ID J1GQH9_9ACTO Unreviewed; 487 AA.
AC J1GQH9;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 49.
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=HMPREF1318_2650 {ECO:0000313|EMBL:EJF35123.1};
OS Actinomyces massiliensis F0489.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Actinomyces.
OX NCBI_TaxID=1125718 {ECO:0000313|EMBL:EJF35123.1, ECO:0000313|Proteomes:UP000002941};
RN [1] {ECO:0000313|EMBL:EJF35123.1, ECO:0000313|Proteomes:UP000002941}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0489 {ECO:0000313|EMBL:EJF35123.1,
RC ECO:0000313|Proteomes:UP000002941};
RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Nelson K.E.;
RL Submitted (MAY-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:EJF35123.1}.
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DR EMBL; AKFT01000231; EJF35123.1; -; Genomic_DNA.
DR RefSeq; WP_008734268.1; NZ_AKFT01000231.1.
DR AlphaFoldDB; J1GQH9; -.
DR PATRIC; fig|1125718.3.peg.2945; -.
DR eggNOG; COG0508; Bacteria.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000002941; 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; IPR014276; 2-oxoglutarate_DH_E2.
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 NCBIfam; TIGR02927; SucB_Actino; 1.
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 Reference proteome {ECO:0000313|Proteomes:UP000002941};
KW Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:EJF35123.1}.
FT DOMAIN 2..77
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 178..215
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 82..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..145
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 487 AA; 49366 MW; 0BEA4ECFE0EC1182 CRC64;
MSESVKMPAL GESVTEGTVS SWLKAVGDTV EVDEPLLEVA TDKVDTEVPS PVAGTILEIR
VPEDETVEVG TVLAVIGAPS EAGAPASAPA APAPAAASAP VPAPPASAPA APAPTAASAP
VPAPPTPSAA PSPAPAAPTP AAAAPTTPAP AYGKHAAPTP AEPADAAPSA AAVASAAYVT
PIVRKLARDK GIDLTTLTGT GVGGRIRKQD VEEAAKRAEA AKAAAQAAPA AAAPATPAAK
PAAGAVDTEL RGTTQKMGRL RQVIAERMIS SLQTSAQLTT VVEVDVTRVA ALRARAKNDF
LAKNGTKLTF LPFFVAAATE ALKAHPKVNA TIDDKQVTYH DVEHIGIAVD TPRGLLVPVV
KNAGDLNIPG LAKHINDLAA RTRENKVNPD ELSGSTFTIT NTGSGGALFD TPIINQPEVA
ILGLGAIQKQ PRVIKGADGN EAIAIRSVCY LALSYDHRLV DGADAARYLM TVKKRLEEGD
FAGELGL
//
