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Database: UniProt
Entry: A0A0F4YHL4_TALEM
LinkDB: A0A0F4YHL4_TALEM
Original site: A0A0F4YHL4_TALEM 
ID   A0A0F4YHL4_TALEM        Unreviewed;       567 AA.
AC   A0A0F4YHL4;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=Pyruvate decarboxylase {ECO:0000256|ARBA:ARBA00014422};
DE            EC=4.1.1.1 {ECO:0000256|ARBA:ARBA00013202};
GN   ORFNames=T310_8280 {ECO:0000313|EMBL:KKA17777.1};
OS   Rasamsonia emersonii CBS 393.64.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Rasamsonia.
OX   NCBI_TaxID=1408163 {ECO:0000313|EMBL:KKA17777.1, ECO:0000313|Proteomes:UP000053958};
RN   [1] {ECO:0000313|EMBL:KKA17777.1, ECO:0000313|Proteomes:UP000053958}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 393.64 {ECO:0000313|EMBL:KKA17777.1,
RC   ECO:0000313|Proteomes:UP000053958};
RA   Heijne W.H., Fedorova N.D., Nierman W.C., Vollebregt A.W., Zhao Z., Wu L.,
RA   Kumar M., Stam H., van den Berg M.A., Pel H.J.;
RL   Submitted (APR-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   -!- 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:KKA17777.1}.
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DR   EMBL; LASV01000557; KKA17777.1; -; Genomic_DNA.
DR   RefSeq; XP_013324389.1; XM_013468935.1.
DR   AlphaFoldDB; A0A0F4YHL4; -.
DR   STRING; 1408163.A0A0F4YHL4; -.
DR   GeneID; 25320540; -.
DR   OrthoDB; 2165606at2759; -.
DR   Proteomes; UP000053958; 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: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   Reference proteome {ECO:0000313|Proteomes:UP000053958};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          1..75
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          148..254
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          353..424
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
FT   REGION          548..567
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   567 AA;  62083 MW;  9A24BEEBD72E8AA7 CRC64;
     MADGYARVTG RPQAVVVHVD VGTQALAHGI HNASVARVPV FIFAGLCPYT ESGELPGSRT
     EYSHWLQDPP DQKAIVRQYC RYTGEIRSGL NVKQNVGRAL QFACSAPKGP VYLAAAREPL
     AEEIEPYSLP QDQWVPIGPS ALPEEAVHTL AEALVHAERP LVITGYSGRD RRCPPLLAAL
     ADKIPGLRVH DTGGSDMCFP FTHPASQGFR LPGYDECTRD ADVILILDCD VPWIPSRNPP
     RKDARIYHID VDPLNQHLPV SFFPAHGRWK ADCYTALAQL LTHIDADSAL SQALQHPKYA
     ARWRELAESH RARLENIAKL PRLGDDEPLN AHNISRLLKD CLPEDTTFVI EAVTCAQTIS
     DQLQCSRPGS WINCGATGIG WSNGAALGVK MALDDQGKDL EEGNKKKPSL VCQIVGDGSY
     MCSAPSSAAW VARWHAPRHS TELVYPEGMN KDATRDELNL SFDPSPNYSQ LAKAAAGSSF
     ESDGGKNDWM QGARVNTVKA LRSQLEQAVT TVREQGRGFL LEALMERSHH SSDVGILNAY
     AMQCDPLADT RNSSRPHRSS GSMIDRI
//
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