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Database: UniProt
Entry: A0A239AC75_9ACTN
LinkDB: A0A239AC75_9ACTN
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ID   A0A239AC75_9ACTN        Unreviewed;       631 AA.
AC   A0A239AC75;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=3D-(3,5/4)-trihydroxycyclohexane-1,2-dione hydrolase {ECO:0000313|EMBL:SNR93190.1};
GN   ORFNames=SAMN06264365_107230 {ECO:0000313|EMBL:SNR93190.1};
OS   Actinoplanes regularis.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Actinoplanes.
OX   NCBI_TaxID=52697 {ECO:0000313|EMBL:SNR93190.1, ECO:0000313|Proteomes:UP000198415};
RN   [1] {ECO:0000313|EMBL:SNR93190.1, ECO:0000313|Proteomes:UP000198415}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 43151 {ECO:0000313|EMBL:SNR93190.1,
RC   ECO:0000313|Proteomes:UP000198415};
RA   Kim H.J., Triplett B.A.;
RL   Submitted (JUN-2017) 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; FZNR01000007; SNR93190.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A239AC75; -.
DR   OrthoDB; 3194735at2; -.
DR   Proteomes; UP000198415; 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: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:SNR93190.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198415};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          57..141
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          227..361
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          420..579
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
FT   REGION          612..631
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   631 AA;  67257 MW;  876090FF65D5E7C6 CRC64;
     MKHRLTVAQA VVRFLANQLT ERDGIRQRAV AGFLGIFGHG NVAGIGQALL QAQRTGQAAS
     GRAEMPYILA RNEQAMVHTA VGYARMRNRL SAMACTASIG PGSTNMLTGA ALATVNRIPV
     LLLPSDVFAT RVATPVLQEL EDSRFGDVSV NDAFRPLSKY FDRVWRPEQL PQALLGAMRV
     LTDPVETGAV TICLPQDVQA EAYEYPDELF AQRVWHVARA VPDPLAVEAA AAVIRGAKRP
     LIVAGGGVIY SEASGQLDRF ARETGIPVAD TQAGKGALSW DHPNAVGGLG ATGSPVANRL
     AGHADVVLGV GTRYSDFTTA SRTAFRHPQV RFVNLNVASF DAGKLSALPL VADARAGLAA
     LRPALHGRRF TGDFHDDVAA WNATVDRAYR KRSGELPTQA EVIGVVNDAC GARDVVVQAA
     GSLPGDLQRL WRAGDPKQYH VEYGYSCMGF EIAGALGIKL ADPSREVYAL VGDGSYLMMA
     QEIVTAIAEG VKLIVVVVQN HGFASIGALS EQVGSQRFGT SYRFKNAQTG DYDGPLLPVD
     LALNAESLGA AVIRCRTAAD LAEGLKRARE ADHLTVVHVE TDPLATGPGS DSWWDVPVAE
     VATLHSTRHA RAGYLEGKRD QRHHLRPGGQ A
//
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