ID A0A1N7DC84_9ACTN Unreviewed; 620 AA.
AC A0A1N7DC84;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=3D-(3,5/4)-trihydroxycyclohexane-1,2-dione acylhydrolase (Decyclizing) {ECO:0000313|EMBL:SIR73443.1};
GN ORFNames=SAMN05421833_11451 {ECO:0000313|EMBL:SIR73443.1};
OS Microbispora rosea.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Microbispora.
OX NCBI_TaxID=58117 {ECO:0000313|EMBL:SIR73443.1, ECO:0000313|Proteomes:UP000186096};
RN [1] {ECO:0000313|EMBL:SIR73443.1, ECO:0000313|Proteomes:UP000186096}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12950 {ECO:0000313|EMBL:SIR73443.1,
RC ECO:0000313|Proteomes:UP000186096};
RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; FTNI01000014; SIR73443.1; -; Genomic_DNA.
DR RefSeq; WP_076436794.1; NZ_FTNI01000014.1.
DR AlphaFoldDB; A0A1N7DC84; -.
DR STRING; 58117.SAMN05421833_11451; -.
DR OrthoDB; 4959782at2; -.
DR Proteomes; UP000186096; 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; 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:SIR73443.1};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 8..137
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 225..356
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 417..575
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 620 AA; 65507 MW; BB9FBFBEE88FF601 CRC64;
MTNTTRLTVA QALVRFLARQ WTERDGVEHR LIAGCMGIFG HGNVAGIGQA LAEQGAGTRD
PLPYYPARNE QAMVHTAAGY ARQSDRLSTL ACTSSIGPGA TNMVTGAALA TINRLPVLLL
PGDLFATRVA SPVLQELEDP RSYDVSVNDC LRPVSRFWDR VNRPEQLPAA LLGAMRVLTD
PAETGAVTLA LPQDVQAEAY DWPGELFARR VWHVARPVPE PAALARAVEL LRGSRRPLIV
AGGGVRYSGA CAELARFAER HGVPVAETQA GKGALPYDHP CAVGAIGHTG TRAADTLARE
ADLVVGIGTR FGDFTTASRT LFRQAGFLNV NVAAFDAAKH AAETLVADAR EALKALGAAF
GDVDWRADPG WTGRAAGLAA AWQAEIDRFY GGTELTQPVV LGVLNEVAAG GVVVNAAGSM
PGDLHRLWRA SDPGQYHVEY GYSCMGYEIA GGLGAKLAAP EREVFVLVGD GSYLMMAQEI
ATAVQEGVKL VIVLVDNHGF ASIGALSESV GALRLGTAYR RRGPGGRLDG ERLPVDLAAN
AASLGADVLT AADPRTLRAA LAKAVASFRT TVVHVETVPG PAPAAEAWWD VPVAEVSGIA
EARAARERYD EAKRDQRPYL
//
