ID   Q4L7N3_STAHJ            Unreviewed;       460 AA.
AC   Q4L7N3;
DT   02-AUG-2005, integrated into UniProtKB/TrEMBL.
DT   02-AUG-2005, sequence version 1.
DT   27-MAR-2024, entry version 130.
DE   RecName: Full=Aldehyde dehydrogenase {ECO:0000256|PIRNR:PIRNR036492};
GN   Name=aldH {ECO:0000313|EMBL:BAE04342.1};
GN   OrderedLocusNames=SH1033 {ECO:0000313|EMBL:BAE04342.1};
OS   Staphylococcus haemolyticus (strain JCSC1435).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=279808 {ECO:0000313|EMBL:BAE04342.1, ECO:0000313|Proteomes:UP000000543};
RN   [1] {ECO:0000313|EMBL:BAE04342.1, ECO:0000313|Proteomes:UP000000543}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCSC1435 {ECO:0000313|EMBL:BAE04342.1,
RC   ECO:0000313|Proteomes:UP000000543};
RX   PubMed=16237012; DOI=10.1128/JB.187.21.7292-7308.2005;
RA   Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA   Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C.,
RA   Hiramatsu K.;
RT   "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT   extreme plasticity of its genome and the evolution of human-colonizing
RT   staphylococcal species.";
RL   J. Bacteriol. 187:7292-7308(2005).
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00009986, ECO:0000256|PIRNR:PIRNR036492,
CC       ECO:0000256|RuleBase:RU003345}.
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DR   EMBL; AP006716; BAE04342.1; -; Genomic_DNA.
DR   RefSeq; WP_011275339.1; NC_007168.1.
DR   AlphaFoldDB; Q4L7N3; -.
DR   GeneID; 58062789; -.
DR   KEGG; sha:SH1033; -.
DR   eggNOG; COG1012; Bacteria.
DR   HOGENOM; CLU_005391_3_1_9; -.
DR   OrthoDB; 9762913at2; -.
DR   Proteomes; UP000000543; Chromosome.
DR   GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   GO; GO:0006081; P:cellular aldehyde metabolic process; IEA:InterPro.
DR   CDD; cd07136; ALDH_YwdH-P39616; 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; PTHR43570; ALDEHYDE DEHYDROGENASE; 1.
DR   PANTHER; PTHR43570:SF16; ALDEHYDE DEHYDROGENASE TYPE III, ISOFORM Q; 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.
PE   3: Inferred from homology;
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|PIRNR:PIRNR036492}.
FT   DOMAIN          4..429
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   ACT_SITE        210
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036492-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU10007"
FT   ACT_SITE        244
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036492-1"
SQ   SEQUENCE   460 AA;  51591 MW;  18CEE99F155CEE66 CRC64;
     MPSIEQQFEE SKAFFKTHKT KDLKFRKHQL KLLSKSIKNH ENDLLDALKT DLGKSPVEAY
     ATEIGITLKS IKTARKELKN WSKTKQVDTP LFMFPAKSYI KQEPYGTVLI IGPFNYPVQL
     LFEPLIGAIA AGNTAIIKPS ELTPHVATVI RQIIEDVFTT DYIGVIEGGI EETQTLINLP
     FDYIFFTGSD KVGQIVYEAA SKNLVPVTLE LGGKSPVIVD DTANIKVASD RISFGKFTNA
     GQTCVAPDYI LVNKKVKNEL IEALKQSIQE FYGTNIEESP DFGRIVNDKH FNRLNELLNV
     HQNHVIFGGN ANATTRYIEP TILDSITSSS KIMQDEIFGP ILPIITYDDF NEAVDIIQSK
     AKPLSLYLFS EDENTTHRVL NELSFGGGAI NDTLMHLANP NLPFGGVGMS GIGQYHGKYT
     FQTFSHSKSY IFRSTRLDSS VMYPPYKGKF KYIRTFFKNL
//