ID   ADHB_BACSU              Reviewed;         378 AA.
AC   O06012; Q795Z4;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 2.
DT   03-AUG-2022, entry version 135.
DE   RecName: Full=Uncharacterized zinc-type alcohol dehydrogenase-like protein AdhB;
DE            EC=1.-.-.-;
GN   Name=adhB; OrderedLocusNames=BSU26970;
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=9141695; DOI=10.1099/00221287-143-4-1321;
RA   Parro V., San Roman M., Galindo I., Purnelle B., Bolotin A., Sorokin A.,
RA   Mellado R.P.;
RT   "A 23911 bp region of the Bacillus subtilis genome comprising genes located
RT   upstream and downstream of the lev operon.";
RL   Microbiology 143:1321-1326(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   SEQUENCE REVISION TO 58.
RX   PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA   Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA   Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT   "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT   168 reference genome a decade later.";
RL   Microbiology 155:1758-1775(2009).
RN   [4]
RP   DISRUPTION PHENOTYPE.
RC   STRAIN=168;
RX   PubMed=19170879; DOI=10.1111/j.1365-2958.2008.06568.x;
RA   Nguyen T.T.H., Eiamphungporn W., Maeder U., Liebeke M., Lalk M., Hecker M.,
RA   Helmann J.D., Antelmann H.;
RT   "Genome-wide responses to carbonyl electrophiles in Bacillus subtilis:
RT   control of the thiol-dependent formaldehyde dehydrogenase AdhA and cysteine
RT   proteinase YraA by the MerR-family regulator YraB (AdhR).";
RL   Mol. Microbiol. 71:876-894(2009).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
CC   -!- DISRUPTION PHENOTYPE: No aldehyde-stress related phenotype.
CC       {ECO:0000269|PubMed:19170879}.
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. Class-III subfamily. {ECO:0000305}.
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DR   EMBL; X92868; CAA63472.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14638.2; -; Genomic_DNA.
DR   PIR; D69583; D69583.
DR   RefSeq; NP_390574.2; NC_000964.3.
DR   RefSeq; WP_003229843.1; NZ_JNCM01000036.1.
DR   AlphaFoldDB; O06012; -.
DR   SMR; O06012; -.
DR   STRING; 224308.BSU26970; -.
DR   PaxDb; O06012; -.
DR   PRIDE; O06012; -.
DR   EnsemblBacteria; CAB14638; CAB14638; BSU_26970.
DR   GeneID; 937604; -.
DR   KEGG; bsu:BSU26970; -.
DR   PATRIC; fig|224308.179.peg.2929; -.
DR   eggNOG; COG1063; Bacteria.
DR   InParanoid; O06012; -.
DR   OMA; CCRNFGT; -.
DR   PhylomeDB; O06012; -.
DR   BioCyc; BSUB:BSU26970-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; IPR027399; ADH_N_assoc.
DR   InterPro; IPR002328; ADH_Zn_CS.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF13823; ADH_N_assoc; 1.
DR   Pfam; PF00107; ADH_zinc_N; 1.
DR   SUPFAM; SSF50129; SSF50129; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS00059; ADH_ZINC; 1.
PE   3: Inferred from homology;
KW   Metal-binding; Oxidoreductase; Reference proteome; Zinc.
FT   CHAIN           1..378
FT                   /note="Uncharacterized zinc-type alcohol dehydrogenase-like
FT                   protein AdhB"
FT                   /id="PRO_0000360860"
FT   BINDING         38
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         60
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         90
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         93
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         96
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         104
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        58
FT                   /note="I -> T (in Ref. 1; CAA63472)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   378 AA;  41208 MW;  7BD86CBBC32FC397 CRC64;
     MKAVTYQGIK NVVVKDVPDP KIEKSDDMII KVTSTAICGS DLHLIHGFIP NMQEDYVIGH
     EPMGIVEEVG SGVTKLKKGD RVIIPFNIAC GECFFCKNQL ESQCDQSNDN GEMGAYFGYS
     GQTGGYPGGQ AEYLRVPFAN FTHFKIPESC EEPDEKLSVI ADAMTTGFWS VDNAGVKKGD
     TVIVLGCGPV GLFAQKFCWL KGAKRVIAVD YVNYRLQHAK RTNKVEIVNF EDHENTGNYL
     KEITKGGADV VIDAVGMDGK MSDLEFLASG LKLHGGTMSA LVIASQAVRK GGTIQITGVY
     GGRYNGFPLG DIMQRNVNIR SGQAPVIHYM PYMFELVSTG KIDPGDVVSH VLPLSEAKHG
     YDIFDSKMDD CIKVVLKP