AL9A1_RAT
ID AL9A1_RAT Reviewed; 494 AA.
AC Q9JLJ3; Q6GMM4;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=4-trimethylaminobutyraldehyde dehydrogenase;
DE Short=TMABA-DH {ECO:0000303|PubMed:10702312};
DE Short=TMABADH;
DE EC=1.2.1.47 {ECO:0000269|PubMed:10702312};
DE AltName: Full=Aldehyde dehydrogenase family 9 member A1;
DE EC=1.2.1.3 {ECO:0000269|PubMed:10702312};
DE AltName: Full=Gamma-aminobutyraldehyde dehydrogenase {ECO:0000303|PubMed:10702312};
DE EC=1.2.1.19 {ECO:0000269|PubMed:10702312};
GN Name=Aldh9a1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, CATALYTIC
RP ACTIVITY, PATHWAY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RC STRAIN=Wistar; TISSUE=Liver;
RX PubMed=10702312; DOI=10.1074/jbc.275.10.7390;
RA Vaz F.M., Fouchier S.W., Ofman R., Sommer M., Wanders R.J.A.;
RT "Molecular and biochemical characterization of rat gamma-
RT trimethylaminobutyraldehyde dehydrogenase and evidence for the involvement
RT of human aldehyde dehydrogenase 9 in carnitine biosynthesis.";
RL J. Biol. Chem. 275:7390-7394(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PROTEIN SEQUENCE OF 50-59; 199-223; 275-293 AND 412-426, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain, and Spinal cord;
RA Lubec G., Afjehi-Sadat L., Kang S.U.;
RL Submitted (JUL-2007) to UniProtKB.
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:0000269|PubMed:10702312}.
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:0000269|PubMed:10702312};
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:0000269|PubMed:10702312};
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:0000269|PubMed:10702312};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=28 uM for NAD {ECO:0000269|PubMed:10702312};
CC KM=1630 uM for NADP {ECO:0000269|PubMed:10702312};
CC KM=1.4 uM for gamma-trimethylaminobutyraldehyde
CC {ECO:0000269|PubMed:10702312};
CC KM=24 uM for 4-aminobutyraldehyde {ECO:0000269|PubMed:10702312};
CC KM=7 uM for heptanal {ECO:0000269|PubMed:10702312};
CC KM=6 uM for octanal {ECO:0000269|PubMed:10702312};
CC -!- PATHWAY: Amine and polyamine biosynthesis; carnitine biosynthesis.
CC {ECO:0000305|PubMed:10702312}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P49189}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:10702312}.
CC -!- TISSUE SPECIFICITY: Detected in lever (at protein level).
CC {ECO:0000269|PubMed:10702312}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; AF170918; AAF43598.1; -; mRNA.
DR EMBL; BC074019; AAH74019.1; -; mRNA.
DR RefSeq; NP_071609.2; NM_022273.2.
DR AlphaFoldDB; Q9JLJ3; -.
DR SMR; Q9JLJ3; -.
DR BioGRID; 248957; 1.
DR IntAct; Q9JLJ3; 1.
DR STRING; 10116.ENSRNOP00000005611; -.
DR iPTMnet; Q9JLJ3; -.
DR PhosphoSitePlus; Q9JLJ3; -.
DR SwissPalm; Q9JLJ3; -.
DR jPOST; Q9JLJ3; -.
DR PaxDb; Q9JLJ3; -.
DR PeptideAtlas; Q9JLJ3; -.
DR PRIDE; Q9JLJ3; -.
DR GeneID; 64040; -.
DR KEGG; rno:64040; -.
DR UCSC; RGD:68409; rat.
DR CTD; 223; -.
DR RGD; 68409; Aldh9a1.
DR eggNOG; KOG2450; Eukaryota.
DR InParanoid; Q9JLJ3; -.
DR OrthoDB; 538179at2759; -.
DR PhylomeDB; Q9JLJ3; -.
DR BioCyc; MetaCyc:MON-14430; -.
DR BRENDA; 1.2.1.47; 5301.
DR Reactome; R-RNO-71262; Carnitine synthesis.
DR SABIO-RK; Q9JLJ3; -.
DR UniPathway; UPA00118; -.
DR PRO; PR:Q9JLJ3; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0033737; F:1-pyrroline dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0047105; F:4-trimethylammoniobutyraldehyde dehydrogenase activity; IDA:RGD.
DR GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; IDA:RGD.
DR GO; GO:0043176; F:amine binding; IDA:RGD.
DR GO; GO:0019145; F:aminobutyraldehyde dehydrogenase activity; IDA:RGD.
DR GO; GO:0043878; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity; IEA:UniProtKB-EC.
DR GO; GO:0042802; F:identical protein binding; IPI:RGD.
DR GO; GO:0051287; F:NAD binding; IDA:RGD.
DR GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; ISO:RGD.
DR GO; GO:0045329; P:carnitine biosynthetic process; TAS:RGD.
DR GO; GO:0009437; P:carnitine metabolic process; ISO:RGD.
DR GO; GO:0006081; P:cellular aldehyde metabolic process; ISS:UniProtKB.
DR GO; GO:0001822; P:kidney development; IEP:RGD.
DR GO; GO:0001889; P:liver development; IEP:RGD.
DR GO; GO:0042136; P:neurotransmitter biosynthetic process; ISO:RGD.
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 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Direct protein sequencing; NAD; Oxidoreductase;
KW 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_0000056489"
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 CONFLICT 493..494
FT /note="AF -> PFENQ (in Ref. 2; AAH74019)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 494 AA; 53653 MW; E417BD52D7DF567C CRC64;
MSTGTFVVSQ PLNYRGGARV EPVDASGTEK AFEPATGREI ATFKCSGEKE VNLAVENAKA
AFKIWSKKSG LERCQVLLEA ARIIKERRDE IAIMETINNG KSIFEARLDV DTSWQCLEYY
AGLAASMAGE HIQLPGGSFG YTRREPLGVC LGIGAWNYPF QIACWKSAPA LACGNAMIFK
PSPFTPVSAL LLAEIYTKAG APNGLFNVVQ GGAATGQFLC QHRDVAKVSF TGSVPTGMKI
MEMAAKGIKP ITLELGGKSP LIIFSDCNMK NAVKGALLAN FLTQGQVCCN GTRVFVQKEI
ADAFTKEVVR QTQRIKIGDP LLEDTRMGPL INAPHLERVL GFVRSAKEQG ATVLCGGEPY
APEDPKLKHG YYMTPCILTN CTDDMTCVKE EIFGPVMSIL TFETEAEVLE RANDTTFGLA
AGVFTRDIQR AHRVAAELQA GTCYINNYNV SPVELPFGGY KKSGFGRENG RVTIEYYSQL
KTVCVEMGDV ESAF
