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Database: UniProt
Entry: A0A1V8UKG9_9PEZI
LinkDB: A0A1V8UKG9_9PEZI
Original site: A0A1V8UKG9_9PEZI 
ID   A0A1V8UKG9_9PEZI        Unreviewed;       377 AA.
AC   A0A1V8UKG9;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=Pyruvate dehydrogenase E1 component subunit beta {ECO:0000256|RuleBase:RU364074};
DE            EC=1.2.4.1 {ECO:0000256|RuleBase:RU364074};
GN   ORFNames=B0A51_11066 {ECO:0000313|EMBL:OQO23937.1};
OS   Rachicladosporium sp. CCFEE 5018.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Cladosporiales; Cladosporiaceae; Rachicladosporium.
OX   NCBI_TaxID=1974281 {ECO:0000313|EMBL:OQO23937.1, ECO:0000313|Proteomes:UP000192386};
RN   [1] {ECO:0000313|Proteomes:UP000192386}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCFEE 5018 {ECO:0000313|Proteomes:UP000192386};
RA   Coleine C., Masonjones S., Stajich J.E.;
RT   "Genomes of endolithic fungi from Antarctica.";
RL   Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall
CC       conversion of pyruvate to acetyl-CoA and CO2.
CC       {ECO:0000256|RuleBase:RU364074}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + N(6)-[(R)-lipoyl]-L-lysyl-[dihydrolipoyllysine-residue
CC         acetyltransferase] + pyruvate = CO2 + N(6)-[(R)-S(8)-
CC         acetyldihydrolipoyl]-L-lysyl-[dihydrolipoyllysine-residue
CC         acetyltransferase]; Xref=Rhea:RHEA:19189, Rhea:RHEA-COMP:10480,
CC         Rhea:RHEA-COMP:10481, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:83099, ChEBI:CHEBI:83111; EC=1.2.4.1;
CC         Evidence={ECO:0000256|RuleBase:RU364074};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964,
CC         ECO:0000256|RuleBase:RU364074};
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:OQO23937.1}.
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DR   EMBL; NAEU01000365; OQO23937.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V8UKG9; -.
DR   STRING; 1974281.A0A1V8UKG9; -.
DR   Proteomes; UP000192386; Unassembled WGS sequence.
DR   GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; IEA:InterPro.
DR   CDD; cd07036; TPP_PYR_E1-PDHc-beta_like; 1.
DR   Gene3D; 3.40.50.920; -; 1.
DR   Gene3D; 3.40.50.970; -; 1.
DR   InterPro; IPR027110; PDHB.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR009014; Transketo_C/PFOR_II.
DR   InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR   InterPro; IPR033248; Transketolase_C.
DR   PANTHER; PTHR11624; DEHYDROGENASE RELATED; 1.
DR   PANTHER; PTHR11624:SF96; PYRUVATE DEHYDROGENASE E1 COMPONENT SUBUNIT BETA, MITOCHONDRIAL; 1.
DR   Pfam; PF02779; Transket_pyr; 1.
DR   Pfam; PF02780; Transketolase_C; 1.
DR   SMART; SM00861; Transket_pyr; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
DR   SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|RuleBase:RU364074};
KW   Pyruvate {ECO:0000256|ARBA:ARBA00023317, ECO:0000256|RuleBase:RU364074};
KW   Reference proteome {ECO:0000313|Proteomes:UP000192386};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU364074}.
FT   DOMAIN          51..226
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   377 AA;  40779 MW;  322C3A21A4AF25DC CRC64;
     MVATRLARPA AQLLRSSPSA ASRCASRVPR VTAPAFSRWR GYATPSAGKE MTVRDALNEA
     MAEEMEKNDK VFVLGEEVAQ YNGAYKVTKG LLDRFGDKRV IDSPITESGF CGLTVGAALA
     GLHPVCEFMT FNFAMQAIDQ IINSAAKTHY MSGGIQPCNI TFRGPNGFAS GVAAQHSQDY
     TAWYASIPGL KVVSPYSAED AKGLLKAAIR DPNPVVVLEN ELLYGLSFPM SEEAQRDDFV
     IPFGKAKIER PGKDLTIVTL SRCVGQSLRA AEALKSKYGV EAEVLNLRSI KPMDVEAIVR
     SVKKTGTMMV VESGFPSFGV GAEIIALTAE YAFDYLNAPP VRVTGAEVPT PYAEKLEQMA
     FPSEQLIEDY AAKLLKV
//
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