ID K9ATY1_9MICO Unreviewed; 510 AA.
AC K9ATY1;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 27-MAR-2024, entry version 37.
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=C272_12502 {ECO:0000313|EMBL:EKU46072.1};
OS Brevibacterium casei S18.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Brevibacteriaceae;
OC Brevibacterium.
OX NCBI_TaxID=1229781 {ECO:0000313|EMBL:EKU46072.1, ECO:0000313|Proteomes:UP000009879};
RN [1] {ECO:0000313|EMBL:EKU46072.1, ECO:0000313|Proteomes:UP000009879}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S18 {ECO:0000313|EMBL:EKU46072.1,
RC ECO:0000313|Proteomes:UP000009879};
RA Sharma R., Singh A., Jangir P.K.;
RT "Genome Sequence of Brevibacterium casei S18.";
RL Submitted (SEP-2012) 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:EKU46072.1}.
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DR EMBL; AMSP01000011; EKU46072.1; -; Genomic_DNA.
DR AlphaFoldDB; K9ATY1; -.
DR PATRIC; fig|1229781.4.peg.2508; -.
DR eggNOG; COG0508; Bacteria.
DR Proteomes; UP000009879; 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:UP000009879};
KW Transferase {ECO:0000256|RuleBase:RU003423}.
FT DOMAIN 6..81
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 215..252
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 86..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..216
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 510 AA; 51715 MW; CB3B402C42306523 CRC64;
MTSAGARDFI LPDLGEGLTE AELISWKVAV GDTVHVDQMV VEVESAKSVV ELPCPFAGTV
VALHAEAGDT VEAGQALLSV AEAGAEAGGS PAGAGGSAAA AGGSSAAAGT GAEEDPTEPP
AADDAEDPVG VEGGGANLIG YGASEPKARS GKKRTFGGKR SAGSGSSAET SNAGNSSAAA
TAPETATTPA PAQSASATTQ PAAPAAPSSP TTSPVTSPIV RRLAQEHGLS AKHLTGTGPG
GVVTRADVLA AIETGTTTDL TSSTAGQPAA SATASTVEIT DRDTRTPITG LRKVVSERLT
QSRNEIPEAT IWLDVDATEL LRTKKALEAR TGEKYSLLAL VARFVIAGLK QYPILNSSID
TAANEIVTHG DINLGLAAQT PRGLMVPVVH GAGEMNLRQL RDSIVDTVGK ASTGKFAASE
LSGGTFTLNN YGVFGVDGSA PIINLPEVAM LGLGRIKDRP WVVDGELTVR KVMYLSFVFD
HRACDGAEPS EFLTFVADCI ENPISLLPEV
//
