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Database: UniProt
Entry: A0A0G4EFN9_VITBC
LinkDB: A0A0G4EFN9_VITBC
Original site: A0A0G4EFN9_VITBC 
ID   A0A0G4EFN9_VITBC        Unreviewed;       573 AA.
AC   A0A0G4EFN9;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=Pyruvate decarboxylase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=Vbra_3752 {ECO:0000313|EMBL:CEL94316.1};
OS   Vitrella brassicaformis (strain CCMP3155).
OC   Eukaryota; Sar; Alveolata; Colpodellida; Vitrellaceae; Vitrella.
OX   NCBI_TaxID=1169540 {ECO:0000313|EMBL:CEL94316.1, ECO:0000313|Proteomes:UP000041254};
RN   [1] {ECO:0000313|EMBL:CEL94316.1, ECO:0000313|Proteomes:UP000041254}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Zhu J., Qi W., Song R.;
RL   Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|PIRSR:PIRSR036565-2};
CC       Note=Binds 1 Mg(2+) per subunit. {ECO:0000256|PIRSR:PIRSR036565-2};
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; CDMY01000214; CEL94316.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G4EFN9; -.
DR   STRING; 1169540.A0A0G4EFN9; -.
DR   VEuPathDB; CryptoDB:Vbra_3752; -.
DR   InParanoid; A0A0G4EFN9; -.
DR   OMA; EQRYNDI; -.
DR   OrthoDB; 1000728at2759; -.
DR   PhylomeDB; A0A0G4EFN9; -.
DR   Proteomes; UP000041254; 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; IPR000399; TPP-bd_CS.
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   PIRSF; PIRSF036565; Pyruvt_ip_decrb; 1.
DR   SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR   PROSITE; PS00187; TPP_ENZYMES; 1.
PE   3: Inferred from homology;
KW   Decarboxylase {ECO:0000256|ARBA:ARBA00022793};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR036565-2};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR036565-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000041254};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW   ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          9..112
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          203..325
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          402..532
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
FT   BINDING         443
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
FT   BINDING         471
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
FT   BINDING         473
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
SQ   SEQUENCE   573 AA;  63095 MW;  E51E3262FE46CB8A CRC64;
     MGSTDLCVGV YLLKRLKDAG VDHIFGVPGD FVLGFFNQIL QSDIKFVGTC NELNAAYAAD
     GYARVKGIGC LSTTYCVGEL SAINGVAGAW AEDLPIVKIT GAPATHHYSR KTMLHHTLGD
     YHIPQRMFEK ITVAHTVLMN EETAAAEIDR VLSACLTRKK PVYIALPADV IKKPIKQTYI
     PYTIPPLQKS DPTAVQEAVV ESLTILQRSK KPILLPGIEI CRYGLRDKFR TLLEKSGFPY
     STMMLAKTVL DEDHPQFIGL YQGAKSRPYV KDRVEKSDCI IVFGEKMTDF NTGGFTASLN
     EFVTINASVN EVQISHHVYP DVYLWDYMDA LTMHLVTRDA KDLDIHPASL GCTHTRATKF
     EPKPDKEIRM GRFFDRMSSF LPEGTIVIAE TGASLFSAAE TLMPKGGRFV GQTFYGSIGY
     TVGATLGLAL AAPDKTVVLF IGDGSFQVTV QDVSTMLRYG CKNVIIFLVN NDGYTIERVI
     VDHAYNDIQP WKYYKLCEVF GGGFAADCWT EGQLEDALAK TKTANDLCFI EVHMPRWDCS
     DSLRAAGEAM AKNNSLLEPG GVGPLKPPEG AEL
//
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