ID A0A318ZTG2_ASPLB Unreviewed; 498 AA. AC A0A318ZTG2; DT 10-OCT-2018, integrated into UniProtKB/TrEMBL. DT 10-OCT-2018, sequence version 1. DT 24-JAN-2024, entry version 14. DE RecName: Full=4-trimethylaminobutyraldehyde dehydrogenase {ECO:0000256|ARBA:ARBA00040275}; DE EC=1.2.1.47 {ECO:0000256|ARBA:ARBA00039125}; DE AltName: Full=Aldehyde dehydrogenase family 9 member A1 {ECO:0000256|ARBA:ARBA00041858}; GN ORFNames=BO96DRAFT_416776 {ECO:0000313|EMBL:PYH50889.1}; OS Aspergillus lacticoffeatus (strain CBS 101883). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus; OC Aspergillus subgen. Circumdati. OX NCBI_TaxID=1450533 {ECO:0000313|EMBL:PYH50889.1, ECO:0000313|Proteomes:UP000247441}; RN [1] {ECO:0000313|EMBL:PYH50889.1, ECO:0000313|Proteomes:UP000247441} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CBS 101883 {ECO:0000313|EMBL:PYH50889.1, RC ECO:0000313|Proteomes:UP000247441}; RG DOE Joint Genome Institute; RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F., RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A., RA Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V., RA Mortensen U.H., Andersen M.R., Baker S.E.; RT "The genomes of Aspergillus section Nigri reveals drivers in fungal RT speciation."; RL Submitted (DEC-2016) 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. {ECO:0000256|ARBA:ARBA00037704}. 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=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 -!- PATHWAY: Amine and polyamine biosynthesis; carnitine biosynthesis. CC {ECO:0000256|ARBA:ARBA00005022}. CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family. CC {ECO:0000256|RuleBase:RU003345}. 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; KZ821387; PYH50889.1; -; Genomic_DNA. DR AlphaFoldDB; A0A318ZTG2; -. DR OrthoDB; 2291791at2759; -. DR Proteomes; UP000247441; 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; 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 Oxidoreductase {ECO:0000256|RuleBase:RU003345}. FT DOMAIN 20..482 FT /note="Aldehyde dehydrogenase" FT /evidence="ECO:0000259|Pfam:PF00171" FT ACT_SITE 253 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007" SQ SEQUENCE 498 AA; 53400 MW; 5A81F563B0A6B833 CRC64; MSLPFPTRQL YYDGKVQPAT SGKTFQTINP SNDTPLADIQ VAAHADVDSA IAAADRAFPS WSQTPAIARA RILQKAASLL RERNDEIARV ETLDSGKAYT ETSTVDVVTG ADVLEYYANL VGGGGLNGET TQLREDAWVY TKKAPLGVCA GIGAWNYPIQ IALWKSAPCL AAGNTMVYKP SEFTPLHAQT LAQIYTEAGL PAGVFNVVYG AGDVGAYLTA HPTIAKVSFT GQVSTGMKVA GSAAGNMKYV TMELGGKSPL IVLPDADLDN AVDGAMMANF YSTGQVCTNG TRVFVPSSMK AAFEKRLLEK MQYIRPGPLF DEATNMGPLS SAVHMEKVAS YIRHGIETDK ATLLYGGLGK PQVPKDLESG YWVRPTVFTD CTDDMRIVKE EIFGPVMSIL SYETVEEAVK RANTTELGLA AGVFTKDLNL AHRVIDQLQA GITWINSWGE SPAEMAVGGW KNSGVGVENG RRGIEAWVRN KSTLVDMNGS VATVFAKL //