ID   ALDH4_BACSU             Reviewed;         495 AA.
AC   O34660; Q796C4;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 124.
DE   RecName: Full=Putative aldehyde dehydrogenase DhaS {ECO:0000255|PROSITE-ProRule:PRU10007};
DE            EC=1.2.1.3 {ECO:0000255|PROSITE-ProRule:PRU10007};
GN   Name=dhaS; OrderedLocusNames=BSU19310;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Lapidus A., Galleron N., Sorokin A., Ehrlich D.;
RT   "Sequence analysis of the Bacillus subtilis chromosome region between the
RT   terC and odhAB loci cloned in a yeast artificial chromosome.";
RL   Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
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 / 3NA;
RX   PubMed=26658822; DOI=10.1007/s00253-015-7197-6;
RA   Graf N., Wenzel M., Altenbuchner J.;
RT   "Identification and characterization of the vanillin dehydrogenase YfmT in
RT   Bacillus subtilis 3NA.";
RL   Appl. Microbiol. Biotechnol. 100:3511-3521(2016).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) + NADH;
CC         Xref=Rhea:RHEA:16185, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17478, ChEBI:CHEBI:29067, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945; EC=1.2.1.3; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU10007};
CC   -!- DISRUPTION PHENOTYPE: No effect on vanillin degradation.
CC       {ECO:0000269|PubMed:26658822}.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; AF027868; AAB84440.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB13823.1; -; Genomic_DNA.
DR   PIR; H69614; H69614.
DR   RefSeq; NP_389813.1; NC_000964.3.
DR   RefSeq; WP_004399332.1; NZ_JNCM01000036.1.
DR   AlphaFoldDB; O34660; -.
DR   SMR; O34660; -.
DR   STRING; 224308.BSU19310; -.
DR   jPOST; O34660; -.
DR   PaxDb; O34660; -.
DR   PRIDE; O34660; -.
DR   EnsemblBacteria; CAB13823; CAB13823; BSU_19310.
DR   GeneID; 939963; -.
DR   KEGG; bsu:BSU19310; -.
DR   PATRIC; fig|224308.179.peg.2112; -.
DR   eggNOG; COG1012; Bacteria.
DR   InParanoid; O34660; -.
DR   OMA; RKAFEKW; -.
DR   PhylomeDB; O34660; -.
DR   BioCyc; BSUB:BSU19310-MON; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0043878; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity; IEA:UniProtKB-EC.
DR   GO; GO:0006081; P:cellular aldehyde metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.309.10; -; 1.
DR   Gene3D; 3.40.605.10; -; 1.
DR   InterPro; IPR016161; Ald_DH/histidinol_DH.
DR   InterPro; IPR016163; Ald_DH_C.
DR   InterPro; IPR029510; Ald_DH_CS_GLU.
DR   InterPro; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH_dom.
DR   InterPro; IPR012394; Aldehyde_DH_NAD(P).
DR   Pfam; PF00171; Aldedh; 1.
DR   PIRSF; PIRSF036492; ALDH; 1.
DR   SUPFAM; SSF53720; SSF53720; 1.
DR   PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE   3: Inferred from homology;
KW   NAD; Oxidoreductase; Reference proteome.
FT   CHAIN           1..495
FT                   /note="Putative aldehyde dehydrogenase DhaS"
FT                   /id="PRO_0000379509"
FT   ACT_SITE        266
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10007"
FT   ACT_SITE        300
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10007"
FT   BINDING         244..249
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   495 AA;  53882 MW;  24EBC782F47034A8 CRC64;
     MSSLTMQVTK RLETFLQGTK KLYIDGKFVP SASGATFDTP NPATGETLMT LYEAQAADVD
     KAVKAARKAF DQGEWRTMSP ASRSRLMYKL ADLMEEHKTE LAQLETLDNG KPINETTNGD
     IPLAIEHMRY YAGWCTKITG QTIPVSGAYF NYTRHEPVGV VGQIIPWNFP LLMAMWKMGA
     ALATGCTIVL KPAEQTPLSA LYLAELIDQA GFPAGVINII PGFGEDAGEA LTNHEAVDKI
     AFTGSTEIGK KIMSTAAKSI KRVTLELGGK SPNILLPDAN LKKAIPGALN GVMFNQGQVC
     CAGSRVFIHK DQYDEVVDEM ASYAESLRQG AGLHKDTQIG PLVSKEQHER VLSYIQKGKD
     EGAKAVTGGS CPFEAGYFVA PTVFANVEDE MTIAKEEIFG PVLTAIPYET VDEVIERANH
     SEYGLAAGLW TENVKQAHYI ADRLQAGTVW VNCYNVFDAA SPFGGYKQSG LGREMGSYAL
     DNYTEVKSVW VNLED