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Database: UniProt
Entry: W6N5M2_CLOTY
LinkDB: W6N5M2_CLOTY
Original site: W6N5M2_CLOTY 
ID   W6N5M2_CLOTY            Unreviewed;       645 AA.
AC   W6N5M2;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=Epi-inositol hydrolase {ECO:0000313|EMBL:CDL90559.1};
DE            EC=3.7.1.- {ECO:0000313|EMBL:CDL90559.1};
GN   ORFNames=CTDIVETGP_0629 {ECO:0000313|EMBL:CDL90559.1};
OS   Clostridium tyrobutyricum DIVETGP.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1408889 {ECO:0000313|EMBL:CDL90559.1, ECO:0000313|Proteomes:UP000019482};
RN   [1] {ECO:0000313|EMBL:CDL90559.1, ECO:0000313|Proteomes:UP000019482}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DIVETGP {ECO:0000313|EMBL:CDL90559.1,
RC   ECO:0000313|Proteomes:UP000019482};
RA   Soggiu A., Piras C., Gaiarsa S., Sassera D., Roncada P., Bendixen E.,
RA   Brasca M., Bonizzi L.;
RT   "Draft Genome Sequence of Clostridium tyrobutyricum Strain DIVETGP,
RT   Isolated from Cow's Milk for Grana Padano Production.";
RL   Genome Announc. 3:213-215(2015).
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:CDL90559.1}.
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DR   EMBL; CBXI010000008; CDL90559.1; -; Genomic_DNA.
DR   AlphaFoldDB; W6N5M2; -.
DR   OrthoDB; 4494979at2; -.
DR   Proteomes; UP000019482; 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:CDL90559.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019482};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          6..133
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          219..350
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          441..599
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   645 AA;  71121 MW;  4A2678D4003B9891 CRC64;
     MNRVKMTVGQ AIVKFLNNQY IEFDGVENQF IDGIFTIFGH GMVAGLGQAL EEDPGHLRVY
     QGRNEQGMAH AAMSYAKQNN RRRIIACTSS IGPGAANMVT AALTASINNI PLLLFPSDTF
     STRQPDPVLQ QIEQPYNLSI TTNDCFKPVT RYWDRVARPE HLMTALINAM RVLTDVSNTG
     AVCIGIPQDV QGESFDFPEY FFKKRVHHIA RRKADDREIE NAVDLIMVSK KPLFIGGGGV
     RYSEAGETLQ SFCEEFGIPY AETQAGKSST KSSSPMNLGG VGITGTLAAN TAAEMADLVV
     GVGTRFNDFV TGSKEIFRNP DVRFVTINTS EFHAEKMDAE RVVGDAKLNL EIIVKELHSK
     KYKPAYKEDE IAKIQSVWEK ERQSVCNVVY TGKDFVPCVP SWTPEIINDY IRDIGGTITE
     SNGVGIVRDV IDDDAIVVAA AGSLPADLER LWTTDVKDSY NMEYGASCMG YEIAGALGSK
     LAEPDREVYA LVGDGSFLML NSEITTAVQE NAKITIIVFD NAAFGCINNL QMGNGIGSMC
     TEFRYRNEKS GRTDGNYIYV DFAKVGEGYG LKGYVAKTPE ELRAALEDSK KQTRSCIIDA
     KVLPKTMAEG YKSWWHIGVA SVSKSEVTQA SYKSRLERLK KARIY
//
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