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Database: UniProt/SWISS-PROT
Entry: ALDH5_BACSU
LinkDB: ALDH5_BACSU
Original site: ALDH5_BACSU 
ID   ALDH5_BACSU             Reviewed;         485 AA.
AC   O06478; Q797A6;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   16-JAN-2019, entry version 112.
DE   RecName: Full=Benzaldehyde dehydrogenase YfmT {ECO:0000255|PROSITE-ProRule:PRU10007, ECO:0000305|PubMed:26658822};
DE            EC=1.2.1.28 {ECO:0000269|PubMed:26658822};
DE   AltName: Full=Vanillin dehydrogenase {ECO:0000303|PubMed:26658822};
DE            EC=1.2.1.67 {ECO:0000269|PubMed:26658822};
GN   Name=yfmT; OrderedLocusNames=BSU07350;
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 / AC327;
RX   PubMed=9141694; DOI=10.1099/00221287-143-4-1317;
RA   Yamamoto H., Uchiyama S., Nugroho F.A., Sekiguchi J.;
RT   "A 23.4 kb segment at the 69 degrees-70 degrees region of the Bacillus
RT   subtilis genome.";
RL   Microbiology 143:1317-1320(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.,
RA   Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S.,
RA   Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S.,
RA   Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M.,
RA   Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A.,
RA   Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T.,
RA   Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D.,
RA   Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N.,
RA   Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G.,
RA   Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A.,
RA   Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M.,
RA   Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M.,
RA   Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S.,
RA   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.,
RA   Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B.,
RA   Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R.,
RA   Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P.,
RA   Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H.,
RA   Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P.,
RA   Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F.,
RA   Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H.,
RA   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   INDUCTION, AND OPERON STRUCTURE.
RC   STRAIN=168;
RX   PubMed=15033535; DOI=10.1016/j.gene.2003.12.024;
RA   Serizawa M., Yamamoto H., Yamaguchi H., Fujita Y., Kobayashi K.,
RA   Ogasawara N., Sekiguchi J.;
RT   "Systematic analysis of SigD-regulated genes in Bacillus subtilis by
RT   DNA microarray and Northern blotting analyses.";
RL   Gene 329:125-136(2004).
RN   [4]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND 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
RT   YfmT in Bacillus subtilis 3NA.";
RL   Appl. Microbiol. Biotechnol. 100:3511-3521(2016).
CC   -!- FUNCTION: A benzaldehyde dehydrogenase able to act on substrates
CC       with 3- and 4-hydroxy and methoxy substitutions; converts vanillin
CC       (4-hydroxy-3-methoxybenzaldehyde) to vanillic acid in vitro
CC       (PubMed:26658822). The physiological substrate is unknown
CC       (PubMed:26658822). {ECO:0000269|PubMed:26658822}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=benzaldehyde + H2O + NAD(+) = benzoate + 2 H(+) + NADH;
CC         Xref=Rhea:RHEA:11840, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16150, ChEBI:CHEBI:17169, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945; EC=1.2.1.28;
CC         Evidence={ECO:0000269|PubMed:26658822};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-hydroxy-3-methoxybenzaldehyde + H2O + NAD(+) = 4-
CC         hydroxy-3-methoxybenzoate + 2 H(+) + NADH; Xref=Rhea:RHEA:13309,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16632,
CC         ChEBI:CHEBI:18346, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC         EC=1.2.1.67; Evidence={ECO:0000269|PubMed:26658822};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 7.0. {ECO:0000269|PubMed:26658822};
CC       Temperature dependence:
CC         Optimum temperature is 37-40 degrees Celsius.
CC         {ECO:0000269|PubMed:26658822};
CC   -!- INDUCTION: Transcriptionally regulated by SigD; part of the
CC       yfmT/yfmS operon. {ECO:0000269|PubMed:15033535}.
CC   -!- DISRUPTION PHENOTYPE: Loss of conversion of vanillin to vanillic
CC       acid (PubMed:26658822). {ECO:0000269|PubMed:26658822}.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000305}.
DR   EMBL; D86418; BAA20109.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB12554.1; -; Genomic_DNA.
DR   PIR; C69814; C69814.
DR   RefSeq; NP_388616.1; NC_000964.3.
DR   RefSeq; WP_003244104.1; NZ_JNCM01000032.1.
DR   ProteinModelPortal; O06478; -.
DR   SMR; O06478; -.
DR   IntAct; O06478; 1.
DR   MINT; O06478; -.
DR   STRING; 224308.Bsubs1_010100004118; -.
DR   jPOST; O06478; -.
DR   PaxDb; O06478; -.
DR   PRIDE; O06478; -.
DR   EnsemblBacteria; CAB12554; CAB12554; BSU07350.
DR   GeneID; 938788; -.
DR   KEGG; bsu:BSU07350; -.
DR   PATRIC; fig|224308.179.peg.797; -.
DR   eggNOG; ENOG4105C26; Bacteria.
DR   eggNOG; COG1012; LUCA.
DR   HOGENOM; HOG000271509; -.
DR   InParanoid; O06478; -.
DR   KO; K21802; -.
DR   OMA; QVCMAAN; -.
DR   PhylomeDB; O06478; -.
DR   BioCyc; BSUB:BSU07350-MONOMER; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0018479; F:benzaldehyde dehydrogenase (NAD+) activity; IDA:UniProtKB.
DR   GO; GO:0050608; F:vanillin dehydrogenase activity; IEA:UniProtKB-EC.
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   Pfam; PF00171; Aldedh; 1.
DR   SUPFAM; SSF53720; SSF53720; 1.
DR   PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; NAD; Oxidoreductase; Reference proteome.
FT   CHAIN         1    485       Benzaldehyde dehydrogenase YfmT.
FT                                /FTId=PRO_0000379510.
FT   NP_BIND     231    236       NAD. {ECO:0000250}.
FT   ACT_SITE    253    253       {ECO:0000255|PROSITE-ProRule:PRU10007}.
FT   ACT_SITE    287    287       {ECO:0000255|PROSITE-ProRule:PRU10007}.
SQ   SEQUENCE   485 AA;  53321 MW;  C87E9AA12C704B68 CRC64;
     MFQYEELNKQ FIGGKWQEGS SPNVLENKNP YTQKTFTTFR KATADDVDEA YRAAALAKKK
     WDAVNPFEKR TILEKAVTYI EENEEAIIYL IMEELGGTRL KAAFEIGLVK NIIKEAATFP
     IRMEGKILPS TIDGKENRLY RVPAGVVGVI SPFNFPFFLS MKSVAPALGA GNGVVLKPHE
     ETPICGGTLI AKIFENAGIP AGLLNVVVTD IAEIGDSFVE HPVPRIISFT GSTKVGSYIG
     QLAMKHFKKP LLELGGNSAF IVLEDADIEY AVNAAVFSRF THQGQICMSA NRVLVHSSIY
     DKFLELYQAK VESLKVGDPM DPDTIIGPLI NSRQTDGLMK TVEQAIEEGA VPVKLGGFNG
     TIVEPTILKD VKPFMSIAKE ELFGPVVSFM KFDSEDEAVD IANETPFGLS GAVHTSNLER
     GVAFAKRIET GMIHVNDTTI NDEPNVAFGG EKQSGLGRLN GEWSLEEFTT LKWISVQHEK
     RSFPY
//
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