ID A0A1B7LZC4_9MICC Unreviewed; 588 AA.
AC A0A1B7LZC4;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=A6F49_10285 {ECO:0000313|EMBL:OAV60867.1};
OS Enteractinococcus helveticum.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae.
OX NCBI_TaxID=1837282 {ECO:0000313|EMBL:OAV60867.1, ECO:0000313|Proteomes:UP000078292};
RN [1] {ECO:0000313|EMBL:OAV60867.1, ECO:0000313|Proteomes:UP000078292}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UASWS1574 {ECO:0000313|EMBL:OAV60867.1,
RC ECO:0000313|Proteomes:UP000078292};
RA Crovadore J., Chablais R., Lefort F.;
RT "First whole genome shotgun sequence of the bacterium Enteractinococcus sp.
RT strain UASWS1574.";
RL Submitted (APR-2016) 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}.
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:OAV60867.1}.
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DR EMBL; LXEY01000018; OAV60867.1; -; Genomic_DNA.
DR RefSeq; WP_043057902.1; NZ_LXEY01000018.1.
DR AlphaFoldDB; A0A1B7LZC4; -.
DR STRING; 1837282.A6F49_10285; -.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000078292; 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; IPR014276; 2-oxoglutarate_DH_E2.
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 NCBIfam; TIGR02927; SucB_Actino; 1.
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|RuleBase:RU003423};
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:OAV60867.1}.
FT DOMAIN 2..77
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 127..202
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 272..309
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 80..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 198..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 322..359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..257
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 588 AA; 61675 MW; 2DA154CEF600A774 CRC64;
MSETITLPEL GESVTEGTVT RWLKEVGDTI EVDEPIVEIS TDKVDTEIPS PVAGTVLEIL
VQEDEDIEVG QALAVIGEEG ESASDAPADD SAAEEAPVAE EPAQETTEEA PAEQASAPAS
GGGSGDAQEV TLPELGESVT EGTITRWLKE VGDEVEVDEP IVEISTDKVD TEIPSPVAGT
VLEIKVQEDE DVEVGQVLAL VGSSDGAPTA SAPEPASAPA EDAPAAEEAP AEEPAQQAAP
EPEPTPEPTP APAPAAERAP SSPEETPRGD GYVTPLVRRL AREQDVDLAE VTGTGVGGRI
RKQDVLAAAA AKEYEARQEA PAAAAPAAAA PAASRPAPKD PASSVDPSKR GTTEKAPRIR
QVIADRMIES LETSAQLTQV HEIDMTRIVN LRNQVKARFK AENGVNLTFL AFITQAATEA
LRAHPALNAE YNAETKEITY HDREDIGIAV DTERGLMVPV IKGAGNLNLS GIANAISDLA
LRTRDSKVKP DELSGGTFSI TNLGSFGALF DTPVINQPQV AILGPGNIVK RPVVSTDAEG
NDVIAIRHMM YLSLTYDHRI VDGADAGRFM TQLKNRLEGG EFGGQLGL
//
