ID A0A0K1JHH4_9MICO Unreviewed; 646 AA.
AC A0A0K1JHH4;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=3D-(3,5/4)-trihydroxycyclohexane-1,2-dione hydrolase {ECO:0000313|EMBL:AKU16151.1};
GN ORFNames=VV02_10225 {ECO:0000313|EMBL:AKU16151.1};
OS Luteipulveratus mongoliensis.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermacoccaceae;
OC Luteipulveratus.
OX NCBI_TaxID=571913 {ECO:0000313|EMBL:AKU16151.1, ECO:0000313|Proteomes:UP000066480};
RN [1] {ECO:0000313|EMBL:AKU16151.1, ECO:0000313|Proteomes:UP000066480}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MN07-A0370 {ECO:0000313|EMBL:AKU16151.1,
RC ECO:0000313|Proteomes:UP000066480};
RA Juboi H., Basik A., Shamsul S.S., Arnold P., Schmitt E.K., Sanglier J.-J.,
RA Yeo T.;
RT "Luteipulveratus halotolerans sp. nov., a novel actinobacterium
RT (Dermacoccaceae) from Sarawak, Malaysia.";
RL Submitted (MAR-2015) 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; CP011112; AKU16151.1; -; Genomic_DNA.
DR RefSeq; WP_052591411.1; NZ_CP011112.1.
DR AlphaFoldDB; A0A0K1JHH4; -.
DR STRING; 571913.VV02_10225; -.
DR KEGG; lmoi:VV02_10225; -.
DR PATRIC; fig|571913.6.peg.2086; -.
DR OrthoDB; 3194735at2; -.
DR Proteomes; UP000066480; Chromosome.
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:AKU16151.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000066480};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 5..131
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 220..354
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 424..585
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT REGION 621..646
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 646 AA; 69304 MW; F4ACD182418046B1 CRC64;
MKLTVGQAMV RFLGQQWTER DGERQRMFAG CLGIFGHGNV AGVGQALLQD ERSGIPALPY
VLARNEQAMV HTASAYARAS NRLRMWACTA SVGPGSTNMV TGAALATVNR VPVLLLPSGT
FATRATGTVL QQLESPTAGD ITVNDALRPV SRYFDRIQRP EQLPSALLEA MGVLTDPADT
GAVTLALPQD VQAEAYDWPE DLFDERLWHI ARAPAEGSQI AAAARLIRSA ERPFVVVGGG
VHYSGAEDAL DALCRATGIA VGETQAGKGS LTHGHPQLLG AVGSTGTTAA NAFARDADVV
IGIGTRWSDF TTASRTAFQR RGVRFININV ARFDAGKHAG LAVVGDAREA IVALTQQLDG
YRTDTAYADR ATREWTAWDE QVEQAYDPPA EVTERLGDGI LSQGQVLGIV NETSAPEDVV
VCAAGSMPGD LHKLWRVRDR GGYHVEYGYS CMGYEIPGGI GVRLAHPDRD VFVMVGDGSY
LMMPTELVTA VQERVKVIVV LVQNHGFHSI GSLSESLGSQ RFGTSYRYRS PDGTLDGDYL
PVDLAANARS LGAHVVEVRS ADELTAAVRE AKAAPHDFGP FVIHVETDPL VAAPDSDSWW
DVPVAEVSEL ETTRAAYEQY VDQKKGQRPL LRPGVDPAPR EADSAH
//
