ID A0A1H8B4J7_9RHOB Unreviewed; 608 AA.
AC A0A1H8B4J7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=3D-(3,5/4)-trihydroxycyclohexane-1,2-dione hydrolase {ECO:0000313|EMBL:SEM77855.1};
GN ORFNames=SAMN04488103_10252 {ECO:0000313|EMBL:SEM77855.1};
OS Gemmobacter aquatilis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Gemmobacter.
OX NCBI_TaxID=933059 {ECO:0000313|EMBL:SEM77855.1, ECO:0000313|Proteomes:UP000198761};
RN [1] {ECO:0000313|EMBL:SEM77855.1, ECO:0000313|Proteomes:UP000198761}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 3857 {ECO:0000313|EMBL:SEM77855.1,
RC ECO:0000313|Proteomes:UP000198761};
RA de Groot N.N.;
RL Submitted (OCT-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; FOCE01000002; SEM77855.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H8B4J7; -.
DR STRING; 933059.SAMN04488103_10252; -.
DR OrthoDB; 3194735at2; -.
DR Proteomes; UP000198761; 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:SEM77855.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000198761};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 23..129
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 216..349
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 411..560
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 608 AA; 64585 MW; 9C47A41914930517 CRC64;
MTTIRLTAAQ AMVKWLSVQM TEEGERFIEG IWAIFGHGNV AGIGEALYHA QDVFPTWRGH
NEQTMAHTAI AYAKTMKRKR AMAVTSSIGP GALNLVTAAA LAHVNRLPVL FIPGDVFANR
APDPVLQQIE DFDDGMVSAN DCFRPVVRYY DRISRPEHIL TALPRALRVM TDPANCGPVC
LAFCQDTQAE AYDYPVEFFT PKVWHIRRPE PDQRELEAAV AAILAAERPL IVAGGGVIYS
EAEADLLAFA KRHNIPLVET QAGKGAIDWE EPLHFGSPGV TGTGCGNALA AAADLVIGVG
TRFQDFTTGS WTVFSAPGRK ILSINIHGYD GAKRGAQALV SDAKVALAKI SAGLGAKRFA
DPDFASRAAW FATTDALFAA PEGNALPTDA QIIGAVTRAT GKESVIMSAA GTMPGALHVL
WRAAAGGYHM EYGFSCMGYE VAGAMGIKMA APDKHVVCMV GDGSYMMANS ELATAVMMAV
PFTVVLTDNR GYGCINRLQQ GCGGAPFNNM LDDSYHVNPA QIDFVAHAGS MGAIAKKVGS
VAELEAAMAE AKGASLPTVI LIETDSVPGT GAGGTWWDVA VPEVSVRPQV NAARETYVTN
TARQWLGN
//
