ID   AL9A1_PONAB             Reviewed;         494 AA.
AC   Q5R8A4;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 2.
DT   24-JAN-2024, entry version 91.
DE   RecName: Full=4-trimethylaminobutyraldehyde dehydrogenase;
DE            Short=TMABA-DH;
DE            Short=TMABADH;
DE            EC=1.2.1.47 {ECO:0000250|UniProtKB:P49189};
DE   AltName: Full=Aldehyde dehydrogenase family 9 member A1;
DE            EC=1.2.1.3 {ECO:0000250|UniProtKB:P49189};
DE   AltName: Full=Formaldehyde dehydrogenase;
DE            EC=1.2.1.46 {ECO:0000250|UniProtKB:P49189};
DE   AltName: Full=Gamma-aminobutyraldehyde dehydrogenase;
DE            EC=1.2.1.19 {ECO:0000250|UniProtKB:P49189};
GN   Name=ALDH9A1;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) 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:0000250|UniProtKB:P49189}.
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:0000250|UniProtKB:P49189};
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:0000250|UniProtKB:P49189};
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:0000250|UniProtKB:P49189};
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:0000250|UniProtKB:P49189};
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:0000250|UniProtKB:P49189};
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:0000250|UniProtKB:P49189};
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:0000250|UniProtKB:P49189};
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:0000250|UniProtKB:P49189};
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:0000250|UniProtKB:P49189};
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:0000250|UniProtKB:P49189};
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:0000250|UniProtKB:P49189};
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:0000250|UniProtKB:P49189};
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:0000250|UniProtKB:P49189};
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:0000250|UniProtKB:P49189};
CC   -!- PATHWAY: Amine and polyamine biosynthesis; carnitine biosynthesis.
CC       {ECO:0000250|UniProtKB:P49189}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P49189}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:Q9JLJ3}. Cytoplasm
CC       {ECO:0000250|UniProtKB:P49189}.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAH92006.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CR859849; CAH92006.1; ALT_INIT; mRNA.
DR   RefSeq; NP_001126165.1; NM_001132693.1.
DR   AlphaFoldDB; Q5R8A4; -.
DR   SMR; Q5R8A4; -.
DR   STRING; 9601.ENSPPYP00000000664; -.
DR   GeneID; 100173126; -.
DR   KEGG; pon:100173126; -.
DR   CTD; 223; -.
DR   eggNOG; KOG2450; Eukaryota.
DR   InParanoid; Q5R8A4; -.
DR   OrthoDB; 2291791at2759; -.
DR   UniPathway; UPA00118; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0047105; F:4-trimethylammoniobutyraldehyde dehydrogenase activity; ISS:UniProtKB.
DR   GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; ISS:UniProtKB.
DR   GO; GO:0019145; F:aminobutyraldehyde dehydrogenase activity; ISS:UniProtKB.
DR   GO; GO:0018467; F:formaldehyde dehydrogenase activity; ISS:UniProtKB.
DR   GO; GO:0043878; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity; IEA:UniProtKB-EC.
DR   GO; GO:0045329; P:carnitine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006081; P:cellular aldehyde metabolic process; ISS:UniProtKB.
DR   GO; GO:0051289; P:protein homotetramerization; ISS:UniProtKB.
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   2: Evidence at transcript level;
KW   Acetylation; Cytoplasm; NAD; Oxidoreductase; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P49189"
FT   CHAIN           2..494
FT                   /note="4-trimethylaminobutyraldehyde dehydrogenase"
FT                   /id="PRO_0000056488"
FT   ACT_SITE        254
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10007"
FT   ACT_SITE        288
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10008"
FT   BINDING         180
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P56533"
FT   BINDING         232..236
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P56533"
FT   BINDING         391
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P56533"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250|UniProtKB:P49189"
FT   MOD_RES         30
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9JLJ2"
FT   MOD_RES         30
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9JLJ2"
FT   MOD_RES         59
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9JLJ2"
FT   MOD_RES         298
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P49189"
FT   MOD_RES         303
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9JLJ2"
FT   MOD_RES         303
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9JLJ2"
FT   MOD_RES         344
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9JLJ2"
SQ   SEQUENCE   494 AA;  53787 MW;  96B4B5EF2C17EF06 CRC64;
     MSTGTFVVSQ PLNYRGGARV EPADASGTEK AFEPATGRVI ATFTCSGEKE VNLAVQNAKA
     AFKIWSQKSG MERCRILLEA ARIIREREGE IATMECINNG KSIFEARLDI NISWQCLEYY
     AGLAASMAGE HIQLPGGSFG YTRREPLGVC VGIGAWNYPF QITSWKSAPA LACGNAMVFK
     PSPFTPVSAL LLAEIYTEAG VPPGLFNVVQ GGAATGQFLC QHPDVAKVSF TGSVPTGMKI
     MEMSAKGIKP VTLELGGKSP LIIFSDCDMN NAVKGALMAN FLTQGQVCCN GTRVFVQKEI
     LDKFTEEVVK QTQRIKIGDP LLEDTRMGPL INRPHLERVL GFVKVAKEQG AKVLCGGDIY
     VPEDPKLKDG YYMRPCVLTN CRDDMTCVKE EIFGPVMSIL SFDTEAEVLE RANDTTFGLA
     AGVFTRDIQR AHRVVAELQA GTCFINNYNV SPVELPFGGY KKSGFGRENG RVTIEYYSQL
     KTVCVEMGDV ESAF
//