ID A0A1N7LP62_9RHOB Unreviewed; 621 AA.
AC A0A1N7LP62;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=3D-(3,5/4)-trihydroxycyclohexane-1,2-dione hydrolase {ECO:0000313|EMBL:SIS75559.1};
GN ORFNames=SAMN05421759_10320 {ECO:0000313|EMBL:SIS75559.1};
OS Roseivivax lentus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseivivax.
OX NCBI_TaxID=633194 {ECO:0000313|EMBL:SIS75559.1, ECO:0000313|Proteomes:UP000186684};
RN [1] {ECO:0000313|EMBL:SIS75559.1, ECO:0000313|Proteomes:UP000186684}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 29430 {ECO:0000313|EMBL:SIS75559.1,
RC ECO:0000313|Proteomes:UP000186684};
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}.
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DR EMBL; FTOQ01000003; SIS75559.1; -; Genomic_DNA.
DR RefSeq; WP_076446460.1; NZ_FTOQ01000003.1.
DR AlphaFoldDB; A0A1N7LP62; -.
DR STRING; 633194.SAMN05421759_10320; -.
DR OrthoDB; 3194735at2; -.
DR Proteomes; UP000186684; 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:SIS75559.1};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 9..133
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 221..354
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 430..573
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT REGION 600..621
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 621 AA; 66638 MW; 9E9EC51F716D9A34 CRC64;
MIGDTIRLTT AQAIIRYLNA QFIEIDGARQ RLCGGGFGIF GHGNVTCLGE ALYDHRDTLP
LYRGQNEQSM GFAAAAYAKY HLRRRFMFCT ASAGPGTANL LTASALAHAN RLPMLMLCGD
TFLTRLPDPV LQQLEHFNNP TLGVNDAFRA VTRYWDRITH PAQVIQSLPA AIATMLDPAD
CGPAFLGLPQ DVQGWAYDYP LSFFEARTHR IRRVTPDADE VADAVAALRA AQRPIIIAGG
GVQYSGAVAE LMAFAETHQI PVIETIAGRA NLTAEHPLNI GPVGVTGSDS ANAVAEAADV
ILSVGCRLQD FTTGSWTAFA KEARIVSLNA ARHDAGKHMS LPVVGDAKLG LAALAEGMAG
YTAPETWTGF AQDERRKWDA YVAENTKSGN RPNSYAQAIG VVNALCDPRD RVVAAAGGLP
AEVTANWRTR DIGTVDVEFG FSCMGYEIAG GWGARIAQSE VEPDADTIVF CGDGSYLLMN
SDIYSSVLTG KKLIVLVLDN GGFAVINKLQ NNTGNESFNN LFADAPTIPQ PFAVDFAAHA
AAMGAHAVHV DNPEQLAEAF KTAKAADKTS VIVMNVDAYE GWTAQGHTWW EVGTPHVSEH
ASVRDKHAEI EAERAKQRRG V
//
