PDC1_MAIZE
ID PDC1_MAIZE Reviewed; 610 AA.
AC P28516;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Pyruvate decarboxylase 1;
DE Short=PDC;
DE EC=4.1.1.1;
GN Name=PDC1; Synonyms=PDC;
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Wisconsin 22;
RX PubMed=1932699; DOI=10.1007/bf00028743;
RA Kelley P.M., Godfrey K., Lal S.K., Alleman M.;
RT "Characterization of the maize pyruvate decarboxylase gene.";
RL Plant Mol. Biol. 17:1259-1261(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RX PubMed=2519113; DOI=10.1007/bf00016139;
RA Kelley P.M.;
RT "Maize pyruvate decarboxylase mRNA is induced anaerobically.";
RL Plant Mol. Biol. 13:213-222(1989).
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 -!- COFACTOR:
CC Name=a metal cation; Xref=ChEBI:CHEBI:25213;
CC Note=Binds 1 metal ion per subunit.;
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Note=Binds 1 thiamine pyrophosphate per subunit.;
CC -!- SUBUNIT: Homotetramer. {ECO:0000305}.
CC -!- INDUCTION: By hypoxic stress.
CC -!- SIMILARITY: Belongs to the TPP enzyme family. {ECO:0000305}.
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 EMBL; X59546; CAA42120.1; -; Genomic_DNA.
DR EMBL; X17555; CAA35589.1; -; mRNA.
DR PIR; S18347; DCZMP.
DR AlphaFoldDB; P28516; -.
DR SMR; P28516; -.
DR STRING; 4577.AC197705.4_FGP001; -.
DR PaxDb; P28516; -.
DR PRIDE; P28516; -.
DR MaizeGDB; 25417; -.
DR eggNOG; KOG1184; Eukaryota.
DR Proteomes; UP000007305; Unplaced.
DR ExpressionAtlas; P28516; baseline and differential.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0016831; F:carboxy-lyase activity; IBA:GO_Central.
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 InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR InterPro; IPR012110; TPP_enzyme.
DR InterPro; IPR011766; TPP_enzyme-bd_C.
DR PANTHER; PTHR43452; PTHR43452; 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; SSF52467; 1.
DR SUPFAM; SSF52518; SSF52518; 2.
PE 2: Evidence at transcript level;
KW Decarboxylase; Lyase; Magnesium; Metal-binding; Reference proteome;
KW Stress response; Thiamine pyrophosphate.
FT CHAIN 1..610
FT /note="Pyruvate decarboxylase 1"
FT /id="PRO_0000090774"
FT REGION 437..519
FT /note="Thiamine pyrophosphate binding"
FT BINDING 72
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 159
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 487
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 514
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 516
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 520
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CONFLICT 567..568
FT /note="TV -> MA (in Ref. 2; CAA35589)"
FT /evidence="ECO:0000305"
FT CONFLICT 571
FT /note="A -> D (in Ref. 2; CAA35589)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 610 AA; 65428 MW; 42A8C2B0E7208E93 CRC64;
METLLAGNPA NGVAKPTCNG VGALPVANSH AIIATPAAAA ATLAPAGATL GRHLARRLVQ
IGASDVFAVP GDFNLTLLDY LIAEPGLTLV GCCNELNAGY AADGYARSRG VGACAVTFTV
GGLSVLNAIA GAYSENLPVV CIVGGPNSND YGTNRILHHT IGLPDFSQEL RCFQTITCYQ
AIINNLDDAH EQIDTAIATA LRESKPVYIS VSCNLAGLSH PTFSRDPVPM FISPRLSNKA
NLEYAVEAAA DFLNKAVKPV MVGGPKIRVA KAREAFAAVA DASGYPFAVM PAAKGLVPEH
HPRFIGTYWG AVSTTFCAEI VESADAYLFA GPIFNDYSSV GYSLLLKREK AVIVQPDRMV
VGDGPAFGCI LMPEFLRALA KRLRRNTTAY DNYRRIFVPD REPPNGKPNE PLRVNVLFKH
IKGMLSGDSA VVAETGDSWF NCQKLRLPEG CGYEFQMQYG SIGWSVGATL GYAQAAKDKR
VIACIGDGSF QVTAQDVSTM LRCGQKSIIF LINNGGYTIE VEIHDGPYNV IKNWDYTGLV
NAIHNSEGNC WTMKVRTEEQ LKEAIATVTG AKKDCLCFIE VIVHKDDTSK ELLEWGSRVS
AANSRPPNPQ
