ID   A0A059BT70_EUCGR        Unreviewed;       479 AA.
AC   A0A059BT70;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=Pyruvate decarboxylase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=EUGRSUZ_F02797 {ECO:0000313|EMBL:KCW69307.1};
OS   Eucalyptus grandis (Flooded gum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Myrtales; Myrtaceae; Myrtoideae; Eucalypteae; Eucalyptus.
OX   NCBI_TaxID=71139 {ECO:0000313|EMBL:KCW69307.1};
RN   [1] {ECO:0000313|EMBL:KCW69307.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaf extractions {ECO:0000313|EMBL:KCW69307.1};
RA   Schmutz J., Hayes R., Myburg A., Tuskan G., Grattapaglia D., Rokhsar D.S.;
RT   "The genome of Eucalyptus grandis.";
RL   Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
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; KK198758; KCW69307.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A059BT70; -.
DR   EnsemblPlants; KCW69307; KCW69307; EUGRSUZ_F02797.
DR   Gramene; KCW69307; KCW69307; EUGRSUZ_F02797.
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; IEA:InterPro.
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   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          21..130
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          209..335
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          409..470
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   479 AA;  51399 MW;  BE495225883A41E0 CRC64;
     MADPNPNPTG APARIDGNVL AAKSLARFGV DRMFGVVGIP VTSLANRAVA LGVRFIAFHN
     EQSAGYAASS YGYLTGRPGV LLTVSGPGCV HGLAGMSNAM ANAWPMVMIS GSCDQQDFGR
     GDFQELDQVE AVKPFSKFSA KARDIREVPG CVARVLDHAV SGRPGGCYLD LPTDVLHQTV
     TESEAESLLD EAEKCRLKEE MSNVLSSQIE EAVALLRGAA RPLIVFGKGA AFARAEDELR
     KLVEVSGIPF LPTPMGKGLL PDTHELAATA ARSLAIGKCD VALVVGARLN WLLHFGEPPK
     WSRDVKFILV DVSKEEIELR KPFLGLVGDA KRVLELINKE IKDDPFCLGR SHPWVEAISK
     KSKENVLRME AQLAKEVVPF NFLTPMKIIR DAILGMGSPA PILVSEGANT MDIGRAVLVQ
     TEPRTRLDAG TWGTMGVGLG YCVAAAVASP DRLVVAVEGD SGFGFSAMEV EFDISYRWL
//