ID F2F394_SOLSS Unreviewed; 508 AA.
AC F2F394;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=Putative aldehyde dehydrogenase AldA {ECO:0000256|ARBA:ARBA00039869};
DE EC=1.2.1.3 {ECO:0000256|ARBA:ARBA00024226};
GN OrderedLocusNames=SSIL_0174 {ECO:0000313|EMBL:BAK14597.1};
OS Solibacillus silvestris (strain StLB046) (Bacillus silvestris).
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Solibacillus.
OX NCBI_TaxID=1002809 {ECO:0000313|EMBL:BAK14597.1, ECO:0000313|Proteomes:UP000006691};
RN [1] {ECO:0000313|Proteomes:UP000006691}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=StLB046 {ECO:0000313|Proteomes:UP000006691};
RA Morohoshi T., Someya N., Ikeda T.;
RT "Genome sequence of Solibacillus silvestris StLB046.";
RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:BAK14597.1, ECO:0000313|Proteomes:UP000006691}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=StLB046 {ECO:0000313|EMBL:BAK14597.1,
RC ECO:0000313|Proteomes:UP000006691};
RX PubMed=22019407; DOI=10.1016/j.jbiosc.2011.09.006;
RA Morohoshi T., Tominaga Y., Someya N., Ikeda T.;
RT "Complete genome sequence and characterization of the N-acylhomoserine
RT lactone-degrading gene of the potato leaf-associated Solibacillus
RT silvestris.";
RL J. Biosci. Bioeng. 113:20-25(2012).
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 Evidence={ECO:0000256|ARBA:ARBA00024149};
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000256|RuleBase:RU003345}.
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DR EMBL; AP012157; BAK14597.1; -; Genomic_DNA.
DR RefSeq; WP_014822392.1; NC_018065.1.
DR AlphaFoldDB; F2F394; -.
DR STRING; 1002809.SSIL_0174; -.
DR KEGG; siv:SSIL_0174; -.
DR PATRIC; fig|1002809.3.peg.176; -.
DR eggNOG; COG1012; Bacteria.
DR HOGENOM; CLU_005391_0_0_9; -.
DR Proteomes; UP000006691; 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; cd07116; ALDH_ACDHII-AcoD; 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; PTHR43111; ALDEHYDE DEHYDROGENASE B-RELATED; 1.
DR PANTHER; PTHR43111:SF1; ALDEHYDE DEHYDROGENASE B-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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003345};
KW Reference proteome {ECO:0000313|Proteomes:UP000006691}.
FT DOMAIN 29..495
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 264
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ SEQUENCE 508 AA; 56054 MW; 8D0D8116B6EC09B5 CRC64;
MAAVYQNPNT DGALVNFKER YDNFIGGKWT PPVKGEYFDN ITPVTGKVFT QVARSTEEDI
ELALDAAHAA KDAWGKTSAT ERSNILLKIA DRMEQNLEML AVAETWDNGK AVRETLNADL
PLGIDHFRYF AGALRAQEGS LSQIDENTVA YHFHEPIGVV GQIIPWNFPL LMAVWKLAPA
LAAGNCVVLK PAEQTPASIL VLVELIEDLL PPGVLNVVNG FGLEAGKPLA SNPRIGKIAF
TGETTTGRLI MQYASQNLIP VTLELGGKSP NIFFEDIMDA DDAFLDKAVE GFVLFALNQG
EVCTCPSRAL IQESIYEKFM ERVLKRVEAI KTGNPLDTDT MMGAQASSEQ MEKIQSYLQI
GKEEGAECLI GGEKNDLGGD YADGYYIKPT VFKGHNKMRI FQEEIFGPVV AVTTFKTKEE
ALEIANDTLY GLGSGVWTRD MNTAYRFGRG IQAGRVWTNC YHAYPAHAAF GGYKMSGVGR
ENHKMMLSHY QQTKNLLVSY DENRLGFF
//