ID   A0A158KRY3_9BURK        Unreviewed;       632 AA.
AC   A0A158KRY3;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=IolD protein {ECO:0000313|EMBL:SAL83350.1};
GN   ORFNames=AWB68_06874 {ECO:0000313|EMBL:SAL83350.1};
OS   Caballeronia choica.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Caballeronia.
OX   NCBI_TaxID=326476 {ECO:0000313|EMBL:SAL83350.1, ECO:0000313|Proteomes:UP000054770};
RN   [1] {ECO:0000313|Proteomes:UP000054770}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Peeters C.;
RL   Submitted (JAN-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; FCON02000136; SAL83350.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A158KRY3; -.
DR   OrthoDB; 3194735at2; -.
DR   Proteomes; UP000054770; 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; 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   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          21..143
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          230..362
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          429..583
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   632 AA;  67063 MW;  7AAB8DB21E1BA6B2 CRC64;
     MNQRAMQTEA RQATAGTIRL TTAQALVRYL AALRTVSGEP LFGGVFAIFG HGNVAGIGEA
     LYQHREELPT WRAHNEQAMA HSAIAYAKAN FRRRLMAVTT SIGPGATNLV TAAALAHVNR
     LPVLLLPGDI FVSRAPDPVL QQVEDLQDGG LSANDALKPV SRYFDRIVHP AQLLSALPRA
     IRVLTDAALC GPVTLALPQD VQAMAYDYPA AFFEPRAVSF HAPAPVAQEI EQAAAALRES
     HEPLIVSGGG VLYGDATDAL RTFAERHGIP VAETQAGKSA LAWDHPLNTG GIGVTGSSSA
     NELANAADCV LAVGTRLQDF TTGSNTLFAQ ARLIGINANA FDALKQDGIA VESDARLALD
     ALSAALGDWR AAPQWTTRAH HLADDWRTTV ASVTGTPHEG LLPREADVIG AVQRSDPQSA
     ANDIVVCAAG TLPADLQKLW RTSTPGGYHV EYGYSCMGYE IAGGLGVKLA KPDREVIVIV
     GDGSYLMMNS ELATSVMLGA KLIVVLLDNR GYGCINRLQQ ACGGAPFNNL IDDCRQGPQG
     APAIDFAMHA RALGATAEHV ANIGELEAAM QRARAADRSY LISIDTDPAR PTEEGGWWWE
     VAVPEVSERE AVRNARAGYE RALTARSTST SQ
//