ID A0A372GNJ2_9ACTN Unreviewed; 391 AA.
AC A0A372GNJ2;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
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=D0T12_08680 {ECO:0000313|EMBL:RFS86623.1};
OS Actinomadura spongiicola.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Thermomonosporaceae; Actinomadura.
OX NCBI_TaxID=2303421 {ECO:0000313|EMBL:RFS86623.1, ECO:0000313|Proteomes:UP000262882};
RN [1] {ECO:0000313|EMBL:RFS86623.1, ECO:0000313|Proteomes:UP000262882}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LHW52907 {ECO:0000313|EMBL:RFS86623.1,
RC ECO:0000313|Proteomes:UP000262882};
RA Li L., Lin H.W.;
RT "Actinomadura spongicola sp. nov., isolated from marine sponge Leucetta
RT chagosensis.";
RL Submitted (AUG-2018) 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:RFS86623.1}.
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DR EMBL; QVNQ01000002; RFS86623.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A372GNJ2; -.
DR OrthoDB; 3681540at2; -.
DR Proteomes; UP000262882; Unassembled WGS sequence.
DR GO; GO:0004742; F:dihydrolipoyllysine-residue acetyltransferase activity; IEA:RHEA.
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 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; 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 SUPFAM; SSF52777; CoA-dependent acyltransferases; 1.
DR SUPFAM; SSF51230; Single hybrid motif; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS00189; LIPOYL; 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:RFS86623.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000262882};
KW Transferase {ECO:0000256|RuleBase:RU003423}.
FT DOMAIN 1..75
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT REGION 70..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 372..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 391 AA; 41165 MW; B321C47B76F6E95E CRC64;
MTEIRVPKLN NNDSAYTLVG WLVDDGDTVD ADTPVVELET SKAVEELCSP DAGVVRHLVP
AGGECAPGDL IGRVAAPGET EPGTPPTGTP RPDARAPRPG TSGPVITAPA RALLDELSLD
HDVVNGLDVK VVRRADVERL AAAHAPSRAD ASDGAVELSP AQRAVARTVE TSHRTIPAAY
SVIQVDVDAV LRRAAALTES LRRLVGLPEF VVCAAARLHG RFPEIFATPV DGLRLRPATA
AHVGVTIDVG RGLFVPVIAD ASSLGIAEIV EAFTGFRRTA ISGAFRERDL AGANLVVALH
QDRDIVSAVP IVFPGRLCAL SLAGTRREVR LDADGTATAH TVVNIGLAYD HRFVNGREAT
LFLQDLKDAL EDPDRLAGPD GAPTTPTETR R
//
