ID S3D3P0_GLAL2 Unreviewed; 583 AA.
AC S3D3P0;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=Pyruvate decarboxylase {ECO:0000256|ARBA:ARBA00014422};
DE EC=4.1.1.1 {ECO:0000256|ARBA:ARBA00013202};
GN ORFNames=GLAREA_06109 {ECO:0000313|EMBL:EPE33097.1};
OS Glarea lozoyensis (strain ATCC 20868 / MF5171).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Helotiaceae; Glarea.
OX NCBI_TaxID=1116229 {ECO:0000313|EMBL:EPE33097.1, ECO:0000313|Proteomes:UP000016922};
RN [1] {ECO:0000313|EMBL:EPE33097.1, ECO:0000313|Proteomes:UP000016922}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 20868 / MF5171 {ECO:0000313|Proteomes:UP000016922};
RX PubMed=23688303; DOI=10.1186/1471-2164-14-339;
RA Chen L., Yue Q., Zhang X., Xiang M., Wang C., Li S., Che Y.,
RA Ortiz-Lopez F.J., Bills G.F., Liu X., An Z.;
RT "Genomics-driven discovery of the pneumocandin biosynthetic gene cluster in
RT the fungus Glarea lozoyensis.";
RL BMC Genomics 14:339-339(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2-oxocarboxylate + H(+) = an aldehyde + CO2;
CC Xref=Rhea:RHEA:11628, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:17478, ChEBI:CHEBI:35179; EC=4.1.1.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001041};
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; KE145358; EPE33097.1; -; Genomic_DNA.
DR RefSeq; XP_008079714.1; XM_008081523.1.
DR AlphaFoldDB; S3D3P0; -.
DR STRING; 1116229.S3D3P0; -.
DR GeneID; 19465163; -.
DR KEGG; glz:GLAREA_06109; -.
DR eggNOG; KOG1185; Eukaryota.
DR HOGENOM; CLU_013748_4_0_1; -.
DR OrthoDB; 2291769at2759; -.
DR Proteomes; UP000016922; 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; 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:UP000016922};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 4..135
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 207..311
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 412..568
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 583 AA; 62843 MW; 17B7F67B7B7579AC CRC64;
MYTASFAFFE ALWEAGVTHC FVNLGSDHPS IIEAMVKGQN EKKGEFPRII TCPNEMVALS
MADGFARLTR RPQCVIIHVD VGTQGLGAAV HNASCGRAPV LIFAGLSPYT IEGEHRGSRT
EYIHWIQDVP DQKQIVAQYC RYVGEIKSGK NVKQMVNRAL QFATSEPAGP VYLCGAREVM
EMDLEPYTLQ QEHWGAVEAG ALSEGGVKRV AEALMAANEP LVITGYSGRN HDAVGALVKL
ADMVKGLRVL DTGGSDMCFP ANHPAWLGLR YGVDESIKSA DMILVLDCDV PWINTQNHPS
TACEIYHIDT DVLKRQMPVH YIAALARYTA DAFTSLTQLT DYISASQNYT KKVSTYDVRW
EALQTSYALR LENIVAAAKP KEGKFGTGYL CSTLRKMCPQ DTIWAIEAVT NSFFVADNLQ
CSVPGSWINC GGGGLGWSGG GALGIKLGSS YYSNPKDGGK FVVQIVGDGT YLFSVPSSVY
WISQRYSIPI LTIVLNNKGW NAPKKSLLLV HPEGLGSKAT NAELNIEIAG PDFGGIAKAA
AGGNCYTGKV SEVDELEKVL GEAIKSVQGG ITAVVEAVVA SGC
//