ID A0A0Q9K2N1_9MICO Unreviewed; 642 AA.
AC A0A0Q9K2N1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=3D-(3,5/4)-trihydroxycyclohexane-1,2-dione acylhydrolase (Decyclizing) {ECO:0000313|EMBL:KRE31426.1};
GN ORFNames=ASG80_03000 {ECO:0000313|EMBL:KRE31426.1};
OS Agromyces sp. Soil535.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Agromyces.
OX NCBI_TaxID=1736390 {ECO:0000313|EMBL:KRE31426.1, ECO:0000313|Proteomes:UP000051793};
RN [1] {ECO:0000313|Proteomes:UP000051793}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil535 {ECO:0000313|Proteomes:UP000051793};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRE31426.1, ECO:0000313|Proteomes:UP000051793}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil535 {ECO:0000313|EMBL:KRE31426.1,
RC ECO:0000313|Proteomes:UP000051793};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRE31426.1}.
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DR EMBL; LMRW01000001; KRE31426.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0Q9K2N1; -.
DR STRING; 1736390.ASG80_03000; -.
DR OrthoDB; 3194735at2; -.
DR Proteomes; UP000051793; 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; 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:KRE31426.1};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 7..137
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 225..359
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 422..590
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 642 AA; 68770 MW; B5B5C8D7A667851C CRC64;
MAATRRMTVS QALIEFLARQ WTVDGDIRER TIPGVFGIFG HGNVAGVGQA LKQLNVDQPE
LMPYFQARNE QAMVHQSVGY ARMHRRRATF ASAASVGPGA TNMLTGAALA TTNRLPALLL
PSDTFATRVA DPVLQQLEQP WDIGLTVNDA FRPLSKFFDR VQRPEQLYSI ALGAMRVLTD
PVETGAVTIA LPEDVQAETL DVPIEFLQDR EWHLRRPLPE HGALARAVAT IRGAERPFIV
AGGGVLYSGA EDQLRALVGA TGIPVGTTQA GGGSLPWDHP QYLGAVGATG TTAANRLAAE
ADVVIGIGTR YSDFTTASRT AFRDPSVRFV NINVAAFDAY KHGTQLPVVA DARETLVALA
AELAGHRVAA GYSERIAHEK SEWDAAVDVA FAPSGRALPG QPEIIGAVQS ATAPEDVIVQ
AAGSLPGDLH QLWRVRDPLG YHVEYAYSCM GYEIAGGLGV KRGLTAAGDE RDVIVMVGDG
SYLMLSSELA TVVAEGIKLI VILIQNHGFA SIGHLSETVG SERFGTKYRV YDAEARNFQG
DRVLPVDLAM NARSYGIDVI EITPGSDAIA DLAAAVAAAK ASDRATFIHV HSDPLVYGPD
GEGWWDVPVS EVSTLESTQR ARAEYERLRQ AQRPLLGAED AR
//