ID A0A1I5R9W5_9BRAD Unreviewed; 423 AA.
AC A0A1I5R9W5;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=SAMN05216330_10894 {ECO:0000313|EMBL:SFP54806.1};
OS Bradyrhizobium sp. Ghvi.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=1855319 {ECO:0000313|EMBL:SFP54806.1, ECO:0000313|Proteomes:UP000198509};
RN [1] {ECO:0000313|EMBL:SFP54806.1, ECO:0000313|Proteomes:UP000198509}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ghvi {ECO:0000313|EMBL:SFP54806.1,
RC ECO:0000313|Proteomes:UP000198509};
RA de Groot N.N.;
RL Submitted (OCT-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 -!- SUBUNIT: Forms a 24-polypeptide structural core with octahedral
CC symmetry. {ECO:0000256|ARBA:ARBA00011484}.
CC -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00007317, ECO:0000256|RuleBase:RU003423}.
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DR EMBL; FOVU01000008; SFP54806.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I5R9W5; -.
DR STRING; 1855319.SAMN05216330_10894; -.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000198509; Unassembled WGS sequence.
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; 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: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; PS00189; LIPOYL; 1.
DR PROSITE; PS51826; PSBD; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003423};
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW Transferase {ECO:0000256|RuleBase:RU003423}.
FT DOMAIN 3..78
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 139..176
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 86..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 423 AA; 45355 MW; 00720EE4BB19180B CRC64;
MAERVVRLPD VGEGIAEAEL VEWHVKVGDV VREDAVLGAV MTDKATVEIP APTDGRVTWL
AGNVGDLLAI GSDFVRLEVD GKGEPAKEQA KLASHVTAAA AKRSDPVATA PRAPASEPPD
AQGSQPSASP LHRAVERPLA APAVRLRARE AGVDLRQIRG TGPAGRITHD DLDGYLARGR
TGTTARPHPA QTAVTDIKIV GLRRKIAEKM SIANSRMPHI TYVEEVDVTA LEDLRAKVNG
QKRPGKPKLT LLPFLMRAMV RAIAELPHLN AHFDDEAGIV HQHAGVHIGI ATQTPTGLMV
PVVRHAEARD IWDCATEVAR LAEAARHGNA TRDELTGSTI TITSLGALGG LATTPIINHP
EVAIVGVNRI AIRPHWDGTA FVPRQMMNLS SSFDHRVIDG FDAAQFVQRI KLLLETPAMI
FID
//
