL:RDG36767.1, ECO:0000313|Proteomes:UP000253741}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AC230 {ECO:0000313|EMBL:RDG36767.1,
RC ECO:0000313|Proteomes:UP000253741};
RA Dunlap C.;
RT "Streptomyces species from bats.";
RL Submitted (JUL-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:RDG36767.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; QQNA01000140; RDG36767.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A370B4K3; -.
DR OrthoDB; 3194735at2; -.
DR Proteomes; UP000253741; 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; 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; 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.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:RDG36767.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000253741};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 43..166
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 256..389
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 507..664
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 419..483
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..37
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 714 AA; 75331 MW; D9BA66AF61D8E6D7 CRC64;
MTTDPDLTGP GAPDNAADAL GSDARRPDAR RADGLRPATR RLTVAQALIR FLSRQYTERD
GHRQRLIAAT WGIFGHGNVA GIGQALVEAA PDMRYLQGRN EQSMVHAAVG YARQSTRLSA
HAVTTSIGPG ATNLVTGAAL ATINRLPVLL LPGDTFATRP ADPVLQQLEV RSAGDVSVND
ALRPVSAYFD RVSRPEALIP AALAAMRVLG DPAETGAVTL ALPQDVQAEA YDWPEEFFAE
RIWRVRRQAP DPDELADAVR LVRAARRPLI VAGGGVHYSA AEEALAAFAE TTGMPVASTQ
AGKGSLRHDH PADVGGIGHT GSATADDLAR TADLVIGVGT RWSDFSTASA TLFQNPAVRF
LNLNVTGFDA HKLAAHPLVA DARTALQQLA AGLTGHRVDS AYTAEFREGK ARWEERVRTA
FTGSAAEPAD GRAGGSGTGH EKAGSGGAGD EKAADVRAGD GKTGGGGAGD LVRPAQERRD
AVRPTQAQVL GVLDGLVTDE DILINAAGSL PGDLHKLWRA RSRDQYHVEY GYSCMGYEIP
AAIGVQLAAP DRPVWALVGD GTYLMNPTEI VTAVQEGLPV NVVILQNHGY ASIGGLSETV
GAERFGTAYR FRAADATYTG APLPVDLAAN AASLGLRTIR AKTVDDLREA LAEARAHDGP
TCVYVETETA DTVSGVPPAQ AWWDVPVAET ATRTSAVSAR EEYERFAAAR RRHL
//