ID A0A1P8JRP3_9BURK Unreviewed; 625 AA.
AC A0A1P8JRP3;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=3D-(3,5/4)-trihydroxycyclohexane-1,2-dione acylhydrolase (Decyclizing) {ECO:0000313|EMBL:APW36433.1};
GN ORFNames=RD110_03815 {ECO:0000313|EMBL:APW36433.1};
OS Rhodoferax koreense.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Rhodoferax.
OX NCBI_TaxID=1842727 {ECO:0000313|EMBL:APW36433.1, ECO:0000313|Proteomes:UP000186609};
RN [1] {ECO:0000313|EMBL:APW36433.1, ECO:0000313|Proteomes:UP000186609}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DCY110 {ECO:0000313|EMBL:APW36433.1,
RC ECO:0000313|Proteomes:UP000186609};
RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL Submitted (JAN-2017) 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; CP019236; APW36433.1; -; Genomic_DNA.
DR RefSeq; WP_076196837.1; NZ_CP019236.1.
DR AlphaFoldDB; A0A1P8JRP3; -.
DR STRING; 1842727.RD110_03815; -.
DR KEGG; rhy:RD110_03815; -.
DR Proteomes; UP000186609; 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; 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:APW36433.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000186609};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 11..137
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 225..356
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 426..580
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 625 AA; 66983 MW; 290F0E9A989FE73C CRC64;
MKTVVKTQRL TMTQALVKHL AALRIEMDDG SVLPYCGGVF SIFGHGNVAG LGEALWAERA
SLRTYRAHNE QGMAHAAIAY GKAYFRQRMM AVTTSIGPGA TNLLTAAALA HVNRLPVLLL
PGDTFASRAP DPVLQQLEDF GHGDVSVNDA FRPLTRFFDR ISRPEQILTA LPRAIQVMTD
PAQCGPVCLA LPQDVQAQAF DCPEDFLRPA VLRVRRAPAD AGELARAASL LRNARRPLIV
AGGGVLYSQA GEMLRVFAHS CGIPVAETQA GKSSLAWNDT LNVGAIGVTG SPAANTLARE
ADLVCAIGTR LQDFTTGSHS LFAGTPILGL NVQVADAGKW HSTTLVADAR TALAQLMLDQ
LGDWRADAAW TTRAEHFAQG WTERVDAVTT FDPQSAGAVP YDAEVIGAVR DSAADSDSRD
VVVCAAGTLP AELHKLWRAA RPGNYHMEYG YSCMGYEIAG GLGVKMARPE QEVVVMVGDG
SYLMLNSEIA TSVMLGRKLI IVVLDNRGYG CIQRLQIASG SPRFNNMLED CADEAGSLPE
IDFAMHARSL GAEAVHVAGI GELKAAMARA RAASRTQVIV IDTTHTRTTD DGGCWWEVAI
PEVSERLEVQ AAHAQYLQEK QGQHP
//
