ID A0A0W8D919_PHYNI Unreviewed; 491 AA.
AC A0A0W8D919;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=4-trimethylaminobutyraldehyde dehydrogenase {ECO:0000256|ARBA:ARBA00040275};
DE EC=1.2.1.46 {ECO:0000256|ARBA:ARBA00044057};
DE EC=1.2.1.47 {ECO:0000256|ARBA:ARBA00039125};
DE AltName: Full=Aldehyde dehydrogenase family 9 member A1 {ECO:0000256|ARBA:ARBA00041858};
DE AltName: Full=Formaldehyde dehydrogenase {ECO:0000256|ARBA:ARBA00044324};
DE AltName: Full=Gamma-aminobutyraldehyde dehydrogenase {ECO:0000256|ARBA:ARBA00044302};
GN ORFNames=AM587_10007655 {ECO:0000313|EMBL:KUF86321.1}, AM587_10014397
GN {ECO:0000313|EMBL:KUF76396.1}, AM588_10007240
GN {ECO:0000313|EMBL:KUF92725.1};
OS Phytophthora nicotianae (Buckeye rot agent).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=4790 {ECO:0000313|EMBL:KUF92725.1, ECO:0000313|Proteomes:UP000054636};
RN [1] {ECO:0000313|Proteomes:UP000052943, ECO:0000313|Proteomes:UP000054636}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=race 0 {ECO:0000313|Proteomes:UP000052943}, Race 0
RC {ECO:0000313|EMBL:KUF76396.1}, Race 1 {ECO:0000313|EMBL:KUF92725.1},
RC and race 1 {ECO:0000313|Proteomes:UP000054636};
RA Liu H., Ma X., Yu H., Fang D., Li Y., Wang X., Wang W., Dong Y., Xiao B.;
RT "Genomes and virulence difference between two physiological races of
RT Phytophthora nicotianae.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Converts gamma-trimethylaminobutyraldehyde into gamma-
CC butyrobetaine with high efficiency (in vitro). Can catalyze the
CC irreversible oxidation of a broad range of aldehydes to the
CC corresponding acids in an NAD-dependent reaction, but with low
CC efficiency. Catalyzes the oxidation of aldehydes arising from biogenic
CC amines and polyamines. {ECO:0000256|ARBA:ARBA00043882}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5-hydroxyindol-3-yl)acetaldehyde + H2O + NAD(+) = (5-
CC hydroxyindol-3-yl)acetate + 2 H(+) + NADH; Xref=Rhea:RHEA:31215,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:50157,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:62622;
CC Evidence={ECO:0000256|ARBA:ARBA00043724};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3,4-dihydroxyphenylacetaldehyde + H2O + NAD(+) = 3,4-
CC dihydroxyphenylacetate + 2 H(+) + NADH; Xref=Rhea:RHEA:69080,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17612,
CC ChEBI:CHEBI:27978, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC Evidence={ECO:0000256|ARBA:ARBA00043811};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-(trimethylamino)butanal + H2O + NAD(+) = 4-
CC (trimethylamino)butanoate + 2 H(+) + NADH; Xref=Rhea:RHEA:17985,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16244,
CC ChEBI:CHEBI:18020, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.2.1.47;
CC Evidence={ECO:0000256|ARBA:ARBA00036400};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-aminobutanal + H2O + NAD(+) = 4-aminobutanoate + 2 H(+) +
CC NADH; Xref=Rhea:RHEA:19105, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58264,
CC ChEBI:CHEBI:59888; EC=1.2.1.19;
CC Evidence={ECO:0000256|ARBA:ARBA00043799};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NAD(+) + pentanal = 2 H(+) + NADH + pentanoate;
CC Xref=Rhea:RHEA:69092, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:31011, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:84069; Evidence={ECO:0000256|ARBA:ARBA00043741};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NAD(+) + propanal = 2 H(+) + NADH + propanoate;
CC Xref=Rhea:RHEA:67256, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17153, ChEBI:CHEBI:17272, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; Evidence={ECO:0000256|ARBA:ARBA00043823};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NAD(+) + spermine monoaldehyde = 2 H(+) + N-(2-
CC carboxyethyl)spermidine + NADH; Xref=Rhea:RHEA:69168,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:180903, ChEBI:CHEBI:180913;
CC Evidence={ECO:0000256|ARBA:ARBA00043708};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + hexanal + NAD(+) = 2 H(+) + hexanoate + NADH;
CC Xref=Rhea:RHEA:67276, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17120, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:88528; Evidence={ECO:0000256|ARBA:ARBA00043662};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + imidazole-4-acetaldehyde + NAD(+) = 2 H(+) + imidazole-
CC 4-acetate + NADH; Xref=Rhea:RHEA:31059, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:27398, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:57969;
CC Evidence={ECO:0000256|ARBA:ARBA00043820};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetaldehyde + H2O + NAD(+) = acetate + 2 H(+) + NADH;
CC Xref=Rhea:RHEA:25294, ChEBI:CHEBI:15343, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.2.1.3;
CC Evidence={ECO:0000256|ARBA:ARBA00043790};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acrolein + H2O + NAD(+) = acrylate + 2 H(+) + NADH;
CC Xref=Rhea:RHEA:69084, ChEBI:CHEBI:15368, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:37080, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; Evidence={ECO:0000256|ARBA:ARBA00043666};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=butanal + H2O + NAD(+) = butanoate + 2 H(+) + NADH;
CC Xref=Rhea:RHEA:69088, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15743, ChEBI:CHEBI:17968, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; Evidence={ECO:0000256|ARBA:ARBA00043754};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=formaldehyde + H2O + NAD(+) = formate + 2 H(+) + NADH;
CC Xref=Rhea:RHEA:16425, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15740, ChEBI:CHEBI:16842, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.2.1.46;
CC Evidence={ECO:0000256|ARBA:ARBA00043759};
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000256|RuleBase:RU003345}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KUF92725.1}.
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DR EMBL; LNFO01005810; KUF76396.1; -; Genomic_DNA.
DR EMBL; LNFO01002307; KUF86321.1; -; Genomic_DNA.
DR EMBL; LNFP01000445; KUF92725.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0W8D919; -.
DR STRING; 4790.A0A0W8D919; -.
DR EnsemblProtists; KUF76396; KUF76396; AM587_10014397.
DR EnsemblProtists; KUF86321; KUF86321; AM587_10007655.
DR EnsemblProtists; KUF92725; KUF92725; AM588_10007240.
DR OMA; TCEQLMP; -.
DR OrthoDB; 2291791at2759; -.
DR Proteomes; UP000052943; Unassembled WGS sequence.
DR Proteomes; UP000054636; Unassembled WGS sequence.
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; cd07090; ALDH_F9_TMBADH; 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; PTHR11699:SF228; 4-TRIMETHYLAMINOBUTYRALDEHYDE DEHYDROGENASE; 1.
DR PANTHER; PTHR11699; ALDEHYDE DEHYDROGENASE-RELATED; 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 NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|RuleBase:RU003345};
KW Reference proteome {ECO:0000313|Proteomes:UP000052943}.
FT DOMAIN 22..478
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 249
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ SEQUENCE 491 AA; 53142 MW; 84C861FD7244AECF CRC64;
MARVVKSFIN GKYVAPRASA PSFTLLNATT RKPETSFTAA DKAQVDEAVG AARSAQKHWR
RLSPAERGSI LRKAADILTA KTDEIATLET IDTGRPIAET IVTDVLSATD CLNYYGGVSP
SVGGQHLELT GGSWAYTKRE PLGVTAGIGA WNYPLQSAAW KSAPALAFGN SMVFKPSEET
PLTALKLAEA YMEAGVPEGV FNVVLGAGET GQALVEHQDV AKVSFTGSVG TGRNVYAGAA
KDLKKVTMEL GGKSPLIVFD DADIEQAVAG AMMGNWYSSG QVCSNGTRVF VQRKIFDKFV
QRMHERTLKL RIGDPLDPST DIGPMIHEKH MKLVESYIEK GVAEGATLLK GGGERIMPSE
ATKDGFFLTP AIFVDCKDDM TIVREEIFGM VMCILPFDTE EEVLTRANDT IFGLSAGVFT
KDITRAHRMI DELQAGTTWI NNYNLAPVET PWGGYKKSGV GRENGLAGVD SWTQLKSVYV
EMNEVWCPYA K
//
