AL9A1_BOVIN
ID AL9A1_BOVIN Reviewed; 494 AA.
AC Q2KJH9;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 93.
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};
GN Name=ALDH9A1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) 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: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 -!- 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}.
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; BC105335; AAI05336.1; -; mRNA.
DR RefSeq; NP_001039888.1; NM_001046423.1.
DR AlphaFoldDB; Q2KJH9; -.
DR SMR; Q2KJH9; -.
DR STRING; 9913.ENSBTAP00000033996; -.
DR PaxDb; Q2KJH9; -.
DR PeptideAtlas; Q2KJH9; -.
DR PRIDE; Q2KJH9; -.
DR GeneID; 537539; -.
DR KEGG; bta:537539; -.
DR CTD; 223; -.
DR eggNOG; KOG2450; Eukaryota.
DR InParanoid; Q2KJH9; -.
DR OrthoDB; 538179at2759; -.
DR UniPathway; UPA00118; -.
DR Proteomes; UP000009136; Unplaced.
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:AgBase.
DR GO; GO:0019145; F:aminobutyraldehyde dehydrogenase activity; ISS:AgBase.
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:AgBase.
DR GO; GO:0042136; P:neurotransmitter biosynthetic process; ISS:AgBase.
DR GO; GO:0051289; P:protein homotetramerization; ISS:UniProtKB.
DR Gene3D; 3.40.309.10; -; 1.
DR Gene3D; 3.40.605.10; -; 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 Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; SSF53720; 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_0000236270"
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 344
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9JLJ2"
SQ SEQUENCE 494 AA; 53977 MW; 74476EDC839F3241 CRC64;
MSTGTFVVSQ PLNYRGGARV EPVDASGTEK AFEPASGRVI ATFTCSGEKE VNLAVQDAKA
AFKIWSQKSG MERCRILLEA ARIIRERRDE IATMETINNG KSIFEARWDI DTSWQCLEYY
AGLAGSMAGE HIQLPGGSFG YTRREPLGVC VGIGAWNYPF QIACWKSAPA LACGNAMVFK
PSPFTPVSVL LLAEIYTEAG VPPGLFNVVQ GGAATGQFLC QHRDVAKVSF TGSVPTGSKI
MEMSAKGIKP VTLELGGKSP LIIFSDCDMK NAVKGALMAN FLTQGEVCCN GTRVFVQKEI
LDQFTEEVVK QTQRIKIGDP LLEDTRMGPL INRPHLERVL GFVKVAKEQG AKVLCGGDVF
VPEDPKLKDG YYMRPCVLTN CRDDMTCVKE EIFGPVMSIL SFDTEAEVLE RANDTTFGLA
AGVFTRDIQR AHRVVAELQA GMCFINNYNV SPVELPFGGY KKSGFGRENG RVTIEYYSQL
KTVCVEMGDV ESAF
