ID ALD1_STAHJ Reviewed; 475 AA.
AC Q4L803;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 2.
DT 27-MAR-2024, entry version 123.
DE RecName: Full=Putative aldehyde dehydrogenase SH0913;
DE EC=1.2.1.3;
GN OrderedLocusNames=SH0913;
OS Staphylococcus haemolyticus (strain JCSC1435).
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=279808;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCSC1435;
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 -!- 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 -!- SEQUENCE CAUTION:
CC Sequence=BAE04222.1; Type=Erroneous initiation; Evidence={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; AP006716; BAE04222.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_029376675.1; NC_007168.1.
DR AlphaFoldDB; Q4L803; -.
DR SMR; Q4L803; -.
DR GeneID; 58062903; -.
DR KEGG; sha:SH0913; -.
DR eggNOG; COG1012; Bacteria.
DR HOGENOM; CLU_005391_0_0_9; -.
DR OrthoDB; 9762913at2; -.
DR Proteomes; UP000000543; 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: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 PANTHER; PTHR42804; ALDEHYDE DEHYDROGENASE; 1.
DR PANTHER; PTHR42804:SF1; ALDEHYDE DEHYDROGENASE-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.
PE 3: Inferred from homology;
KW NAD; Oxidoreductase.
FT CHAIN 1..475
FT /note="Putative aldehyde dehydrogenase SH0913"
FT /id="PRO_0000293563"
FT ACT_SITE 245
FT /evidence="ECO:0000250"
FT ACT_SITE 279
FT /evidence="ECO:0000250"
FT BINDING 201..207
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
SQ SEQUENCE 475 AA; 51949 MW; 8B75A796F9CDCCE7 CRC64;
MRNYTQQYIN GEWIDSDSNE TIEVINPATE EVIGKVAKGN SNDVEKAVEA ANNVYLEFRH
SSVKERKELL DKIVEEYKNR KQDIIEAITD ELGAPLTLSE NVHYQMGLNH FEEASRALDS
FEFEERRGDA LVTKEAIGVS GLVTPWNFPT NQTSLKLAAA FAAGSPVVLK PSEETPFAAV
ILAEIFDKVG VPKGVFNLVN GDGEGVGNPL SEHPKVRMMS FTGSGRTGSK IMEKASKDFK
KVSLELGGKS PYIVLDDVDV KEAAKATTGK VVNNTGQVCT AGTRILIPES KKEDFLTALK
EEFSKVKVGD PREEGTQVGP IISKKQFDTV QSYIDKGIEE GAELFYGGPG KPEGLNTGYF
ARPTIFINVD NDMTIAQEEI FGPVASVITY NNLDEAIKIA NDTKYGLAGY VIGKDKETLQ
KVARSIEAGR IEINEAGNQP DLPFGGYKQS GIGREWGDYG IEEFLEVKSI AGYFS
//
