ID   ACOC_CUPNH              Reviewed;         374 AA.
AC   P27747; Q0K4X2;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   27-MAR-2024, entry version 143.
DE   RecName: Full=Dihydrolipoyllysine-residue acetyltransferase component of acetoin cleaving system;
DE            EC=2.3.1.12;
DE   AltName: Full=Acetoin dehydrogenase E2 component;
DE   AltName: Full=Dihydrolipoamide acetyltransferase component of acetoin cleaving system;
DE   AltName: Full=Fast-migrating protein;
DE            Short=FMP;
GN   Name=acoC; OrderedLocusNames=H16_B0146;
OS   Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442
OS   / H16 / Stanier 337) (Ralstonia eutropha).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=381666;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-28.
RX   PubMed=2061286; DOI=10.1128/jb.173.13.4056-4071.1991;
RA   Priefert H., Hein S., Krueger N., Zeh K., Schmidt B., Steinbuechel A.;
RT   "Identification and molecular characterization of the Alcaligenes eutrophus
RT   H16 aco operon genes involved in acetoin catabolism.";
RL   J. Bacteriol. 173:4056-4071(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier
RC   337;
RX   PubMed=16964242; DOI=10.1038/nbt1244;
RA   Pohlmann A., Fricke W.F., Reinecke F., Kusian B., Liesegang H., Cramm R.,
RA   Eitinger T., Ewering C., Poetter M., Schwartz E., Strittmatter A., Voss I.,
RA   Gottschalk G., Steinbuechel A., Friedrich B., Bowien B.;
RT   "Genome sequence of the bioplastic-producing 'Knallgas' bacterium Ralstonia
RT   eutropha H16.";
RL   Nat. Biotechnol. 24:1257-1262(2006).
CC   -!- FUNCTION: Dihydrolipoamide acetyltransferase involved in acetoin
CC       catabolism.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + N(6)-[(R)-dihydrolipoyl]-L-lysyl-[protein] = CoA
CC         + N(6)-[(R)-S(8)-acetyldihydrolipoyl]-L-lysyl-[protein];
CC         Xref=Rhea:RHEA:17017, Rhea:RHEA-COMP:10475, Rhea:RHEA-COMP:10478,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:83100,
CC         ChEBI:CHEBI:83111; EC=2.3.1.12;
CC   -!- COFACTOR:
CC       Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088; Evidence={ECO:0000250};
CC       Note=Binds 1 lipoyl cofactor covalently. {ECO:0000250};
CC   -!- PATHWAY: Ketone degradation; acetoin degradation.
CC   -!- INDUCTION: By growth on acetoin.
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DR   EMBL; M66060; AAA21950.1; -; Genomic_DNA.
DR   EMBL; AM260480; CAJ94952.1; -; Genomic_DNA.
DR   RefSeq; WP_010813530.1; NZ_CP039288.1.
DR   AlphaFoldDB; P27747; -.
DR   SMR; P27747; -.
DR   STRING; 381666.H16_B0146; -.
DR   ESTHER; cupnh-acoc; AcoC_BiotinLipoyl-ABH.
DR   MEROPS; S33.010; -.
DR   GeneID; 57646025; -.
DR   KEGG; reh:H16_B0146; -.
DR   eggNOG; COG0508; Bacteria.
DR   eggNOG; COG0596; Bacteria.
DR   HOGENOM; CLU_020336_13_2_4; -.
DR   OrthoDB; 8562572at2; -.
DR   UniPathway; UPA00040; -.
DR   Proteomes; UP000008210; Chromosome 2.
DR   GO; GO:0004742; F:dihydrolipoyllysine-residue acetyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0045150; P:acetoin catabolic process; IEA:UniProtKB-UniPathway.
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   1: Evidence at protein level;
KW   Acetoin catabolism; Acyltransferase; Direct protein sequencing; Lipoyl;
KW   Reference proteome; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:2061286"
FT   CHAIN           2..374
FT                   /note="Dihydrolipoyllysine-residue acetyltransferase
FT                   component of acetoin cleaving system"
FT                   /id="PRO_0000162304"
FT   DOMAIN          9..84
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT   DOMAIN          137..360
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         50
FT                   /note="N6-lipoyllysine"
FT                   /evidence="ECO:0000250, ECO:0000255|PROSITE-
FT                   ProRule:PRU01066"
FT   CONFLICT        95
FT                   /note="D -> G (in Ref. 1; AAA21950)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        121
FT                   /note="V -> G (in Ref. 1; AAA21950)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   374 AA;  39135 MW;  0EBD42C03A81A189 CRC64;
     MATEISPTII PIVMPKWGLS MKEGTVNAWL VDEGTEITVG LPILDVETDK IANAVEAPDA
     GTLRRKVAQA GDVLPVKALL GVLAPAEVSD AQIDDYVAAY ETPADDAGEE DAAAAYQFAD
     VDGIRVRYAR KGGGAETVLF IHGFGGDLDN WLFNLDPLAD AYTVVALDLP GHGQSSPRLA
     GTTLAQMAGF VARFMDETGI EAAHVVGHSM GGGVAAQLAV DAPQRVLSVA LVSPVGFGDA
     VNSGYTEGFV SAQSRRELKP VVELLFADAG LVSRQMLDDL LRYKRLDGVT EALTALGQGL
     FGGGRQSEQP GQRLANSGKR VLVVWGGQDQ IIPAAHAEAA PPGATVKVFA DAGHMSQMEK
     ANDFNALLKK HLGG
//