ID   A0A010S6U8_9PEZI        Unreviewed;       689 AA.
AC   A0A010S6U8;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   SubName: Full=Thiamine pyrophosphate enzyme {ECO:0000313|EMBL:EXF86494.1};
GN   ORFNames=CFIO01_10712 {ECO:0000313|EMBL:EXF86494.1};
OS   Colletotrichum fioriniae PJ7.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum acutatum species complex.
OX   NCBI_TaxID=1445577 {ECO:0000313|EMBL:EXF86494.1, ECO:0000313|Proteomes:UP000020467};
RN   [1] {ECO:0000313|EMBL:EXF86494.1, ECO:0000313|Proteomes:UP000020467}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PJ7 {ECO:0000313|EMBL:EXF86494.1,
RC   ECO:0000313|Proteomes:UP000020467};
RA   Baroncelli R., Thon M.R.;
RT   "The genome sequence of Colletotrichum fioriniae PJ7.";
RL   Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
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:EXF86494.1}.
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DR   EMBL; JARH01000010; EXF86494.1; -; Genomic_DNA.
DR   RefSeq; XP_007589840.1; XM_007589778.1.
DR   AlphaFoldDB; A0A010S6U8; -.
DR   STRING; 1445577.A0A010S6U8; -.
DR   KEGG; cfj:CFIO01_10712; -.
DR   eggNOG; KOG1184; Eukaryota.
DR   HOGENOM; CLU_013748_4_0_1; -.
DR   OrthoDB; 2291769at2759; -.
DR   Proteomes; UP000020467; Unassembled WGS sequence.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0004737; F:pyruvate decarboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   CDD; cd02002; TPP_BFDC; 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; 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   PANTHER; PTHR18968:SF164; PYRUVATE DECARBOXYLASE; 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   Reference proteome {ECO:0000313|Proteomes:UP000020467};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          108..239
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          311..417
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          517..683
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
FT   REGION          54..78
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        57..75
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   689 AA;  74072 MW;  F1B69611D03BE3F9 CRC64;
     MPFRQLPVPM ARCLRSFGPA GGRPGKLVRF KQTLAPSIAV VGGPARQLAG FSSAAPLHRS
     GGSTSPSSSH VGAGIKPTTS RPLVEDEFKA TIEQARNLSS KSTEMYTASF AFFEALWDAG
     VTHCFVNLGS DHPSIIEAMV KGQRERKGNF PRIITCPNEM VAMSMADGYA RLTGKPQCVI
     VHVDVGTQGL GAAVHNSSCG RAPVLVFAGL SPFTIEGEMR GSRTEYIHWI QDVPDQKQIV
     SQYCRYSGEL KTATNVKQMV NRALQFSKSD PQGPVYLCGA REVMEAEVEP YSIRQEDWDP
     VELGGLPKNA VNKIAEALAG AKEPLIVTGF GGRDHQFPGA LVELANTVKG LRVVDTGGSD
     MCFPADHPGW LGLRFGIEDA VNTADVIVVL DCDVPWINTL CHPKKDAKIF HIDVDPLKQQ
     MPVFYIAAQS RYRASSLLSI EQITAHLKGQ YAAQLESAEA KERGEKVKES HKQLLAKIEE
     KARPKADGEF GTGHLTRSLK KLCPEDTIWA IEAVTNTIFV HDNLQPTLPG SWINCGGGGL
     GWSGGGALGI KLATDFENGG NNKGKFVVQI VGDGTFLFSV PGSVYWIAKR YNIPILTIIL
     NNKGWNAPRR SLLLVHPDGE GSRATNEEIN ISFDPAPDYA GIAKAAAGGD LFAARVDNAA
     DLDGVLKKAI ETVQGGQPAV LDIKVALGS
//