ID A0A0S2DMA8_LYSEN Unreviewed; 455 AA.
AC A0A0S2DMA8;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=GLE_4319 {ECO:0000313|EMBL:ALN59660.1};
OS Lysobacter enzymogenes.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Lysobacter.
OX NCBI_TaxID=69 {ECO:0000313|EMBL:ALN59660.1, ECO:0000313|Proteomes:UP000061569};
RN [1] {ECO:0000313|EMBL:ALN59660.1, ECO:0000313|Proteomes:UP000061569}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C3 {ECO:0000313|EMBL:ALN59660.1,
RC ECO:0000313|Proteomes:UP000061569};
RA Kobayashi D.Y.;
RT "Genome sequences of Lysobacter enzymogenes strain C3 and Lysobacter
RT antibioticus ATCC 29479.";
RL Submitted (NOV-2015) 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; CP013140; ALN59660.1; -; Genomic_DNA.
DR RefSeq; WP_057948958.1; NZ_CP067396.1.
DR AlphaFoldDB; A0A0S2DMA8; -.
DR STRING; 69.GLE_4319; -.
DR KEGG; lez:GLE_4319; -.
DR PATRIC; fig|69.6.peg.4258; -.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000061569; 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; 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:SF12; DIHYDROLIPOAMIDE ACETYLTRANSFERASE COMPONENT OF PYRUVATE DEHYDROGENASE COMPLEX; 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:UP000061569};
KW Transferase {ECO:0000256|RuleBase:RU003423}.
FT DOMAIN 4..79
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 153..190
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 83..129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 215..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 455 AA; 46934 MW; DE251AD1D6091CDD CRC64;
MSDTKTFLLP DLGEGLPDAT IVEWAVKVGD TIRLDDTLVS METAKAVVEV PSPVSGKVLK
LAGAAGDVIV TGTMLAEFEI DPNMPQRADG QDTGHHHGGG HAAPAAAPAP AKTEEAPAKA
EGNERADSGT VVGAMQSSDA VRSEQAVAVG GVKAMPAVRA LARKLGVDLG RVRATGADGT
VSSDDVKRAA ADGSAKIGSA PAAAVAPRAA AVAEAPAPAA APARSTLSQS GRPMRTQPPG
AAVTGQPEQL KGVRRNMARV MADAHSKVVP TTLADDADIH AWLPGNDITG RLVRAIVVAC
KTVPALNAWF DGDKLTRTLH PHVDIGIAVD TDDGLFVPAL RNADVLDPRG VREAINRLRA
QVEDRSIPAS ELSGYTISLS NFGMFAGRYA TPVVVPPTVA IVAAGKGRHQ MTPVMGGFES
HKVIPLSLTF DHRACTGGEA ARFLKAMIDD LARAN
//
