ID A0A0W8IEQ2_9MICO Unreviewed; 513 AA.
AC A0A0W8IEQ2;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
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=AVL62_11160 {ECO:0000313|EMBL:KUG58451.1};
OS Serinicoccus chungangensis.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales;
OC Ornithinimicrobiaceae; Serinicoccus.
OX NCBI_TaxID=767452 {ECO:0000313|EMBL:KUG58451.1, ECO:0000313|Proteomes:UP000054837};
RN [1] {ECO:0000313|EMBL:KUG58451.1, ECO:0000313|Proteomes:UP000054837}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CD08_5 {ECO:0000313|EMBL:KUG58451.1,
RC ECO:0000313|Proteomes:UP000054837};
RA Chander A.M., Kaur G., Nair G.R., Dhawan D.K., Kochhar R.K., Mayilraj S.,
RA Bhadada S.K.;
RT "Serinicoccus chungangenesis strain CD08_5 genome sequencing and
RT assembly.";
RL Submitted (DEC-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:KUG58451.1}.
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DR EMBL; LQBL01000003; KUG58451.1; -; Genomic_DNA.
DR RefSeq; WP_058890128.1; NZ_LQBL01000003.1.
DR AlphaFoldDB; A0A0W8IEQ2; -.
DR STRING; 767452.AVL62_11160; -.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000054837; 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|RuleBase:RU003423};
KW Lipoyl {ECO:0000256|RuleBase:RU003423};
KW Reference proteome {ECO:0000313|Proteomes:UP000054837};
KW Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:KUG58451.1}.
FT DOMAIN 1..76
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 166..203
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 76..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 204..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..245
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 271..285
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 513 AA; 53029 MW; 37B6077A7FA9A890 CRC64;
MPEFKLPDPG EGLVEATIIQ WKVAEGDTVR TNDIVVEVET AKSLVELPIP WAGTVTKILA
AEGDEVEVGT PIVVVDDGSG EGGGGAAAAG GGAGTDVEDV TDEAAAASDD LVPSPPEDGG
SSTGSTREAM LVGYGAIEGS TTRRKRRRGA SGAEAEAASA PQRKAKASPP VRKYAKDRGV
DINEVDAAGP TGIVRRSDID AFLEGAPAGA PAPRPTPPGA ASGSSSTPPG AAGGSSSTPP
GAADGSPSTG ATGRAGEAAG VTGRSAYQRP VFDRSGEREE RTDVKGVRKM TAQAMVGSAF
TAPHVTEFVT VDVTRTMELI DRLKADRAFR DLRINPLLVL AKAMTVAVRR NPGMNAVWDE
DAQQIVQRNY VNLGIAAATP RGLVVPNIKD ADLMDLRQLA EAMTDLVATA KAGRTQPADM
SGGTITITNV GVFGIDTGTP IINPGESAIV CFGAVRRMPW VVGEGEQERI EPRWVTQLAV
SFDHRLIDGE LGSMFLADLA ALLEDPARAL AWA
//
