ID A0A059A6L1_EUCGR Unreviewed; 644 AA.
AC A0A059A6L1;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=pyruvate decarboxylase {ECO:0000256|ARBA:ARBA00013202};
DE EC=4.1.1.1 {ECO:0000256|ARBA:ARBA00013202};
GN ORFNames=EUGRSUZ_K02969 {ECO:0000313|EMBL:KCW49438.1};
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:KCW49438.1, ECO:0000313|Proteomes:UP000030711};
RN [1] {ECO:0000313|Proteomes:UP000030711}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. BRASUZ1 {ECO:0000313|Proteomes:UP000030711};
RX PubMed=24919147; DOI=10.1038/nature13308;
RA Myburg A.A., Grattapaglia D., Tuskan G.A., Hellsten U., Hayes R.D.,
RA Grimwood J., Jenkins J., Lindquist E., Tice H., Bauer D., Goodstein D.M.,
RA Dubchak I., Poliakov A., Mizrachi E., Kullan A.R., Hussey S.G., Pinard D.,
RA van der Merwe K., Singh P., van Jaarsveld I., Silva-Junior O.B.,
RA Togawa R.C., Pappas M.R., Faria D.A., Sansaloni C.P., Petroli C.D.,
RA Yang X., Ranjan P., Tschaplinski T.J., Ye C.Y., Li T., Sterck L.,
RA Vanneste K., Murat F., Soler M., Clemente H.S., Saidi N., Cassan-Wang H.,
RA Dunand C., Hefer C.A., Bornberg-Bauer E., Kersting A.R., Vining K.,
RA Amarasinghe V., Ranik M., Naithani S., Elser J., Boyd A.E., Liston A.,
RA Spatafora J.W., Dharmwardhana P., Raja R., Sullivan C., Romanel E.,
RA Alves-Ferreira M., Kulheim C., Foley W., Carocha V., Paiva J., Kudrna D.,
RA Brommonschenkel S.H., Pasquali G., Byrne M., Rigault P., Tibbits J.,
RA Spokevicius A., Jones R.C., Steane D.A., Vaillancourt R.E., Potts B.M.,
RA Joubert F., Barry K., Pappas G.J., Strauss S.H., Jaiswal P.,
RA Grima-Pettenati J., Salse J., Van de Peer Y., Rokhsar D.S., Schmutz J.;
RT "The genome of Eucalyptus grandis.";
RL Nature 510:356-362(2014).
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; KK198763; KCW49438.1; -; Genomic_DNA.
DR RefSeq; XP_010037690.1; XM_010039388.2.
DR AlphaFoldDB; A0A059A6L1; -.
DR STRING; 71139.A0A059A6L1; -.
DR EnsemblPlants; KCW49438; KCW49438; EUGRSUZ_K02969.
DR Gramene; KCW49438; KCW49438; EUGRSUZ_K02969.
DR eggNOG; KOG1184; Eukaryota.
DR InParanoid; A0A059A6L1; -.
DR OrthoDB; 1000728at2759; -.
DR Proteomes; UP000030711; 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:SF25; PYRUVATE DECARBOXYLASE; 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};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR036565-2};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR036565-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000030711};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 83..188
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 279..398
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 491..615
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT BINDING 521
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
FT BINDING 548
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
FT BINDING 550
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
SQ SEQUENCE 644 AA; 69748 MW; AA17E1814AD485CC CRC64;
MATSLLSAPF SHWITDSSRP YRKTNHLITK SAKIHSAINR DARVGSLETS TLPSKVARPH
NGVASIVQPS YSIAALGPSE ATLGCHLARR LVEIGVGDVF SVPGDFNLSL LDHLVTEPGL
NLIGCCNELN AGYAADGYAR SRGVGACVVT FTVGGLSVIN AIAGAYSENL PLICIVGGPN
SNDYGRNQVL HHTIGLPDFT QELRCFQTVT CHQAVVNNLE DAQEQIDTAI FTALRESKPV
YISISCNLTS IPHPTFSRKP ITFSLSPRLS DQMVLEAAVE AAAEFLNKAV KPVMVAGPNL
RIAKACDTFV ELADVSGYAH AVMASAKGLV STEHHAHFLG TYWGTVSTAF CAEIVESADA
YLFAGPIFND VSSVGYSLLI KKEKAIIVQP DRVVIGNGPT FGFVEMNDFL KALAKRLNRN
TTAYENYHRI YIPEGRPLKR DPKEPLRVNV LVQHIQNMLS SKTTVIAETG DMWFNCQKLK
LPSGCGYEHQ MHYASIGWSV GATLGYAAGA PNKRVIACIG DGSFQMTAQD VSTMLRCGQN
SIIFLINNGG YTVEAEIHDG PYNLIKNWNY AGLVDAIHNG EGKCWTTKVC CEEELVEAIE
TATGPKKDCL CFIEVIVHKD DTCKELLPFG CRLAAVNSRA PVPR
//