ID ALDA_STAAN Reviewed; 495 AA. AC Q7A825; DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 27-MAR-2024, entry version 106. DE RecName: Full=Putative aldehyde dehydrogenase AldA; DE EC=1.2.1.3; GN Name=aldA; OrderedLocusNames=SA0162; OS Staphylococcus aureus (strain N315). OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae; OC Staphylococcus. OX NCBI_TaxID=158879; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=N315; RX PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2; RA Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L., RA Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M., RA Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y., RA Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H., RA Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K., RA Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H., RA Hiramatsu K.; RT "Whole genome sequencing of meticillin-resistant Staphylococcus aureus."; RL Lancet 357:1225-1240(2001). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=N315; RX PubMed=15590099; DOI=10.1016/j.mimet.2004.09.017; RA Scherl A., Francois P., Bento M., Deshusses J.M., Charbonnier Y., RA Converset V., Huyghe A., Walter N., Hoogland C., Appel R.D., Sanchez J.-C., RA Zimmermann-Ivol C.G., Corthals G.L., Hochstrasser D.F., Schrenzel J.; RT "Correlation of proteomic and transcriptomic profiles of Staphylococcus RT aureus during the post-exponential phase of growth."; RL J. Microbiol. Methods 60:247-257(2005). RN [3] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC STRAIN=N315; RA Vaezzadeh A.R., Deshusses J., Lescuyer P., Hochstrasser D.F.; RT "Shotgun proteomic analysis of total and membrane protein extracts of S. RT aureus strain N315."; RL Submitted (OCT-2007) to UniProtKB. 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; CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BA000018; BAB41382.1; -; Genomic_DNA. DR PIR; C89778; C89778. DR RefSeq; WP_000290397.1; NC_002745.2. DR AlphaFoldDB; Q7A825; -. DR SMR; Q7A825; -. DR EnsemblBacteria; BAB41382; BAB41382; BAB41382. DR KEGG; sau:SA0162; -. DR HOGENOM; CLU_005391_0_2_9; -. DR Proteomes; UP000000751; 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 CDD; cd07117; ALDH_StaphAldA1; 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 PANTHER; PTHR43111; ALDEHYDE DEHYDROGENASE B-RELATED; 1. DR PANTHER; PTHR43111:SF1; ALDEHYDE DEHYDROGENASE B-RELATED; 1. DR Pfam; PF00171; Aldedh; 1. DR SUPFAM; SSF53720; ALDH-like; 1. DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1. DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1. DR SWISS-2DPAGE; Q7A825; -. PE 1: Evidence at protein level; KW NAD; Oxidoreductase. FT CHAIN 1..495 FT /note="Putative aldehyde dehydrogenase AldA" FT /id="PRO_0000056457" FT ACT_SITE 256 FT /evidence="ECO:0000250" FT ACT_SITE 290 FT /evidence="ECO:0000250" FT BINDING 212..218 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" SQ SEQUENCE 495 AA; 53660 MW; 36B448F85BFECD02 CRC64; MAVNVRDYIA ENYGLFINGE FVKGSSDETI EVTNPATGET LSHITRAKDK DVDHAVKVAQ EAFESWSLTS KSERAQMLRD IGDKLMAQKD KIAMIETLNN GKPIRETTAI DIPFAARHFH YFASVIETEE GTVNDIDKDT MSIVRHEPIG VVGAVVAWNF PMLLAAWKIA PAIAAGNTIV IQPSSSTPLS LLEVAKIFQE VLPKGVVNIL TGKGSESGNA IFNHDGVDKL SFTGSTDVGY QVAEAAAKHL VPATLELGGK SANIILDDAN LDLAVEGIQL GILFNQGEVC SAGSRLLVHE KIYDQLVPRL QEAFSNIKVG DPQDEATQMG SQTGKDQLDK IQSYIDAAKE SDAQILAGGH RLTENGLDKG FFFEPTLIAV PDNHHKLAQE EIFGPVLTVI KVKDDQEAID IANDSEYGLA GGVFSQNITR ALNIAKAVRT GRIWINTYNQ VPEGAPFGGY KKSGIGRETY KGALSNYQQV KNIYIDTSNA LKGLY //