ID   ACOC_BACSU              Reviewed;         398 AA.
AC   O31550;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 144.
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; Synonyms=yfjI; OrderedLocusNames=BSU08080;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / AC327;
RX   PubMed=8969503; DOI=10.1099/13500872-142-11-3057;
RA   Yamamoto H., Uchiyama S., Sekiguchi J.;
RT   "Cloning and sequencing of a 40.6 kb segment in the 73 degrees-76 degrees
RT   region of the Bacillus subtilis chromosome containing genes for trehalose
RT   metabolism and acetoin utilization.";
RL   Microbiology 142:3057-3065(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
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.
CC   -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; D78509; BAA24294.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB12637.1; -; Genomic_DNA.
DR   PIR; F69581; F69581.
DR   RefSeq; NP_388689.1; NC_000964.3.
DR   RefSeq; WP_003244059.1; NZ_JNCM01000032.1.
DR   AlphaFoldDB; O31550; -.
DR   SMR; O31550; -.
DR   IntAct; O31550; 6.
DR   STRING; 224308.BSU08080; -.
DR   jPOST; O31550; -.
DR   PaxDb; O31550; -.
DR   PRIDE; O31550; -.
DR   EnsemblBacteria; CAB12637; CAB12637; BSU_08080.
DR   GeneID; 936147; -.
DR   KEGG; bsu:BSU08080; -.
DR   PATRIC; fig|224308.179.peg.874; -.
DR   eggNOG; COG0508; Bacteria.
DR   InParanoid; O31550; -.
DR   OMA; TPIFMEA; -.
DR   PhylomeDB; O31550; -.
DR   BioCyc; BSUB:BSU08080-MON; -.
DR   UniPathway; UPA00040; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0045254; C:pyruvate dehydrogenase complex; IEA:InterPro.
DR   GO; GO:0004742; F:dihydrolipoyllysine-residue acetyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0045150; P:acetoin catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; IEA:InterPro.
DR   Gene3D; 3.30.559.10; -; 1.
DR   Gene3D; 4.10.320.10; -; 1.
DR   InterPro; IPR001078; 2-oxoacid_DH_actylTfrase.
DR   InterPro; IPR000089; Biotin_lipoyl.
DR   InterPro; IPR023213; CAT-like_dom_sf.
DR   InterPro; IPR045257; E2/Pdx1.
DR   InterPro; IPR036625; E3-bd_dom_sf.
DR   InterPro; IPR004167; PSBD.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   PANTHER; PTHR23151; PTHR23151; 1.
DR   Pfam; PF00198; 2-oxoacid_dh; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   Pfam; PF02817; E3_binding; 1.
DR   SUPFAM; SSF47005; SSF47005; 1.
DR   SUPFAM; SSF51230; SSF51230; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR   PROSITE; PS51826; PSBD; 1.
PE   3: Inferred from homology;
KW   Acetoin catabolism; Acyltransferase; Lipoyl; Reference proteome;
KW   Transferase.
FT   CHAIN           1..398
FT                   /note="Dihydrolipoyllysine-residue acetyltransferase
FT                   component of acetoin cleaving system"
FT                   /id="PRO_0000162306"
FT   DOMAIN          2..77
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT   DOMAIN          118..155
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01170"
FT   ACT_SITE        371
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        375
FT                   /evidence="ECO:0000255"
FT   MOD_RES         43
FT                   /note="N6-lipoyllysine"
FT                   /evidence="ECO:0000250, ECO:0000255|PROSITE-
FT                   ProRule:PRU01066"
SQ   SEQUENCE   398 AA;  42886 MW;  559564C27C1C64F6 CRC64;
     MAVKVVMPKL GMAMKQGEVS IWNKKVGDPV EKGESIASIQ SEKIEMEIEA PEKGTLIDIK
     VKEGEEVPPG TAICYIGDAN ESVQEEAGAP VAEDNMPQAV QPVKQENKPA ASKKDRMKIS
     PVARKIAEKA GLDLKQLKGT GPGGRIVKDD VTKALAEQKK DQAKPVSEQK AQEIPVTGMR
     KVIAARMQES LANSAQLTIT MKADITKLAT LQKQLSPTAE ERYGTKLTIT HFVSRAAVLA
     LQAHPVLNSF YQNERIITHP HVHLGMAVAL ENGLVVPVIR HAEKLSLIEL AQSISENAKK
     AREGRAGSEE LQGSTFSITN LGAFGVEHFT PILNPPETGI LGIGASYDTP VYQGEEIVRS
     TILPLSLTFD HRACDGAPAA AFLKAMKTYL EEPAALIL