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 27-MAR-2024, entry version 130.
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; Bacillota; 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; 224308-BSU19310; -.
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 OrthoDB; 9762913at2; -.
DR PhylomeDB; O34660; -.
DR BioCyc; BSUB:BSU19310-MONOMER; -.
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 CDD; cd07091; ALDH_F1-2_Ald2-like; 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 PANTHER; PTHR11699:SF211; ALDEHYDE DEHYDROGENASE FAMILY 16 MEMBER A1; 1.
DR PANTHER; PTHR11699; ALDEHYDE DEHYDROGENASE-RELATED; 1.
DR Pfam; PF00171; Aldedh; 1.
DR PIRSF; PIRSF036492; ALDH; 1.
DR SUPFAM; SSF53720; ALDH-like; 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
//
