ID AL9A1_PIG Reviewed; 494 AA. AC Q29228; A0A286ZNV5; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 03-JUL-2019, sequence version 2. DT 27-MAR-2024, entry version 109. 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; Synonyms=ALDH9; OS Sus scrofa (Pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus. OX NCBI_TaxID=9823; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Duroc; RG Porcine genome sequencing project; RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 33-101. RC TISSUE=Small intestine; RX PubMed=8672129; DOI=10.1007/s003359900153; RA Winteroe A.K., Fredholm M., Davies W.; RT "Evaluation and characterization of a porcine small intestine cDNA library: RT analysis of 839 clones."; RL Mamm. Genome 7:509-517(1996). 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 --------------------------------------------------------------------------- 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; AEMK02000022; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; F14819; CAA23277.1; -; mRNA. DR AlphaFoldDB; Q29228; -. DR SMR; Q29228; -. DR STRING; 9823.ENSSSCP00000006743; -. DR PaxDb; 9823-ENSSSCP00000006743; -. DR PeptideAtlas; Q29228; -. DR Ensembl; ENSSSCT00000062442.2; ENSSSCP00000033148.1; ENSSSCG00000006324.5. DR Ensembl; ENSSSCT00005030555.1; ENSSSCP00005018658.1; ENSSSCG00005019318.1. DR Ensembl; ENSSSCT00025041829.1; ENSSSCP00025017804.1; ENSSSCG00025030737.1. DR Ensembl; ENSSSCT00035052649.1; ENSSSCP00035021175.1; ENSSSCG00035039640.1. DR Ensembl; ENSSSCT00040054143.1; ENSSSCP00040022537.1; ENSSSCG00040040317.1. DR Ensembl; ENSSSCT00045043382.1; ENSSSCP00045030152.1; ENSSSCG00045025328.1. DR Ensembl; ENSSSCT00050067971.1; ENSSSCP00050029148.1; ENSSSCG00050049960.1. DR Ensembl; ENSSSCT00055016858.1; ENSSSCP00055013302.1; ENSSSCG00055008579.1. DR Ensembl; ENSSSCT00060094541.1; ENSSSCP00060040884.1; ENSSSCG00060069250.1. DR Ensembl; ENSSSCT00065072386.1; ENSSSCP00065031530.1; ENSSSCG00065052868.1. DR Ensembl; ENSSSCT00070049160.1; ENSSSCP00070041517.1; ENSSSCG00070024633.1. DR VGNC; VGNC:109625; ALDH9A1. DR eggNOG; KOG2450; Eukaryota. DR GeneTree; ENSGT00940000162687; -. DR InParanoid; Q29228; -. DR OMA; GDHTSYV; -. DR Reactome; R-SSC-71262; Carnitine synthesis. DR UniPathway; UPA00118; -. DR Proteomes; UP000008227; Chromosome 4. DR Proteomes; UP000314985; Chromosome 4. DR Proteomes; UP000694570; Unplaced. DR Proteomes; UP000694571; Unplaced. DR Proteomes; UP000694720; Unplaced. DR Proteomes; UP000694722; Unplaced. DR Proteomes; UP000694723; Unplaced. DR Proteomes; UP000694724; Unplaced. DR Proteomes; UP000694725; Unplaced. DR Proteomes; UP000694726; Unplaced. DR Proteomes; UP000694727; Unplaced. DR Proteomes; UP000694728; Unplaced. DR Bgee; ENSSSCG00000006324; Expressed in oocyte and 44 other cell types or tissues. DR ExpressionAtlas; Q29228; baseline and differential. 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_0000056487" 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:Q9JLJ2" 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" FT CONFLICT 43 FT /note="F -> L (in Ref. 2; CAA23277)" FT /evidence="ECO:0000305" SQ SEQUENCE 494 AA; 53941 MW; 8C0C40E45EE12161 CRC64; MSTGTFIVSQ PLNYRGGARV DPVDASGTEK AFEPATGRVI ATFTCSGEKE VNLAVQDAKA AFKIWSQKSG MERCRILLEA ARIIRERKEE IATMETINNG KSIFEARLDV DISWQCLEYY AGLAGSMAGE HIQLPGGSFG YTRREPLGVC VGIGAWNYPF QIACWKSAPA LACGNAMIFK PSPFTPLSVL LLAEIYTEAG VPPGLFNVVQ GGATTGQLLC QHRDVAKISF TGSVPTGSKI MEMSAKGIKP VTLELGGKSP LIIFSDCDMG NAVKGALMAN FLTQGEVCCN GTRVFVQKEI LDKFTEEVVK QTQRIKIGDP LLEDTRMGPL INRPHLERIL GFVKVAKEQG AKVLCGGDLY VPEDPKLKEG YYMRPCVLTN CRDDMTCVKE EIFGPVMSIL SFDTEAEVVE RANDTTFGLA AGVFTRDIQR AHRVVAELQA GMCFINNYNV SPVELPFGGY KKSGFGRENG RVTIEYYSQL KTVCVEMGDV ESVF //