BDHA_BACSU
ID BDHA_BACSU Reviewed; 346 AA.
AC O34788; Q797C2;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=(R,R)-butanediol dehydrogenase;
DE EC=1.1.1.4 {ECO:0000305|PubMed:18820069};
DE AltName: Full=Acetoin reductase/2,3-butanediol dehydrogenase;
DE Short=AR/BDH;
GN Name=bdhA {ECO:0000303|PubMed:18820069}; Synonyms=ydjL;
GN OrderedLocusNames=BSU06240;
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 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=9455482; DOI=10.1093/dnares/4.5.335;
RA Kasahara Y., Nakai S., Ogasawara N., Yata K., Sadaie Y.;
RT "Sequence analysis of the groESL-cotA region of the Bacillus subtilis
RT genome, containing the restriction/modification system genes.";
RL DNA Res. 4:335-339(1997).
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).
RN [3]
RP FUNCTION, PROBABLE CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RC STRAIN=168;
RX PubMed=18820069; DOI=10.1128/aem.00881-08;
RA Nicholson W.L.;
RT "The Bacillus subtilis ydjL (bdhA) gene encodes acetoin reductase/2,3-
RT butanediol dehydrogenase.";
RL Appl. Environ. Microbiol. 74:6832-6838(2008).
RN [4]
RP INTERACTION WITH BRXC, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=168 / CU1065 {ECO:0000303|PubMed:33722570};
RX PubMed=33722570; DOI=10.1016/j.redox.2021.101935;
RA Gaballa A., Su T.T., Helmann J.D.;
RT "The Bacillus subtilis monothiol bacilliredoxin BrxC (YtxJ) and the Bdr
RT (YpdA) disulfide reductase reduce S-bacillithiolated proteins.";
RL Redox Biol. 42:101935-101935(2021).
RN [5] {ECO:0007744|PDB:6IE0}
RP X-RAY CRYSTALLOGRAPHY (2.98 ANGSTROMS) IN COMPLEX WITH ZINC, AND SUBUNIT.
RA Wang X.F., Feng Y.B., Ji F.L.;
RT "X-ray crystal structure of 2R,3R-butanediol dehydrogenase from Bacillus
RT subtilis.";
RL Submitted (SEP-2018) to the PDB data bank.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R,R)-butane-2,3-diol + NAD(+) = (R)-acetoin + H(+) + NADH;
CC Xref=Rhea:RHEA:24340, ChEBI:CHEBI:15378, ChEBI:CHEBI:15686,
CC ChEBI:CHEBI:16982, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.4;
CC Evidence={ECO:0000305|PubMed:18820069};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0007744|PDB:6IE0};
CC Note=Binds 1 Zn(2+) per subunit. {ECO:0007744|PDB:6IE0};
CC -!- SUBUNIT: Homotetramer (Ref.5). Interacts with BrxC (PubMed:33722570).
CC {ECO:0000269|PubMed:33722570, ECO:0000305|Ref.5}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene have no acetoin
CC reductase/2,3-butanediol dehydrogenase activity.
CC {ECO:0000269|PubMed:18820069}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; AB007638; BAA22767.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12443.1; -; Genomic_DNA.
DR PIR; H69789; H69789.
DR RefSeq; NP_388505.1; NC_000964.3.
DR RefSeq; WP_003234015.1; NZ_JNCM01000032.1.
DR PDB; 6IE0; X-ray; 2.98 A; A/B/C/D=1-346.
DR PDBsum; 6IE0; -.
DR AlphaFoldDB; O34788; -.
DR SMR; O34788; -.
DR IntAct; O34788; 1.
DR MINT; O34788; -.
DR STRING; 224308.BSU06240; -.
DR jPOST; O34788; -.
DR PaxDb; O34788; -.
DR PRIDE; O34788; -.
DR EnsemblBacteria; CAB12443; CAB12443; BSU_06240.
DR GeneID; 939490; -.
DR KEGG; bsu:BSU06240; -.
DR PATRIC; fig|224308.179.peg.676; -.
DR eggNOG; COG1063; Bacteria.
DR InParanoid; O34788; -.
DR OMA; ETWYAMS; -.
DR PhylomeDB; O34788; -.
DR BioCyc; BSUB:BSU06240-MON; -.
DR BRENDA; 1.1.1.4; 658.
DR BRENDA; 1.1.1.B20; 658.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0000721; F:(R,R)-butanediol dehydrogenase activity; IMP:CACAO.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH_N.
DR InterPro; IPR002328; ADH_Zn_CS.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00059; ADH_ZINC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Metal-binding; NAD; Oxidoreductase; Reference proteome; Zinc.
FT CHAIN 1..346
FT /note="(R,R)-butanediol dehydrogenase"
FT /id="PRO_0000378092"
FT BINDING 37
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0007744|PDB:6IE0"
FT BINDING 70
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0007744|PDB:6IE0"
FT BINDING 152
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0007744|PDB:6IE0"
FT STRAND 1..8
FT /evidence="ECO:0007829|PDB:6IE0"
FT STRAND 11..17
FT /evidence="ECO:0007829|PDB:6IE0"
FT STRAND 26..35
FT /evidence="ECO:0007829|PDB:6IE0"
FT HELIX 39..46
FT /evidence="ECO:0007829|PDB:6IE0"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:6IE0"
FT TURN 58..60
FT /evidence="ECO:0007829|PDB:6IE0"
FT STRAND 64..67
FT /evidence="ECO:0007829|PDB:6IE0"
FT STRAND 71..79
FT /evidence="ECO:0007829|PDB:6IE0"
FT STRAND 91..94
FT /evidence="ECO:0007829|PDB:6IE0"
FT STRAND 102..106
FT /evidence="ECO:0007829|PDB:6IE0"
FT HELIX 107..109
FT /evidence="ECO:0007829|PDB:6IE0"
FT TURN 116..118
FT /evidence="ECO:0007829|PDB:6IE0"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:6IE0"
FT STRAND 124..132
FT /evidence="ECO:0007829|PDB:6IE0"
FT HELIX 133..135
FT /evidence="ECO:0007829|PDB:6IE0"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:6IE0"
FT HELIX 145..149
FT /evidence="ECO:0007829|PDB:6IE0"
FT HELIX 151..162
FT /evidence="ECO:0007829|PDB:6IE0"
FT STRAND 172..175
FT /evidence="ECO:0007829|PDB:6IE0"
FT HELIX 179..190
FT /evidence="ECO:0007829|PDB:6IE0"
FT STRAND 196..199
FT /evidence="ECO:0007829|PDB:6IE0"
FT HELIX 203..211
FT /evidence="ECO:0007829|PDB:6IE0"
FT STRAND 215..217
FT /evidence="ECO:0007829|PDB:6IE0"
FT TURN 219..221
FT /evidence="ECO:0007829|PDB:6IE0"
FT HELIX 225..233
FT /evidence="ECO:0007829|PDB:6IE0"
FT STRAND 237..242
FT /evidence="ECO:0007829|PDB:6IE0"
FT HELIX 247..255
FT /evidence="ECO:0007829|PDB:6IE0"
FT STRAND 257..265
FT /evidence="ECO:0007829|PDB:6IE0"
FT STRAND 273..275
FT /evidence="ECO:0007829|PDB:6IE0"
FT HELIX 277..282
FT /evidence="ECO:0007829|PDB:6IE0"
FT STRAND 286..289
FT /evidence="ECO:0007829|PDB:6IE0"
FT HELIX 297..304
FT /evidence="ECO:0007829|PDB:6IE0"
FT TURN 305..309
FT /evidence="ECO:0007829|PDB:6IE0"
FT HELIX 311..314
FT /evidence="ECO:0007829|PDB:6IE0"
FT STRAND 315..320
FT /evidence="ECO:0007829|PDB:6IE0"
FT HELIX 321..323
FT /evidence="ECO:0007829|PDB:6IE0"
FT HELIX 324..327
FT /evidence="ECO:0007829|PDB:6IE0"
FT HELIX 329..334
FT /evidence="ECO:0007829|PDB:6IE0"
FT STRAND 340..344
FT /evidence="ECO:0007829|PDB:6IE0"
SQ SEQUENCE 346 AA; 37341 MW; 5E327192D678F8A2 CRC64;
MKAARWHNQK DIRIEHIEEP KTEPGKVKIK VKWCGICGSD LHEYLGGPIF IPVDKPHPLT
NETAPVTMGH EFSGEVVEVG EGVENYKVGD RVVVEPIFAT HGHQGAYNLD EQMGFLGLAG
GGGGFSEYVS VDEELLFKLP DELSYEQGAL VEPSAVALYA VRSSKLKAGD KAAVFGCGPI
GLLVIEALKA AGATDIYAVE LSPERQQKAE ELGAIIVDPS KTDDVVAEIA ERTGGGVDVA
FEVTGVPVVL RQAIQSTTIA GETVIVSIWE KGAEIHPNDI VIKERTVKGI IGYRDIFPAV
LSLMKEGYFS ADKLVTKKIV LDDLIEEGFG ALIKEKSQVK ILVRPN
