ID A0A0C2VAC4_9BACL Unreviewed; 434 AA.
AC A0A0C2VAC4;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
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=KR50_25970 {ECO:0000313|EMBL:KIL45922.1};
OS Jeotgalibacillus campisalis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Jeotgalibacillus.
OX NCBI_TaxID=220754 {ECO:0000313|EMBL:KIL45922.1, ECO:0000313|Proteomes:UP000031972};
RN [1] {ECO:0000313|EMBL:KIL45922.1, ECO:0000313|Proteomes:UP000031972}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SF-57 {ECO:0000313|EMBL:KIL45922.1,
RC ECO:0000313|Proteomes:UP000031972};
RA Goh K.M., Chan K.-G., Yaakop A.S., Ee R., Gan H.M., Chan C.S.;
RT "Jeotgalibacillus campisalis genome sequencing.";
RL Submitted (JAN-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:KIL45922.1}.
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DR EMBL; JXRR01000017; KIL45922.1; -; Genomic_DNA.
DR RefSeq; WP_041059130.1; NZ_JXRR01000017.1.
DR AlphaFoldDB; A0A0C2VAC4; -.
DR PATRIC; fig|220754.4.peg.2612; -.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000031972; 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:UP000031972};
KW Transferase {ECO:0000256|RuleBase:RU003423}.
FT DOMAIN 3..78
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 121..158
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 78..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 155..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..99
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..122
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 166..180
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 434 AA; 47632 MW; 7E315019C3FF9DE3 CRC64;
MAIEKMTMPQ LGESVTEGTI EKWLVSPGDH VNKYDPIAEV NTDKVNAEVP SSFTGVMKDL
LVKEGETLEV GEEICTIEVE GGESSEKPSD SENESKDEKQ SSPSSANVKS DQPKEKSSNA
RYSPAVLRLS QEHDIDLMQV NGSGKEGRIT RKDLQKLIDS GGIPQKNESE VRERKEQQTA
SKSSESTIPA KTAQPAISAS PGDIEIPVTG VRKAIAANML KSKHEAPHAW TMMEVDVTNL
VSFRDAMKAD FKTKEGFNLT YFAFFVKAIA QALKEFPQMN SMWAGDKIIQ KKDINISIAV
ATEDALFVPV IKHADEKTIK GIGREINELA QKVRAGKLKS EEMQGGTFTV NNTGSFGSVQ
SMGIINHPQA AILQVESIVK RPVVMDHGMI GVRDMVNLCL SLDHRVLDGL ICGRFLQRVK
QILENISDEN TSVY
//
