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Database: UniProt
Entry: A0A0Q9K5F2_9BACL
LinkDB: A0A0Q9K5F2_9BACL
Original site: A0A0Q9K5F2_9BACL 
ID   A0A0Q9K5F2_9BACL        Unreviewed;       621 AA.
AC   A0A0Q9K5F2;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=3D-(3,5/4)-trihydroxycyclohexane-1,2-dione acylhydrolase (Decyclizing) {ECO:0000313|EMBL:KRE35269.1};
GN   ORFNames=ASG81_22135 {ECO:0000313|EMBL:KRE35269.1};
OS   Paenibacillus sp. Soil522.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1736388 {ECO:0000313|EMBL:KRE35269.1, ECO:0000313|Proteomes:UP000051180};
RN   [1] {ECO:0000313|Proteomes:UP000051180}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Soil522 {ECO:0000313|Proteomes:UP000051180};
RA   Garrido-Oter R., Bai Y.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRE35269.1, ECO:0000313|Proteomes:UP000051180}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Soil522 {ECO:0000313|EMBL:KRE35269.1,
RC   ECO:0000313|Proteomes:UP000051180};
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:KRE35269.1}.
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DR   EMBL; LMRV01000066; KRE35269.1; -; Genomic_DNA.
DR   RefSeq; WP_056639322.1; NZ_LMRV01000066.1.
DR   AlphaFoldDB; A0A0Q9K5F2; -.
DR   STRING; 1736388.ASG81_22135; -.
DR   OrthoDB; 4494979at2; -.
DR   Proteomes; UP000051180; 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:KRE35269.1};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          7..131
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          219..353
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          417..576
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   621 AA;  67088 MW;  CFEEEA92BC784498 CRC64;
     MDKIRLTMAQ ALLRFLDNQY VSVDGVETKF VQGLMGIFGH GNVTGIGEAL ERSPGSLTFI
     QGKNEQGMVH AATAFAKQKN RLQIYACTSS IGPGALNMIT AAATATVNRI PVLLLPGDHF
     ASRQPDPVLQ QLEVVSDYTI SAVDAFKPVS KYWDRIVRPE QLMQAAIQAM RVLTDPAETG
     AVTLALPQDV QAEAYDYPVS FFEKKVHFID RRLPAPASLQ RAVELIKKKR RPLIIAGGGV
     LYSSAMKELA AFAEAFGIPV AETQAGKSSL PWNHPLNAGA IGVTGTLAAN RLAADADLII
     GIGTRYSDFT TSSKSAFRNE AVQFVNLNVS AFDSSKLDAF SVTCDAKAGL QALQQSLNAA
     NYRTGYEPAE IAGLKEQWDA EVDRLYAAEH KDGLAQTRAL GVINETLGES DIILCAAGSL
     PGDLHRVWRS VEPKTYHMEY GFSCMGYEIS GAFGAALAEP DKNVYAILGD GSYLMLHSEL
     ITSIQEGRKI TVLLLDNHGY QCIHNLQRGH GSDGFGNEFR FRSGTTGRLT GGYMPIDFSA
     HASSMGAATY KASTAEELRD ALLKARNETG TTLIEIPVVP GTNTGGYESW WNVGVPEVSV
     SEKVVAAHED MKRNIDAVLF I
//
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