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Database: UniProt
Entry: A0A1H2K2D0_9ACTN
LinkDB: A0A1H2K2D0_9ACTN
Original site: A0A1H2K2D0_9ACTN 
ID   A0A1H2K2D0_9ACTN        Unreviewed;       635 AA.
AC   A0A1H2K2D0;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=3D-(3,5/4)-trihydroxycyclohexane-1,2-dione hydrolase {ECO:0000313|EMBL:SDU62712.1};
GN   ORFNames=SAMN04488563_3335 {ECO:0000313|EMBL:SDU62712.1};
OS   Jiangella alkaliphila.
OC   Bacteria; Actinomycetota; Actinomycetes; Jiangellales; Jiangellaceae;
OC   Jiangella.
OX   NCBI_TaxID=419479 {ECO:0000313|EMBL:SDU62712.1, ECO:0000313|Proteomes:UP000182977};
RN   [1] {ECO:0000313|Proteomes:UP000182977}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45079 {ECO:0000313|Proteomes:UP000182977};
RA   Varghese N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
CC   -!- SIMILARITY: Belongs to the TPP enzyme family.
CC       {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR   EMBL; LT629791; SDU62712.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H2K2D0; -.
DR   STRING; 419479.SAMN04488563_3335; -.
DR   Proteomes; UP000182977; Chromosome i.
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   Hydrolase {ECO:0000313|EMBL:SDU62712.1};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          9..132
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          417..578
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
FT   REGION          606..635
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   635 AA;  67029 MW;  0696DBB746CE1110 CRC64;
     MRLTVAQATV RFLAAQFTER DGVEHRLIEG CFGIFGHGNV AGLGQALLEA ELADPAALPY
     HQARNEQGMV HAAVGYARMR NRLSTLACTS SIGPGATNMV TGAALATINR LPVLLLPGDV
     FATRVADPVL QQLEMPHAPE VTVNDAFRPV SRFFDRVWRP EQLPAALLGA MRVLTDPAET
     GAVTLAMPQD VQAEAYDWPA ELFAKRVWHV PRAVPEPGAL ARAVALLRTA RRPLIVAGGG
     VIYSEATDAL RAFAEATGVP VAETQAGKGS LPYDHPLALG AVGATGTPGA NRVAREADVV
     IGIGTRYSDF TTASRTAFQD PGVRFVNVNV TGFDGAKQAG LPVVADARAA LEALTEALAA
     WSVPDGHREA AAAANREWDA VVTAAYTAQH RPLPAQTEVI GAVNEVSAPR DVVVNAAGSM
     PGELHKLWRT RDPKGYHVEY GYSTMGYEIA AGVGVRMAAP DRDVFVLVGD GSYLMMAQEL
     VTAVQERIKI VVVLVQNHGF ASIGSLSESL GSQRFGTAYR FRSGSGRLDG EVLPVDLAAN
     AASLGVHVVR VATVSELRAA LSDAKAAPAD GGPVLIHVET DPLAGAPDSE SWWDVPVSET
     AALDTTRAAR AEYERQKKAQ RPLVGPASGT EENEA
//
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