ID A0A0D0E0W8_9AGAM Unreviewed; 610 AA.
AC A0A0D0E0W8;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Pyruvate decarboxylase {ECO:0008006|Google:ProtNLM};
GN ORFNames=PAXRUDRAFT_502856 {ECO:0000313|EMBL:KIK93644.1};
OS Paxillus rubicundulus Ve08.2h10.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Paxilineae; Paxillaceae; Paxillus.
OX NCBI_TaxID=930991 {ECO:0000313|EMBL:KIK93644.1, ECO:0000313|Proteomes:UP000054538};
RN [1] {ECO:0000313|EMBL:KIK93644.1, ECO:0000313|Proteomes:UP000054538}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ve08.2h10 {ECO:0000313|EMBL:KIK93644.1,
RC ECO:0000313|Proteomes:UP000054538};
RG DOE Joint Genome Institute;
RA Kuo A., Kohler A., Jargeat P., Nagy L.G., Floudas D., Copeland A.,
RA Barry K.W., Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A.,
RA Lipzen A., Lundell T., Morin E., Murat C., Sun H., Tunlid A., Henrissat B.,
RA Grigoriev I.V., Hibbett D.S., Martin F., Nordberg H.P., Cantor M.N.,
RA Hua S.X.;
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000054538}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ve08.2h10 {ECO:0000313|Proteomes:UP000054538};
RG DOE Joint Genome Institute;
RG Mycorrhizal Genomics Consortium;
RA Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812}.
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DR EMBL; KN825169; KIK93644.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D0E0W8; -.
DR STRING; 930991.A0A0D0E0W8; -.
DR HOGENOM; CLU_013748_4_0_1; -.
DR InParanoid; A0A0D0E0W8; -.
DR OrthoDB; 2291769at2759; -.
DR Proteomes; UP000054538; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
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; 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; 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 Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Reference proteome {ECO:0000313|Proteomes:UP000054538}.
FT DOMAIN 4..133
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 442..604
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 610 AA; 65510 MW; E9B0B214503F2E20 CRC64;
MVFTTSSLFL HTISEVGITH VFVNWGSDHP AMLEELQRQR VTNGSHTLTI VTSPNEMVAL
SAAHGYARAT GKPAAVIVHV DVGTQALAGA VHNADRGRVP ILIYAGSSPF TTEGELKGSR
NEWIHWIQDV HDQPTIVRQY MRYTAQIGSP SNLPHLVRRA LQIATSEPKG PVYLWGRREV
MEQEIDQSLL ERPITLTKWP SVEPTALPIT AAQRISSALL AAKVPLLITS HLGCNHAASV
ELATLSRILA LPVFLTCPST TNLPTSHPFL VGVSYLTPGT HTPLLQSADV VVVIDAEVAW
IPMNKDSDGV HERPQETAQV FVIDGGDPLK RGIGMHHDEA DLICQADAAI ALTQIREAVG
SQAAFDLSER GERVRKMHEV WIAQLRAAES FPIVPSSSGR SAPYTTPQIL AALRTAIHAS
GASREGTLIL NESISSYPLT WSHMQPEIPG EMMSSGGSSL GWALGAGIGA VLGGRELVAS
IVGDGTFLFG VPASAFWMAR RYMTPFLTIV LNNGGWKSPK LSMLGVYPHG YGSSAVGDQL
TVGLGPDCPD YSQIAVAASG GWAWGRKISA DLAVDGKNAE ELLQETIAEA VRIVTEERRC
AVVDCVLECI
//
