ID A0A0L0QP89_VIRPA Unreviewed; 420 AA.
AC A0A0L0QP89;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=AFK71_18915 {ECO:0000313|EMBL:KNE20445.1};
OS Virgibacillus pantothenticus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Virgibacillus.
OX NCBI_TaxID=1473 {ECO:0000313|EMBL:KNE20445.1, ECO:0000313|Proteomes:UP000036780};
RN [1] {ECO:0000313|Proteomes:UP000036780}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 26 {ECO:0000313|Proteomes:UP000036780};
RA Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., Ge C.,
RA Shi H., Pan Z., Liu X.;
RT "Fjat-10053 dsm26.";
RL Submitted (JUL-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 -!- 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:KNE20445.1}.
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DR EMBL; LGTO01000007; KNE20445.1; -; Genomic_DNA.
DR RefSeq; WP_050353019.1; NZ_LGTO01000007.1.
DR AlphaFoldDB; A0A0L0QP89; -.
DR GeneID; 66870389; -.
DR PATRIC; fig|1473.5.peg.2523; -.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000036780; 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; 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; PS51826; PSBD; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW ECO:0000256|RuleBase:RU003423}; Lipoyl {ECO:0000256|RuleBase:RU003423};
KW Reference proteome {ECO:0000313|Proteomes:UP000036780};
KW Transferase {ECO:0000256|RuleBase:RU003423}.
FT REGION 92..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 150..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..108
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 420 AA; 46169 MW; D084B41B5FC508E9 CRC64;
MAIEKIKMPQ LGESVTEGTV SSWLVQVGDE VNKYDPIAEV LTDKVNAEVP SSYSGTIKEL
VAKEGDTIEV GELMCYIDTG GEAEAVEEER QLVSEKTEQE EAKPATDQSM KKRYSPAVLR
LAQEHDINLE QVTGTGKSGR ITRKDVEKII ASGKIPAPSK EQPDSKAEEQ VSQQPAKPSA
APKPDTYPGD VEIPVTGVRK AIAQNMVRST QEIPHAWMTV EVDVTDLVTY RNAIKDDFKA
KEGYGLTFFA FFVKAVAQAL KEFPQLNSTW AEDKIIQRKE VNISIAVAKE QELFVPVIHH
ADDKSIKGIA KQIHELAVKA RTGKLTADDM KGGTFTVNNT GSFGSIHSMG VINYPQAAIL
QVESIVKRPM IVNNMFAARD MVNLSLSLDH RILDGLICGQ FLARVKAILE QMNAQTVNVY
//
