ID A0A0G3GXH5_9CORY Unreviewed; 673 AA.
AC A0A0G3GXH5;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU003423};
DE EC=2.3.1.- {ECO:0000256|RuleBase:RU003423};
GN Name=aceF {ECO:0000313|EMBL:AKK03562.1};
GN ORFNames=CEPID_08560 {ECO:0000313|EMBL:AKK03562.1};
OS Corynebacterium epidermidicanis.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1050174 {ECO:0000313|EMBL:AKK03562.1, ECO:0000313|Proteomes:UP000035368};
RN [1] {ECO:0000313|EMBL:AKK03562.1, ECO:0000313|Proteomes:UP000035368}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45586 {ECO:0000313|EMBL:AKK03562.1,
RC ECO:0000313|Proteomes:UP000035368};
RA Ruckert C., Albersmeier A., Winkler A., Tauch A.;
RT "Complete genome sequence of Corynebacterium epidermidicanis DSM 45586,
RT isolated from the skin of a dog suffering from pruritus.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CP011541; AKK03562.1; -; Genomic_DNA.
DR RefSeq; WP_047240570.1; NZ_CP011541.1.
DR AlphaFoldDB; A0A0G3GXH5; -.
DR STRING; 1050174.CEPID_08560; -.
DR KEGG; cei:CEPID_08560; -.
DR PATRIC; fig|1050174.4.peg.1725; -.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000035368; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR CDD; cd06849; lipoyl_domain; 3.
DR Gene3D; 2.40.50.100; -; 3.
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; IPR014276; 2-oxoglutarate_DH_E2.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR036625; E3-bd_dom_sf.
DR InterPro; IPR004167; PSBD.
DR InterPro; IPR011053; Single_hybrid_motif.
DR NCBIfam; TIGR02927; SucB_Actino; 1.
DR PANTHER; PTHR43178; DIHYDROLIPOAMIDE ACETYLTRANSFERASE COMPONENT OF PYRUVATE DEHYDROGENASE COMPLEX; 1.
DR PANTHER; PTHR43178:SF5; LIPOAMIDE ACYLTRANSFERASE COMPONENT OF BRANCHED-CHAIN ALPHA-KETO ACID DEHYDROGENASE COMPLEX, MITOCHONDRIAL; 1.
DR Pfam; PF00198; 2-oxoacid_dh; 1.
DR Pfam; PF00364; Biotin_lipoyl; 3.
DR Pfam; PF02817; E3_binding; 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; 3.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 3.
DR PROSITE; PS00189; LIPOYL; 3.
DR PROSITE; PS51826; PSBD; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003423,
KW ECO:0000313|EMBL:AKK03562.1};
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW Reference proteome {ECO:0000313|Proteomes:UP000035368};
KW Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:AKK03562.1}.
FT DOMAIN 2..77
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 119..194
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 239..314
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 369..406
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 79..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 197..247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 319..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 408..438
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..108
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..228
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..348
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 673 AA; 71608 MW; F2765F599A19D50B CRC64;
MAFSVEMPEL GESVTEGTIT RWLKQVGDTV AADEPLLEVS TDKVDTEIPA PRAGVLTKIL
FEEDDTVDVG EVIAEIGEEG EAADSAAAEP AKEEPKAEPA KEETKEEPQA SNNAASGEAT
DVKMPELGES VTEGTITRWL KSVGDTVEVD EALLEVSTDK VDTEVPSPVA GTIVEILFDE
DDTVDVGEVI VRIGDANAQP AAKEETKAEP AKEEPKAEPA KEETKEEPQA SNNAASGEAT
DVKMPELGES VTEGTITRWL KSVGDTVEVD EALLEVSTDK VDTEVPSPVA GTIVEILFDE
DDTVDVGEVI VRIGDANAQP AAKEETKAEP AKEETKAEPA KEEPKVEVAA KVEAPKEEAA
KVDNSNAPYV TPLVRKLADK HGVDLSKVEG TGVGGRIRKQ DVLAAAGQGE APATTAAAKG
SAISTKSVDP EKAKLRGTTQ RVNRIREITA KKTLESLHSA AQLTQLHEVD MTKVAELRKQ
AKPKFVEKHG VNLTYLPFFA KAIVEALVSH PNVNASYNAE TKEMTYHAQV NLGIAVDTPA
GLLSPVIHNA QDKSLPELAK AIVDIADRAR NNKLKPNDLT GGTFTITNIG SEGALSDTPI
LVPPQAAMVG TGAIVKRPVV VTEDGNDAIA IRQMVYLPMT YDHQVVDGAD AGRFMTTVRD
RLETGNFEGD LEL
//
