ID A0A194PUD8_PAPXU Unreviewed; 566 AA.
AC A0A194PUD8;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU003423};
DE EC=2.3.1.- {ECO:0000256|RuleBase:RU003423};
GN ORFNames=RR46_05554 {ECO:0000313|EMBL:KPI96937.1};
OS Papilio xuthus (Asian swallowtail butterfly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC Papilionidae; Papilioninae; Papilio.
OX NCBI_TaxID=66420 {ECO:0000313|EMBL:KPI96937.1, ECO:0000313|Proteomes:UP000053268};
RN [1] {ECO:0000313|EMBL:KPI96937.1, ECO:0000313|Proteomes:UP000053268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ya'a_city_454_Px {ECO:0000313|EMBL:KPI96937.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KPI96937.1};
RX PubMed=26354079; DOI=10.1038/ncomms9212;
RA Li X., Fan D., Zhang W., Liu G., Zhang L., Zhao L., Fang X., Chen L.,
RA Dong Y., Chen Y., Ding Y., Zhao R., Feng M., Zhu Y., Feng Y., Jiang X.,
RA Zhu D., Xiang H., Feng X., Li S., Wang J., Zhang G., Kronforst M.R.,
RA Wang W.;
RT "Outbred genome sequencing and CRISPR/Cas9 gene editing in butterflies.";
RL Nat. Commun. 6:8212-8212(2015).
CC -!- COFACTOR:
CC Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC Evidence={ECO:0000256|ARBA:ARBA00001938,
CC ECO:0000256|RuleBase:RU003423};
CC -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00007317, ECO:0000256|RuleBase:RU003423}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KQ459591; KPI96937.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A194PUD8; -.
DR STRING; 66420.A0A194PUD8; -.
DR Proteomes; UP000053268; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0045254; C:pyruvate dehydrogenase complex; IEA:InterPro.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; IEA:InterPro.
DR CDD; cd06849; lipoyl_domain; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR InterPro; IPR003016; 2-oxoA_DH_lipoyl-BS.
DR InterPro; IPR001078; 2-oxoacid_DH_actylTfrase.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR045257; E2/Pdx1.
DR InterPro; IPR011053; Single_hybrid_motif.
DR PANTHER; PTHR23151; DIHYDROLIPOAMIDE ACETYL/SUCCINYL-TRANSFERASE-RELATED; 1.
DR PANTHER; PTHR23151:SF90; DIHYDROLIPOYLLYSINE-RESIDUE ACETYLTRANSFERASE COMPONENT OF PYRUVATE DEHYDROGENASE COMPLEX, MITOCHONDRIAL; 1.
DR Pfam; PF00198; 2-oxoacid_dh; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 1.
DR SUPFAM; SSF51230; Single hybrid motif; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS00189; LIPOYL; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003423};
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW Membrane {ECO:0000256|SAM:Phobius}; Pyruvate {ECO:0000313|EMBL:KPI96937.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053268};
KW Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:KPI96937.1};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 162..180
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 68..144
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT REGION 231..253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..253
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 566 AA; 62494 MW; BF31E8E562BA6AA8 CRC64;
MLRTIIVRNQ VLSESLKKAV RVNLTRCMTT ELIRRKSSNK FINSESKSGL LALQWRPQIR
YYSDLPSHNK VNLPALSPTM ESGSIVRWEK KEGDKLGEGD LLCEIETDKA TMGFETPEEG
YLAKFLIPEG TKGVPVGKLL CIIVENQADV AAFKDFKDDC MYLFLFICDF FFICMGVIYM
KTVNSFAMIM LVVRNNQCKQ DNKNCYNLGK ALVIQQERLR NQRPPKLRMR LRQHPLRLRP
PPPPPRPLVP QPLQPPRLLQ PPLLLKAEYT PVPWPADWLN SETYDLEVSL PIQGSGLYGS
LKSGDLAGAA PLAAAGAVAA PAFASAPAPA PGAAFLDIPL SGMRETIAKR LSAAKQTIPH
YQLSATVNIE KTLKMRKDIN ERLAKEEPGL KISVNDFIVK AVASACKRVP TANSHWMESF
IRQFSNVDVS VAVATPTGLI TPIVFNADSR GVIDISKTVK ELAQKAKDGK LQPQEYQGGT
VTVSNLGMYG ITMFNAIINP PQSLILACGG LQELVIPDKN EPQGFRVAKF VTFTASADHR
VIDGAVGAQW MKALKDNLED PANMIL
//
