ID F3Z7A8_9ACTN Unreviewed; 608 AA.
AC F3Z7A8;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=Putative IolD protein {ECO:0000313|EMBL:EGJ77263.1};
GN ORFNames=STTU_4474 {ECO:0000313|EMBL:EGJ77263.1};
OS Streptomyces sp. Tu6071.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=355249 {ECO:0000313|EMBL:EGJ77263.1};
RN [1] {ECO:0000313|EMBL:EGJ77263.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Tu6071 {ECO:0000313|EMBL:EGJ77263.1};
RA Erxleben A., Wunsch-Palasis J., Gruening B.A., Luzhetska M., Bechthold A.,
RA Gunther S.;
RT "Genome sequence of Streptomyces sp. Tu6071.";
RL Submitted (APR-2011) 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; CM001165; EGJ77263.1; -; Genomic_DNA.
DR AlphaFoldDB; F3Z7A8; -.
DR HOGENOM; CLU_013748_6_0_11; -.
DR Proteomes; UP000003955; 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; 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 Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 31..105
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 194..334
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 401..558
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT REGION 587..608
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 589..608
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 608 AA; 64707 MW; 99D10463EEAE23C6 CRC64;
MQGLWGIFGH GNVAGFGQAV VEYGAVDGPY AMPFHQGRNE QAMVHAASGF ARHRRRLATH
AVTTSIGPGA TNLVTGAALA TVNRLPVLLL PGDYFATHPA DPVLQQLEHP VSSDITVNDA
LRPVSRYFAR VHRPEALIPA ALEALRVLTD PAETGAVTLA LPQDVQAEAY DWPEEFLAER
TWHIRRPPPD PAALDEAVAA IRAARRPLLV AGGGVRYSAA EDALRALADA TGIPVASTQA
GKGALRHDHP ADVGGIGHTG TATADELARA ADLVLGVGTR WSDFTTASAT LFEGGARTGG
DGVRFVNLNI TSFDGHKQGA IPLVADARAG LEALTERLAG WRVDEAEVAQ YTLDKALWEE
RVEGYTQPDD GVADLVRPNQ AHVVGALQAV VGDEDVVINA AGSLPGDLHK LWRTRGPLQY
HVEYGYSCMG YEIPAALGVC LAQPGVPVWA LVGDGTYLML PGELVTAVQE NLPLTLVILQ
NHGYASIGGL SRAVGADGFA TAYRYRTADG AYNGAPLPVD LAANAASLGL RVLRARTVRE
VREALAEARE ADRPTCVYVE TETTDTVSGA PPAQAWWDVP VAETTTHPST VRARKEYERH
SAERRRHL
//
