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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//