ID A0A0U3Q3B9_9ACTN Unreviewed; 624 AA.
AC A0A0U3Q3B9;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, 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:ALV38453.1};
GN ORFNames=AS200_08470 {ECO:0000313|EMBL:ALV38453.1};
OS Streptomyces sp. CdTB01.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1725411 {ECO:0000313|EMBL:ALV38453.1, ECO:0000313|Proteomes:UP000068029};
RN [1] {ECO:0000313|EMBL:ALV38453.1, ECO:0000313|Proteomes:UP000068029}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CdTB01 {ECO:0000313|EMBL:ALV38453.1,
RC ECO:0000313|Proteomes:UP000068029};
RA Tian Y., Zhou G., Yang H., Lu X.;
RT "Complete genome sequence of the Streptomyces sp. strain CdTB01, a
RT bacterium tolerant to cadmium.";
RL Submitted (DEC-2015) 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; CP013743; ALV38453.1; -; Genomic_DNA.
DR RefSeq; WP_058928023.1; NZ_CP013743.1.
DR AlphaFoldDB; A0A0U3Q3B9; -.
DR STRING; 1725411.AS200_08470; -.
DR KEGG; scx:AS200_08470; -.
DR OrthoDB; 3194735at2; -.
DR Proteomes; UP000068029; 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; 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:ALV38453.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000068029};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 9..132
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 222..355
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 419..576
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 624 AA; 66781 MW; 8ABE17D1702BD624 CRC64;
MMSNTRRLTV AQALVRFLSA QYTERDGVRH RLIAGTWGIF GHGNVAGIGQ ALVEYADDMP
YHQGRNEQSM VHAAVGYARQ LNRLSAQAVT TSIGPGATNL VTGAALATIN RLPVLLLPGD
YFASHAPDPL LQQLEHPTEA DVSVNDTLRP VSRYFDRITR PEALIPSALH AMRVLADPAE
TGAVTLALPQ DVQAEAHDWP EEFFAERVWH VRRPAPDPYE LAEAVAAIRA AERPLIVAGG
GVHHSEAEDA LKALVEATGI PVASTQAGKG SLRHDHPADL GGIGHTGTAV SDAVARTADL
VIGVGTRYTD FTTASGTLFQ NPDVRFVNLN ITAFDAHKLS ARTLVCDART GLTALTEALA
DHRVNPVHEA ASREGKERWE RLVDAAYTAA DENAVPTQTQ VLGALDAVVG DDDVVINAAG
SLPGDLHKLW RARSPRQYHL EYGYSCMGYE IPAAIGVQQA APGTPVWSLV GDGTYLMMPT
EIVTAVQEGL PVNLVLIQNH GYASIGGLSE SVGGERFGTA YRYRAADGTF SGAPLPVDLA
ANAGSLGMDV LRAKTVRELR EALAAARASD RPTCVYVETD TAGPAAPPAE AWWDVPVAET
ATREAAVRAR EEYDRQVADR RHHL
//
