ID   A0A2T6BAZ6_9RHOB        Unreviewed;       624 AA.
AC   A0A2T6BAZ6;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=3D-(3,5/4)-trihydroxycyclohexane-1,2-dione hydrolase {ECO:0000313|EMBL:PTX53237.1};
GN   ORFNames=C8N34_101149 {ECO:0000313|EMBL:PTX53237.1};
OS   Gemmobacter caeni.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Gemmobacter.
OX   NCBI_TaxID=589035 {ECO:0000313|EMBL:PTX53237.1, ECO:0000313|Proteomes:UP000244224};
RN   [1] {ECO:0000313|EMBL:PTX53237.1, ECO:0000313|Proteomes:UP000244224}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21823 {ECO:0000313|EMBL:PTX53237.1,
RC   ECO:0000313|Proteomes:UP000244224};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT   (KMG-II): from individual species to whole genera.";
RL   Submitted (APR-2018) 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:PTX53237.1}.
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DR   EMBL; QBKP01000001; PTX53237.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T6BAZ6; -.
DR   OrthoDB; 3194735at2; -.
DR   Proteomes; UP000244224; 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:0016740; F:transferase activity; IEA:UniProtKB-KW.
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:PTX53237.1};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          67..137
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          225..357
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          418..570
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   624 AA;  66167 MW;  16F9C2D7DE5976A9 CRC64;
     MTQTIRLTAA QAMVKWLSVQ MTAEGERFIE GCWAIFGHGN VAGLGEALHQ GLHGQLCGNT
     PFPTWRGQNE QTMAHAAIAF AKGRARRQAH AVTSSIGPGA TNMVTAAAMA HVNRLPVLFI
     AGDVFASRRP DPVLQQVEDF DDGTVSANDC FRPVVRYFDR IQRPEHLLTA LPRALRVMTD
     PADCGPVCLA FCQDVQAEAF DWPEAFFAPK VWHIRRPAPD ARELAEVSAQ IRAAERPLIL
     CGGGVIYSGA EAVLAAFASR HGIAVTETQA GKSALAQAHP MNFGAAGVDG SAAANAALRA
     ADLVIGIGTR LQDFTTGSRT LFAPDARLVS INVHGYDAAK HGALSLVADA RIALEALSPL
     LDGYCAGVDA AARADWLRAV DAHCSAPVAE DALPSDAQVI GAVQAVSTEA TIALCAAGTM
     PGALKLLWQA APGGYHMEYG YSCMGYELAG AMGLKLAQPA REVICFVGDG SYMMANAELA
     TAVMRRIPFT VVLTDNRGYG CINRLQTLGC GGAAFNNLYE DCLIEDQPRI DYAAHAASMG
     AHAVKVAGLA GLQRAIREAR GRQKPTVIVI ETTARDFPGT GIETAAGPHG HFWEVAVPAV
     GDRDTMREAY ERYIANTARA RLTN
//