ID A0A066WEM3_TILAU Unreviewed; 663 AA.
AC A0A066WEM3;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Thiamin diphosphate-binding protein {ECO:0000313|EMBL:KDN52367.1};
GN ORFNames=K437DRAFT_277635 {ECO:0000313|EMBL:KDN52367.1};
OS Tilletiaria anomala (strain ATCC 24038 / CBS 436.72 / UBC 951).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Exobasidiomycetes; Georgefischeriales; Tilletiariaceae; Tilletiaria.
OX NCBI_TaxID=1037660 {ECO:0000313|EMBL:KDN52367.1, ECO:0000313|Proteomes:UP000027361};
RN [1] {ECO:0000313|EMBL:KDN52367.1, ECO:0000313|Proteomes:UP000027361}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UBC 951 {ECO:0000313|EMBL:KDN52367.1,
RC ECO:0000313|Proteomes:UP000027361};
RG DOE Joint Genome Institute;
RA Toome M., Kuo A., Henrissat B., Lipzen A., Tritt A., Yoshinaga Y., Zane M.,
RA Barry K., Grigoriev I.V., Spatafora J.W., Aimea M.C.;
RT "Draft genome sequence of a rare smut relative, Tilletiaria anomala UBC
RT 951.";
RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
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:KDN52367.1}.
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DR EMBL; JMSN01000011; KDN52367.1; -; Genomic_DNA.
DR RefSeq; XP_013245212.1; XM_013389758.1.
DR AlphaFoldDB; A0A066WEM3; -.
DR STRING; 1037660.A0A066WEM3; -.
DR GeneID; 25266827; -.
DR HOGENOM; CLU_013748_0_2_1; -.
DR InParanoid; A0A066WEM3; -.
DR OMA; GPEQRYN; -.
DR OrthoDB; 1000728at2759; -.
DR Proteomes; UP000027361; Unassembled WGS sequence.
DR GO; GO:0016831; F:carboxy-lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR CDD; cd02005; TPP_PDC_IPDC; 1.
DR CDD; cd07038; TPP_PYR_PDC_IPDC_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; IPR012110; PDC/IPDC-like.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR InterPro; IPR047214; TPP_PDC_IPDC.
DR InterPro; IPR047213; TPP_PYR_PDC_IPDC-like.
DR PANTHER; PTHR43452; PYRUVATE DECARBOXYLASE; 1.
DR PANTHER; PTHR43452:SF30; PYRUVATE DECARBOXYLASE ISOZYME 1-RELATED; 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 Decarboxylase {ECO:0000256|ARBA:ARBA00022793};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000027361};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 14..134
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 251..361
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 473..579
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT REGION 589..609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 663 AA; 72463 MW; 8D0BE1F93D929B44 CRC64;
MSSSAGTRNS ILLSEYLLSR LEQLNVPVIQ GVPGDYSLGL LSQFLDHHAK SGSKQNHGIN
GKAPEWIGNA NELNATYSAD GLARVLGPQR PSVVVTTMGV GELSAANGIA GCYSERIPVI
HIVGTPTSSA QEHGLLLHHT LGDHKFVAFG QIARQITAAQ LDFALLKREG RMQLMEKDSE
GTGEDAAREL DRILEVCVRQ ALPVYIALPS DLVHFPLPAS CKHRLTEQSL QTGFSPNKAD
SEAYVLRVIT DKVTNAKCPV ILVDACTLRH NVVKETRALV ASSGLPIFTT PMGKTAVDES
DANPQYGGVY IGSISSPEVK EVIEEKADLI IAIGTLQSDF NTGNFSYRTR RESTIELHSD
RICVAFATYE GVRMKGLLPK LTDALKKHGR QRLEKTEELL RVARRIPTFN NKLPTPQEEL
STFTHEQIGA MGGSQSVTSS IISQAYLWPR VGQFLRPGDR VIGETGTSAF GLMEVRFPRD
AQFLAQVLWG SIGWSCPATL GVSLGMRELT KQGDAAAKQG RTILFIGDGS LQLTLQEIGT
MIRQGLTPLI FVLNNDGYEI ERQIHGAEAS YNDIQPYNHS LLLDLLRPPP NYRRPTNPSH
ASDPEMSKTA YHATHTKAEL HALLKDEEFN KADKCTLVEV FMPRGDAPAA LRRQAEMSSS
TNA
//
