ID A0A069JTM7_9ACTN Unreviewed; 634 AA.
AC A0A069JTM7;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=3D-(3,5/4)-trihydroxycyclohexane-1,2-dione hydrolase {ECO:0000313|EMBL:KDQ67355.1};
GN ORFNames=DT87_09025 {ECO:0000313|EMBL:KDQ67355.1};
OS Streptomyces sp. NTK 937.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1487711 {ECO:0000313|EMBL:KDQ67355.1, ECO:0000313|Proteomes:UP000027475};
RN [1] {ECO:0000313|EMBL:KDQ67355.1, ECO:0000313|Proteomes:UP000027475}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NTK 937 {ECO:0000313|EMBL:KDQ67355.1,
RC ECO:0000313|Proteomes:UP000027475};
RA Olano C., Cano-Prieto C., Losada A., Mendez C., Salas J.A.;
RT "Draft genome sequence of marine actinomycete Streptomyces sp. NTK 937,
RT producer of the benzoxazol antibiotic caboxamycin.";
RL Submitted (APR-2014) 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:KDQ67355.1}.
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DR EMBL; JJOB01000001; KDQ67355.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A069JTM7; -.
DR OrthoDB; 3194735at2; -.
DR Proteomes; UP000027475; 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; 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; 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:KDQ67355.1};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 14..138
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 228..361
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 427..585
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 634 AA; 67708 MW; 827BBEDB0DABF61D CRC64;
MTTTARTRAP ARRMTTAQAL ITFLARQYTE RDGRRHRLIG ATWGIFGHGN VAGVGQALVE
AGPAMPYYQG RSEQAMVHAA VGYARQSNRL SAHAVTTSIG PGATNLVTGA ALATVNHLPV
LLLPGDTFAT RPADPVLQQL EVAHTGDVSV NDCLRPVSRY FDRITRPEAL IPAALQAMRT
LTDPAATGAV TLALPQDVQA EAYDWPAEFF TERVWHVRRP APDPDELARA VRAVRAARRP
LIVAGGGVHH SAAEETLAAF AAATRIPVAS TQAGKGSLRH DHPADVGGIG HTGTATADDL
ARKADLVIGV GTRYTDFTTA SGTLFAAPAV RFLNLNITGF DAHKLAAHPL VGDARTCLEA
LGAALDAPAY RVDPAYETEY TDAKDRWERR VDAAFAAPDP DARPTQAQVL GLLDALVTED
DILINAAGSL PGDLHKLWRA RSPRQYHVEY GYSCMGYEIP AALGVQLAAP GRPVWALVGD
GTYLMNPTEI VTAVQESLPV KLVILQNHGY ASIGGLSESV GAERFGTAYR YRDQDGGYTG
LPLPVDLAAN AASLGMRVLR ARTVRDLREA LTEARGADRP TCVHVETGTA DTASGPPPAQ
AWWDVPVAET ASRPPAAEAR KTYDRQIAAR RRHL
//