ID F8GNM9_CUPNN Unreviewed; 374 AA.
AC F8GNM9;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=Dihydrolipoyllysine-residue acetyltransferase component of acetoin cleaving system {ECO:0000313|EMBL:AEI79122.1};
DE EC=2.3.1.12 {ECO:0000313|EMBL:AEI79122.1};
GN Name=acoC {ECO:0000313|EMBL:AEI79122.1};
GN OrderedLocusNames=CNE_2c01310 {ECO:0000313|EMBL:AEI79122.1};
OS Cupriavidus necator (strain ATCC 43291 / DSM 13513 / CCUG 52238 / LMG 8453
OS / N-1) (Ralstonia eutropha).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=1042878 {ECO:0000313|EMBL:AEI79122.1, ECO:0000313|Proteomes:UP000006798};
RN [1] {ECO:0000313|EMBL:AEI79122.1, ECO:0000313|Proteomes:UP000006798}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43291 / DSM 13513 / CCUG 52238 / LMG 8453 / N-1
RC {ECO:0000313|Proteomes:UP000006798};
RX PubMed=21742890; DOI=10.1128/JB.05660-11;
RA Poehlein A., Kusian B., Friedrich B., Daniel R., Bowien B.;
RT "Complete genome sequence of the type strain Cupriavidus necator N-1.";
RL J. Bacteriol. 193:5017-5017(2011).
CC -!- COFACTOR:
CC Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC Evidence={ECO:0000256|ARBA:ARBA00001938};
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DR EMBL; CP002878; AEI79122.1; -; Genomic_DNA.
DR RefSeq; WP_013951851.1; NC_015723.1.
DR AlphaFoldDB; F8GNM9; -.
DR KEGG; cnc:CNE_2c01310; -.
DR HOGENOM; CLU_020336_13_2_4; -.
DR Proteomes; UP000006798; Chromosome 2.
DR GO; GO:0004742; F:dihydrolipoyllysine-residue acetyltransferase activity; IEA:UniProtKB-EC.
DR CDD; cd06849; lipoyl_domain; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR003016; 2-oxoA_DH_lipoyl-BS.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR011053; Single_hybrid_motif.
DR PANTHER; PTHR43798; MONOACYLGLYCEROL LIPASE; 1.
DR PANTHER; PTHR43798:SF33; SERINE HYDROLASE-LIKE PROTEIN DDB_G0286239; 1.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR PRINTS; PR00111; ABHYDROLASE.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF51230; Single hybrid motif; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS00189; LIPOYL; 1.
PE 4: Predicted;
KW Acyltransferase {ECO:0000313|EMBL:AEI79122.1};
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823};
KW Transferase {ECO:0000313|EMBL:AEI79122.1}.
FT DOMAIN 9..84
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 374 AA; 39022 MW; A3675AB1D623C4E3 CRC64;
MATAISPTII PIVMPKWGLS MKEGTVNAWL VDEGTEITVG LPILDVETDK IANAVEAPDA
GTLRRKVAQA GDVLPVKALL GVLAPAEVSD AQIDDYVAAY ETPADDAGEE EAAAAYQFAD
VDGIRVRYAR KGGGAETVLF IHGFGGDLDN WLFNLDPLAD AYTVVALDLP GHGQSSPRLA
GTTLAQMAGF VARFMDETGI EAAHVVGHSM GGGVAAQLAV DAPQRVLSVA LVSPVGFGDA
VNSGYTEGFV SAQSRRELKP VVELLFADAG LVSRQMLDDL LRYKRLDGVT EALTALGQGL
FGGGRQSEQP GQRLAGSGKR VLVVWGGQDQ IIPAAHAEAA PAGATVKVFA DAGHMSQMEK
ANDFNALLKK HLAG
//
