ID A0A0L0BNE9_LUCCU Unreviewed; 542 AA.
AC A0A0L0BNE9;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Pyruvate dehydrogenase E1 component subunit beta, mitochondrial {ECO:0000256|ARBA:ARBA00016220};
DE EC=1.2.4.1 {ECO:0000256|ARBA:ARBA00012281};
GN ORFNames=FF38_12600 {ECO:0000313|EMBL:KNC21453.1};
OS Lucilia cuprina (Green bottle fly) (Australian sheep blowfly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Oestroidea;
OC Calliphoridae; Luciliinae; Lucilia.
OX NCBI_TaxID=7375 {ECO:0000313|EMBL:KNC21453.1, ECO:0000313|Proteomes:UP000037069};
RN [1] {ECO:0000313|EMBL:KNC21453.1, ECO:0000313|Proteomes:UP000037069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LS {ECO:0000313|EMBL:KNC21453.1,
RC ECO:0000313|Proteomes:UP000037069};
RC TISSUE=Full body {ECO:0000313|EMBL:KNC21453.1};
RX PubMed=26108605; DOI=10.1038/ncomms8344;
RA Anstead C.A., Korhonen P.K., Young N.D., Hall R.S., Jex A.R., Murali S.C.,
RA Hughes D.S., Lee S.F., Perry T., Stroehlein A.J., Ansell B.R.,
RA Breugelmans B., Hofmann A., Qu J., Dugan S., Lee S.L., Chao H., Dinh H.,
RA Han Y., Doddapaneni H.V., Worley K.C., Muzny D.M., Ioannidis P.,
RA Waterhouse R.M., Zdobnov E.M., James P.J., Bagnall N.H., Kotze A.C.,
RA Gibbs R.A., Richards S., Batterham P., Gasser R.B.;
RT "Lucilia cuprina genome unlocks parasitic fly biology to underpin future
RT interventions.";
RL Nat. Commun. 6:7344-7344(2015).
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
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:KNC21453.1}.
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DR EMBL; JRES01001623; KNC21453.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L0BNE9; -.
DR STRING; 7375.A0A0L0BNE9; -.
DR EnsemblMetazoa; KNC21453; KNC21453; FF38_12600.
DR EnsemblMetazoa; XM_023441269.2; XP_023297037.2; LOC111679671.
DR Proteomes; UP000037069; Unassembled WGS sequence.
DR GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IEA:UniProtKB-EC.
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; -; 2.
DR InterPro; IPR027110; PDHB.
DR InterPro; IPR013177; Ribosomal_mS38_C.
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; PF08213; COX24_C; 1.
DR Pfam; PF02779; Transket_pyr; 2.
DR Pfam; PF02780; Transketolase_C; 1.
DR SMART; SM01155; DUF1713; 1.
DR SMART; SM00861; Transket_pyr; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Pyruvate {ECO:0000256|ARBA:ARBA00023317};
KW Reference proteome {ECO:0000313|Proteomes:UP000037069};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 29..389
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT DOMAIN 205..238
FT /note="Ribosomal protein mS38 C-terminal"
FT /evidence="ECO:0000259|SMART:SM01155"
SQ SEQUENCE 542 AA; 60545 MW; 29AFFF05214212B0 CRC64;
MMKPMKMVMS VARRGLSTTA SRSLAAQQMT VRDALNSALD EEMARDERVF ILGEEVAQYD
GAYKVSRGLW KKYGDKRVID TPITEMGFAG IAVGAAMAGL RPVCEFMTFN FSMQAIDQGS
LLKPTLSNST SMRLMHSYNG LTRSNNIPIY AVVRPQINPL PIGDVLNKKQ IGDPTKQNWL
DEIGDILNEI NQIRAPTVGK TDKMEAARMI VVRRRKMKKH KLKKLRRKMK FEWAKVRQRR
EMRKEKAFQA KLIAQIKDAE AFNAEKFVAD KLQKAKETPL PRYWKGRRLP AFIIKEKLET
QLLVINSAAK TFYMSAGQVN VPIVFRGPNG AAMGVGAQHS QCFAAWYAHC PGLKVISPYD
SEDARGLLKA AIRDPDPVVF LENEVLYGSS YPIDPKVLDK DFVLPIGKAK IMKPGKNITI
VAHSRAVEIS LQAAAELAKK GIDAEVINLR SIRPLDVETI FNSVRKTHHL ITVEQGWPQS
GVGSEICARV MEDETFFHLD APVWRVCGVD VPMPYAKTLE ANALPQPKDV IEAATKILGG
KK
//
