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Database: UniProt
Entry: A0A072NV35_9EURO
LinkDB: A0A072NV35_9EURO
Original site: A0A072NV35_9EURO 
ID   A0A072NV35_9EURO        Unreviewed;       622 AA.
AC   A0A072NV35;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   24-JAN-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=A1O9_12403 {ECO:0000313|EMBL:KEF51486.1};
OS   Exophiala aquamarina CBS 119918.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX   NCBI_TaxID=1182545 {ECO:0000313|EMBL:KEF51486.1, ECO:0000313|Proteomes:UP000027920};
RN   [1] {ECO:0000313|EMBL:KEF51486.1, ECO:0000313|Proteomes:UP000027920}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 119918 {ECO:0000313|EMBL:KEF51486.1,
RC   ECO:0000313|Proteomes:UP000027920};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Exophiala aquamarina CBS 119918.";
RL   Submitted (MAR-2013) 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   -!- 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:KEF51486.1}.
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DR   EMBL; AMGV01000023; KEF51486.1; -; Genomic_DNA.
DR   RefSeq; XP_013254076.1; XM_013398622.1.
DR   AlphaFoldDB; A0A072NV35; -.
DR   STRING; 1182545.A0A072NV35; -.
DR   GeneID; 25287297; -.
DR   VEuPathDB; FungiDB:A1O9_12403; -.
DR   HOGENOM; CLU_013748_3_3_1; -.
DR   OrthoDB; 1328249at2759; -.
DR   Proteomes; UP000027920; 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; 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:SF169; ACETOLACTATE SYNTHASE CATALYTIC SUBUNIT, MITOCHONDRIAL; 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   Reference proteome {ECO:0000313|Proteomes:UP000027920};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          18..131
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          207..352
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          422..575
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
FT   REGION          379..399
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   622 AA;  65248 MW;  266E3536537E09C4 CRC64;
     MASPELKWTH PEKRELLGGD LLAQTLSQLG VEVSFGIHGG HLDAFLIGCN LAGIKLIDTR
     HETTAVQAAE GYAKVSGKVG CAFVTANSGF CNSIPGLATA FADRSPVFVV TSSPPLRDAE
     TNCLQGFHDQ VVLAKPLTKF AHRVTNVEEI PRITAYAFKT AMSGIPGPVV VDFPIDVLFH
     PPRMSAIAYG SVMRAPAAAP GPDPASVDEL VQLWKAAARP VIISGTGAAR TTTRGDGATT
     KSPLLDLANA TSTPVFYSQK YAPALPHSHP LRGGPAGSLA MLPYIGKQQP DLVLLLGART
     GFLLGGRSGA IIPASSSGCK LVQVDIDGAE IGKSQPVDLG IVSDANNFIS ALLTKLQASS
     DGEGAGIGKH ESWIQDISDL KSTPSPHASD PEKNASDGRL HPYHTIRAIY SSIPAGSIII
     LDGGEASVWA SESMELARPS AGIVSTGYLG FLGNGWGYSL GAAVAAGPDT LVLNVHGDGS
     AGFHIQELDT YARHNLNIVT VIMNNYVWGM SIAGQDIIYG SEDPARMVSS LSEATHYEVV
     AQGFGCQGAI ASESIDEVKT KVKELVAAKG PGLLNAVISK SPVTMVTKAM VGKTDDKNVI
     VVPYYDNVPR PYYRTDELKN GH
//
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