YYCR_BACSU
ID YYCR_BACSU Reviewed; 408 AA.
AC Q45604; Q794W4;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Uncharacterized zinc-type alcohol dehydrogenase-like protein YycR;
DE EC=1.-.-.-;
GN Name=yycR; OrderedLocusNames=BSU40250;
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;
RX PubMed=9205843; DOI=10.1093/dnares/4.2.155;
RA Kasahara Y., Nakai S., Ogasawara N.;
RT "Sequence analysis of the 36-kb region between gntZ and trnY genes of
RT Bacillus subtilis genome.";
RL DNA Res. 4:155-159(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 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).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305};
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene retain 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; D78193; BAA11284.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB16062.1; -; Genomic_DNA.
DR PIR; F70090; F70090.
DR RefSeq; NP_391905.1; NC_000964.3.
DR RefSeq; WP_003226972.1; NZ_JNCM01000034.1.
DR AlphaFoldDB; Q45604; -.
DR SMR; Q45604; -.
DR STRING; 224308.BSU40250; -.
DR PaxDb; Q45604; -.
DR PRIDE; Q45604; -.
DR EnsemblBacteria; CAB16062; CAB16062; BSU_40250.
DR GeneID; 937754; -.
DR KEGG; bsu:BSU40250; -.
DR PATRIC; fig|224308.43.peg.4223; -.
DR eggNOG; COG1063; Bacteria.
DR InParanoid; Q45604; -.
DR OMA; GNCNHRK; -.
DR PhylomeDB; Q45604; -.
DR BioCyc; BSUB:BSU40250-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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; IPR014184; HCHO_DH_non_GSH.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR02819; fdhA_non_GSH; 1.
DR PROSITE; PS00059; ADH_ZINC; 1.
PE 3: Inferred from homology;
KW Metal-binding; Oxidoreductase; Reference proteome; Zinc.
FT CHAIN 1..408
FT /note="Uncharacterized zinc-type alcohol dehydrogenase-like
FT protein YycR"
FT /id="PRO_0000378094"
FT BINDING 61
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255"
FT BINDING 82
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255"
FT BINDING 112
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255"
FT BINDING 115
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255"
FT BINDING 118
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255"
FT BINDING 126
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255"
SQ SEQUENCE 408 AA; 42947 MW; 1F2069A25B8F4479 CRC64;
MGGMALTGNK AVVYKGKGTV AVEDIGYPEL ILRDGPGVPK ANVNRKCEHG VILKVITTNI
CGSDQHMVRG RTTAPEGLVL GHEITGEVIE TGRDVEFIKK GDIVSVPFNI ACGRCVMCKT
QKTHVCLNVN PDRPGSAYGY VDMGGWVGGQ SEYVMVPYAD FQLLVFPDKE QALEKILDLT
MLSDIFPTGF HGAYTAGVQT GSTVYIAGAG PVGLAAAHSA QLLGASTVIV GDLNEDRLAQ
ARSFGCETVN VQKHDRLGEQ IEQILGEPTV DAAVDCVGFE ASGHGNQGEA PAAVLNSIMD
VTQVGGSLGI PGLYVTEDPG AKDADAKTGS LKIRFGLGWA KAHTFVTGQT PAMTYNRNLM
KAILSGRAQI AKAVNATVIS LDDAPKGYSD FDKGAAKKFV IDPHGTLK