ID B8KKU4_9GAMM Unreviewed; 398 AA.
AC B8KKU4;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 59.
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=NOR53_3678 {ECO:0000313|EMBL:EED31711.1};
OS gamma proteobacterium NOR5-3.
OC Bacteria; Pseudomonadota; Gammaproteobacteria.
OX NCBI_TaxID=566466 {ECO:0000313|EMBL:EED31711.1};
RN [1] {ECO:0000313|EMBL:EED31711.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NOR5-3 {ECO:0000313|EMBL:EED31711.1};
RA Amann R., Fuchs B., Ferriera S., Johnson J., Kravitz S., Beeson K.,
RA Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (SEP-2008) 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; DS999406; EED31711.1; -; Genomic_DNA.
DR AlphaFoldDB; B8KKU4; -.
DR STRING; 566466.NOR53_3678; -.
DR eggNOG; COG0508; Bacteria.
DR HOGENOM; CLU_016733_10_0_6; -.
DR Proteomes; UP000003977; 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 ECO:0000313|EMBL:EED31711.1};
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:EED31711.1}.
FT DOMAIN 1..70
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 111..148
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 79..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 398 AA; 42244 MW; C938771FEF89F885 CRC64;
MPKLAMAMNE GTIAEWLVSH GDHVEKGQAL ASIETEKVAY DVESPEAGYL HIVVEAGETV
PCETLIAYFL ATPDEEVASG TSESADEANS KVEAPAVASS VGAATKPQRI KASPLAKKIA
ADAGLNLGDI TGTGPGGRIV KRDVIAAQES QARTSHSRGG TRVLAEVPLK GMRGTIASRM
QESLQSTAQL SSNWESDITT LLAMRKSFVA REDALGTRVS FNAFLIKAMV YAIRQVPMAN
ACLENDLISV YENINMGIAI SMPGNSEYDS ALVVGVLRDV DQMGVVQIDK HMRALIERVR
SGEATADELS GSTITLSSTA GIGPPGLMST PVLNLPNVAL LGPSTPIERI VPVKGKKRIR
TMLPLSFTFD HRALDGDPAA RYMSALHDAL ENPELLLA
//
