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
//