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Database: UniProt
Entry: G3Y553_ASPNA
LinkDB: G3Y553_ASPNA
Original site: G3Y553_ASPNA 
ID   G3Y553_ASPNA            Unreviewed;       596 AA.
AC   G3Y553;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   RecName: Full=Pyruvate decarboxylase {ECO:0000256|ARBA:ARBA00014422};
DE            EC=4.1.1.1 {ECO:0000256|ARBA:ARBA00013202};
DE   Flags: Fragment;
GN   ORFNames=ASPNIDRAFT_139646 {ECO:0000313|EMBL:EHA21718.1};
OS   Aspergillus niger (strain ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 /
OS   NCTC 3858a / NRRL 328 / USDA 3528.7).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=380704 {ECO:0000313|EMBL:EHA21718.1, ECO:0000313|Proteomes:UP000009038};
RN   [1] {ECO:0000313|EMBL:EHA21718.1, ECO:0000313|Proteomes:UP000009038}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 / NCTC 3858a /
RC   NRRL 328 / USDA 3528.7 {ECO:0000313|Proteomes:UP000009038};
RX   PubMed=21543515; DOI=10.1101/gr.112169.110;
RA   Andersen M.R., Salazar M.P., Schaap P.J., van de Vondervoort P.J.,
RA   Culley D., Thykaer J., Frisvad J.C., Nielsen K.F., Albang R., Albermann K.,
RA   Berka R.M., Braus G.H., Braus-Stromeyer S.A., Corrochano L.M., Dai Z.,
RA   van Dijck P.W., Hofmann G., Lasure L.L., Magnuson J.K., Menke H.,
RA   Meijer M., Meijer S.L., Nielsen J.B., Nielsen M.L., van Ooyen A.J.,
RA   Pel H.J., Poulsen L., Samson R.A., Stam H., Tsang A., van den Brink J.M.,
RA   Atkins A., Aerts A., Shapiro H., Pangilinan J., Salamov A., Lou Y.,
RA   Lindquist E., Lucas S., Grimwood J., Grigoriev I.V., Kubicek C.P.,
RA   Martinez D., van Peij N.N., Roubos J.A., Nielsen J., Baker S.E.;
RT   "Comparative genomics of citric-acid-producing Aspergillus niger ATCC 1015
RT   versus enzyme-producing CBS 513.88.";
RL   Genome Res. 21:885-897(2011).
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   -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC   -!- SIMILARITY: Belongs to the TPP enzyme family.
CC       {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EHA21718.1}.
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DR   EMBL; ACJE01000013; EHA21718.1; -; Genomic_DNA.
DR   AlphaFoldDB; G3Y553; -.
DR   STRING; 380704.G3Y553; -.
DR   HOGENOM; CLU_013748_4_0_1; -.
DR   Proteomes; UP000009038; Unassembled WGS sequence.
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   CDD; cd02002; TPP_BFDC; 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; IPR029061; THDP-binding.
DR   InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR   InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR   InterPro; IPR045229; TPP_enz.
DR   InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR   PANTHER; PTHR18968:SF164; PYRUVATE DECARBOXYLASE; 1.
DR   PANTHER; PTHR18968; THIAMINE PYROPHOSPHATE ENZYMES; 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.
PE   3: Inferred from homology;
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          5..136
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          214..321
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          417..595
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EHA21718.1"
FT   NON_TER         596
FT                   /evidence="ECO:0000313|EMBL:EHA21718.1"
SQ   SEQUENCE   596 AA;  63658 MW;  486BFEE7723F8A08 CRC64;
     TAPHTVADAF LEALAEAGVD YLFTVLGSDH PSIIEAYVRR QNDPARQYPK MVLFQHEFVA
     ISAADGYARM SHKPACVIAH VDVGTAALGQ GLHNASSGRA PVVIFAGVAP STLLGEAPGS
     RSEHVQWYQD IRDQAALVAP YSRFSAEIKS PHNVGSLVHR AVLMATTGSP GPVYLTATRE
     ILATPLPSPQ ARLKPIPSCQ LGSLSPQAVE LIGSALLNAK SPLVVTGYLG RNHSAVQELI
     KLADTIHGLR VFDSELREVC FPATHPACVT RGTGAAPAVQ SADVILVLDA DVPWIPRRIH
     PSPDAVIYHI DLDPRKERMN MFDIGAAATF HADTGPALTQ INAHITSSAR LADLQTNWTD
     RHEALRAAHA EGRARIDARA TKLLETPDAP CSVDFLCSRI RELVPDDTIF VTDSVTNQVA
     MTEQLQLTRP GSHLTKGGSG LGWAGGASIG VKLATTRYDT SDRPDVRVKA DTNSPFICNI
     TGDGSFIFSV PSAVYWASHR YGCPFLTVIL NNGGWNATRQ CLVDVHPGGE AARLSSKDLG
     ISLVEDGPDY GGIAKAAANG NLWATRVRSV KELDEALREG VRVVLEEGRG AVVDVV
//
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