ID A0A1Q2D4D5_9ENTE Unreviewed; 532 AA.
AC A0A1Q2D4D5;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=BW732_02740 {ECO:0000313|EMBL:AQP53256.1}, CBF34_04315
GN {ECO:0000313|EMBL:RSU04025.1};
OS Vagococcus penaei.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae; Vagococcus.
OX NCBI_TaxID=633807 {ECO:0000313|EMBL:AQP53256.1, ECO:0000313|Proteomes:UP000188246};
RN [1] {ECO:0000313|EMBL:AQP53256.1, ECO:0000313|Proteomes:UP000188246}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CD276 {ECO:0000313|EMBL:AQP53256.1,
RC ECO:0000313|Proteomes:UP000188246};
RX PubMed=19897618; DOI=10.1099/ijs.0.012872-0;
RA Jaffres E., Prevost H., Rossero A., Joffraud J.J., Dousset X.;
RT "Vagococcus penaei sp. nov., isolated from spoilage microbiota of cooked
RT shrimp (Penaeus vannamei).";
RL Int. J. Syst. Evol. Microbiol. 60:2159-2164(2010).
RN [2] {ECO:0000313|EMBL:AQP53256.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CD276 {ECO:0000313|EMBL:AQP53256.1};
RA Peterson S.W.;
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:RSU04025.1, ECO:0000313|Proteomes:UP000286995}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 24833 {ECO:0000313|EMBL:RSU04025.1,
RC ECO:0000313|Proteomes:UP000286995};
RA Gulvik C.A.;
RT "Vagococcus spp. assemblies.";
RL Submitted (MAY-2017) 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 -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00007317, ECO:0000256|RuleBase:RU003423}.
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DR EMBL; CP019609; AQP53256.1; -; Genomic_DNA.
DR EMBL; NGJV01000007; RSU04025.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q2D4D5; -.
DR STRING; 633807.BW732_02740; -.
DR KEGG; vpi:BW732_02740; -.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000188246; Chromosome.
DR Proteomes; UP000286995; 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; 2.
DR Gene3D; 2.40.50.100; -; 2.
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; 2.
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; 2.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 2.
DR PROSITE; PS00189; LIPOYL; 2.
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:UP000188246};
KW Transferase {ECO:0000256|RuleBase:RU003423}.
FT DOMAIN 2..76
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 109..183
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 220..257
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
SQ SEQUENCE 532 AA; 57694 MW; B338816674BB60E5 CRC64;
MAYIFKLPDV GEGLVEADIL QWFVKEGDFV KADDSLVEIQ NDKSTMEIPS PVSGKVIRIL
VPDGVAKVEE GIVEIETDEV ASEATQTPVD EAAPQVAPQV APQTVSSANY IFKLPDVGEG
LVEADILQWF VKEGDVVKAD DSLVEIQNDK STMEIPSPVS GTIVKILVPD GVAKVEEGIV
EIKTTDGQVT TQDFANDTVS VGTQTVASTP INATRTTNVR ALPSVRRYAR QHGVDLTGVT
PTGPNHKILK SDIDAYLSGG QTVAPKPVLE TVEATHEVKS ETVTAPKPAP ALENDNGDWV
EKMSPLRRAI AKAMVTSRTE IPHVTVFDKL RTEKLVEHRT MYKEIAKAEN VRLTYLPYVV
KAMVAMLKAY PSLNASVDMK NSTIIHRGSI NIGIATNTEH GLFVPVIKHA DRKSVFEIAQ
EISELSEKAL NNKLTKADMS HSSATITNIG GMPDAGGIWS TPIINYPESM IMGISRISDE
AVVNAEREVE VASIMRLSFA FDHRLVDGVE AQNALAVFKQ ALGDPNLMLL KN
//
