ID A0A067RJD6_ZOONE Unreviewed; 396 AA.
AC A0A067RJD6;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
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=L798_04603 {ECO:0000313|EMBL:KDR20584.1};
OS Zootermopsis nevadensis (Dampwood termite).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Polyneoptera; Dictyoptera; Blattodea; Blattoidea; Termitoidae;
OC Termopsidae; Zootermopsis.
OX NCBI_TaxID=136037 {ECO:0000313|EMBL:KDR20584.1, ECO:0000313|Proteomes:UP000027135};
RN [1] {ECO:0000313|EMBL:KDR20584.1, ECO:0000313|Proteomes:UP000027135}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Whole organism {ECO:0000313|EMBL:KDR20584.1};
RX PubMed=24845553; DOI=10.1038/ncomms4636;
RA Terrapon N., Li C., Robertson H.M., Ji L., Meng X., Booth W., Chen Z.,
RA Childers C.P., Glastad K.M., Gokhale K., Gowin J., Gronenberg W.,
RA Hermansen R.A., Hu H., Hunt B.G., Huylmans A.K., Khalil S.M.,
RA Mitchell R.D., Munoz-Torres M.C., Mustard J.A., Pan H., Reese J.T.,
RA Scharf M.E., Sun F., Vogel H., Xiao J., Yang W., Yang Z., Yang Z., Zhou J.,
RA Zhu J., Brent C.S., Elsik C.G., Goodisman M.A., Liberles D.A., Roe R.M.,
RA Vargo E.L., Vilcinskas A., Wang J., Bornberg-Bauer E., Korb J., Zhang G.,
RA Liebig J.;
RT "Molecular traces of alternative social organization in a termite genome.";
RL Nat. Commun. 5:3636-3636(2014).
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; KK852597; KDR20584.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A067RJD6; -.
DR STRING; 136037.A0A067RJD6; -.
DR EnsemblMetazoa; KDR20584; KDR20584; L798_04603.
DR eggNOG; KOG0524; Eukaryota.
DR InParanoid; A0A067RJD6; -.
DR OMA; SRMRHHC; -.
DR OrthoDB; 5473567at2759; -.
DR Proteomes; UP000027135; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 Membrane {ECO:0000256|SAM:Phobius};
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:UP000027135};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|RuleBase:RU364074}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 25..46
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 68..243
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 396 AA; 43535 MW; B4803A8F37E47092 CRC64;
MALHLTTCHL YKWNYHSQKR KSTRFLLAVI YRVIKMVTHG GIVFLLNAAK FLSRRAFSTS
RIVNAQQMTV RDALNAGLDE EMERDERVFV LGEEVAMYDG AYKVSRGLWK KYGDKRVIDT
PITEMGFAGI AVGAAMAGLR PVCEFMTFNF SMQAIDHVIN SAAKTFYMSA GKVNVPIVFR
GPNGAAAGVA AQHSQCFGAW YSHCPGLKVV SPYTAEDHKG LIKAAIRDPD PVVVLENEIL
YGVAFPVSDE AMSKDFLVPI GKAKIERTGS HITLVAHSRA VELSLDAAKE LAGEGIECEV
INLRSIRPLD EETIIKSVIK TNHLVTVEQG WPQCGIGSEI CARIMESEAF YHLDSPVVRV
TGVDAPMPYT KSLEAAALPQ PHDIVRAVKQ VLTVKS
//
