ID ALDH_STAAM Reviewed; 475 AA. AC Q99SD6; DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 27-MAR-2024, entry version 123. DE RecName: Full=Putative aldehyde dehydrogenase {ECO:0000305}; DE EC=1.2.1.3 {ECO:0000305}; GN OrderedLocusNames=SAV2122; OS Staphylococcus aureus (strain Mu50 / ATCC 700699). OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae; OC Staphylococcus. OX NCBI_TaxID=158878; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Mu50 / ATCC 700699; 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 X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS), AND SUBUNIT. RA Kim Y., Joachimiak G., Jedrzejczak R., Rubin E., Ioerger T., RA Sacchettini J., Joachimiak A.; RT "Crystal structure of aldehyde dehydrogenase family protein from RT Staphylococcus aureus."; RL Submitted (SEP-2011) to the PDB data bank. 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:0000305}; CC -!- SUBUNIT: Homodimer. {ECO:0000305|Ref.2}. 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; BA000017; BAB58284.1; -; Genomic_DNA. DR RefSeq; WP_001206093.1; NC_002758.2. DR PDB; 3TY7; X-ray; 2.40 A; A/B=1-475. DR PDBsum; 3TY7; -. DR AlphaFoldDB; Q99SD6; -. DR SMR; Q99SD6; -. DR KEGG; sav:SAV2122; -. DR HOGENOM; CLU_005391_0_2_9; -. DR PhylomeDB; Q99SD6; -. DR EvolutionaryTrace; Q99SD6; -. DR Proteomes; UP000002481; 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 GO; GO:0006081; P:cellular aldehyde metabolic process; IEA:InterPro. DR GO; GO:0070887; P:cellular response to chemical stimulus; IEA:UniProt. DR CDD; cd07138; ALDH_CddD_SSP0762; 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; PTHR42804; ALDEHYDE DEHYDROGENASE; 1. DR PANTHER; PTHR42804:SF1; ALDEHYDE DEHYDROGENASE-RELATED; 1. DR Pfam; PF00171; Aldedh; 1. DR PIRSF; PIRSF036492; ALDH; 1. DR SUPFAM; SSF53720; ALDH-like; 1. DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1. DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1. DR World-2DPAGE; 0002:Q99SD6; -. PE 1: Evidence at protein level; KW 3D-structure; NAD; Oxidoreductase. FT CHAIN 1..475 FT /note="Putative aldehyde dehydrogenase" FT /id="PRO_0000293556" FT ACT_SITE 245 FT /note="Proton acceptor" FT /evidence="ECO:0000250|UniProtKB:P25526" FT ACT_SITE 279 FT /note="Nucleophile" FT /evidence="ECO:0000250|UniProtKB:P25526" FT BINDING 146..147 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P25526" FT BINDING 223..224 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P25526" FT BINDING 246 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P25526" FT BINDING 379 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P25526" FT STRAND 6..9 FT /evidence="ECO:0007829|PDB:3TY7" FT STRAND 12..15 FT /evidence="ECO:0007829|PDB:3TY7" FT STRAND 17..19 FT /evidence="ECO:0007829|PDB:3TY7" FT STRAND 21..25 FT /evidence="ECO:0007829|PDB:3TY7" FT TURN 27..29 FT /evidence="ECO:0007829|PDB:3TY7" FT STRAND 32..37 FT /evidence="ECO:0007829|PDB:3TY7" FT HELIX 41..59 FT /evidence="ECO:0007829|PDB:3TY7" FT HELIX 63..79 FT /evidence="ECO:0007829|PDB:3TY7" FT HELIX 81..92 FT /evidence="ECO:0007829|PDB:3TY7" FT HELIX 96..101 FT /evidence="ECO:0007829|PDB:3TY7" FT HELIX 103..120 FT /evidence="ECO:0007829|PDB:3TY7" FT STRAND 123..127 FT /evidence="ECO:0007829|PDB:3TY7" FT STRAND 130..136 FT /evidence="ECO:0007829|PDB:3TY7" FT STRAND 140..143 FT /evidence="ECO:0007829|PDB:3TY7" FT STRAND 146..148 FT /evidence="ECO:0007829|PDB:3TY7" FT HELIX 151..163 FT /evidence="ECO:0007829|PDB:3TY7" FT STRAND 167..170 FT /evidence="ECO:0007829|PDB:3TY7" FT HELIX 177..189 FT /evidence="ECO:0007829|PDB:3TY7" FT TURN 193..195 FT /evidence="ECO:0007829|PDB:3TY7" FT STRAND 196..198 FT /evidence="ECO:0007829|PDB:3TY7" FT TURN 203..206 FT /evidence="ECO:0007829|PDB:3TY7" FT HELIX 207..212 FT /evidence="ECO:0007829|PDB:3TY7" FT STRAND 218..221 FT /evidence="ECO:0007829|PDB:3TY7" FT HELIX 225..228 FT /evidence="ECO:0007829|PDB:3TY7" FT TURN 235..239 FT /evidence="ECO:0007829|PDB:3TY7" FT STRAND 241..243 FT /evidence="ECO:0007829|PDB:3TY7" FT STRAND 251..254 FT /evidence="ECO:0007829|PDB:3TY7" FT HELIX 260..272 FT /evidence="ECO:0007829|PDB:3TY7" FT HELIX 273..276 FT /evidence="ECO:0007829|PDB:3TY7" FT STRAND 284..288 FT /evidence="ECO:0007829|PDB:3TY7" FT TURN 289..291 FT /evidence="ECO:0007829|PDB:3TY7" FT HELIX 292..304 FT /evidence="ECO:0007829|PDB:3TY7" FT HELIX 324..340 FT /evidence="ECO:0007829|PDB:3TY7" FT STRAND 343..346 FT /evidence="ECO:0007829|PDB:3TY7" FT STRAND 364..368 FT /evidence="ECO:0007829|PDB:3TY7" FT HELIX 374..377 FT /evidence="ECO:0007829|PDB:3TY7" FT STRAND 382..392 FT /evidence="ECO:0007829|PDB:3TY7" FT HELIX 393..400 FT /evidence="ECO:0007829|PDB:3TY7" FT STRAND 407..412 FT /evidence="ECO:0007829|PDB:3TY7" FT HELIX 416..425 FT /evidence="ECO:0007829|PDB:3TY7" FT STRAND 428..433 FT /evidence="ECO:0007829|PDB:3TY7" FT HELIX 462..464 FT /evidence="ECO:0007829|PDB:3TY7" FT STRAND 465..471 FT /evidence="ECO:0007829|PDB:3TY7" SQ SEQUENCE 475 AA; 51969 MW; 03C66ED0B87BC09A CRC64; MRDYTKQYIN GEWVESNSNE TIEVINPATE EVIGKVAKGN KADVDKAVEA ADDVYLEFRH TSVKERQALL DKIVKEYENR KDDIVQAITD ELGAPLSLSE RVHYQMGLNH FVAARDALDN YEFEERRGDD LVVKEAIGVS GLITPWNFPT NQTSLKLAAA FAAGSPVVLK PSEETPFAAV ILAEIFDKVG VPKGVFNLVN GDGAGVGNPL SEHPKVRMMS FTGSGPTGSK IMEKAAKDFK KVSLELGGKS PYIVLDDVDI KEAAKATTGK VVNNTGQVCT AGTRVLVPNK IKDAFLAELK EQFSQVRVGN PREDGTQVGP IISKKQFDQV QNYINKGIEE GAELFYGGPG KPEGLEKGYF ARPTIFINVD NQMTIAQEEI FGPVMSVITY NDLDEAIQIA NDTKYGLAGY VIGKDKETLH KVARSIEAGT VEINEAGRKP DLPFGGYKQS GLGREWGDYG IEEFLEVKSI AGYFK //