AADH2_MALDO
ID AADH2_MALDO Reviewed; 503 AA.
AC A0A0E3T3B5;
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 2, peroxisomal {ECO:0000303|PubMed:26296314};
DE Short=MdAMADH2 {ECO:0000303|PubMed:26296314};
DE EC=1.2.1.- {ECO:0000269|PubMed:26296314};
DE AltName: Full=Aminobutyraldehyde dehydrogenase AMADH2 {ECO:0000305};
DE EC=1.2.1.19 {ECO:0000269|PubMed:26296314};
GN Name=AMADH2 {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, AND SUBCELLULAR LOCATION.
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=160 uM for 4-aminobutanal {ECO:0000269|PubMed:26296314};
CC KM=8.2 uM for 3-aminopropanal {ECO:0000269|PubMed:26296314};
CC KM=82.8 uM for NAD(+) with 3-aminopropanal as substrate
CC {ECO:0000269|PubMed:26296314};
CC Vmax=1.9 umol/min/mg enzyme with 4-aminobutanal as substrate
CC {ECO:0000269|PubMed:26296314};
CC Vmax=11.2 umol/min/mg enzyme with 3-aminopropanal as substrate
CC {ECO:0000269|PubMed:26296314};
CC Vmax=20.9 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: Peroxisome {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; KP218041; AKC00600.1; -; mRNA.
DR RefSeq; NP_001315965.1; NM_001329036.1.
DR EnsemblPlants; mRNA:MD14G0162800; mRNA:MD14G0162800; MD14G0162800.
DR GeneID; 103455259; -.
DR Gramene; mRNA:MD14G0162800; mRNA:MD14G0162800; MD14G0162800.
DR KEGG; mdm:103455259; -.
DR OrthoDB; 153834at2759; -.
DR BRENDA; 1.2.1.19; 3164.
DR UniPathway; UPA00529; UER00386.
DR GO; GO:0005777; C:peroxisome; 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 Metal-binding; NAD; Oxidoreductase; Peroxisome; Sodium.
FT CHAIN 1..503
FT /note="Aminoaldehyde dehydrogenase 2, peroxisomal"
FT /id="PRO_0000454132"
FT MOTIF 501..503
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
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; 54661 MW; AF009E28692296CC CRC64;
MAIQIPSRQL FIDGEWREPV LKKRIPIINP ATEQIIGDIP AATAEDVEIA VEAARKALAR
NKGRDWALAP GAVRAKYLRA IAAKIAERKS EIAKLEAIDC GKPLDEAAWD IDDVSGCFEY
YADLAEGLDA QQKTPISLPM EQFKSHVLKE PIGVVGLITP WNYPLLMATW KVAPALAAGC
AAILKPSELA SVTCLELADV CREVGLPPGV LNILTGLGHE AGAPLASHPH VDKIAFTGST
MTGSKIMTAA AQLVKPVSLE LGGKSPIVVF DDVDIDKAAE WTAFGIFWTN GQICSATSRL
IIHENIAAKF LDRLVQWCKN IKIADPLEEG CRLGPVVSGG QYEKILKFIA TAKSEGARVL
SGGARPEHLK KGFFIEPTII TDVTTSMQIW REEVFGPVLC VKTFSSEDEA LELANDSHYG
LGAAVISKDL ERCERVSKAL QAGIVWINCS QPCFCQAPWG GNKRSGFGRE LGKWGLDNYL
TVKQVTEYVS DDPWGWYKSP SKL
