ID A0A367Y863_9MICO Unreviewed; 702 AA.
AC A0A367Y863;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
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:RCK61800.1};
GN ORFNames=DTO57_04060 {ECO:0000313|EMBL:RCK61800.1};
OS Microbacterium sorbitolivorans.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1867410 {ECO:0000313|EMBL:RCK61800.1, ECO:0000313|Proteomes:UP000253508};
RN [1] {ECO:0000313|EMBL:RCK61800.1, ECO:0000313|Proteomes:UP000253508}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C1.15228 {ECO:0000313|EMBL:RCK61800.1,
RC ECO:0000313|Proteomes:UP000253508};
RA An D.;
RT "Microbacterium endoborsara sp. nov., a novel actinobacterium isolated from
RT Borszczowia aralocaspica.";
RL Submitted (JUL-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:RCK61800.1}.
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DR EMBL; QORO01000001; RCK61800.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A367Y863; -.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000253508; 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; 3.
DR Gene3D; 2.40.50.100; -; 3.
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; 3.
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; 3.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 3.
DR PROSITE; PS00189; LIPOYL; 3.
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:UP000253508};
KW Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:RCK61800.1}.
FT DOMAIN 2..77
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 118..193
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 240..315
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 399..436
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 80..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 330..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 702 AA; 69675 MW; 70C082DBAD172F92 CRC64;
MSTSVVLPAL GESVTEGTVT RWLKQVGDTV EVDEPLLEVS TDKVDTEIPS PVSGVLEAIF
ADEDETIEVG AQLAIVGDGS GATAAPAAPA AEPAAAPEAP AQEAAPAAAP APAASGDATD
VTLPELGESV TEGTVTRWLK QVGDTIEVDE PLLEISTDKV DTEVPSPVAG TVLELLAAED
DTVEIGAVLA RIGSGAASAP AAPAAAPAAP AAAPAAEAPA PEAAPAAAAP APAAAASGDA
TDVTLPELGE SVTEGTVTRL LKQVGDTIEV DEALIEISTD KVDTEVPSPV AGTIIELLVG
EDDTVEIGAV LARIGSGTPA AAPAAAPAAP APAAAPAPAA APAPAAAPAA PAPAAAPTPA
AAPAPAAAPA AAAAPAPAAA PAPDAAPAAA STDASGKTYV TPLVRKIAAQ NGVDLATVTG
TGVGGRIRKE DVLAAAKAPA AAAPAAAPAA APAAAAPATA LETSPLRGTT QPMSRLRKVV
ASRAVESLNT TAQLTTIVEV DVTKLSQFRD QYKNDFLAKT GQKLSFLSFF SLAAVEALKA
YPIINSTVDG DNIVYPDHEN LSIAVDTPKG LYTPVLRDAS SKSIAEIAAG IADLAARTRD
SKLKPDDLAG GTFTITNTGS RGALFDTPLV FLPQSAILGT GIVYKRPGVT KVDGIDAIGV
RSYVYLALSY DHRTIDGADA ARYLSAVKNR LEEANFTANL GM
//
