ID A0A1A9GIP0_9ACTN Unreviewed; 471 AA.
AC A0A1A9GIP0;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=pdhC_1 {ECO:0000313|EMBL:ANH37493.1};
GN ORFNames=I601_1051 {ECO:0000313|EMBL:ANH37493.1};
OS Nocardioides dokdonensis FR1436.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=1300347 {ECO:0000313|EMBL:ANH37493.1, ECO:0000313|Proteomes:UP000077868};
RN [1] {ECO:0000313|EMBL:ANH37493.1, ECO:0000313|Proteomes:UP000077868}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FR1436 {ECO:0000313|EMBL:ANH37493.1,
RC ECO:0000313|Proteomes:UP000077868};
RA Kwon S.-K., Kim K., Kim J.F.;
RT "Complete genome sequence of a soil Actinobacterium, Nocardioides
RT dokdonensis FR1436.";
RL Submitted (MAR-2016) 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; CP015079; ANH37493.1; -; Genomic_DNA.
DR RefSeq; WP_068107120.1; NZ_CP015079.1.
DR AlphaFoldDB; A0A1A9GIP0; -.
DR STRING; 1300347.I601_1051; -.
DR KEGG; ndk:I601_1051; -.
DR PATRIC; fig|1300347.3.peg.1050; -.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000077868; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0016746; F:acyltransferase activity; 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; 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: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; 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; PS51826; PSBD; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003423,
KW ECO:0000313|EMBL:ANH37493.1}; Lipoyl {ECO:0000256|RuleBase:RU003423};
KW Pyruvate {ECO:0000313|EMBL:ANH37493.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000077868};
KW Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:ANH37493.1}.
FT DOMAIN 1..76
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 179..216
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 80..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 215..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..245
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 471 AA; 49668 MW; E41DFDBD8EEBE78C CRC64;
MPEYKLPDVG EGLTEAEIVT WKVKVGDVIE INDIVVEIET AKSLVELPSP YAGEVTALLV
PEGEMVPVGT PIIRIGAEEP AAPGASPATP EPEMEIDLSN PAASGGGEGE SLVGRNKADR
GPTRRARRGA AGATAANRQV QSAFEPGASP VVEEETTEEP VPARAVEAPP ASPSGARALA
KPPVRKLAKD LGVDLSTLTG SGPQGSITRD DVQAAVGDGR AATSSAEERP SRPRATGERE
TREPIKGVRK MMAQAMSQSA FTSPHVTEWV TVDVTATMAL LERLKQRREL REVRVSPLLV
LARAVVLAMR RTPEINSYWD EAAQEVVYKH YVNLGIAAAT PRGLVVPNVK DADSLSLVEL
ATALGELTAT AREGRTQPAE MSGGTFTITN VGVFGVDAGT PIINPGESAI LCFGAINKRP
WVDEATGEIV ARDVTTLALS FDHRHIDGEK GSRFLADIAG LLQDPASALL F
//
