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 03-AUG-2022, entry version 124.
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., 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 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 DNA
RT microarray and Northern blotting analyses.";
RL Gene 329:125-136(2004).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL
RP 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 YfmT in
RT Bacillus subtilis 3NA.";
RL Appl. Microbiol. Biotechnol. 100:3511-3521(2016).
CC -!- FUNCTION: A benzaldehyde dehydrogenase able to act on substrates with
CC 3- and 4-hydroxy and methoxy substitutions; converts vanillin (4-
CC 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=H2O + NAD(+) + vanillin = 2 H(+) + NADH + vanillate;
CC Xref=Rhea:RHEA:13309, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16632, ChEBI:CHEBI:18346, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.2.1.67;
CC 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 yfmT/yfmS
CC operon. {ECO:0000269|PubMed:15033535}.
CC -!- DISRUPTION PHENOTYPE: Loss of conversion of vanillin to vanillic acid
CC (PubMed:26658822). {ECO:0000269|PubMed:26658822}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000305}.
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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 AlphaFoldDB; O06478; -.
DR SMR; O06478; -.
DR IntAct; O06478; 1.
DR MINT; O06478; -.
DR STRING; 224308.BSU07350; -.
DR jPOST; O06478; -.
DR PaxDb; O06478; -.
DR PRIDE; O06478; -.
DR EnsemblBacteria; CAB12554; CAB12554; BSU_07350.
DR GeneID; 938788; -.
DR KEGG; bsu:BSU07350; -.
DR PATRIC; fig|224308.179.peg.797; -.
DR eggNOG; COG1012; Bacteria.
DR InParanoid; O06478; -.
DR OMA; KAMRWYA; -.
DR PhylomeDB; O06478; -.
DR BioCyc; BSUB:BSU07350-MON; -.
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 NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..485
FT /note="Benzaldehyde dehydrogenase YfmT"
FT /id="PRO_0000379510"
FT ACT_SITE 253
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007"
FT ACT_SITE 287
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007"
FT BINDING 231..236
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
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
