AL9A1_PIG
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 03-AUG-2022, entry version 100.
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; 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. {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}.
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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 PeptideAtlas; Q29228; -.
DR PRIDE; Q29228; -.
DR Ensembl; ENSSSCT00000062442; ENSSSCP00000033148; ENSSSCG00000006324.
DR Ensembl; ENSSSCT00005030555; ENSSSCP00005018658; ENSSSCG00005019318.
DR Ensembl; ENSSSCT00025041829; ENSSSCP00025017804; ENSSSCG00025030737.
DR Ensembl; ENSSSCT00035052649; ENSSSCP00035021175; ENSSSCG00035039640.
DR Ensembl; ENSSSCT00040054143; ENSSSCP00040022537; ENSSSCG00040040317.
DR Ensembl; ENSSSCT00045043382; ENSSSCP00045030152; ENSSSCG00045025328.
DR Ensembl; ENSSSCT00050067971; ENSSSCP00050029148; ENSSSCG00050049960.
DR Ensembl; ENSSSCT00055016858; ENSSSCP00055013302; ENSSSCG00055008579.
DR Ensembl; ENSSSCT00060094541; ENSSSCP00060040884; ENSSSCG00060069250.
DR Ensembl; ENSSSCT00065072386; ENSSSCP00065031530; ENSSSCG00065052868.
DR Ensembl; ENSSSCT00070049160; ENSSSCP00070041517; ENSSSCG00070024633.
DR eggNOG; KOG2450; Eukaryota.
DR GeneTree; ENSGT00940000162687; -.
DR OMA; GMKYVTM; -.
DR UniPathway; UPA00118; -.
DR Proteomes; UP000008227; Chromosome 4.
DR Proteomes; UP000314985; Chromosome 4.
DR Bgee; ENSSSCG00000006324; Expressed in oocyte and 44 other tissues.
DR ExpressionAtlas; Q29228; baseline and differential.
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; IEA:UniProtKB-EC.
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 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_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
