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Database: UniProt
Entry: A0A2T4CE88_TRILO
LinkDB: A0A2T4CE88_TRILO
Original site: A0A2T4CE88_TRILO 
ID   A0A2T4CE88_TRILO        Unreviewed;       227 AA.
AC   A0A2T4CE88;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 15.
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=M440DRAFT_974 {ECO:0000313|EMBL:PTB79889.1};
OS   Trichoderma longibrachiatum ATCC 18648.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=983965 {ECO:0000313|EMBL:PTB79889.1, ECO:0000313|Proteomes:UP000240760};
RN   [1] {ECO:0000313|EMBL:PTB79889.1, ECO:0000313|Proteomes:UP000240760}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 18648 {ECO:0000313|EMBL:PTB79889.1,
RC   ECO:0000313|Proteomes:UP000240760};
RG   DOE Joint Genome Institute;
RA   Aerts A., Atanasova L., Chenthamara K., Zhang J., Grujic M., Henrissat B.,
RA   Kuo A., Salamov A., Lipzen A., Labutti K., Barry K., Miao Y., Rahimi M.J.,
RA   Shen Q., Grigoriev I.V., Kubicek C.P., Druzhinina I.S.;
RT   "Multiple horizontal gene transfer events from other fungi enriched the
RT   ability of initially mycotrophic Trichoderma (Ascomycota) to feed on dead
RT   plant biomass.";
RL   Submitted (JUL-2016) 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};
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DR   EMBL; KZ679127; PTB79889.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T4CE88; -.
DR   STRING; 983965.A0A2T4CE88; -.
DR   Proteomes; UP000240760; 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   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   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:UP000240760};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU364074}.
FT   DOMAIN          1..74
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02779"
FT   DOMAIN          94..215
FT                   /note="Transketolase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02780"
SQ   SEQUENCE   227 AA;  24567 MW;  43A14520AE130FAA CRC64;
     MSGGIQPCNI TFRGPNGFAA GVAAQHSQDY SAWYGSVPGL KVVSPWSAED AKGLLKAAIR
     DPNPVVVLEN ELMYGQSFPM SEAAQKDDFV LPFGKAKIER AGSDLTIVSL SRCVGQSLVA
     AENLKKNYGV EAEVINLRSI KPLDLDSIVQ SIKKTHRLLV VESGYPAFGV GAEILALAME
     YAFDYLDGPA QRVTGAEVPT PYAQKLEEMS FPNEQLIEQF AAKMLRV
//
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