ALDH_GEOSE
ID ALDH_GEOSE Reviewed; 488 AA.
AC P42329;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Aldehyde dehydrogenase, thermostable;
DE EC=1.2.1.5;
GN Name=aldHT;
OS Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=1422;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=SIC1;
RA Imanaka T., Ohta T., Sakoda H., Widhyastuti N., Matsuoka M.;
RT "Cloning, nucleotide sequence, and efficient expression of the gene coding
RT for thermostable aldehyde dehydrogenase from Bacillus stearothermophilus,
RT and characterization of the enzyme.";
RL J. Ferment. Bioeng. 76:161-167(1993).
CC -!- FUNCTION: Oxidizes several aliphatic aldehydes, particularly c6-
CC aliphatic aldehyde and hexanal, but does not oxidize benzaldehyde.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an aldehyde + H2O + NADP(+) = a carboxylate + 2 H(+) + NADPH;
CC Xref=Rhea:RHEA:11888, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17478, ChEBI:CHEBI:29067, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; EC=1.2.1.5;
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=1.2.1.5;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Optimum temperature is 55-60 degrees Celsius.;
CC -!- PATHWAY: Alcohol metabolism; ethanol degradation; acetate from ethanol:
CC step 2/2.
CC -!- SUBUNIT: Homotetramer.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; D13846; BAA02975.1; -; Genomic_DNA.
DR PIR; I39769; I39769.
DR AlphaFoldDB; P42329; -.
DR SMR; P42329; -.
DR UniPathway; UPA00780; UER00768.
DR GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; IEA:RHEA.
DR GO; GO:0033721; F:aldehyde dehydrogenase (NADP+) activity; IEA:RHEA.
DR GO; GO:0006068; P:ethanol catabolic process; IEA:UniProtKB-UniPathway.
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 Pfam; PF00171; Aldedh; 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 NAD; Oxidoreductase.
FT CHAIN 1..488
FT /note="Aldehyde dehydrogenase, thermostable"
FT /id="PRO_0000056442"
FT ACT_SITE 255
FT /evidence="ECO:0000250"
FT ACT_SITE 289
FT /evidence="ECO:0000250"
FT BINDING 233..238
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
SQ SEQUENCE 488 AA; 52915 MW; 29E824451985D9ED CRC64;
MKVQTEIKTY FNYINGNWVS SVSNNVEPSI NPANRHDIVG YVQRSTLEDV NEAVTAANEA
QTSWWKRSGV ERGEYLYKAA HILEQCLQDI AETMTREMGK TLAEAKAETM RGVHILRYYA
GEGARKIGDV IPSSDSEGLL FTTRVPLGVV GVISPWNFPV AIPIWKMAPA LVYGNTVVLK
PASETAVTAA KVIECFHEAG FPKGVVNMVC GSGSVVGQGI ANHPDIDGVT FTGSNTVGKQ
VGRAAFERGA KYQLEMGGKN PVIVAKDADL DLAVEGTISG GLRSTGQKCT ATSRVFIERE
VYEPFKAKLL ERVKQLKIGN GLDAETWMGP CASESQFHTV LSYIEKGKSE GAKLIYGGNR
CLEGELANGF FVEPTIFEDV DLQMTIAREE IFGPVLALIQ VDSIEEAIKL ANDTEYGLSA
SIYTKNIGNA LEFIKDIEAG LIKVNAETAG VEFQAPFGGM KQSSSHSREQ GQAAIEFFTS
IKTVFVKA