GenomeNet

Database: UniProt
Entry: A0A061GER3_THECC
LinkDB: A0A061GER3_THECC
Original site: A0A061GER3_THECC 
ID   A0A061GER3_THECC        Unreviewed;       406 AA.
AC   A0A061GER3;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=pyruvate decarboxylase {ECO:0000256|ARBA:ARBA00013202};
DE            EC=4.1.1.1 {ECO:0000256|ARBA:ARBA00013202};
GN   ORFNames=TCM_029740 {ECO:0000313|EMBL:EOY28061.1};
OS   Theobroma cacao (Cacao) (Cocoa).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Malvales; Malvaceae; Byttnerioideae; Theobroma.
OX   NCBI_TaxID=3641 {ECO:0000313|EMBL:EOY28061.1, ECO:0000313|Proteomes:UP000026915};
RN   [1] {ECO:0000313|EMBL:EOY28061.1, ECO:0000313|Proteomes:UP000026915}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Matina 1-6 {ECO:0000313|Proteomes:UP000026915};
RX   PubMed=23731509; DOI=10.1186/gb-2013-14-6-r53;
RA   Motamayor J.C., Mockaitis K., Schmutz J., Haiminen N., Iii D.L.,
RA   Cornejo O., Findley S.D., Zheng P., Utro F., Royaert S., Saski C.,
RA   Jenkins J., Podicheti R., Zhao M., Scheffler B.E., Stack J.C., Feltus F.A.,
RA   Mustiga G.M., Amores F., Phillips W., Marelli J.P., May G.D., Shapiro H.,
RA   Ma J., Bustamante C.D., Schnell R.J., Main D., Gilbert D., Parida L.,
RA   Kuhn D.N.;
RT   "The genome sequence of the most widely cultivated cacao type and its use
RT   to identify candidate genes regulating pod color.";
RL   Genome Biol. 14:R53.1-R53.24(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   -!- COFACTOR:
CC       Name=a metal cation; Xref=ChEBI:CHEBI:25213;
CC         Evidence={ECO:0000256|ARBA:ARBA00001920};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC   -!- SIMILARITY: Belongs to the TPP enzyme family.
CC       {ECO:0000256|ARBA:ARBA00007812}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CM001884; EOY28061.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A061GER3; -.
DR   EnsemblPlants; EOY28061; EOY28061; TCM_029740.
DR   Gramene; EOY28061; EOY28061; TCM_029740.
DR   HOGENOM; CLU_013748_0_0_1; -.
DR   Proteomes; UP000026915; Chromosome 6.
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; cd07038; TPP_PYR_PDC_IPDC_like; 1.
DR   Gene3D; 3.40.50.970; -; 1.
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; IPR047213; TPP_PYR_PDC_IPDC-like.
DR   PANTHER; PTHR43452; PYRUVATE DECARBOXYLASE; 1.
DR   PANTHER; PTHR43452:SF1; PYRUVATE DECARBOXYLASE; 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); 1.
PE   3: Inferred from homology;
KW   Decarboxylase {ECO:0000256|ARBA:ARBA00022793};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Pyruvate {ECO:0000313|EMBL:EOY28061.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000026915}.
FT   DOMAIN          28..133
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          225..342
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
SQ   SEQUENCE   406 AA;  43490 MW;  731B6EC0E0877964 CRC64;
     MEAGNKIRSS AHPNSLAPPV CGGASRGTLG RYLARRLVEI GVKDVFSVPG DFNLTLLDHL
     IAEPELNLIG CCNELNAGYA ADGYARSKGV GACVVTFTVG GLSALNAIAG AYSENLPVIC
     IVGGPNSNDY GTNRILHHTI GLPDFSQELR CFQTITCAQA VVNNLDDAHE LIDTAISTAL
     KESKPVYISI SCNLPGIPHP TFAREPVPFL LAPKVSNQLG LEAAVEATAD FLNKAVKPVL
     VGGPKLRVAK AQEAFVELAD ASGYPIAVMP SAKGLVPEHH PHFIGTYWGA VSTSFCGEIV
     ESADAYVFVG PIFNDYSSVG YSLLFTKEKA VIVQPNRVTI GNGPSFGWVF MTDFLSALAK
     KLKRNSTAVE NYRRIFIPPG MPLKRGNDEP LRVNVLFKHI QVNRIC
//
DBGET integrated database retrieval system