ID T0G6A4_9SPHN Unreviewed; 415 AA.
AC T0G6A4;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
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=L286_20140 {ECO:0000313|EMBL:EQA99245.1};
OS Sphingobium sp. HDIP04.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=428994 {ECO:0000313|EMBL:EQA99245.1, ECO:0000313|Proteomes:UP000015528};
RN [1] {ECO:0000313|EMBL:EQA99245.1, ECO:0000313|Proteomes:UP000015528}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HDIP04 {ECO:0000313|EMBL:EQA99245.1,
RC ECO:0000313|Proteomes:UP000015528};
RX PubMed=24051321;
RA Mukherjee U., Kumar R., Mahato N.K., Khurana J.P., Lal R.;
RT "Draft Genome Sequence of Sphingobium sp. Strain HDIPO4, an Avid Degrader
RT of Hexachlorocyclohexane.";
RL Genome Announc. 1:e00749-e00713(2013).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EQA99245.1}.
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DR EMBL; ATDO01000125; EQA99245.1; -; Genomic_DNA.
DR RefSeq; WP_020818911.1; NZ_ATDO01000125.1.
DR AlphaFoldDB; T0G6A4; -.
DR PATRIC; fig|428994.3.peg.3863; -.
DR Proteomes; UP000015528; 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 133..168
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 79..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 415 AA; 44609 MW; C91104F4C133952F CRC64;
MALFTFRLPD IGEGIAEAEI VGWHVKVGDR VEEDQPIADM MTDKATVEME SPVAGTVVRL
AGEPGQQIAI GSMLVEIETE GEGETPAPTS LLPSGEGPGV GGERSELAPA FEEQPAPPEA
TPDPSLREKG EVLASPAVRA RAKQLGIDLA QVKPSGDHIR HSDLDAFLLY GAGQGYRPAG
RSAMRADEEV KVIGLRRRIA ENMAASKRAI PHFSYVEEID VTALEETREQ LNAHRGERPK
LTLLPLLIVA ICRALPDFPM LNARYDDEAG VVTRHGAVHM GIATQTDAGL MVPVIRDAQD
RNVWQLAAEI KRLADAVRAG KARSDELSGS TLTLTSLGPL GGVATTPVIN RPEVAIIGPN
RIVERPVFRG KEVVPAKLMN LSISCDHRVV DGWDAASFVQ AVRKLLETPV LLFAD
//
