ID A0A344L8L8_9PSEU Unreviewed; 607 AA.
AC A0A344L8L8;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=3D-(3,5/4)-trihydroxycyclohexane-1,2-dione acylhydrolase (Decyclizing) {ECO:0000313|EMBL:AXB44392.1};
GN ORFNames=A4R43_19250 {ECO:0000313|EMBL:AXB44392.1};
OS Amycolatopsis albispora.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Amycolatopsis.
OX NCBI_TaxID=1804986 {ECO:0000313|EMBL:AXB44392.1, ECO:0000313|Proteomes:UP000250434};
RN [1] {ECO:0000313|EMBL:AXB44392.1, ECO:0000313|Proteomes:UP000250434}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WP1 {ECO:0000313|EMBL:AXB44392.1,
RC ECO:0000313|Proteomes:UP000250434};
RA Wang H., Chen S., Wu Q.;
RT "Complete genome sequence and analysis of deep-sea sediment isolate,
RT Amycolatopsis sp. WP1.";
RL Submitted (APR-2016) 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; CP015163; AXB44392.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A344L8L8; -.
DR KEGG; aab:A4R43_19250; -.
DR OrthoDB; 3194735at2; -.
DR Proteomes; UP000250434; 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; 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; 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.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:AXB44392.1};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 4..129
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 218..350
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 431..567
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 607 AA; 64193 MW; 328C18CD5BCD7869 CRC64;
MKLTTSEALV RWLLAQRSET LAGDEVPLFP GVFAIFGHGN VLGIGTALSR YRDELPVWRG
HTEQGMALAA TGFAKAADRR QVGVVTSSIG PGALNMVTAA GVAHANRLPL LLLPGDTFVS
RAPDPVLQQI EPFGDATATV NDAFRAVSRY FDRITRPEQL ISTLPQVARV LTDPAEAGPV
TLALPQDVQA ETFDFPDSLF EPVVHRVRRI RPDTRELAAA AAALRASDRP LLVLGGGVRY
SGAGARALDF ASRYGIPVVE TTAGRTLVPH DHPLYGGPLG VTGSSSANAL AAEADLVFAV
GTRLQDFTTA SWTVFGPGVK LVTLNAARFD AVKHGALAVV GDAEAGLSEL DLGDWRVSSS
WSGRAASERA RWDAHVSSLR SASGEPTYAQ VVGVVNDLSS PDDYVMTASG GLPGELIGGW
RGSGQVSMDV EYGFSCMGYE LAGAWGAAMA LPDRVVTTLL GDGSYLMLNS ELFSAAFAGH
PFVAVVCDND GYAVIARLQE GQGGEPFNNQ YADCRTSHAD PPRVDFAGHA EALGCLVFRA
SSVSELRSAY ARAREASVSS RRPAVVVIRT RPDAWTESGA WWEVGVPESL AGREGYEAGK
AAQIRYA
//
