ID M1D0M1_SOLTU Unreviewed; 574 AA.
AC M1D0M1;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 24-JAN-2024, entry version 50.
DE SubName: Full=Pyruvate decarboxylase {ECO:0000313|EnsemblPlants:PGSC0003DMT400078735};
GN Name=102604551 {ECO:0000313|EnsemblPlants:PGSC0003DMT400078735};
OS Solanum tuberosum (Potato).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX NCBI_TaxID=4113 {ECO:0000313|EnsemblPlants:PGSC0003DMT400078735, ECO:0000313|Proteomes:UP000011115};
RN [1] {ECO:0000313|Proteomes:UP000011115}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DM1-3 516 R44 {ECO:0000313|Proteomes:UP000011115};
RX PubMed=21743474; DOI=10.1038/nature10158;
RG The Potato Genome Sequencing Consortium;
RT "Genome sequence and analysis of the tuber crop potato.";
RL Nature 475:189-195(2011).
RN [2] {ECO:0000313|EnsemblPlants:PGSC0003DMT400078735}
RP IDENTIFICATION.
RC STRAIN=DM1-3 516 R44 {ECO:0000313|EnsemblPlants:PGSC0003DMT400078735};
RG EnsemblPlants;
RL Submitted (JUN-2015) to UniProtKB.
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}.
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 RefSeq; XP_006357805.1; XM_006357743.2.
DR AlphaFoldDB; M1D0M1; -.
DR STRING; 4113.M1D0M1; -.
DR PaxDb; 4113-PGSC0003DMT400078735; -.
DR EnsemblPlants; PGSC0003DMT400078735; PGSC0003DMT400078735; PGSC0003DMG400030633.
DR GeneID; 102604551; -.
DR Gramene; PGSC0003DMT400078735; PGSC0003DMT400078735; PGSC0003DMG400030633.
DR KEGG; sot:102604551; -.
DR eggNOG; KOG1185; Eukaryota.
DR HOGENOM; CLU_013748_3_3_1; -.
DR InParanoid; M1D0M1; -.
DR OMA; DIGSHYI; -.
DR OrthoDB; 1966690at2759; -.
DR Proteomes; UP000011115; Unassembled WGS sequence.
DR GO; GO:0005777; C:peroxisome; IBA:GO_Central.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IBA:GO_Central.
DR GO; GO:0001561; P:fatty acid alpha-oxidation; IBA:GO_Central.
DR CDD; cd02004; TPP_BZL_OCoD_HPCL; 1.
DR CDD; cd07035; TPP_PYR_POX_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; IPR045025; HACL1-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 PANTHER; PTHR43710; 2-HYDROXYACYL-COA LYASE; 1.
DR PANTHER; PTHR43710:SF2; 2-HYDROXYACYL-COA LYASE 1; 1.
DR Pfam; PF02775; TPP_enzyme_C; 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); 2.
DR PROSITE; PS00187; TPP_ENZYMES; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000011115};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 14..127
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 208..334
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 409..557
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 574 AA; 61644 MW; FE9D10072D288448 CRC64;
MSDSDHQTLS TVDGNTFVAM CLARAGVDRM FGVVGIPVTS LANRSVGLGI RFIAFHNEQS
AGYAASAYGY LTGRPGILLT VSGPGCVHGL AGLSNATVNT WPMVLISGSS DQKEMGRGDF
QELDQIEAVK PFSKYSAKAT DITKIPSCVF SVLDWAISGR PGGCYLDLPT DVLHQTISDT
EAHKLIDDAE SCRNKELIAK PIVQHSEIAK AAALLRKAER PLIVFGKGAT FSRAENALKN
LVERTGIPFL PTPMAKGLLP DNHELAATAA RSLAIGKCDV ALIVGARLNW LLHFGEPPKW
SKDVKFILVD VDKEEIELRK PCLGLVGDAT KVVEMIHKEI KDDPFCLGKS HPWVEALSKK
SKENVLKMEA QLAKDVVPFN FMTPMRIIRD AILQLGSPAP IVVSEGANTM DVGRSVLVQT
EPRTRLDAGT WGTMGVGLGY CIAAAVASPE RLVVAVEGDS GFGFSAMEVE TLVRYQLPVV
VIVFNNGGVY GGDRRNPEEI TGPYKEDPAP TSFVPGASYH LLIEAFGGKG YLVGTPDELK
SALTESFSAR KPAVINVTID PYAGAESGRM QHKN
//