ID Q9FVF0_FRAAN Unreviewed; 605 AA.
AC Q9FVF0;
DT 01-MAR-2001, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2001, sequence version 1.
DT 24-JAN-2024, entry version 69.
DE RecName: Full=pyruvate decarboxylase {ECO:0000256|ARBA:ARBA00013202};
DE EC=4.1.1.1 {ECO:0000256|ARBA:ARBA00013202};
GN Name=PDC {ECO:0000313|EMBL:AAG13131.1};
OS Fragaria ananassa (Strawberry) (Fragaria chiloensis x Fragaria virginiana).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Rosoideae; Potentilleae; Fragariinae;
OC Fragaria.
OX NCBI_TaxID=3747 {ECO:0000313|EMBL:AAG13131.1};
RN [1] {ECO:0000313|EMBL:AAG13131.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=10810141; DOI=10.1105/tpc.12.5.647;
RA Aharoni A., Keizer L.C.P., Bouwmeester H.J., Sun Z., Alvarez-Huerta M.,
RA Verhoeven H.A., Blaas J., Van Houwelingen A.M.M.L., De Vos R.C.H.,
RA Van der Voet H., Jansen R.C., Guis M., Mol J., Davis R.W., Schena M.,
RA van Tunen A.J., O'Connell A.P.O.;
RT "Identification of the SAAT gene involved in strawberry flavor biogenesis
RT by use of DNA microarrays.";
RL Plant Cell 12:647-662(2000).
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; AF193791; AAG13131.1; -; mRNA.
DR AlphaFoldDB; Q9FVF0; -.
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; 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: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.
DR PROSITE; PS00187; TPP_ENZYMES; 1.
PE 2: Evidence at transcript level;
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}; Pyruvate {ECO:0000313|EMBL:AAG13131.1};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 44..149
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 241..359
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 451..576
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT BINDING 482
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
FT BINDING 509
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"
SQ SEQUENCE 605 AA; 65244 MW; DC8C023ADE5C024E CRC64;
MDTKIGSIDV CKTENHDVGC LPNSATSTVQ NSVPSTSLSS ADATLGRHLA RRLVQIGVTD
VFTVPGDFNL TLLDHLIAEP GLTNIGCCNE LNAGYAADGY ARSRGVGACV VTFTVGGLSV
LNAIAGAYSE NLPVICIVGG PNSNDYGTNR ILHHTIGLPD FSQELRCFQT VTCFQAVVNN
LEDAHEMIDT AISTALKESK PVYISIGCNL AGIPHPTFSR EPVPFSLSPK LSNKWGLEAA
VEAAAEFLNK AVKPVMVGGP KLRSAHAGDA FVELADASGF ALAVMPSAKG QVPEHHPHFI
GTYWGAVSTA FCAEIVESAD AYLFAGPIFN DYSSVGYSLL LKKEKAIIVQ PDRVTIGNGP
TFGCVLMKDF LLGLAKKLKH NNTAHENYRR IFVPDGHPLK AAPKEPLRVN VLFKHIQNML
SAETAVIAET GDSWFNCQKL KLPPGCGYEF QMQYGSIGWS VGATLGYAQA VPEKRVISFI
GDGSFQVTAQ DVSTMIRNGQ RTIIFLINNG GYTIEVEIHD GPYNVIKNWN YTGLVDAIHN
GEGKCWTTKV RCEEELIEAI ETANGPKKDS FCFIEVIVHK DDTSKELLEW GSRVSAANSR
PPNPQ
//
