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Database: UniProt
Entry: A0A0F8V273_9EURO
LinkDB: A0A0F8V273_9EURO
Original site: A0A0F8V273_9EURO 
ID   A0A0F8V273_9EURO        Unreviewed;       603 AA.
AC   A0A0F8V273;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=Pyruvate decarboxylase {ECO:0000256|ARBA:ARBA00014422};
DE            EC=4.1.1.1 {ECO:0000256|ARBA:ARBA00013202};
GN   ORFNames=ARAM_000475 {ECO:0000313|EMBL:KKK25843.1};
OS   Aspergillus rambellii.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=308745 {ECO:0000313|EMBL:KKK25843.1, ECO:0000313|Proteomes:UP000034291};
RN   [1] {ECO:0000313|EMBL:KKK25843.1, ECO:0000313|Proteomes:UP000034291}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SRRC1468 {ECO:0000313|EMBL:KKK25843.1,
RC   ECO:0000313|Proteomes:UP000034291};
RA   Moore G.G., Beltz S.B., Mack B.M.;
RT   "Draft Genome Sequences of Two Closely-Related Aflatoxigenic Aspergillus
RT   Species Obtained from the Cote d'Ivoire.";
RL   Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
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=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}.
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:KKK25843.1}.
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DR   EMBL; JZBS01000657; KKK25843.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F8V273; -.
DR   STRING; 308745.A0A0F8V273; -.
DR   OrthoDB; 2020042at2759; -.
DR   Proteomes; UP000034291; 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; cd02004; TPP_BZL_OCoD_HPCL; 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; 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; 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.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000313|EMBL:KKK25843.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000034291};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          5..119
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          198..326
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          400..577
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   603 AA;  64420 MW;  862FC0FC9CCE276E CRC64;
     MAVETGAQLI ARTLRDLGVT VIFGIVGIPV VEIAEEAINL GIRFVAFRNE QACSYAASVY
     GYMTGRPGVC LVVGGPGVLH TMAGIGNSSV NYFPLLVLAG SAETSAITKG AFQEMDAISL
     LTPHTKLAVR ASSLDFLPGA VKNAYRTCWY GRPGPTFVDL PADIIQGKLS PEFPLPLPEN
     ILVAPPPRAG GDPALILKAV ALLKAARAPL LIIGKGAAYA RAETGIRKLV DQTQIPFLPT
     PMGKGVVPDS HPLNVSSARS AALKNADVVL VLGARLNWIL HFGEVPKWSP QAKIIQVDIA
     AEEIGRNAGN SELGILGDLT LVVDQLTTSL SNWRYSPSGQ FPALLAESAK KNEARAQRAA
     LLPTPRGAPL TYQRAYHIIK STLNSLTPCE DGGIVYVSEG ANTMDISRSI FPLFHPRQRL
     DAGTYATMGV GMGYIVAAHE AFNATTTHPG SRNKPKKKIV ALEGDSAFGF SAMEIETLAR
     YRIPALIYVV NNSGIYHGDS TSESAWKALQ DQTASNDTKA DGKDTAKGLR STSLLYETRY
     EMLATMCGGR GYFVRNEQEL EAATREGFLS DTVTVVNMIV EPGIGKEIGF AWQNKGQEGQ
     AKL
//
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