ID A0A3G9IZU5_9ACTN Unreviewed; 430 AA.
AC A0A3G9IZU5;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
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:BBH17873.1};
GN ORFNames=Back2_21600 {ECO:0000313|EMBL:BBH17873.1};
OS Nocardioides baekrokdamisoli.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=1804624 {ECO:0000313|EMBL:BBH17873.1, ECO:0000313|Proteomes:UP000271573};
RN [1] {ECO:0000313|EMBL:BBH17873.1, ECO:0000313|Proteomes:UP000271573}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 39748 {ECO:0000313|EMBL:BBH17873.1,
RC ECO:0000313|Proteomes:UP000271573};
RA Kang S.W., Lee K.C., Kim K.K., Kim J.S., Kim D.S., Ko S.H., Yang S.H.,
RA Shin Y.K., Lee J.S.;
RT "Complete genome sequence of Nocardioides baekrokdamisoli strain KCTC
RT 39748.";
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall
CC conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple
CC copies of three enzymatic components: pyruvate dehydrogenase (E1),
CC dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase
CC (E3). {ECO:0000256|ARBA:ARBA00025211}.
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; AP019307; BBH17873.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3G9IZU5; -.
DR KEGG; nbe:Back2_21600; -.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000271573; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0004742; F:dihydrolipoyllysine-residue acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
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 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; IPR036625; E3-bd_dom_sf.
DR InterPro; IPR004167; PSBD.
DR InterPro; IPR011053; Single_hybrid_motif.
DR PANTHER; PTHR43178; DIHYDROLIPOAMIDE ACETYLTRANSFERASE COMPONENT OF PYRUVATE DEHYDROGENASE COMPLEX; 1.
DR PANTHER; PTHR43178:SF2; DIHYDROLIPOYLLYSINE-RESIDUE ACETYLTRANSFERASE COMPONENT OF PYRUVATE DEHYDROGENASE COMPLEX; 1.
DR Pfam; PF00198; 2-oxoacid_dh; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
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; 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:RU003423};
KW Glycolysis {ECO:0000256|ARBA:ARBA00023152};
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW Pyruvate {ECO:0000313|EMBL:BBH17873.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000271573};
KW Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:BBH17873.1}.
FT DOMAIN 1..74
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 140..177
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 76..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..130
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 430 AA; 45400 MW; F112DCA3605E5E45 CRC64;
MDIKVPDLGN FTDVAVIEIF VEPGQVVAAE DPLVTLETDK ATMDIPAPFA GTITSLTVKL
GDKLNKGDLI AIGEPEEATE SPAASEGAPA SAVVSDEARR SLGEDAPTSE RSEQGARGGA
TATRATSETA VDAGDTDGLR ATPLVRRLAR DLEINLDGVS GSGGRGRVTK QDVLTAYDTS
RGASGGGSGI PPIPAVDFSQ FGPIHEVPLS RIKKISGPYL HRSWLNIPHV THNDEADITD
LDAYRRELDE AAKAEGYRVT LLSFLLKAAA ASLRKFPEVN SSLSGDNLIL KDYVHIGVAV
DTEGGLVVPV IRDVDRKGIT ELSHELADLS SRAREGKLSG AEMQGASFTI SSLGGIGGTS
FTPIVNAPEV AILGVVRSKM APVWDGEAFV PRLMLPLSLS YDHRVIDGAL AARFVAHFGR
IVEDVRRLVL
//
