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
//