ID E3RP74_PYRTT Unreviewed; 323 AA.
AC E3RP74;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=4-trimethylaminobutyraldehyde dehydrogenase {ECO:0000256|ARBA:ARBA00040275};
DE EC=1.2.1.19 {ECO:0000256|ARBA:ARBA00039138};
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};
DE Flags: Fragment;
GN ORFNames=PTT_10408 {ECO:0000313|EMBL:EFQ92475.1};
OS Pyrenophora teres f. teres (strain 0-1) (Barley net blotch fungus)
OS (Drechslera teres f. teres).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC Pyrenophora.
OX NCBI_TaxID=861557 {ECO:0000313|Proteomes:UP000001067};
RN [1] {ECO:0000313|EMBL:EFQ92475.1, ECO:0000313|Proteomes:UP000001067}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0-1 {ECO:0000313|EMBL:EFQ92475.1,
RC ECO:0000313|Proteomes:UP000001067};
RX PubMed=21067574; DOI=10.1186/gb-2010-11-11-r109;
RA Ellwood S.R., Liu Z., Syme R.A., Lai Z., Hane J.K., Keiper F., Moffat C.S.,
RA Oliver R.P., Friesen T.L.;
RT "A first genome assembly of the barley fungal pathogen Pyrenophora teres f.
RT teres.";
RL Genome Biol. 11:R109.1-R109.14(2010).
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=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 -!- 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|ARBA:ARBA00009986, ECO:0000256|RuleBase:RU003345}.
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DR EMBL; GL534286; EFQ92475.1; -; Genomic_DNA.
DR RefSeq; XP_003299429.1; XM_003299381.1.
DR AlphaFoldDB; E3RP74; -.
DR STRING; 861557.E3RP74; -.
DR KEGG; pte:PTT_10408; -.
DR eggNOG; KOG2450; Eukaryota.
DR HOGENOM; CLU_005391_0_0_1; -.
DR OrthoDB; 2291791at2759; -.
DR Proteomes; UP000001067; 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 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; 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; PS00070; ALDEHYDE_DEHYDR_CYS; 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:UP000001067}.
FT DOMAIN 2..322
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 128
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
FT NON_TER 323
FT /evidence="ECO:0000313|EMBL:EFQ92475.1"
SQ SEQUENCE 323 AA; 34814 MW; 95D02A660C419DA6 CRC64;
MNGDTAQLRP DAWVYTTKNA LGVCAGIGAW NYPIQIALWK SAPCLAAGNC MVYKPSEFTP
LHSTVLADIY AEAGVPAGVF NVVQGGGEVG AYLTKHSGIA KVSFTGQVST GKKVAGSASG
EMKYVTMELG GKSACVILPD ADVDQAVDGA MLANFFSTGQ VCTNGTRVFV PEAMKPEFEE
RLLEKIQYIR PGDLYDINTN FGPLVSKPHY EKVVSYIKHG IENDKAKLLC GGPETPSWLA
SHSNKAYQNG YWVQPTVFTN CTDDMKIVRE EIFGPVMSIL SYKTIDEVVR RANNTDVGLA
ASVFTKDINL AHKVIAQLEA GIT
//
