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Database: UniProt
Entry: Q4L914_STAHJ
LinkDB: Q4L914_STAHJ
Original site: Q4L914_STAHJ 
ID   Q4L914_STAHJ            Unreviewed;       475 AA.
AC   Q4L914;
DT   02-AUG-2005, integrated into UniProtKB/TrEMBL.
DT   02-AUG-2005, sequence version 1.
DT   27-MAR-2024, entry version 126.
DE   RecName: Full=Aldehyde dehydrogenase domain-containing protein {ECO:0000259|Pfam:PF00171};
GN   OrderedLocusNames=SH0552 {ECO:0000313|EMBL:BAE03861.1};
OS   Staphylococcus haemolyticus (strain JCSC1435).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=279808 {ECO:0000313|EMBL:BAE03861.1, ECO:0000313|Proteomes:UP000000543};
RN   [1] {ECO:0000313|EMBL:BAE03861.1, ECO:0000313|Proteomes:UP000000543}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCSC1435 {ECO:0000313|EMBL:BAE03861.1,
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|RuleBase:RU003345}.
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DR   EMBL; AP006716; BAE03861.1; -; Genomic_DNA.
DR   RefSeq; WP_011274877.1; NC_007168.1.
DR   AlphaFoldDB; Q4L914; -.
DR   KEGG; sha:SH0552; -.
DR   eggNOG; COG1012; Bacteria.
DR   HOGENOM; CLU_005391_1_0_9; -.
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   CDD; cd07088; ALDH_LactADH-AldA; 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   PANTHER; PTHR43353; SUCCINATE-SEMIALDEHYDE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43353:SF5; SUCCINATE-SEMIALDEHYDE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR   Pfam; PF00171; Aldedh; 1.
DR   SUPFAM; SSF53720; ALDH-like; 1.
DR   PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003345}.
FT   DOMAIN          11..467
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   ACT_SITE        247
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ   SEQUENCE   475 AA;  52276 MW;  B0D5252A99A649DF CRC64;
     MTNQLFINNE FVESKSNDTM EVINPATGEA FDTITFATEE EVNEAIEKSK HAQLEWEKVP
     APTRAEHVKL LIPLLEQNKD ELAKLYVKEQ GKTLAQAEGE IDKAVQFIDY MTSLSMRNKG
     EVLQNSVSHE MIQLIKKPIG VTAGIVPWNA PIMVLMRKVI PALVTGCSIV IKPSEETTLL
     TLRLAELFRA STIPAGLVQI VPGTGETVGT QLATHKDVQL ISLTGSMRAG KAVYKNAADT
     VKKVNLELGG NAPVLVTPHA NLDKAVDYIV TARINNAGQV CTCPERIFVH EDVHDDFVSK
     AKQRMSDLQV GDPLDDNTDY GAIINQTQLD SIDNKVQEAI KNGADLVLGG HKLDRAGFFY
     EPTILDNVKK DDSAFKEEIF GPVLAITTYN DFDEAIDAAN DTNAGLSSYI FSENLKEVME
     ATERLKFGEV YANCEAEEVV NGYHAGWRES GLGGADGIHG FEEYYNTTVS YIRYE
//
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