ID Q03ZS7_LEUMM Unreviewed; 258 AA.
AC Q03ZS7;
DT 14-NOV-2006, integrated into UniProtKB/TrEMBL.
DT 14-NOV-2006, sequence version 1.
DT 27-MAR-2024, entry version 98.
DE RecName: Full=Diacetyl reductase [(S)-acetoin forming] {ECO:0000256|ARBA:ARBA00016110};
DE EC=1.1.1.304 {ECO:0000256|ARBA:ARBA00012848};
DE AltName: Full=Acetoin(diacetyl) reductase {ECO:0000256|ARBA:ARBA00029989};
DE AltName: Full=Meso-2,3-butanediol dehydrogenase {ECO:0000256|ARBA:ARBA00031758};
GN OrderedLocusNames=LEUM_0145 {ECO:0000313|EMBL:ABJ61295.1};
OS Leuconostoc mesenteroides subsp. mesenteroides (strain ATCC 8293 / DSM
OS 20343 / BCRC 11652 / CCM 1803 / JCM 6124 / NCDO 523 / NBRC 100496 / NCIMB
OS 8023 / NCTC 12954 / NRRL B-1118 / 37Y).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Leuconostoc.
OX NCBI_TaxID=203120 {ECO:0000313|EMBL:ABJ61295.1, ECO:0000313|Proteomes:UP000000362};
RN [1] {ECO:0000313|EMBL:ABJ61295.1, ECO:0000313|Proteomes:UP000000362}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8293 / DSM 20343 / BCRC 11652 / CCM 1803 / JCM 6124 / NCDO
RC 523 / NBRC 100496 / NCIMB 8023 / NCTC 12954 / NRRL B-1118 / 37Y
RC {ECO:0000313|Proteomes:UP000000362};
RX PubMed=17030793; DOI=10.1073/pnas.0607117103;
RA Makarova K., Slesarev A., Wolf Y., Sorokin A., Mirkin B., Koonin E.,
RA Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V.,
RA Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M.,
RA Hawkins T., Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A.,
RA Baldwin K., Lee J.H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W.,
RA Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y.,
RA Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J., Hutkins R.,
RA O'Sullivan D., Steele J., Unlu G., Saier M., Klaenhammer T., Richardson P.,
RA Kozyavkin S., Weimer B., Mills D.;
RT "Comparative genomics of the lactic acid bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006).
CC -!- FUNCTION: Catalyzes the irreversible reduction of 2,3-butanediol to
CC (S)-acetoin in the presence of NADH. {ECO:0000256|ARBA:ARBA00003200}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-acetoin + NAD(+) = diacetyl + H(+) + NADH;
CC Xref=Rhea:RHEA:27286, ChEBI:CHEBI:15378, ChEBI:CHEBI:15687,
CC ChEBI:CHEBI:16583, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC EC=1.1.1.304; Evidence={ECO:0000256|ARBA:ARBA00001034};
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000256|ARBA:ARBA00006484, ECO:0000256|RuleBase:RU000363}.
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DR EMBL; CP000414; ABJ61295.1; -; Genomic_DNA.
DR RefSeq; WP_010290041.1; NC_008531.1.
DR AlphaFoldDB; Q03ZS7; -.
DR EnsemblBacteria; ABJ61295; ABJ61295; LEUM_0145.
DR GeneID; 61177376; -.
DR KEGG; lme:LEUM_0145; -.
DR eggNOG; COG1028; Bacteria.
DR HOGENOM; CLU_010194_1_0_9; -.
DR Proteomes; UP000000362; Chromosome.
DR GO; GO:0052588; F:diacetyl reductase ((S)-acetoin forming) activity; IEA:UniProtKB-EC.
DR GO; GO:0045150; P:acetoin catabolic process; IEA:InterPro.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR014007; 23BDH.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR NCBIfam; TIGR02415; 23BDH; 1.
DR PANTHER; PTHR43639; OXIDOREDUCTASE, SHORT-CHAIN DEHYDROGENASE/REDUCTASE FAMILY (AFU_ORTHOLOGUE AFUA_5G02870); 1.
DR PANTHER; PTHR43639:SF1; OXIDOREDUCTASE, SHORT-CHAIN DEHYDROGENASE_REDUCTASE FAMILY (AFU_ORTHOLOGUE AFUA_5G02870); 1.
DR Pfam; PF00106; adh_short; 1.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|PIRSR:PIRSR614007-2}.
FT ACT_SITE 154
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR614007-1"
FT BINDING 14..16
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR614007-2"
FT BINDING 61..62
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR614007-2"
FT BINDING 88
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR614007-2"
FT BINDING 154
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR614007-2"
FT BINDING 158
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR614007-2"
FT BINDING 184..189
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR614007-2"
SQ SEQUENCE 258 AA; 27247 MW; 2F33674F6BC4F91D CRC64;
MSENKVALVT GAGQGIGQAI AERLSKDGFK VALVGRHIEK VQKVADEINE NGGEAIAIKA
DVAKRDEVFA AVKETKEKFN GFDVIVNNAG VAPTTPIMSV TEDDMNWTWG INVNGIVWGT
QAATEAFKEF GHGGKIINAT SQAGVQGNAN LTAYGSTKFA IRGITQTTAK ELAEFGITVN
AFAPGIVKTP MMEDIAHEVS VNAGKDDEWG MAQFSEGITL GRLSEPEDIA NVVSFLSSSD
SNYVTGQTLI VDGGMVFS
//
