ID A0A127NWW9_9CORY Unreviewed; 681 AA.
AC A0A127NWW9;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
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:AMO89937.1};
GN ORFNames=WM42_2240 {ECO:0000313|EMBL:AMO89937.1};
OS Corynebacterium simulans.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=146827 {ECO:0000313|EMBL:AMO89937.1, ECO:0000313|Proteomes:UP000074804};
RN [1] {ECO:0000313|EMBL:AMO89937.1, ECO:0000313|Proteomes:UP000074804}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PES1 {ECO:0000313|EMBL:AMO89937.1,
RC ECO:0000313|Proteomes:UP000074804};
RX PubMed=26861018;
RG NISC Comparative Sequencing Program;
RA Tsai Y.C., Conlan S., Deming C., Segre J.A., Kong H.H., Korlach J., Oh J.;
RT "Resolving the Complexity of Human Skin Metagenomes Using Single-Molecule
RT Sequencing.";
RL MBio 7:e01948-15(2016).
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}.
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DR EMBL; CP014634; AMO89937.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A127NWW9; -.
DR STRING; 146827.WM42_2240; -.
DR KEGG; csp:WM42_2240; -.
DR PATRIC; fig|146827.5.peg.2208; -.
DR Proteomes; UP000074804; Chromosome.
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; 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; 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|RuleBase:RU003423,
KW ECO:0000313|EMBL:AMO89937.1};
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:AMO89937.1}.
FT DOMAIN 1..71
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 114..189
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 234..309
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 374..411
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 66..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 189..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 309..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 411..440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..106
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 199..226
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 319..350
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 353..371
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 681 AA; 71813 MW; F67D1B552C827C45 CRC64;
MPELGESVTE GTITQWLKSV GDTVEVDEPL LEVSTDKVDT EIPSPVAGTI LEIKADEDDD
VEVGSVIAII GDEGESASDS SAEKPAEEKE EAKEEPKAEE KKEEASAPAA SGSATDVAMP
ELGESVTEGT ITQWLKSVGD TVEVDEPLLE VSTDKVDTEI PSPVAGTLTE ILADEDDTVD
VGAIIARIGD GNAAPAASSE KEEAKEEPKA EEKAEPKAEE KKEEASAPAA SGSATDVAMP
ELGESVTEGT ITQWLKSVGD TVEVDEPLLE VSTDKVDTEI PSPVAGTLTE ILADEDDTVD
VGAIIARIGD GNAAPAASSE KEEAKEEPKA EEKAEPKAEE KKEEPKAEKS ADASSTPAAS
EGSSKINNGD NVPYVTPLVR KLAEKHGVDL STVSGTGVGG RIRKQDVLAA AGEGEAPAAS
AAGSSNPRAR WSTKSVDPEK QELIGTTQKV NRIREITAAK MVEALQISAQ LTHVQEVDMT
AIWDMRKKSK QAFIDKHGAN LSFLPFIVKA TVEALVSHPN VNASYNPETK EMTYHADVNV
AIAVDTPRGL LTPVIHKAQD MSLPEIAKAI AELADKARNN KLKPNDLTGA TFTVTNIGSE
GALLDTPILV PPQAGILGTA AITKRAVVVN ENGQDAIAIR QMCYLPFTYD HQVVDGADAG
RFITTIKDRL ETADFEADLE V
//
