ID A0A0X3S4G3_9ACTN Unreviewed; 627 AA.
AC A0A0X3S4G3;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=3D-(3,5/4)-trihydroxycyclohexane-1,2-dione acylhydrolase (Decyclizing) {ECO:0000313|EMBL:KUJ36671.1};
GN ORFNames=ADL25_31555 {ECO:0000313|EMBL:KUJ36671.1};
OS Streptomyces sp. NRRL F-5122.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1609098 {ECO:0000313|EMBL:KUJ36671.1, ECO:0000313|Proteomes:UP000054048};
RN [1] {ECO:0000313|Proteomes:UP000054048}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL F-5122 {ECO:0000313|Proteomes:UP000054048};
RA Ju K.-S., Doroghazi J.R., Metcalf W.W.;
RL Submitted (OCT-2015) 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:KUJ36671.1}.
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DR EMBL; LMWH01000252; KUJ36671.1; -; Genomic_DNA.
DR RefSeq; WP_059131303.1; NZ_LMWH01000252.1.
DR AlphaFoldDB; A0A0X3S4G3; -.
DR OrthoDB; 3194735at2; -.
DR Proteomes; UP000054048; Unassembled WGS sequence.
DR GO; GO:0016823; F:hydrolase activity, acting on acid carbon-carbon bonds, in ketonic substances; IEA:InterPro.
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:KUJ36671.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054048};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 8..131
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 221..354
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 420..577
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT REGION 607..627
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 627 AA; 67548 MW; 0BF8DA2919A5C5B2 CRC64;
MTSTTRLTVA QALVRFLAAQ YTERDGVRRR LIGATWGIFG HGNVAGVGQA LLEYGGVMPY
HQGRNEQAMV HAAVGWARQC DRLSTHAVTT SIGPGATNLV TGAALATVNR LPVLLLPGDV
FATRPADPVL QQLEVPHAGD TSVNDCLRPV SKYFDRITRP EALIPAVLQA MRVLTDPVET
GAVTLALPQD VQAEAHDWPQ DLFAERTWTV RRPGPDPVEL AEAVQAIRAA RRPLVVAGGG
VHHSRAEDAL AEFAGTTGIP VASTQAGKGS LRWDHPQDVG GIGHTGTATA DELARTADLV
IGVGTRYTDF TTASGTLFIR DGVRFLNLNI APFDGHKLSG LPLVADARSG LEELTEALEM
HGHRVEPAYV VEYTEDKERW EQRVDACFDA DEPDIRPTQT QVIGALDALV DESDVIVNAA
GSLPGDLHRL WRSRSRDQYH VEYGYSCMGY EIPAAIGVKM AAPDRAVWAL VGDGTYLMMP
TEIVTAVQEG IAIKVLIVQN HGYASIGGLS ESVGGERFGT AYRYRSEDGA YTGAPLPVDL
AANAASLGMR VLRAKTVRDL RRALAEARAA DTPTCVYVET QTADTVSGAP GTQAWWDVPV
AETATRSSAV KAREEYDRHV STRRRHL
//