ID   ALDH3_BACSU             Reviewed;         445 AA.
AC   P46329;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 2.
DT   27-MAR-2024, entry version 144.
DE   RecName: Full=Putative aldehyde dehydrogenase AldX {ECO:0000255|PROSITE-ProRule:PRU10007};
DE            EC=1.2.1.3 {ECO:0000255|PROSITE-ProRule:PRU10007};
GN   Name=aldX; Synonyms=yxaS, yxbE; OrderedLocusNames=BSU39860;
GN   ORFNames=VE7FR;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / BGSC1A1;
RX   PubMed=7584049; DOI=10.1093/dnares/2.2.61;
RA   Yoshida K., Seki S., Fujimura M., Miwa Y., Fujita Y.;
RT   "Cloning and sequencing of a 36-kb region of the Bacillus subtilis genome
RT   between the gnt and iol operons.";
RL   DNA Res. 2:61-69(1995).
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 163.
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 / 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; AB005554; BAA21599.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB16022.2; -; Genomic_DNA.
DR   PIR; B69584; B69584.
DR   RefSeq; NP_391865.2; NC_000964.3.
DR   RefSeq; WP_003243415.1; NZ_JNCM01000034.1.
DR   AlphaFoldDB; P46329; -.
DR   SMR; P46329; -.
DR   STRING; 224308.BSU39860; -.
DR   PaxDb; 224308-BSU39860; -.
DR   EnsemblBacteria; CAB16022; CAB16022; BSU_39860.
DR   GeneID; 937653; -.
DR   KEGG; bsu:BSU39860; -.
DR   PATRIC; fig|224308.179.peg.4312; -.
DR   eggNOG; COG1012; Bacteria.
DR   InParanoid; P46329; -.
DR   OrthoDB; 9762913at2; -.
DR   PhylomeDB; P46329; -.
DR   BioCyc; BSUB:BSU39860-MONOMER; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; IBA:GO_Central.
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; IBA:GO_Central.
DR   CDD; cd07134; ALDH_AlkH-like; 1.
DR   InterPro; IPR016161; Ald_DH/histidinol_DH.
DR   InterPro; IPR016163; Ald_DH_C.
DR   InterPro; IPR016160; Ald_DH_CS_CYS.
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; PTHR43570; ALDEHYDE DEHYDROGENASE; 1.
DR   PANTHER; PTHR43570:SF16; ALDEHYDE DEHYDROGENASE TYPE III, ISOFORM Q; 1.
DR   Pfam; PF00171; Aldedh; 1.
DR   PIRSF; PIRSF036492; ALDH; 1.
DR   SUPFAM; SSF53720; ALDH-like; 1.
DR   PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR   PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE   3: Inferred from homology;
KW   NAD; Oxidoreductase; Reference proteome.
FT   CHAIN           1..445
FT                   /note="Putative aldehyde dehydrogenase AldX"
FT                   /id="PRO_0000056446"
FT   ACT_SITE        214
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10007"
FT   ACT_SITE        248
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10008"
FT   CONFLICT        163
FT                   /note="D -> N (in Ref. 1; BAA21599)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   445 AA;  49571 MW;  B705ABD3EFF43A2E CRC64;
     MEQQVKDDIQ RVFQLQKKQQ KALRASTAEQ RREKLQRFLD SVIAHEEEII EAIRKDVRKP
     YHEVKKAEIE GTKKAIRDNM NNLEQWMAPK EVGSSLSPDA NGILMYEPKG VTLILGPWNY
     PFMLTMAPLA ASLAAGNSAI VKLSDFTMNT SNIAAKVIRD AFDEKEVAIF EGEVEVATEL
     LDQPFDHIFF TGSTNVGKIV MTAAAKHLAS VTLELGGKSP TIIDSEYDLM DAAKKIAVGK
     FVNAGQTCIA PDYLFIKKDV QDRFAGILQT VVNAGFMEDD HTPDRSKFTQ IVNDRNFNRV
     KDLFDDAIER GAEVVFGGVF DASDRTISPT VLKNVTPDMK IMQEEIFASI LPMMNYEDID
     EVIDYVNDRD KPLALYVFSK NQDLIDNVLQ HTTSGNAAIN DVVVHFSDVN LPFGGVNTSG
     IGSYHGVYGF KEFSHEKGVF IQAAE
//