ID A8TWB8_9PROT Unreviewed; 433 AA.
AC A8TWB8;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 75.
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=BAL199_28360 {ECO:0000313|EMBL:EDP63312.1};
OS alpha proteobacterium BAL199.
OC Bacteria; Pseudomonadota; Alphaproteobacteria.
OX NCBI_TaxID=331869 {ECO:0000313|EMBL:EDP63312.1, ECO:0000313|Proteomes:UP000003417};
RN [1] {ECO:0000313|EMBL:EDP63312.1, ECO:0000313|Proteomes:UP000003417}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BAL199 {ECO:0000313|EMBL:EDP63312.1,
RC ECO:0000313|Proteomes:UP000003417};
RA Hagstrom A., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (OCT-2007) 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}.
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:EDP63312.1}.
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DR EMBL; ABHC01000015; EDP63312.1; -; Genomic_DNA.
DR AlphaFoldDB; A8TWB8; -.
DR STRING; 331869.BAL199_28360; -.
DR eggNOG; COG0508; Bacteria.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000003417; 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 Reference proteome {ECO:0000313|Proteomes:UP000003417};
KW Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:EDP63312.1}.
FT DOMAIN 3..78
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 141..178
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 88..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..110
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 433 AA; 45930 MW; 5E57D9B6C628BAF0 CRC64;
MAEHVIKLPD VGEGVAEAEV VEWNVKVGDI VQEDAILASV MTDKAAVEIP SPVAGTVSWL
GAEVGESLAV GSPLVKIEIA GDAPVPVDEE LSAESDGPPP PAPMPSRSKP VATPAPRAKT
TAASMAQPQA GMPRREGEKP SASPAVRKRA RDAGIDLRQV RGSGPAGRIN HEDLEAFIEA
GPLAAAGTAL RADTSVNDVK VVGLRRKIAE KMALSKSRIA HITYVDEVDV TALEDLRAQL
NRQKQDTQPK LTLLPFLMRA MVKAIADQPA MNAHYDDDAG VIHQFGGVHI GIAAQTPNGL
VVPVVKHAEA RDIWSCGSEM NRLAEVAKAG TASRDELSGS TITITSLGAM GGLVTTPVIN
HPEVAIVGVN KIQVRPVWDG SQFVPRKMMN LSSSFDHRVI DGWDAAVFVQ RIKSLLEAPA
MIFMSDHLYK STS
//
