ID A0A319DGE1_9EURO Unreviewed; 970 AA.
AC A0A319DGE1;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Pyruvate decarboxylase {ECO:0000256|ARBA:ARBA00014422};
DE EC=4.1.1.1 {ECO:0000256|ARBA:ARBA00013202};
GN ORFNames=BO82DRAFT_434767 {ECO:0000313|EMBL:PYH78722.1};
OS Aspergillus uvarum CBS 121591.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1448315 {ECO:0000313|EMBL:PYH78722.1, ECO:0000313|Proteomes:UP000248340};
RN [1] {ECO:0000313|EMBL:PYH78722.1, ECO:0000313|Proteomes:UP000248340}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 121591 {ECO:0000313|EMBL:PYH78722.1,
RC ECO:0000313|Proteomes:UP000248340};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|RuleBase:RU361277};
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 -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000256|RuleBase:RU361277}.
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DR EMBL; KZ821726; PYH78722.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A319DGE1; -.
DR STRING; 1448315.A0A319DGE1; -.
DR VEuPathDB; FungiDB:BO82DRAFT_434767; -.
DR OrthoDB; 1000728at2759; -.
DR Proteomes; UP000248340; Unassembled WGS sequence.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0004737; F:pyruvate decarboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion 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; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.40.50.1220; TPP-binding domain; 1.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH-like_N.
DR InterPro; IPR002328; ADH_Zn_CS.
DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR012110; PDC/IPDC-like.
DR InterPro; IPR020843; PKS_ER.
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:SF6; PYRUVATE DECARBOXYLASE C186.09-RELATED; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR Pfam; PF00205; TPP_enzyme_M; 1.
DR Pfam; PF02776; TPP_enzyme_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR PROSITE; PS00059; ADH_ZINC; 1.
PE 3: Inferred from homology;
KW Decarboxylase {ECO:0000256|ARBA:ARBA00022793};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU361277};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000248340};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|RuleBase:RU362132}; Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 2..314
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
FT REGION 699..718
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 929..970
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 935..970
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 970 AA; 104921 MW; BA52201120149B9B CRC64;
MSCVPSPAPD EVLVKLEYSG LCHSDIHAWK GTPSIIKREK RVEGHEGTGI VTAVGSEVED
ISVGDHVGVQ WVNKTCGVCE ADKRADYLAC PKAQMTGFSV DGTFGTCCVI QARHAVRIPK
EYPLDTVAPI ICAGTTCFRA VEETGVKEGD ILAVVGPAGG IGSLACQYAK AHGCRVLAIS
TGGDGRILYR DKLRVDFYVD CNTSTDIVTE VRKLTGGGLD AAIMIEGTEA LLEDAAQYIR
PRGSIVVVGK PPENTVGLGM SNLLLRMGQI KSSPYGGPRE QIEKAIEIFF EKNFYQSSHV
ISLDQLPQML QPVHQRDPED HSNGHSSRYE SSLLGQETVK IPSFSESTRT EKTFPKPTFY
QDSFNIGTYI GYRLEELGIR DFLAVPGDTN LVLLDNILKN PNLRMIGCCN ELNGGYAADG
YARASPAKVA VLVVPYVVGA LSALNAVAGA CSQNIKIIVL SGCPTTGMLA SKKFLHHAPS
AANRDQALDA YRGVTAASIR LQSTNTAVQA LDDAISKCFA SSLPIFIEIP NDIAGAACSS
PSPFKIPETM IQTSRNEEAV NSITGTWNKS EKPVLLFGSL ARRLLSAHDI EALADRLGCA
VLCQPDGRCI SESHPQYCGQ LWNGLTNPEG EKVFMDSDLW LIVGANWCDF HGIFTSIDEE
KSRMISIGKG WVELPDGTCI QGVDFATVVR QLIRSSMESK HKSVPRPKPT LGAKPSQTED
LDAPLTLEHA MYGIQNILRS GDTMLCDAGE AWFLANHIRL PPGTDCQIQM PYCSIGWALP
AGLGAQLGRS QGRSIILIGD GGFQMTAQEV STIVRQHLNP IIIIFNNLGY KIETAVHDGP
YNYIANWNYP QLAASLSASP HASSHNPYST KKQECMESYP SLFTLQVKTQ RDLKMALKRA
YDEHDKLAFL ELCIQPNDLS QEVRQLGKAF AQKNAEESSG PSESFAFKTP SAATSGPNSP
RVGSPANTSV
//
