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Database: UniProt
Entry: A0A370B4K3_9ACTN
LinkDB: A0A370B4K3_9ACTN
Original site: A0A370B4K3_9ACTN 
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}.
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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
//
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