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Database: UniProt
Entry: S3D3P0_GLAL2
LinkDB: S3D3P0_GLAL2
Original site: S3D3P0_GLAL2 
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
//
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