ID A0A373DIL6_9MICO Unreviewed; 583 AA.
AC A0A373DIL6;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU003423};
DE EC=2.3.1.- {ECO:0000256|RuleBase:RU003423};
GN Name=sucB {ECO:0000313|EMBL:RGE19628.1};
GN ORFNames=D1J51_11275 {ECO:0000313|EMBL:RGE19628.1};
OS Leucobacter sp. wl10.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Leucobacter.
OX NCBI_TaxID=2304677 {ECO:0000313|EMBL:RGE19628.1, ECO:0000313|Proteomes:UP000263010};
RN [1] {ECO:0000313|EMBL:RGE19628.1, ECO:0000313|Proteomes:UP000263010}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=wl10 {ECO:0000313|Proteomes:UP000263010};
RA Liu H.;
RT "Leucobacter sp. wl 10 isolated from wastewater.";
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:RGE19628.1}.
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DR EMBL; QWBV01000015; RGE19628.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A373DIL6; -.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000263010; 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; 2.
DR Gene3D; 2.40.50.100; -; 2.
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; PTHR43416:SF8; DIHYDROLIPOYLLYSINE-RESIDUE ACETYLTRANSFERASE COMPONENT OF PYRUVATE DEHYDROGENASE COMPLEX; 1.
DR PANTHER; PTHR43416; DIHYDROLIPOYLLYSINE-RESIDUE SUCCINYLTRANSFERASE COMPONENT OF 2-OXOGLUTARATE DEHYDROGENASE COMPLEX, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF00198; 2-oxoacid_dh; 1.
DR Pfam; PF00364; Biotin_lipoyl; 2.
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; 2.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 2.
DR PROSITE; PS00189; LIPOYL; 2.
DR PROSITE; PS51826; PSBD; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW ECO:0000256|RuleBase:RU003423};
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW Reference proteome {ECO:0000313|Proteomes:UP000263010};
KW Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:RGE19628.1}.
FT DOMAIN 2..77
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 139..214
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 285..322
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 76..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 215..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 328..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..139
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 253..273
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 583 AA; 59513 MW; CCE562A56F47C363 CRC64;
MSESVVLPAL GESVTEGTVT RWLKNVGDTV EVDEPLLEVS TDKVDTEIPS PVAGVLEEIL
VQEDETAEVG AVLARVGDGS GSGSEPAEPA ETEDEPEAEP SASSEGPAEP APAEPAPAAP
APAETSAPQA STPASGGDSQ DVVLPSLGES ITEGTVTRWL KNVGDTVEVD EPLLEISTDK
VDTEVPSPVA GVLQEILVQE DDTVEVGGAL ARIGSGAAPA EPEAAEAPVE QAAPAASAEE
APPASAEPTT PAEAPAEPEP EPEPAPAKPA APAHAEPAPA DAAGYITPIV RKLANDSGVD
LSTVTGTGVG GRIRKEDVLA AAEKAAAPAP AAAPAPAAPA EAEVSPLRGT TQKMTRLRKV
IAERAVASLQ GTAQLTTVVE VDVTRIAQLR QSKKDEFLAK TGSKLSFMPF FALAAAEALR
SFPIVNATVD GDSIVYPATE NISIAVDTEK GLLTPVLRDA GDKNIAQIAG EIADLAARTR
ENQLKPDELA GGTFTLTNTG SRGALFDTPL VFLPQSAILG TGAVVKKPAV VSGPEGDAIA
IRSTVYLALS YDHRIIDGAD AARFLGQLRQ RLEAGDFASD LGI
//
