ALDY_BACSU
ID ALDY_BACSU Reviewed; 485 AA.
AC P94358; Q794X7;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Putative aldehyde dehydrogenase AldY {ECO:0000255|PROSITE-ProRule:PRU10007};
DE EC=1.2.1.3 {ECO:0000255|PROSITE-ProRule:PRU10007};
GN Name=aldY; Synonyms=yxkE; OrderedLocusNames=BSU38830;
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=8969509; DOI=10.1099/13500872-142-11-3113;
RA Yoshida K., Shindo K., Sano H., Seki S., Fujimura M., Yanai N., Miwa Y.,
RA Fujita Y.;
RT "Sequencing of a 65 kb region of the Bacillus subtilis genome containing
RT the lic and cel loci, and creation of a 177 kb contig covering the gnt-
RT sacXY region.";
RL Microbiology 142:3113-3123(1996).
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 FUNCTION, AND INDUCTION BY STRESS.
RX PubMed=10482513; DOI=10.1128/jb.181.18.5718-5724.1999;
RA Petersohn A., Bernhardt J., Gerth U., Hoeper D., Koburger T., Voelker U.,
RA Hecker M.;
RT "Identification of sigma(B)-dependent genes in Bacillus subtilis using a
RT promoter consensus-directed search and oligonucleotide hybridization.";
RL J. Bacteriol. 181:5718-5724(1999).
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).
RN [5] {ECO:0007744|PDB:4DNG}
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS).
RA Malashkevich V.N., Bhosle R., Toro R., Seidel R., Almo S.C.;
RT "Crystal structure of putative aldehyde dehydrogenase from Bacillus
RT subtilis subsp. subtilis str. 168.";
RL Submitted (FEB-2012) to the PDB data bank.
CC -!- FUNCTION: May contribute to protect cells against stress due to ethanol
CC and related compounds. {ECO:0000305|PubMed:10482513}.
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 -!- INDUCTION: Activated by SigB in response to stress due to ethanol.
CC {ECO:0000269|PubMed:10482513}.
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; D83026; BAA11721.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15909.1; -; Genomic_DNA.
DR PIR; C69584; C69584.
DR RefSeq; NP_391762.1; NC_000964.3.
DR RefSeq; WP_003243062.1; NZ_JNCM01000034.1.
DR PDB; 4DNG; X-ray; 2.50 A; A/B=1-485.
DR PDBsum; 4DNG; -.
DR AlphaFoldDB; P94358; -.
DR SMR; P94358; -.
DR STRING; 224308.BSU38830; -.
DR PaxDb; P94358; -.
DR PRIDE; P94358; -.
DR EnsemblBacteria; CAB15909; CAB15909; BSU_38830.
DR GeneID; 937414; -.
DR KEGG; bsu:BSU38830; -.
DR PATRIC; fig|224308.179.peg.4202; -.
DR eggNOG; COG1012; Bacteria.
DR InParanoid; P94358; -.
DR OMA; PFGGEKH; -.
DR PhylomeDB; P94358; -.
DR BioCyc; BSUB:BSU38830-MON; -.
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 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 3D-structure; NAD; Oxidoreductase; Reference proteome; Stress response.
FT CHAIN 1..485
FT /note="Putative aldehyde dehydrogenase AldY"
FT /id="PRO_0000360858"
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"
FT HELIX 3..5
FT /evidence="ECO:0007829|PDB:4DNG"
FT STRAND 8..11
FT /evidence="ECO:0007829|PDB:4DNG"
FT STRAND 14..16
FT /evidence="ECO:0007829|PDB:4DNG"
FT STRAND 19..21
FT /evidence="ECO:0007829|PDB:4DNG"
FT STRAND 23..27
FT /evidence="ECO:0007829|PDB:4DNG"
FT TURN 29..31
FT /evidence="ECO:0007829|PDB:4DNG"
FT STRAND 34..39
FT /evidence="ECO:0007829|PDB:4DNG"
FT HELIX 43..60
FT /evidence="ECO:0007829|PDB:4DNG"
FT HELIX 65..81
FT /evidence="ECO:0007829|PDB:4DNG"
FT HELIX 83..94
FT /evidence="ECO:0007829|PDB:4DNG"
FT HELIX 98..118
FT /evidence="ECO:0007829|PDB:4DNG"
FT HELIX 119..121
FT /evidence="ECO:0007829|PDB:4DNG"
FT STRAND 135..143
FT /evidence="ECO:0007829|PDB:4DNG"
FT STRAND 146..150
FT /evidence="ECO:0007829|PDB:4DNG"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:4DNG"
FT HELIX 156..169
FT /evidence="ECO:0007829|PDB:4DNG"
FT STRAND 173..177
FT /evidence="ECO:0007829|PDB:4DNG"
FT HELIX 180..182
FT /evidence="ECO:0007829|PDB:4DNG"
FT HELIX 183..186
FT /evidence="ECO:0007829|PDB:4DNG"
FT HELIX 188..196
FT /evidence="ECO:0007829|PDB:4DNG"
FT STRAND 203..206
FT /evidence="ECO:0007829|PDB:4DNG"
FT HELIX 211..214
FT /evidence="ECO:0007829|PDB:4DNG"
FT HELIX 217..220
FT /evidence="ECO:0007829|PDB:4DNG"
FT STRAND 225..231
FT /evidence="ECO:0007829|PDB:4DNG"
FT HELIX 233..246
FT /evidence="ECO:0007829|PDB:4DNG"
FT STRAND 249..254
FT /evidence="ECO:0007829|PDB:4DNG"
FT STRAND 258..262
FT /evidence="ECO:0007829|PDB:4DNG"
FT HELIX 268..279
FT /evidence="ECO:0007829|PDB:4DNG"
FT STRAND 290..296
FT /evidence="ECO:0007829|PDB:4DNG"
FT HELIX 297..313
FT /evidence="ECO:0007829|PDB:4DNG"
FT HELIX 332..347
FT /evidence="ECO:0007829|PDB:4DNG"
FT STRAND 351..354
FT /evidence="ECO:0007829|PDB:4DNG"
FT STRAND 366..370
FT /evidence="ECO:0007829|PDB:4DNG"
FT HELIX 376..379
FT /evidence="ECO:0007829|PDB:4DNG"
FT STRAND 384..394
FT /evidence="ECO:0007829|PDB:4DNG"
FT HELIX 395..403
FT /evidence="ECO:0007829|PDB:4DNG"
FT STRAND 409..414
FT /evidence="ECO:0007829|PDB:4DNG"
FT HELIX 418..425
FT /evidence="ECO:0007829|PDB:4DNG"
FT STRAND 430..436
FT /evidence="ECO:0007829|PDB:4DNG"
FT HELIX 462..468
FT /evidence="ECO:0007829|PDB:4DNG"
FT STRAND 469..477
FT /evidence="ECO:0007829|PDB:4DNG"
SQ SEQUENCE 485 AA; 52821 MW; 98629186CD05C4A0 CRC64;
MSFETLNKSF INGKWTGGES GRTEDILNPY DQSVITTASL ATGKQLEDAF DIAQKAQKEW
AKSTTEDRKA VLQKARGYLH ENRDDIIMMI ARETGGTIIK STIELEQTIA ILDEAMTYTG
ELGGVKEVPS DIEGKTNKIY RLPLGVISSI SPFNFPMNLS MRSIAPAIAL GNSVVHKPDI
QTAISGGTII AKAFEHAGLP AGVLNVMLTD VKEIGDGMLT NPIPRLISFT GSTAVGRHIG
EIAGRAFKRM ALELGGNNPF AVLSDADVDR AVDAAIFGKF IHQGQICMII NRIIVHQDVY
DEFVEKFTAR VKQLPYGDQT DPKTVVGPLI NERQIEKALE IIEQAKTDGI ELAVEGKRVG
NVLTPYVFVG ADNNSKIAQT ELFAPIATII KAGSDQEAID MANDTEYGLS SAVFTSDLEK
GEKFALQIDS GMTHVNDQSV NDSPNIAFGG NKASGVGRFG NPWVVEEFTV TKWISIQKQY
RKYPF
