ADHA_BACSU
ID ADHA_BACSU Reviewed; 349 AA.
AC C0SPA5; O06007; Q795Z0;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Probable formaldehyde dehydrogenase AdhA;
DE EC=1.1.1.-;
GN Name=adhA; OrderedLocusNames=BSU27010;
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 226.
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 FUNCTION, INDUCTION, OPERON STRUCTURE, AND 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 -!- FUNCTION: Functions in the protection against aldehyde-stress.
CC {ECO:0000269|PubMed:19170879}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000305};
CC -!- INDUCTION: By formaldehyde and methylgloxal, under the control of AdhR.
CC Encoded in an operon with yraA. {ECO:0000269|PubMed:19170879}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene show significantly
CC reduced growth in the presence of formaldehyde but not methylglyoxal.
CC {ECO:0000269|PubMed:19170879}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; X92868; CAA63467.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14643.2; -; Genomic_DNA.
DR PIR; C69583; C69583.
DR RefSeq; NP_390579.2; NC_000964.3.
DR RefSeq; WP_003229837.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; C0SPA5; -.
DR SMR; C0SPA5; -.
DR STRING; 224308.BSU27010; -.
DR PaxDb; C0SPA5; -.
DR PRIDE; C0SPA5; -.
DR EnsemblBacteria; CAB14643; CAB14643; BSU_27010.
DR GeneID; 938739; -.
DR KEGG; bsu:BSU27010; -.
DR PATRIC; fig|224308.179.peg.2934; -.
DR eggNOG; COG1064; Bacteria.
DR InParanoid; C0SPA5; -.
DR OMA; YRFSIDM; -.
DR PhylomeDB; C0SPA5; -.
DR BioCyc; BSUB:BSU27010-MON; -.
DR BioCyc; MetaCyc:BSU27010-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Metal-binding; Oxidoreductase; Reference proteome; Stress response; Zinc.
FT CHAIN 1..349
FT /note="Probable formaldehyde dehydrogenase AdhA"
FT /id="PRO_0000378093"
FT BINDING 44
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255"
FT BINDING 66
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255"
FT BINDING 97
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 100
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 103
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 111
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 161
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255"
FT CONFLICT 226
FT /note="F -> Y (in Ref. 1; CAA63467)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 349 AA; 37806 MW; 48E7A7A0E831F6C3 CRC64;
MCNQHQTRVL SVSHAKAKFE QTTIERRGLR PHDVLIDIKF SGICHSDIHS AFDEWGGGIF
PMVPGHEIAG VVTAVGTKVT KLAVGDRVGV GCFVDSCGEC EYCLNAEEQF CTKGVVQTYN
SVDYDGNPTY GGYSQKIVVT DRFVVRIPDR LEMDVASPLL CAGITTYSPL KHWNVGPGKK
VAIVGVGGLG HLAIQFAHAM GAEVTVLSRS MNKKEEALEL GANHYFATSD PATFTALAGR
FDVILNTVSA NLDVDAYLSM LRIDGTLVSV GAPAKPDTYS VFSLIMGRRS IAGSLVGGIQ
ETQEMLDFAA EHGIEPKIEV IGADQVDEAY ERILRSDVRY RFVIDISTL
