ID A1CDQ6_ASPCL Unreviewed; 851 AA.
AC A1CDQ6;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 100.
DE RecName: Full=Acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU361137};
DE EC=2.3.1.12 {ECO:0000256|RuleBase:RU361137};
GN ORFNames=ACLA_007420 {ECO:0000313|EMBL:EAW11983.1};
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612 {ECO:0000313|EMBL:EAW11983.1, ECO:0000313|Proteomes:UP000006701};
RN [1] {ECO:0000313|EMBL:EAW11983.1, ECO:0000313|Proteomes:UP000006701}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1
RC {ECO:0000313|Proteomes:UP000006701};
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
CC -!- FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall
CC conversion of pyruvate to acetyl-CoA and CO(2).
CC {ECO:0000256|RuleBase:RU361137}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N(6)-[(R)-dihydrolipoyl]-L-lysyl-[protein] = CoA
CC + N(6)-[(R)-S(8)-acetyldihydrolipoyl]-L-lysyl-[protein];
CC Xref=Rhea:RHEA:17017, Rhea:RHEA-COMP:10475, Rhea:RHEA-COMP:10478,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:83100,
CC ChEBI:CHEBI:83111; EC=2.3.1.12;
CC Evidence={ECO:0000256|RuleBase:RU361137};
CC -!- COFACTOR:
CC Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC Evidence={ECO:0000256|RuleBase:RU361137};
CC Note=Binds 1 lipoyl cofactor covalently.
CC {ECO:0000256|RuleBase:RU361137};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|RuleBase:RU361137}.
CC -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00007317, ECO:0000256|RuleBase:RU361137}.
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DR EMBL; DS027051; EAW11983.1; -; Genomic_DNA.
DR RefSeq; XP_001273409.1; XM_001273408.1.
DR AlphaFoldDB; A1CDQ6; -.
DR STRING; 344612.A1CDQ6; -.
DR EnsemblFungi; EAW11983; EAW11983; ACLA_007420.
DR GeneID; 4705482; -.
DR KEGG; act:ACLA_007420; -.
DR VEuPathDB; FungiDB:ACLA_007420; -.
DR eggNOG; KOG0557; Eukaryota.
DR eggNOG; KOG3251; Eukaryota.
DR HOGENOM; CLU_016733_4_0_1; -.
DR OMA; SAAIWTH; -.
DR OrthoDB; 5483022at2759; -.
DR Proteomes; UP000006701; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0045254; C:pyruvate dehydrogenase complex; IEA:InterPro.
DR GO; GO:0004742; F:dihydrolipoyllysine-residue acetyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; IEA:InterPro.
DR CDD; cd06849; lipoyl_domain; 1.
DR CDD; cd15863; SNARE_GS27; 1.
DR Gene3D; 1.20.5.110; -; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR Gene3D; 4.10.320.10; E3-binding 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; IPR036625; E3-bd_dom_sf.
DR InterPro; IPR006257; LAT1.
DR InterPro; IPR039453; OM14_C.
DR InterPro; IPR004167; PSBD.
DR InterPro; IPR011053; Single_hybrid_motif.
DR NCBIfam; TIGR01349; PDHac_trf_mito; 1.
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 Pfam; PF17304; DUF5353; 1.
DR Pfam; PF02817; E3_binding; 1.
DR Pfam; PF12352; V-SNARE_C; 1.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 1.
DR SUPFAM; SSF47005; Peripheral subunit-binding domain of 2-oxo acid dehydrogenase complex; 1.
DR SUPFAM; SSF51230; Single hybrid motif; 1.
DR SUPFAM; SSF58038; SNARE fusion complex; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS00189; LIPOYL; 1.
DR PROSITE; PS51826; PSBD; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU361137};
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU361137};
KW Membrane {ECO:0000256|SAM:Phobius}; Pyruvate {ECO:0000313|EMBL:EAW11983.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006701};
KW Transferase {ECO:0000256|RuleBase:RU361137};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 571..591
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 830..850
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 57..133
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 201..238
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 143..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 529..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 698..746
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 154..170
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 698..717
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 723..746
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 851 AA; 92657 MW; C8D297015AE9288C CRC64;
MVASAVRMRV PSAMLSKGAL CMRRPQVVHR FKDAVQPQLP ALAALSRFYA SKSFPPHTII
SMPALSPTMS AGNIGAWQKK AGDSLVPGDV LVEIETDKAQ MDFEFQEEGV LAKVLKETGE
KDVAVGAPIA VLVEEGTDVS SFESFSLEDA GGDKGAAPAK ETKEEPKADA APAATPEPAP
EAYEPETSAD KLQPSLDREP SISPAAKALA LEKGVPVKAL KGTGRGGQIT KEDVEKYKPS
TSAAAAGPTY EDIPLTSMRK TIASRLQQSV RENPHFFVST TLSVTKLLKL RQALNASSEG
KYKLSVNDFL VKACAAALLK VPAVNSSWRE ENGQVVIRQH NAVDISVAVA TPSGLITPVV
KDVQGLGLSS ISNQIKDLGK RARENKLKPE EYQGGTFTIS NMGMNPAVER FTAVINPPQA
GILAVGTTRK VAVPVETEEG TSVEWDDQIV VTGSFDHKVV DGAIGAEWIK ELKKVVENPL
ELLLRAPNPT RTYLNETAES TASLVDVDSP HVVSVDSDFL NQEVKTTTQA ERLEREAREE
EERKERERAV EAEKAKAKAA RAGHVAKRNP VFVGNAIIYT LVGAALGYGA YRKHLEGRLS
WKLVGAWSGV VGAFGAVDYF VSNEVACHKS VLSHPNENIS ASQIAASLAS LSRTIDDYSA
LSKKELIPAK QEKAFERVKN FRAELADYRT HFDRLRKERE EAQSVTNRNE LLGRRPHHAA
TPENPYAQSS LPQSSPFANA SSSRSGLSFG ASPADFNRET HALREQSFFA NTNTQLDEFL
DRGRAVLADL GQQREVLKGT QRRLYSVANT LGISGDTIRR VERRAKQDKW IFWGGVLTFF
LFCWAVLHFL R
//
