ID G0HE87_CORVD Unreviewed; 563 AA.
AC G0HE87;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 59.
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:AEK36479.1};
GN OrderedLocusNames=CVAR_1123 {ECO:0000313|EMBL:AEK36479.1};
OS Corynebacterium variabile (strain DSM 44702 / CIP 107183 / JCM 12073 /
OS NCIMB 30131) (Corynebacterium mooreparkense).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=858619 {ECO:0000313|EMBL:AEK36479.1, ECO:0000313|Proteomes:UP000006659};
RN [1] {ECO:0000313|EMBL:AEK36479.1, ECO:0000313|Proteomes:UP000006659}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44702 / JCM 12073 / NCIMB 30131
RC {ECO:0000313|Proteomes:UP000006659};
RX PubMed=22053731; DOI=10.1186/1471-2164-12-545;
RA Schroeder J., Maus I., Trost E., Tauch A.;
RT "Complete genome sequence of Corynebacterium variabile DSM 44702 isolated
RT from the surface of smear-ripened cheeses and insights into cheese ripening
RT and flavor generation.";
RL BMC Genomics 12:545-545(2011).
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; CP002917; AEK36479.1; -; Genomic_DNA.
DR RefSeq; WP_014009665.1; NC_015859.1.
DR AlphaFoldDB; G0HE87; -.
DR STRING; 858619.CVAR_1123; -.
DR KEGG; cva:CVAR_1123; -.
DR eggNOG; COG0508; Bacteria.
DR HOGENOM; CLU_016733_10_1_11; -.
DR Proteomes; UP000006659; Chromosome.
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; 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; 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|RuleBase:RU003423,
KW ECO:0000313|EMBL:AEK36479.1};
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:AEK36479.1}.
FT DOMAIN 2..77
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 122..197
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 262..299
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 78..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 199..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..251
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 563 AA; 58952 MW; 216B49D3B9573DBB CRC64;
MAYSVEMPEL GESVTEGTVT QWLKKVGDTV AADEPLLEVS TDKVDTEIPS PAAGVLLEIK
AEEDDTVDVG AVIAVIGEEG ESAGDTGSSA PEAPAEKAEE PADEAPAEEK TGSAAPAASG
DATDVKMPEL GESVTEGTVT NWLKKVGDTV DVDEPLLEVS TDKVDTEVPS PVAGTLVEIL
ADEDDTVDVG AVIARIGDGS AAAAPAEKKA DPKPEPEEET KQEPKAEEKP APKAEPEPKK
EAPKAEAKAE PKSEPAAGNL PYVTPLVRKL AEKHGVDLST VTGSGVGGRI RKQDVLAAAE
AGSTGTEAAP AAVVLKGSDP AKASLRGTTA KVNRIRAITA KTTLESLHGA AQLTQVHEVD
MTRVAELRKS SKAVFQDKYG VNLTYLPFFA KAVVEALLAH PNVNASYNAE TQEMTYHDSV
NLSFAVDTPE GLISPVVHNA QDLSLPELAQ AIVDIADRAR NKKLKPNDIM GGTFTITNIG
SEGALTDTPI LVPPQAAMLG TGAIVKRPVV ISEDGQDAIS IRQMVFLPMT YDHQVIDGAD
AGRFLTSIKD RLENYDFTGD LAL
//
