ID G8Y1H5_PICSO Unreviewed; 385 AA.
AC G8Y1H5;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=Pyruvate dehydrogenase E1 component subunit beta {ECO:0000256|RuleBase:RU364074};
DE EC=1.2.4.1 {ECO:0000256|RuleBase:RU364074};
GN Name=Piso0_005181 {ECO:0000313|EMBL:CCE86678.1};
GN ORFNames=GNLVRS01_PISO0N09583g {ECO:0000313|EMBL:CCE86678.1};
OS Pichia sorbitophila (strain ATCC MYA-4447 / BCRC 22081 / CBS 7064 / NBRC
OS 10061 / NRRL Y-12695) (Hybrid yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Millerozyma.
OX NCBI_TaxID=559304 {ECO:0000313|EMBL:CCE86678.1, ECO:0000313|Proteomes:UP000005222};
RN [1] {ECO:0000313|Proteomes:UP000005222}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4447 / BCRC 22081 / CBS 7064 / NBRC 10061 / NRRL
RC Y-12695 {ECO:0000313|Proteomes:UP000005222};
RX DOI=10.1534/g3.111.000745;
RA Leh Louis V., Despons L., Friedrich A., Martin T., Durrens P.,
RA Casaregola S., Neuveglise C., Fairhead C., Marck C., Cruz J.A.,
RA Straub M.L., Kugler V., Sacerdot C., Uzunov Z., Thierry A., Weiss S.,
RA Bleykasten C., De Montigny J., Jacques N., Jung P., Lemaire M., Mallet S.,
RA Morel G., Richard G.F., Sarkar A., Savel G., Schacherer J., Seret M.L.,
RA Talla E., Samson G., Jubin C., Poulain J., Vacherie B., Barbe V.,
RA Pelletier E., Sherman D.J., Westhof E., Weissenbach J., Baret P.V.,
RA Wincker P., Gaillardin C., Dujon B., Souciet J.L.;
RT "Pichia sorbitophila, an interspecies yeast hybrid reveals early steps of
RT genome resolution following polyploidization.";
RL G3 (Bethesda) 2:299-311(2012).
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; FO082046; CCE86678.1; -; Genomic_DNA.
DR AlphaFoldDB; G8Y1H5; -.
DR STRING; 559304.G8Y1H5; -.
DR eggNOG; KOG0524; Eukaryota.
DR HOGENOM; CLU_012907_1_1_1; -.
DR InParanoid; G8Y1H5; -.
DR OMA; SRMRHHC; -.
DR Proteomes; UP000005222; Chromosome N.
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|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU364074};
KW Pyruvate {ECO:0000256|ARBA:ARBA00023317, ECO:0000256|RuleBase:RU364074};
KW Reference proteome {ECO:0000313|Proteomes:UP000005222};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|RuleBase:RU364074}.
FT DOMAIN 58..233
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 385 AA; 41331 MW; 28FF187D4A42329C CRC64;
MVSKIGQIGQ GVKLGAAVLS KNAAKGPGSK LGALGQQQAQ RMVFPARQAT SGSGAQTMTV
RDALNSAMAE ELDRDDSVFL LGEEVAQYNG AYKVSRGLLD RFGDRRVIDT PITEMGFTGL
AVGAALAGLK PICEFMTFNF AMQSIDQIIN SAAKTYYMSG GIQPCNITFR GPNGAAAGVA
AQHSQCYAAW YGSIPGLKVL SPYSAADYKG LLKASIRDPN PVVFLENEIS YGESFEMTEE
ELSPDFVLPI GKAKIEREGS DITLVSHTRN VMHCLDAAEQ LAKDYGVKAE VINLRSIKPL
DVETIVESVK KTNHLVTCEA GFPAFGVGSE ICAQIMESEA FDYLDAPVER VTGCEVPTPY
AVELENFAFP DTEIVMRASR KVLGL
//
