ALDH3_BACSU
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 03-AUG-2022, entry version 137.
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; ORFNames=VE7FR;
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 / 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; P46329; -.
DR PRIDE; P46329; -.
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 OMA; RRITWAA; -.
DR PhylomeDB; P46329; -.
DR BioCyc; BSUB:BSU39860-MON; -.
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 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; 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; PTHR43570; 1.
DR Pfam; PF00171; Aldedh; 1.
DR PIRSF; PIRSF036492; ALDH; 1.
DR SUPFAM; SSF53720; SSF53720; 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