ID A0A2N0YY43_9BACI Unreviewed; 428 AA.
AC A0A2N0YY43;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=CWS01_18695 {ECO:0000313|EMBL:PKG22172.1};
OS Niallia nealsonii.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Niallia.
OX NCBI_TaxID=115979 {ECO:0000313|EMBL:PKG22172.1, ECO:0000313|Proteomes:UP000233375};
RN [1] {ECO:0000313|EMBL:PKG22172.1, ECO:0000313|Proteomes:UP000233375}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FO-92 {ECO:0000313|EMBL:PKG22172.1,
RC ECO:0000313|Proteomes:UP000233375};
RX PubMed=12656168; DOI=10.1099/ijs.0.02311-0;
RA Venkateswaran K., Kempf M., Chen F., Satomi M., Nicholson W., Kern R.;
RT "Bacillus nealsonii sp. nov., isolated from a spacecraft-assembly facility,
RT whose spores are gamma-radiation resistant.";
RL Int. J. Syst. Evol. Microbiol. 53:165-172(2003).
CC -!- COFACTOR:
CC Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC Evidence={ECO:0000256|ARBA:ARBA00001938,
CC ECO:0000256|RuleBase:RU003423};
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:PKG22172.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; PISE01000046; PKG22172.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N0YY43; -.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000233375; 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|ARBA:ARBA00023315,
KW ECO:0000256|RuleBase:RU003423};
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW Reference proteome {ECO:0000313|Proteomes:UP000233375};
KW Transferase {ECO:0000256|RuleBase:RU003423}.
FT DOMAIN 2..77
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 123..160
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 84..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..104
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 428 AA; 45765 MW; EABFC48C668651F0 CRC64;
MAFQFRLPDI GEGIHEGEIV KWFVKPGDKV QEDDVLCEVQ NDKAVVEIPS PVEGTVEEVL
VDEGTVAIVG DVLITFDAPG YENLQFKGDH GDEAPKEEAK TEAPAAEQTQ EAAVEVDPSK
RIIAMPSVRK YAREKGVDIQ AVTGTGKNGR IGKEDIDAFL NGGAQPAAEA APVAQAQPAA
ETASAPQAVA IPEGDFPETR EKMSGIRKAI AKAMVNSKHT APHVTLMDEI EVSKLVAHRK
KFKDVAAAKG IKLTFLPYVV KALTSALKEF PALNTSLDDA TSEIVHKHYY NIGIAADTEK
GLLVPVVKNA DRKGIFNISN EINELAGKAR DGKLAPNEMK GASCTISNIG SAGGQWFTPV
INHPEVAILG IGRIAEKAIV KDGEIVAAPV LALSLSFDHR MIDGATAQNA MNHIKRLLND
PELLLMEA
//
