ID F8DZQ4_CORRG Unreviewed; 707 AA.
AC F8DZQ4;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 60.
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:AEI09102.1};
GN OrderedLocusNames=CRES_0746 {ECO:0000313|EMBL:AEI09102.1};
OS Corynebacterium resistens (strain DSM 45100 / JCM 12819 / GTC 2026 / SICGH
OS 158).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=662755 {ECO:0000313|EMBL:AEI09102.1, ECO:0000313|Proteomes:UP000000492};
RN [1] {ECO:0000313|EMBL:AEI09102.1, ECO:0000313|Proteomes:UP000000492}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45100 / JCM 12819 / GTC 2026 / SICGH 158
RC {ECO:0000313|Proteomes:UP000000492};
RX PubMed=22524407; DOI=10.1186/1471-2164-13-141;
RA Schroder J., Maus I., Meyer K., Wordemann S., Blom J., Jaenicke S.,
RA Schneider J., Trost E., Tauch A.;
RT "Complete genome sequence, lifestyle, and multi-drug resistance of the
RT human pathogen Corynebacterium resistens DSM 45100 isolated from blood
RT samples of a leukemia patient.";
RL BMC Genomics 13:141-141(2012).
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; CP002857; AEI09102.1; -; Genomic_DNA.
DR RefSeq; WP_013888120.1; NC_015673.1.
DR AlphaFoldDB; F8DZQ4; -.
DR STRING; 662755.CRES_0746; -.
DR KEGG; crd:CRES_0746; -.
DR eggNOG; COG0508; Bacteria.
DR HOGENOM; CLU_016733_10_1_11; -.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000000492; 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; 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:UP000000492};
KW Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:AEI09102.1}.
FT DOMAIN 2..77
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 130..205
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 261..336
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 70..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 199..277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 332..397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 442..464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..112
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..246
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 340..378
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..395
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 707 AA; 74554 MW; 2837D29974F45A49 CRC64;
MAHSVEMPEL GESVTEGTVT QWLKKVGDKV EVDEPLLEVS TDKVDTEIPS PVAGVLLKIL
ADEDDTVDVG TVIAEIGDEG EEASSDDDAK ESSDEGSAGD DASDEDAADS SAAEGADSES
SDDNAGSGEA EDVKMPELGE SVTEGTITQW LKKVGDKVEV DEPLLEVSTD KVDTEVPSPV
AGTLVEILAE EDDTVDVGEV IARVGDGSAK PSKADKKSDE GKSEDESDKA AAEDKAASKK
EDLSSDDDSE SSDDNAGSGE AEDVKMPELG ESVTEGTITQ WLKKVGDKVE VDEPLLEVST
DKVDTEVPSP VAGTLVEILA EEDDTVDVGE VIARVGDGSA KPSKADKKSD EDKSAAKDEA
NKAEDKPAEK KEDKPAKSAA ASSKPSASTN KPAEGNLPYV TPLVRKLADK HEVDLSTIKG
TGVGGRIRKQ DVLAAANGGG AATASSVAEQ SPAGPRASTH RVDLSKQDLR GTTQKVNRIR
EITAKKTLES LHSAAQLTQV HEVDMTHVAD LRKQSKADFQ KKHGVNLTYL PFFAKAIVEA
LVSHPNVNAS YNAQTREMTY HEQVNLGIAV DTPAGLLSPV IHNAQDMSLP ELAKAIVDIA
DRARNNKLKP QDLAGGTFTI TNIGSEGALT DTPILVPPQA AMVGTGAIVR RPVVLSEDGG
ESIGIRSMVF LPMTYDHQVI DGADAGRFMS TVRDRLEHGD FETDLEL
//
