ID   ACOA_BACSU              Reviewed;         333 AA.
AC   O31404; O31549; Q797A1;
DT   24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 2.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=Acetoin:2,6-dichlorophenolindophenol oxidoreductase subunit alpha;
DE            Short=Acetoin:DCPIP oxidoreductase-alpha;
DE            Short=Ao:DCPIP OR;
DE            EC=1.1.1.-;
DE   AltName: Full=TPP-dependent acetoin dehydrogenase E1 subunit alpha;
GN   Name=acoA; Synonyms=yfjK; OrderedLocusNames=BSU08060;
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 [GENOMIC DNA], PATHWAY, AND DISRUPTION PHENOTYPE.
RC   STRAIN=168 / ATCC 33234 / DSM 402 / NBRC 111470 / NCIMB 10106;
RX   PubMed=10368162; DOI=10.1128/jb.181.12.3837-3841.1999;
RA   Huang M., Oppermann-Sanio F.B., Steinbuechel A.;
RT   "Biochemical and molecular characterization of the Bacillus subtilis
RT   acetoin catabolic pathway.";
RL   J. Bacteriol. 181:3837-3841(1999).
RN   [3]
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).
RN   [4]
RP   INDUCTION.
RC   STRAIN=168;
RX   PubMed=11274109; DOI=10.1128/jb.183.8.2497-2504.2001;
RA   Ali N.O., Bignon J., Rapoport G., Debarbouille M.;
RT   "Regulation of the acetoin catabolic pathway is controlled by sigma L in
RT   Bacillus subtilis.";
RL   J. Bacteriol. 183:2497-2504(2001).
RN   [5]
RP   INDUCTION.
RC   STRAIN=168;
RX   PubMed=11160890; DOI=10.1093/nar/29.3.683;
RA   Yoshida K., Kobayashi K., Miwa Y., Kang C.-M., Matsunaga M., Yamaguchi H.,
RA   Tojo S., Yamamoto M., Nishi R., Ogasawara N., Nakayama T., Fujita Y.;
RT   "Combined transcriptome and proteome analysis as a powerful approach to
RT   study genes under glucose repression in Bacillus subtilis.";
RL   Nucleic Acids Res. 29:683-692(2001).
CC   -!- FUNCTION: Catalyzes the 2,6-dichlorophenolindophenol-dependent cleavage
CC       of acetoin into acetate and acetaldehyde. The alpha subunit is probably
CC       the catalytic subunit of the enzyme (By similarity). {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000250};
CC   -!- PATHWAY: Ketone degradation; acetoin degradation.
CC       {ECO:0000269|PubMed:10368162}.
CC   -!- SUBUNIT: Tetramer of 2 alpha and 2 beta subunits. {ECO:0000250}.
CC   -!- INDUCTION: Strongly induced by acetoin. Transcriptionally up-regulated
CC       by AcoR and sigma-L factor. Subject to catabolite repression by
CC       glucose, in a CcpA-independent manner. {ECO:0000269|PubMed:11160890,
CC       ECO:0000269|PubMed:11274109}.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene are unable to utilize
CC       acetoin as carbon source. {ECO:0000269|PubMed:10368162}.
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DR   EMBL; D78509; BAA24296.1; -; Genomic_DNA.
DR   EMBL; AF006075; AAC05582.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB12635.1; -; Genomic_DNA.
DR   PIR; D69581; D69581.
DR   RefSeq; NP_388687.1; NC_000964.3.
DR   RefSeq; WP_003242898.1; NZ_JNCM01000032.1.
DR   AlphaFoldDB; O31404; -.
DR   SMR; O31404; -.
DR   IntAct; O31404; 3.
DR   STRING; 224308.BSU08060; -.
DR   jPOST; O31404; -.
DR   PaxDb; O31404; -.
DR   PRIDE; O31404; -.
DR   EnsemblBacteria; CAB12635; CAB12635; BSU_08060.
DR   GeneID; 936152; -.
DR   KEGG; bsu:BSU08060; -.
DR   PATRIC; fig|224308.179.peg.872; -.
DR   eggNOG; COG1071; Bacteria.
DR   InParanoid; O31404; -.
DR   OMA; FGMPGVT; -.
DR   PhylomeDB; O31404; -.
DR   BioCyc; BSUB:BSU08060-MON; -.
DR   UniPathway; UPA00040; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IBA:GO_Central.
DR   GO; GO:0045150; P:acetoin catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; IBA:GO_Central.
DR   InterPro; IPR001017; DH_E1.
DR   InterPro; IPR029061; THDP-binding.
DR   Pfam; PF00676; E1_dh; 1.
DR   SUPFAM; SSF52518; SSF52518; 1.
PE   2: Evidence at transcript level;
KW   Acetoin catabolism; Oxidoreductase; Reference proteome;
KW   Thiamine pyrophosphate.
FT   CHAIN           1..333
FT                   /note="Acetoin:2,6-dichlorophenolindophenol oxidoreductase
FT                   subunit alpha"
FT                   /id="PRO_0000388966"
SQ   SEQUENCE   333 AA;  36069 MW;  F0CC0FBBDAE23E21 CRC64;
     MKLLKREGLS LTEEKALWMY QKMLEIRGFE DKVHELFAQG VLPGFVHLYA GEEAVAVGVC
     AHLHDGDSIT STHRGHGHCI AKGCDLDGMM AEIFGKATGL CKGKGGSMHI ADLDKGMLGA
     NGIVGGGFTL ACGSALTAKY KQTKNVSVCF FGDGANNQGT FHEGLNLAAV WNLPVVFVAE
     NNGYGEATPF EYASACDSIA DRAAAYNMPG VTVDGKDILA VYQAAEEAIE RARNGGGPSL
     IECMTYRNYG HFEGDAQTYK TKDERVEHLE EKDAIQGFKN YLLKETDANK LSDIEQRVSE
     SIEKAVSFSE DSPYPKDSEL LTDVYVSYEK GGM