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Database: UniProt
Entry: D4N122_ANAHA
LinkDB: D4N122_ANAHA
Original site: D4N122_ANAHA 
ID   D4N122_ANAHA            Unreviewed;       642 AA.
AC   D4N122;
DT   18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT   18-MAY-2010, sequence version 1.
DT   24-JAN-2024, entry version 54.
DE   SubName: Full=3D-(3,5/4)-trihydroxycyclohexane-1,2-dione hydrolase {ECO:0000313|EMBL:CBL38567.1};
DE            EC=3.7.1.- {ECO:0000313|EMBL:CBL38567.1};
GN   ORFNames=CL2_16390 {ECO:0000313|EMBL:CBL38567.1};
OS   Anaerostipes hadrus.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Anaerostipes.
OX   NCBI_TaxID=649756 {ECO:0000313|EMBL:CBL38567.1, ECO:0000313|Proteomes:UP000008960};
RN   [1] {ECO:0000313|EMBL:CBL38567.1, ECO:0000313|Proteomes:UP000008960}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SSC/2 {ECO:0000313|EMBL:CBL38567.1,
RC   ECO:0000313|Proteomes:UP000008960};
RG   metaHIT consortium -- http://www.metahit.eu/;
RA   Pajon A., Turner K., Parkhill J., Duncan S., Flint H.;
RT   "The genome sequence of Clostridiales sp. SSC/2.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBL38567.1, ECO:0000313|Proteomes:UP000008960}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SSC/2 {ECO:0000313|EMBL:CBL38567.1,
RC   ECO:0000313|Proteomes:UP000008960};
RA   Pajon A.;
RL   Submitted (MAR-2010) 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; FP929061; CBL38567.1; -; Genomic_DNA.
DR   RefSeq; WP_008392046.1; NZ_WQRB01000032.1.
DR   AlphaFoldDB; D4N122; -.
DR   GeneID; 15231658; -.
DR   KEGG; bprl:CL2_16390; -.
DR   PATRIC; fig|245018.3.peg.1935; -.
DR   OMA; PNTYHLE; -.
DR   Proteomes; UP000008960; 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; 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:CBL38567.1};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          7..136
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          220..354
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          441..596
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   642 AA;  70513 MW;  EEC1CB419EAF691B CRC64;
     MAKTVRMTVA QAIVKFLDNQ YVSMDGEETK FVEGFFTIFG HGIAVGLGEA LDTNPGNLRV
     LQGRNEQGMC HVATAYAKQN GRKKIIPCAS SVGPGAANMV TACATATVNN IPLLVFPADT
     FASRQPDPVL QQLEQSNSLS TTTNDAFKPV CKYWDRVTRP EHIMTALINA MRVLTDPAET
     GACCIGLCQD VEGESFDFPE YFFEKRVHRI TRPVAVEEEI EDIANVIANA KKPLVIVGGG
     VRYSEAGEEV EKFCEEFKIP FGETQGGKSA CRSSHPYCMG GIGVTGTYAS NVLAKDADVV
     IAIGSRMSDF ATGSKRQFAN PDVKFVSINN SRYHAYKLDS VKAVGDAKVT VKALAEKLRA
     MNYVSSYNGE IEEAKAVWDK EMKRLAEYKY DETFEPMIKN MDPRTIPEFV ELTKGKITQT
     AALATIRDVI DEDATIITAG GSLPSCMQRV WTTDKRGGYH AEYGYSCMGY EVAAALGVKL
     AEPDNEVYAV VGDASFQMLH SEIMTMMQEK QKANILVFDN CGFGCINNLQ MNHGIGSLAT
     EFRYREGNKP CGDLIPVDYA KVAEGYGLKS YTCKTIEELR AALEDAKKQN VACLFDLKVI
     PKTMTDGYES WWNVGIATTS EKESVRKACE GVMEGRKEAR AY
//
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