ID A0A1B1AWG1_9ACTN Unreviewed; 627 AA.
AC A0A1B1AWG1;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=3D-(3,5/4)-trihydroxycyclohexane-1,2-dione acylhydrolase (Decyclizing) {ECO:0000313|EMBL:ANP50850.1};
GN ORFNames=AVL59_15555 {ECO:0000313|EMBL:ANP50850.1};
OS Streptomyces griseochromogenes.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=68214 {ECO:0000313|EMBL:ANP50850.1, ECO:0000313|Proteomes:UP000092659};
RN [1] {ECO:0000313|EMBL:ANP50850.1, ECO:0000313|Proteomes:UP000092659}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14511 {ECO:0000313|EMBL:ANP50850.1,
RC ECO:0000313|Proteomes:UP000092659};
RA Wu L.;
RT "Complete genome sequence of Streptomyces griseochromogenes ATCC 14511, the
RT Blasticidin S producer.";
RL Submitted (JUN-2016) 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; CP016279; ANP50850.1; -; Genomic_DNA.
DR RefSeq; WP_067304275.1; NZ_JAGGLP010000010.1.
DR AlphaFoldDB; A0A1B1AWG1; -.
DR STRING; 68214.AVL59_15555; -.
DR KEGG; sgs:AVL59_15555; -.
DR OrthoDB; 3194735at2; -.
DR Proteomes; UP000092659; Chromosome.
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:ANP50850.1};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 13..128
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 226..359
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 423..580
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 627 AA; 67207 MW; 030FE6237C2B2633 CRC64;
MSLSTSEATS RLTVAQALVR FLSAQYTARD GERHRLIAGT WGIFGHGNVA GIGQALIEYS
DVMPYHQGRN EQAMVHAAVG HARQLDRLSA QAVTTSIGPG ATNLVTGAAL ATVNRLPVLL
LPGDYFATRP ADPLLQQLEH PGQFDMSVND TLRPVSRYFD RITRPEQLIP SALQAMRVLA
DPAETGAVTL ALPQDVQAEA YDWPEQFFAE RVWTVRRPAP DPTELSAAVR AIRAARRPLV
VAGGGVHHSR AEDALKALAD ATGIPVAATQ AGKGSLRHDH PADVGGIGHT GTAVADDLAR
TADLVIGVGT RYTDFTTASG TLFQDPEVRF LNLNITAFDA HKLAAQTVVA DARAVLEALT
ARLAGFRVDA AYETAYRAGK ERWERVVEAA YRAGDEDAVP TQTQVLGALD AVVGDEDVVI
NAAGSLPGDL HKLWRTRSRR QYHLEYGYSC MGYEIPAALG VRQAAPDTVV WALVGDGTYL
MMPTEIVTAV QERLPVKLVL IQNHGYASIG GLSESVGGER FGTAYRYRAA DGTFSGAPLP
VDLAANAASL GMEVLRAKTV RELREALTAA RAADVPTCVY VETDPAPTAP GAEAWWDVPV
AGAATREAAL RAREEYDRQV AGRRRHL
//
