ID   ACOC_PSEPU              Reviewed;         370 AA.
AC   Q59695;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 95.
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;
GN   Name=acoC;
OS   Pseudomonas putida (Arthrobacter siderocapsulatus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=303;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=G2;
RX   PubMed=7813883; DOI=10.1111/j.1574-6968.1994.tb07276.x;
RA   Huang M., Oppermann F.B., Steinbuchel A.;
RT   "Molecular characterization of the Pseudomonas putida 2,3-butanediol
RT   catabolic pathway.";
RL   FEMS Microbiol. Lett. 124:141-150(1994).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + acetyl-CoA = (R)-
CC         N(6)-(S(8)-acetyldihydrolipoyl)-L-lysyl-[protein] + CoA;
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.
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DR   EMBL; L35343; AAB58981.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q59695; -.
DR   SMR; Q59695; -.
DR   ESTHER; psepu-acoc; AcoC_BiotinLipoyl-ABH.
DR   UniPathway; UPA00040; -.
DR   GO; GO:0004742; F:dihydrolipoyllysine-residue acetyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0045150; P:acetoin catabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.50.1820; -; 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   Pfam; PF00561; Abhydrolase_1; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   PRINTS; PR00111; ABHYDROLASE.
DR   SUPFAM; SSF51230; SSF51230; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR   PROSITE; PS00189; LIPOYL; 1.
PE   3: Inferred from homology;
KW   Acetoin catabolism; Acyltransferase; Lipoyl; Transferase.
FT   CHAIN           1..370
FT                   /note="Dihydrolipoyllysine-residue acetyltransferase
FT                   component of acetoin cleaving system"
FT                   /id="PRO_0000162305"
FT   DOMAIN          4..79
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT   DOMAIN          135..355
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         45
FT                   /note="N6-lipoyllysine"
FT                   /evidence="ECO:0000250, ECO:0000255|PROSITE-
FT                   ProRule:PRU01066"
SQ   SEQUENCE   370 AA;  39638 MW;  F3DFA23B14983B9F CRC64;
     MSQIHTLTMP KWGLSMTEGR VDAWLKQEGD EINKGDEVLD VETDKISSSV EAPFSGVLRR
     QVAKPDETLP VGALLAVVVE GEAEESEIDA VVQRFQAEFV AEGGADQAQG PAPQKAEVGG
     RLLRWFELGG EGGTPLVLVH GFGGDLNNWL FNHPALAAER RVIALDLPGH GESAKALQRG
     DLDELSETVL ALLDHLDIAK AHLAGHSMGG AVSLNVAGLA PQRVASLSLI ASAGLGEAIN
     GQYLQGFVAA ANRNALKPQM VQLFADPALV TRQMLEDMLK FKRLEGVDEA LRQLALAIAD
     GDRQRHDLRS VLGQHPALVV WGGKDAIIPA SHARKGPEAE VLVLPEAGHM VQMEAAEQVN
     QQMLAFLRKH