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
//