ID A0A1H3I2U6_9ACTN Unreviewed; 484 AA.
AC A0A1H3I2U6;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
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=SAMN05444365_1011100 {ECO:0000313|EMBL:SDY22021.1};
OS Micromonospora pattaloongensis.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=405436 {ECO:0000313|EMBL:SDY22021.1, ECO:0000313|Proteomes:UP000242415};
RN [1] {ECO:0000313|Proteomes:UP000242415}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45245 {ECO:0000313|Proteomes:UP000242415};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FNPH01000001; SDY22021.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H3I2U6; -.
DR STRING; 405436.SAMN05444365_1011100; -.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000242415; 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|RuleBase:RU003423};
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW Pyruvate {ECO:0000313|EMBL:SDY22021.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000242415};
KW Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:SDY22021.1}.
FT DOMAIN 4..79
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 194..231
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 141..192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 229..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 484 AA; 50095 MW; A80A10971604E4B8 CRC64;
MSRIKEFPLP DLGEGLTEGE ILSWLVKVGD TIELNQPIVE VETAKAAVEI PAKWAGQVHA
IFHPEGTTVE VGTPIIAIDT DPGAGPVGTD GAAAAGDLPT PSAASLAAVE LAPAEGAVEP
GLIGGPAPGG RTAVLVGYGP RTTAAKRRPR KTPAEPAPAP RAAGLAVTAP DRPADPPTSP
APRLPDRRTG AGVLAKPPVR KLAKDLGVDL STVTGTGPLG SITREDVQAA AAGPATGPAP
SRAVSVAPSF DGGREQRIPV KGVRKLTAEN MVASAFSAPH VTEFLTVDVT RSMKALNRLR
ALPEWRDVRV SPLLLVAKAV LLAVRRHPMV NSTWAGDEIV VKEYVNLGIA AATERGLIVP
NIKDAGRLSL RELADAMTGL VQTAKAGRTA PADMSGGTFT ITNVGVFGVD TGTPLLPPGE
SAILAFGAVR EMPWVHKGKI RARQVTTLGL SFDHRIIDGE LGSKFLRDVG AFLADPEATL
LAWT
//
