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Database: UniProt/SWISS-PROT
Entry: ALDH_STAAM
LinkDB: ALDH_STAAM
Original site: ALDH_STAAM 
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   10-APR-2019, entry version 103.
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; Firmicutes; 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.,
RA   Cui L., 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.,
RA   Hirakawa H., Kuhara S., Goto S., Yabuzaki J., Kanehisa M.,
RA   Yamashita A., Oshima K., Furuya K., Yoshino C., Shiba T., Hattori M.,
RA   Ogasawara N., Hayashi H., Hiramatsu K.;
RT   "Whole genome sequencing of meticillin-resistant Staphylococcus
RT   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(+) +
CC         NADH; Xref=Rhea:RHEA:16185, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17478, ChEBI:CHEBI:29067,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.2.1.3;
CC         Evidence={ECO:0000305};
CC   -!- SUBUNIT: Homodimer. {ECO:0000305|Ref.2}.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000305}.
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   ProteinModelPortal; Q99SD6; -.
DR   SMR; Q99SD6; -.
DR   World-2DPAGE; 0002:Q99SD6; -.
DR   PaxDb; Q99SD6; -.
DR   EnsemblBacteria; BAB58284; BAB58284; SAV2122.
DR   KEGG; sav:SAV2122; -.
DR   eggNOG; ENOG4105C26; Bacteria.
DR   eggNOG; COG1012; LUCA.
DR   HOGENOM; HOG000271505; -.
DR   KO; K00128; -.
DR   OMA; KTIWIAL; -.
DR   PhylomeDB; Q99SD6; -.
DR   BioCyc; SAUR158878:SAV_RS11605-MONOMER; -.
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   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; 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   Pfam; PF00171; Aldedh; 1.
DR   PIRSF; PIRSF036492; ALDH; 1.
DR   SUPFAM; SSF53720; SSF53720; 1.
DR   PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR   PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Complete proteome; NAD; Oxidoreductase.
FT   CHAIN         1    475       Putative aldehyde dehydrogenase.
FT                                /FTId=PRO_0000293556.
FT   NP_BIND     146    147       NAD. {ECO:0000250|UniProtKB:P25526}.
FT   NP_BIND     223    224       NAD. {ECO:0000250|UniProtKB:P25526}.
FT   ACT_SITE    245    245       Proton acceptor.
FT                                {ECO:0000250|UniProtKB:P25526}.
FT   ACT_SITE    279    279       Nucleophile.
FT                                {ECO:0000250|UniProtKB:P25526}.
FT   BINDING     246    246       NAD; via carbonyl oxygen.
FT                                {ECO:0000250|UniProtKB:P25526}.
FT   BINDING     379    379       NAD. {ECO:0000250|UniProtKB:P25526}.
FT   STRAND        6      9       {ECO:0000244|PDB:3TY7}.
FT   STRAND       12     15       {ECO:0000244|PDB:3TY7}.
FT   STRAND       17     19       {ECO:0000244|PDB:3TY7}.
FT   STRAND       21     25       {ECO:0000244|PDB:3TY7}.
FT   TURN         27     29       {ECO:0000244|PDB:3TY7}.
FT   STRAND       32     37       {ECO:0000244|PDB:3TY7}.
FT   HELIX        41     59       {ECO:0000244|PDB:3TY7}.
FT   HELIX        63     79       {ECO:0000244|PDB:3TY7}.
FT   HELIX        81     92       {ECO:0000244|PDB:3TY7}.
FT   HELIX        96    101       {ECO:0000244|PDB:3TY7}.
FT   HELIX       103    120       {ECO:0000244|PDB:3TY7}.
FT   STRAND      123    127       {ECO:0000244|PDB:3TY7}.
FT   STRAND      130    136       {ECO:0000244|PDB:3TY7}.
FT   STRAND      140    143       {ECO:0000244|PDB:3TY7}.
FT   STRAND      146    148       {ECO:0000244|PDB:3TY7}.
FT   HELIX       151    163       {ECO:0000244|PDB:3TY7}.
FT   STRAND      167    170       {ECO:0000244|PDB:3TY7}.
FT   HELIX       177    189       {ECO:0000244|PDB:3TY7}.
FT   TURN        193    195       {ECO:0000244|PDB:3TY7}.
FT   STRAND      196    198       {ECO:0000244|PDB:3TY7}.
FT   TURN        203    206       {ECO:0000244|PDB:3TY7}.
FT   HELIX       207    212       {ECO:0000244|PDB:3TY7}.
FT   STRAND      218    221       {ECO:0000244|PDB:3TY7}.
FT   HELIX       225    228       {ECO:0000244|PDB:3TY7}.
FT   TURN        235    239       {ECO:0000244|PDB:3TY7}.
FT   STRAND      241    243       {ECO:0000244|PDB:3TY7}.
FT   STRAND      251    254       {ECO:0000244|PDB:3TY7}.
FT   HELIX       260    272       {ECO:0000244|PDB:3TY7}.
FT   HELIX       273    276       {ECO:0000244|PDB:3TY7}.
FT   STRAND      284    288       {ECO:0000244|PDB:3TY7}.
FT   TURN        289    291       {ECO:0000244|PDB:3TY7}.
FT   HELIX       292    304       {ECO:0000244|PDB:3TY7}.
FT   HELIX       324    340       {ECO:0000244|PDB:3TY7}.
FT   STRAND      343    346       {ECO:0000244|PDB:3TY7}.
FT   STRAND      364    368       {ECO:0000244|PDB:3TY7}.
FT   HELIX       374    377       {ECO:0000244|PDB:3TY7}.
FT   STRAND      382    392       {ECO:0000244|PDB:3TY7}.
FT   HELIX       393    400       {ECO:0000244|PDB:3TY7}.
FT   STRAND      407    412       {ECO:0000244|PDB:3TY7}.
FT   HELIX       416    425       {ECO:0000244|PDB:3TY7}.
FT   STRAND      428    433       {ECO:0000244|PDB:3TY7}.
FT   HELIX       462    464       {ECO:0000244|PDB:3TY7}.
FT   STRAND      465    471       {ECO:0000244|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
//
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