ID E7N669_9ACTO Unreviewed; 635 AA.
AC E7N669;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=3D-(3,5/4)-trihydroxycyclohexane-1,2-dione acylhydrolase (Decyclizing) {ECO:0000313|EMBL:QCT32675.1};
DE EC=3.7.1.22 {ECO:0000313|EMBL:QCT32675.1};
DE SubName: Full=Thiamine pyrophosphate enzyme, central domain protein {ECO:0000313|EMBL:EFW28311.1};
GN Name=iolD {ECO:0000313|EMBL:QCT32675.1};
GN ORFNames=FBF36_03640 {ECO:0000313|EMBL:QCT32675.1}, HMPREF9057_00269
GN {ECO:0000313|EMBL:EFW28311.1};
OS Actinomyces sp. oral taxon 171 str. F0337.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Actinomyces.
OX NCBI_TaxID=706439 {ECO:0000313|EMBL:EFW28311.1, ECO:0000313|Proteomes:UP000005722};
RN [1] {ECO:0000313|EMBL:EFW28311.1, ECO:0000313|Proteomes:UP000005722}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0337 {ECO:0000313|EMBL:EFW28311.1,
RC ECO:0000313|Proteomes:UP000005722};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:QCT32675.1, ECO:0000313|Proteomes:UP000310751}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0337 {ECO:0000313|EMBL:QCT32675.1,
RC ECO:0000313|Proteomes:UP000310751};
RA Collins A.J., Murugkar P., Chen T., Dewhirst F.E.;
RT "Saccharibacteria TM7 and host bacteria genomes.";
RL Submitted (APR-2019) 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; AECW01000031; EFW28311.1; -; Genomic_DNA.
DR EMBL; CP040005; QCT32675.1; -; Genomic_DNA.
DR RefSeq; WP_009393465.1; NZ_GL637702.1.
DR AlphaFoldDB; E7N669; -.
DR eggNOG; COG3962; Bacteria.
DR HOGENOM; CLU_013748_6_0_11; -.
DR Proteomes; UP000005722; Unassembled WGS sequence.
DR Proteomes; UP000310751; Chromosome.
DR GO; GO:0102481; F:3D-(3,5/4)-trihydroxycyclohexane-1,2-dione hydrolase activity; IEA:UniProtKB-EC.
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; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000313|EMBL:QCT32675.1};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 40..147
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 232..366
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 429..589
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT COILED 349..376
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 635 AA; 69186 MW; B561D157EFEECCFE CRC64;
MSNEAYAGTI RLTVAQATIR FLSNQYSERD GVEQRLIAGA FGIFGHGNVA GIGQALLQNE
IARADGEQEM PYIMPRNEQG QVHAAAAFAK TTNRLQTYMC TASIGPGSLN MVTGAALATT
NRLPVLLLPS DQFATRVPDP VLQQLEDPTS LDVSVNDAFR PVSRFFDRIN RPEQLIPSLL
NAMRVLTDPA ETGAVTIAMP QDVQAEVFDW PVELFRKRVW HVRRPVPEPA ALERAVALIK
AAKRPLIIAG GGTIYAGASE ELRALATATG IPVGDTQAGK GAINFDHPSA VGGVGSTGCD
SGNHIADKAD LIIGVGTRYS DFTTASKTQF KNPNVTFVNI NVTPFDAAKE SAEMVVADAR
EALAALREAL ADYRVETAYS EEITAEKEAW LKATERCYHL DHGPLPAQTE VFGALNELMG
EEDVVINAAG SMPGDLQALW QARSPLQYHV EYAFSCMGYE VPAAMGVKLA RPEVEVVSIV
GDGTYQMLPM ELATVVQENI KVIYVLLQNY GFCSIGALSE SRGSQRFGTK YRRRGEGSHL
ADEQVIDGVD IAANARSWGL DVLEVHTIAE FKEAYRKAEA SDRPTMIHIE TDLYGPNPPG
SSWWDVPVSG VSELESTQRA YEEYLRDRKP QRHYL
//
