ID A0A1I3TJE8_9RHOB Unreviewed; 620 AA.
AC A0A1I3TJE8;
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:SFJ70682.1};
GN ORFNames=SAMN04488095_3460 {ECO:0000313|EMBL:SFJ70682.1};
OS Jannaschia pohangensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Jannaschia.
OX NCBI_TaxID=390807 {ECO:0000313|EMBL:SFJ70682.1, ECO:0000313|Proteomes:UP000199110};
RN [1] {ECO:0000313|EMBL:SFJ70682.1, ECO:0000313|Proteomes:UP000199110}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19073 {ECO:0000313|EMBL:SFJ70682.1,
RC ECO:0000313|Proteomes:UP000199110};
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; FORA01000005; SFJ70682.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I3TJE8; -.
DR STRING; 390807.SAMN04488095_3460; -.
DR Proteomes; UP000199110; 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:SFJ70682.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000199110};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 8..132
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 220..352
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 429..572
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT REGION 600..620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 620 AA; 66237 MW; 97B7FC3BC8012891 CRC64;
MTQTVRLTVA QAIVRWLMTQ YIDIDGTETR ICGGGFGIFG HGNAPCLGEA LYPVQPDLPL
YRGQNEQGMG FAAAAYAKYH LRQRFMFCTA SAGPGTANLL TAAALAHANR LPMLMLCGDT
FLTRLPDPVL QQLEHFGNPT LGVNDAFKSV SRYWDRITHP AQILQSLPAA LATMLDPADC
GPAFLSLPQD VQGWAHDYPE VFFARRVHRI RRQAPDTAEV ADAASLLITA KRPVIIAGGG
VQYSRAVAEL AAFAEAHQIP VIETIAGRAN LVDTHPLNIG PVGVTGSDSA NAVAERADVI
LAVGTRLQDF TTGSWTAFAP DARIVHLNAA RHDAAKHGAQ TVVGDARLGL RAIGAEISGY
AAPAQWVDFA RTARAKWVAS VARNVSPGNR PNSYALAIGV VNALCDPSDR IIAAAGGLPA
EVTANWRTLR TGTVDIEFGF SCMGYEIAGG WGARIAQTER EPDQDAIVFT GDGSYLMLNS
DIYSSVLTGK KLIILVLDNG GFAVIDKLQR NTGNESFNTL IADTPTATHP VGVDFAAHAR
ALGAQAETVS DPGELADAFR RAKAADTTCV IVMQVDPYDG WTTEGHSWWE VGMPEVSDSK
RVRDAHAEAE AGRAKQRHGV
//
