ALDC_BACSU
ID ALDC_BACSU Reviewed; 255 AA.
AC Q04777;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Alpha-acetolactate decarboxylase;
DE EC=4.1.1.5;
GN Name=alsD; OrderedLocusNames=BSU36000;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7685336; DOI=10.1128/jb.175.12.3863-3875.1993;
RA Renna M.C., Najimudin N., Winik L.R., Zahler S.A.;
RT "Regulation of the Bacillus subtilis alsS, alsD, and alsR genes involved in
RT post-exponential-phase production of acetoin.";
RL J. Bacteriol. 175:3863-3875(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9353933; DOI=10.1099/00221287-143-10-3313;
RA Presecan E., Moszer I., Boursier L., Cruz Ramos H., De La Fuente V.,
RA Hullo M.-F., Lelong C., Schleich S., Sekowska A., Song B.H., Villani G.,
RA Kunst F., Danchin A., Glaser P.;
RT "The Bacillus subtilis genome from gerBC (311 degrees) to licR (334
RT degrees).";
RL Microbiology 143:3313-3328(1997).
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 REGULATION.
RX PubMed=10809684; DOI=10.1128/jb.182.11.3072-3080.2000;
RA Cruz Ramos H., Hoffmann T., Marino M., Nedjari H., Presecan-Siedel E.,
RA Dreesen O., Glaser P., Jahn D.;
RT "Fermentative metabolism of Bacillus subtilis: physiology and regulation of
RT gene expression.";
RL J. Bacteriol. 182:3072-3080(2000).
CC -!- FUNCTION: Converts acetolactate into acetoin, which can be excreted by
CC the cells. This may be a mechanism for controlling the internal pH of
CC cells in the stationary stage.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2S)-2-acetolactate + H(+) = (R)-acetoin + CO2;
CC Xref=Rhea:RHEA:21580, ChEBI:CHEBI:15378, ChEBI:CHEBI:15686,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:58476; EC=4.1.1.5;
CC -!- PATHWAY: Polyol metabolism; (R,R)-butane-2,3-diol biosynthesis; (R,R)-
CC butane-2,3-diol from pyruvate: step 2/3.
CC -!- INDUCTION: Strongly induced under anaerobic conditions. Activated by
CC ResDE, Fnr and ArfM.
CC -!- SIMILARITY: Belongs to the alpha-acetolactate decarboxylase family.
CC {ECO:0000305}.
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DR EMBL; L04470; AAA22223.1; -; Genomic_DNA.
DR EMBL; Z93767; CAB07786.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15617.1; -; Genomic_DNA.
DR PIR; B47126; B47126.
DR RefSeq; NP_391481.1; NC_000964.3.
DR RefSeq; WP_003244457.1; NZ_JNCM01000034.1.
DR PDB; 5XNE; X-ray; 1.50 A; A/B=19-253.
DR PDBsum; 5XNE; -.
DR AlphaFoldDB; Q04777; -.
DR SMR; Q04777; -.
DR STRING; 224308.BSU36000; -.
DR PaxDb; Q04777; -.
DR PRIDE; Q04777; -.
DR EnsemblBacteria; CAB15617; CAB15617; BSU_36000.
DR GeneID; 936857; -.
DR KEGG; bsu:BSU36000; -.
DR PATRIC; fig|224308.179.peg.3897; -.
DR eggNOG; COG3527; Bacteria.
DR InParanoid; Q04777; -.
DR OMA; YKPMLEA; -.
DR PhylomeDB; Q04777; -.
DR BioCyc; BSUB:BSU36000-MON; -.
DR BRENDA; 4.1.1.5; 658.
DR UniPathway; UPA00626; UER00678.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0047605; F:acetolactate decarboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0045151; P:acetoin biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd17299; acetolactate_decarboxylase; 1.
DR InterPro; IPR005128; Acetolactate_a_deCO2ase.
DR PANTHER; PTHR35524; PTHR35524; 1.
DR Pfam; PF03306; AAL_decarboxy; 1.
DR PIRSF; PIRSF001332; Acetolac_decarb; 1.
DR TIGRFAMs; TIGR01252; acetolac_decarb; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetoin biosynthesis; Decarboxylase; Lyase;
KW Reference proteome.
FT CHAIN 1..255
FT /note="Alpha-acetolactate decarboxylase"
FT /id="PRO_0000218438"
FT STRAND 21..26
FT /evidence="ECO:0007829|PDB:5XNE"
FT HELIX 28..32
FT /evidence="ECO:0007829|PDB:5XNE"
FT HELIX 42..44
FT /evidence="ECO:0007829|PDB:5XNE"
FT HELIX 45..48
FT /evidence="ECO:0007829|PDB:5XNE"
FT STRAND 50..55
FT /evidence="ECO:0007829|PDB:5XNE"
FT HELIX 57..59
FT /evidence="ECO:0007829|PDB:5XNE"
FT STRAND 61..66
FT /evidence="ECO:0007829|PDB:5XNE"
FT STRAND 69..74
FT /evidence="ECO:0007829|PDB:5XNE"
FT TURN 75..77
FT /evidence="ECO:0007829|PDB:5XNE"
FT STRAND 78..81
FT /evidence="ECO:0007829|PDB:5XNE"
FT STRAND 87..94
FT /evidence="ECO:0007829|PDB:5XNE"
FT STRAND 100..104
FT /evidence="ECO:0007829|PDB:5XNE"
FT HELIX 110..118
FT /evidence="ECO:0007829|PDB:5XNE"
FT STRAND 126..142
FT /evidence="ECO:0007829|PDB:5XNE"
FT HELIX 154..157
FT /evidence="ECO:0007829|PDB:5XNE"
FT HELIX 158..160
FT /evidence="ECO:0007829|PDB:5XNE"
FT STRAND 163..178
FT /evidence="ECO:0007829|PDB:5XNE"
FT HELIX 180..182
FT /evidence="ECO:0007829|PDB:5XNE"
FT STRAND 188..196
FT /evidence="ECO:0007829|PDB:5XNE"
FT STRAND 202..226
FT /evidence="ECO:0007829|PDB:5XNE"
FT HELIX 231..235
FT /evidence="ECO:0007829|PDB:5XNE"
FT HELIX 243..251
FT /evidence="ECO:0007829|PDB:5XNE"
SQ SEQUENCE 255 AA; 28799 MW; 1B90C69424D39B10 CRC64;
MKRESNIQVL SRGQKDQPVS QIYQVSTMTS LLDGVYDGDF ELSEIPKYGD FGIGTFNKLD
GELIGFDGEF YRLRSDGTAT PVQNGDRSPF CSFTFFTPDM THKIDAKMTR EDFEKEINSM
LPSRNLFYAI RIDGLFKKVQ TRTVELQEKP YVPMVEAVKT QPIFNFDNVR GTIVGFLTPA
YANGIAVSGY HLHFIDEGRN SGGHVFDYVL EDCTVTISQK MNMNLRLPNT ADFFNANLDN
PDFAKDIETT EGSPE
