AADH1_MALDO
ID AADH1_MALDO Reviewed; 503 AA.
AC A0A0E3T552;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 24-JUN-2015, sequence version 1.
DT 03-AUG-2022, entry version 23.
DE RecName: Full=Aminoaldehyde dehydrogenase 1, peroxisomal {ECO:0000303|PubMed:26296314};
DE Short=MdAMADH1 {ECO:0000303|PubMed:26296314};
DE EC=1.2.1.- {ECO:0000269|PubMed:26296314};
DE AltName: Full=Aminobutyraldehyde dehydrogenase AMADH1 {ECO:0000305};
DE EC=1.2.1.19 {ECO:0000269|PubMed:26296314};
GN Name=AMADH1 {ECO:0000303|PubMed:26296314};
OS Malus domestica (Apple) (Pyrus malus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Maleae; Malus.
OX NCBI_TaxID=3750;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=26296314; DOI=10.1016/j.febslet.2015.08.005;
RA Zarei A., Trobacher C.P., Shelp B.J.;
RT "NAD(+)-aminoaldehyde dehydrogenase candidates for 4-aminobutyrate (GABA)
RT and beta-alanine production during terminal oxidation of polyamines in
RT apple fruit.";
RL FEBS Lett. 589:2695-2700(2015).
CC -!- FUNCTION: Dehydrogenase that catalyzes the oxidation of several
CC aminoaldehydes (PubMed:26296314). Metabolizes and detoxifies aldehyde
CC products of polyamine degradation to non-toxic amino acids (Probable).
CC Catalyzes the oxidation of 4-aminobutanal and 3-aminopropanal to 4-
CC aminobutanoate and beta-alanine, respectively (PubMed:26296314).
CC {ECO:0000269|PubMed:26296314, ECO:0000305}.
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:26296314};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19106;
CC Evidence={ECO:0000269|PubMed:26296314};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-aminopropanal + H2O + NAD(+) = beta-alanine + 2 H(+) + NADH;
CC Xref=Rhea:RHEA:30695, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:57966,
CC ChEBI:CHEBI:58374; Evidence={ECO:0000269|PubMed:26296314};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30696;
CC Evidence={ECO:0000269|PubMed:26296314};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=84.8 uM for 4-aminobutanal {ECO:0000269|PubMed:26296314};
CC KM=16 uM for 3-aminopropanal {ECO:0000269|PubMed:26296314};
CC KM=33.8 uM for NAD(+) with 3-aminopropanal as substrate
CC {ECO:0000269|PubMed:26296314};
CC Vmax=1.2 umol/min/mg enzyme with 4-aminobutanal as substrate
CC {ECO:0000269|PubMed:26296314};
CC Vmax=11.3 umol/min/mg enzyme with 3-aminopropanal as substrate
CC {ECO:0000269|PubMed:26296314};
CC Vmax=5.4 umol/min/mg enzyme toward NAD(+) in presence of 3-
CC aminopropanal {ECO:0000269|PubMed:26296314};
CC pH dependence:
CC Optimum pH is 9.75 with 4-aminobutanal as substrate.
CC {ECO:0000269|PubMed:26296314};
CC -!- PATHWAY: Amine and polyamine biosynthesis; betaine biosynthesis via
CC choline pathway; betaine from betaine aldehyde: step 1/1.
CC {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:26296314}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves, flowers and fruits.
CC {ECO:0000269|PubMed:26296314}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; KP218040; AKC00599.1; -; mRNA.
DR RefSeq; NP_001315693.1; NM_001328764.1.
DR GeneID; 103409732; -.
DR KEGG; mdm:103409732; -.
DR OrthoDB; 153834at2759; -.
DR BRENDA; 1.2.1.19; 3164.
DR UniPathway; UPA00529; UER00386.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0033737; F:1-pyrroline dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0019145; F:aminobutyraldehyde dehydrogenase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0110095; P:cellular detoxification of aldehyde; IDA:UniProtKB.
DR GO; GO:0019285; P:glycine betaine biosynthetic process from choline; IEA:UniProtKB-UniPathway.
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 Cytoplasm; Metal-binding; NAD; Oxidoreductase; Sodium.
FT CHAIN 1..503
FT /note="Aminoaldehyde dehydrogenase 1, peroxisomal"
FT /id="PRO_0000454131"
FT ACT_SITE 260
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007"
FT ACT_SITE 294
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10008"
FT BINDING 28
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000250|UniProtKB:Q8VWZ1"
FT BINDING 99
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000250|UniProtKB:Q8VWZ1"
FT BINDING 189
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000250|UniProtKB:Q8VWZ1"
FT BINDING 238..245
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q8VWZ1"
FT BINDING 294
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q8VWZ1"
FT BINDING 393
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q8VWZ1"
FT SITE 162
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P20000"
SQ SEQUENCE 503 AA; 54779 MW; D9E452F50982A93A CRC64;
MAIQIPSRLL FIDGEWREPV LKKRIPIINP ATEEIIGHIP AATAEDVELA VEAARRALSR
NKGRDWASAP GAVRAKYLRA IAAKIGERKP EIAKLEAIDC GKPLDEAAWD IDDVSGCFEY
YAELAEGLDA QQKAPISLPM EQFKSHVLKE PIGVVGLITP WNYPLLMATW KVAPALAAGC
AAILKPSELA SVTCLELADV CREVGLPPGV LNILTGLGHE AGAPLVSHPH VDKIAFTGST
MTGSKIMTAA AQLVKPVSLE LGGKSPIVVF DDVDIDKAAE WTAFGCFWTN GQICSATSRL
ILHENIATEF LDRLLKWCKN IKIADPLEEG CRLGPVVSGG QYEKILKSIE TAKSEGARVL
SGGDRPEHLK KGFFIEPTII TDVTTSMQIW REEVFGPVLC VKTFSSEDEA LELANDTHYG
LGAAVISKDL ERCDRFSKGL QAGIVWINCS QPCFCQAPWG GNKRSGFGRE LGKWGLDNYL
TVKQVTEYVS DDPWGWYTSP SKL
