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
//