ID A0A316W886_9BASI Unreviewed; 693 AA.
AC A0A316W886;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=Putative PDC1-pyruvate decarboxylase, isozyme 1 {ECO:0000313|EMBL:PWN43885.1};
GN ORFNames=IE81DRAFT_322056 {ECO:0000313|EMBL:PWN43885.1};
OS Ceraceosorus guamensis.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Exobasidiomycetes; Ceraceosorales; Ceraceosoraceae; Ceraceosorus.
OX NCBI_TaxID=1522189 {ECO:0000313|EMBL:PWN43885.1, ECO:0000313|Proteomes:UP000245783};
RN [1] {ECO:0000313|EMBL:PWN43885.1, ECO:0000313|Proteomes:UP000245783}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 4658 {ECO:0000313|EMBL:PWN43885.1,
RC ECO:0000313|Proteomes:UP000245783};
RX PubMed=29771364; DOI=10.1093/molbev/msy072;
RA Kijpornyongpan T., Mondo S.J., Barry K., Sandor L., Lee J., Lipzen A.,
RA Pangilinan J., LaButti K., Hainaut M., Henrissat B., Grigoriev I.V.,
RA Spatafora J.W., Aime M.C.;
RT "Broad genomic sampling reveals a smut pathogenic ancestry of the fungal
RT clade Ustilaginomycotina.";
RL Mol. Biol. Evol. 0:0-0(2018).
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}.
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DR EMBL; KZ819366; PWN43885.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A316W886; -.
DR STRING; 1522189.A0A316W886; -.
DR InParanoid; A0A316W886; -.
DR OrthoDB; 1000728at2759; -.
DR Proteomes; UP000245783; 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; 2.
DR SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 3.
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 Pyruvate {ECO:0000313|EMBL:PWN43885.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000245783};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 20..79
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 141..190
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 297..422
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 513..595
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT REGION 91..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..130
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 693 AA; 75138 MW; E960492D58C21128 CRC64;
MSSATPAKSK HDDAASSTLT LADYILERLS SLGCSSIQGV PGDFSMPFLD AVSQHASFEW
VGNTNELNAA YSADGYARCA QIESRCSDEG QAAALGGGGG VEQEEEEENV SKLRAPTWTS
SEQSGSGGGR KKSPNRRPRG SKIAALCTTF GVGELSALNG IAGSYAERLP VLHIVGVPST
QAQSNKALLH HTLGDGDFAA FSQMSKHVSC AVVHLGELLV GEGQIEEEGD EESSSRGKML
AKEVDALLAR VVREARPGYL ALPTDLVHLP IPTSLLRAPL HTSHAPNEES VEAEVLREIF
KRLDESRNPL IIVDACTIRH AAINATLDLV HRSGCTFVST PMGKSALPES SPQYAGTFIG
PNSEPALLQR VQKSDCYLFV GALRSDFNTA SSFNSLTDQA KTIELHSNRT VLGHAVYPGI
SMHALLPRLA DHLSARANEL RGLYGLSEQE RPSNRLPTKL QEGEMAGQEG ENISQMWLWK
RIGSFLKEAD QVVAETGTSS FGILDTHLPG GRTRLHSQVL WGSIGWSLPA TLGVSLAARE
LHLGRTLLFI GDGSLQLTAT EISTMIRLDL HPILFVLRND GYEIERQIEG PDQAYNNVPS
WNNEKLLQAL YDPSVRQSMG GKEKEAQRSH AHDKEVPVPR YFAVKSKKEL DDLLKDEEFA
SCKRLQLVEI FMRRGDAPRA LVAQAQASAK LNS
//
