ID E5WID1_9BACI Unreviewed; 439 AA.
AC E5WID1;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 55.
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=HMPREF1013_02213 {ECO:0000313|EMBL:EFV77498.1};
OS Bacillus sp. 2_A_57_CT2.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=665959 {ECO:0000313|EMBL:EFV77498.1, ECO:0000313|Proteomes:UP000003283};
RN [1] {ECO:0000313|EMBL:EFV77498.1, ECO:0000313|Proteomes:UP000003283}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2_A_57_CT2 {ECO:0000313|EMBL:EFV77498.1,
RC ECO:0000313|Proteomes:UP000003283};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J.,
RA Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Brown A.,
RA Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Howarth C.,
RA Larson L., Lui A., MacDonald P.J.P., Mehta T., Montmayeur A., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., White J., Yandava C., Nusbaum C., Birren B.;
RT "The Genome Sequence of Bacillus sp. strain 2_A_57_CT2.";
RL Submitted (DEC-2010) 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:EFV77498.1}.
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DR EMBL; ACWD01000032; EFV77498.1; -; Genomic_DNA.
DR RefSeq; WP_009332876.1; NZ_GL635752.1.
DR AlphaFoldDB; E5WID1; -.
DR eggNOG; COG0508; Bacteria.
DR HOGENOM; CLU_016733_10_1_9; -.
DR Proteomes; UP000003283; 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:UP000003283};
KW Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:EFV77498.1}.
FT DOMAIN 3..78
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 124..161
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 81..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 169..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 439 AA; 46807 MW; E2BF836634C7F5D5 CRC64;
MAIEQIKMPQ LGESVTEGTI SKWLVSVGDK VNKYDPLAEV MTDKVNAEVP SSFSGVIKEL
VAEEGETYEV GQVILTIETE GGGEAAQEAP SESKAEDKAE AAPSGVAPSA PAAPISADAP
KGVRYSPAVL KLSQEHGIDL NQVTGTGGGG RITRKDLMKI IESGDIPTAA AAASAPAPEK
TEAPAPAPSQ PAQKQAAPAP NVPVMPGDVE IPVTGVRKAI AANMLRSKHE APHAWTMKEV
DVTNLVEYRN SIKGEFKQKE GFNLTFFAFF VKAVAQALKE FPQINSMWAG DKIIQKKDIN
ISIAVATDDA LFVPVIKAAD EKTIKGIARE INDLALKVRT GKLTSAEMQG GTFTVNNTGS
FGSVQSMGII NYPQAAILQV ESIVKRPVVM NNGMIAVRDM VNLCMSLDHR VLDGLVCGRF
LQRVKEILEN TSKENTTIY
//
