ID B9SWY1_RICCO Unreviewed; 607 AA.
AC B9SWY1;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 24-JAN-2024, entry version 55.
DE RecName: Full=pyruvate decarboxylase {ECO:0000256|ARBA:ARBA00013202};
DE EC=4.1.1.1 {ECO:0000256|ARBA:ARBA00013202};
GN ORFNames=RCOM_0489390 {ECO:0000313|EMBL:EEF31884.1};
OS Ricinus communis (Castor bean).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Acalyphoideae; Acalypheae;
OC Ricinus.
OX NCBI_TaxID=3988 {ECO:0000313|Proteomes:UP000008311};
RN [1] {ECO:0000313|Proteomes:UP000008311}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Hale {ECO:0000313|Proteomes:UP000008311};
RX PubMed=20729833; DOI=10.1038/nbt.1674;
RA Chan A.P., Crabtree J., Zhao Q., Lorenzi H., Orvis J., Puiu D.,
RA Melake-Berhan A., Jones K.M., Redman J., Chen G., Cahoon E.B., Gedil M.,
RA Stanke M., Haas B.J., Wortman J.R., Fraser-Liggett C.M., Ravel J.,
RA Rabinowicz P.D.;
RT "Draft genome sequence of the oilseed species Ricinus communis.";
RL Nat. Biotechnol. 28:951-956(2010).
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=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=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, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; EQ974213; EEF31884.1; -; Genomic_DNA.
DR RefSeq; XP_002530500.1; XM_002530454.2.
DR AlphaFoldDB; B9SWY1; -.
DR STRING; 3988.B9SWY1; -.
DR GeneID; 8283141; -.
DR KEGG; rcu:8283141; -.
DR eggNOG; KOG1184; Eukaryota.
DR InParanoid; B9SWY1; -.
DR OrthoDB; 1000728at2759; -.
DR Proteomes; UP000008311; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004737; F:pyruvate decarboxylase activity; IBA:GO_Central.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR GO; GO:0000949; P:aromatic amino acid family catabolic process to alcohol via Ehrlich pathway; IBA:GO_Central.
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; 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:SF6; PYRUVATE DECARBOXYLASE C186.09-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.
PE 3: Inferred from homology;
KW Decarboxylase {ECO:0000256|ARBA:ARBA00022793};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:EEF31884.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR036565-2};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR036565-2}; Pyruvate {ECO:0000313|EMBL:EEF31884.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008311};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 46..151
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 243..362
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 453..577
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT BINDING 484
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
FT BINDING 511
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
FT BINDING 513
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
SQ SEQUENCE 607 AA; 65370 MW; 0982AF705DD4A400 CRC64;
MDTNIGSIDT LKPTTTDVCC PANGAVCTLQ SSTVSPSSIV SSPDSTLGRH LARRLVQVGV
TDVFSVPGDF NLTLLDHLIA EPGLNVIGCC NELNAGYAAD GYARSRGVGA CVVTFTVGGL
SVLNAIAGAY SENLPVVCIV GGPNSNDYGT NRILHHTIGL PDFSQELRCF QPVTCFQAIV
NNLEDAHELI DTAISTALKE SKPVYLSISC NLSAIPHPTF SREPVPFSLS PRLSNKIGLE
AAVEAAAEFL NKAVKPVLVG GPKLRVAKAC EAFVELADAC GYALAVMPSA KGLVPEHHSH
FIGTYWGAVS TAFCAEIVES ADAYLFAGPI FNDYSSVGYS LLLKKEKSII VQPDRVVIGN
GPAFGCVLMK DFLKALAKRL KNNTTAHENY RRIFVPEGQP LKSQPKEPLR VNVLFQHIQK
MLSSETAVIA ETGDSWFNCQ KLKLPKGCGY EFQMQYGSIG WSVGATLGYA QAVPEKRVIA
CIGDGSFQVT AQDVSTMLRC GQKTIIFLIN NGGYTIEVEI HDGPYNVIKN WNYTGLVDAI
HNGEGKCWTA KVQCEEELIE AIETATESKK DCLCFIEVIA HKDDTSKELL EWGSRVSAAN
SRPPNPQ
//
