AADH2_PEA
ID AADH2_PEA Reviewed; 503 AA.
AC Q93YB2;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 04-NOV-2008, sequence version 2.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Aminoaldehyde dehydrogenase 2, peroxisomal {ECO:0000303|PubMed:20026072};
DE Short=PsAMADH2 {ECO:0000303|PubMed:20026072};
DE EC=1.2.1.- {ECO:0000269|PubMed:20026072, ECO:0000269|PubMed:21740525};
DE AltName: Full=Aminobutyraldehyde dehydrogenase AMADH2 {ECO:0000305};
DE EC=1.2.1.19 {ECO:0000269|PubMed:20026072, ECO:0000269|PubMed:21740525};
DE AltName: Full=Gamma-guanidinobutyraldehyde dehydrogenase AMADH2 {ECO:0000305};
DE EC=1.2.1.54 {ECO:0000269|PubMed:20026072};
GN Name=AMADH2 {ECO:0000303|Ref.1};
OS Pisum sativum (Garden pea).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX NCBI_TaxID=3888;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 1-30, FUNCTION, AND
RP CATALYTIC ACTIVITY.
RC TISSUE=Meristem;
RX DOI=10.1016/S0981-9428(02)00002-5;
RA Brauner F., Sebela M., Snegaroff J., Pec P., Meunier J.C.;
RT "Pea seedling aminoaldehyde dehydrogenase: primary structure and active
RT site residues.";
RL Plant Physiol. Biochem. 41:1-10(2003).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=21740525; DOI=10.1111/j.1742-4658.2011.08239.x;
RA Kopecny D., Tylichova M., Snegaroff J., Popelkova H., Sebela M.;
RT "Carboxylate and aromatic active-site residues are determinants of high-
RT affinity binding of omega-aminoaldehydes to plant aminoaldehyde
RT dehydrogenases.";
RL FEBS J. 278:3130-3139(2011).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) IN COMPLEX WITH NAD AND SODIUM ION,
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RX PubMed=20026072; DOI=10.1016/j.jmb.2009.12.015;
RA Tylichova M., Kopecny D., Morera S., Briozzo P., Lenobel R., Snegaroff J.,
RA Sebela M.;
RT "Structural and functional characterization of plant aminoaldehyde
RT dehydrogenase from Pisum sativum with a broad specificity for natural and
RT synthetic aminoaldehydes.";
RL J. Mol. Biol. 396:870-882(2010).
CC -!- FUNCTION: Dehydrogenase that catalyzes the oxidation of several
CC aminoaldehydes (PubMed:20026072). Metabolizes and detoxifies aldehyde
CC products of polyamine degradation to non-toxic amino acids (Probable).
CC Catalyzes the oxidation of 3-aminopropanal to beta-alanine (Ref.1,
CC PubMed:20026072, PubMed:21740525). Catalyzes the oxidation of 4-
CC aminobutanal to 4-aminobutanoate (PubMed:20026072, PubMed:21740525).
CC Catalyzes the oxidation of 4-guanidinobutanal to 4-guanidinobutanoate
CC (PubMed:20026072). {ECO:0000269|PubMed:20026072,
CC ECO:0000269|PubMed:21740525, ECO:0000269|Ref.1, ECO:0000305}.
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:20026072,
CC ECO:0000269|PubMed:21740525, ECO:0000269|Ref.1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30696;
CC Evidence={ECO:0000269|PubMed:20026072, ECO:0000269|Ref.1};
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:20026072, ECO:0000269|PubMed:21740525};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19106;
CC Evidence={ECO:0000269|PubMed:20026072};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-guanidinobutanal + H2O + NAD(+) = 4-guanidinobutanoate + 2
CC H(+) + NADH; Xref=Rhea:RHEA:14381, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57486, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57854, ChEBI:CHEBI:57945; EC=1.2.1.54;
CC Evidence={ECO:0000269|PubMed:20026072};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14382;
CC Evidence={ECO:0000269|PubMed:20026072};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=10 uM for 3-aminopropanal {ECO:0000269|PubMed:20026072};
CC KM=29 uM for 4-aminobutanal {ECO:0000269|PubMed:20026072};
CC KM=7 uM for 4-guanidinobutanal {ECO:0000269|PubMed:20026072};
CC KM=55 uM for NAD(+) with 3-aminopropanal as substrate
CC {ECO:0000269|PubMed:20026072};
CC Vmax=190 nmol/min/mg enzyme with 3-aminopropanal as substrate
CC {ECO:0000269|PubMed:20026072};
CC Vmax=57 nmol/min/mg enzyme with 4-aminobutanal as substrate
CC {ECO:0000269|PubMed:20026072};
CC Vmax=78 nmol/min/mg enzyme with 4-guanidinobutanal as substrate
CC {ECO:0000269|PubMed:20026072};
CC -!- PATHWAY: Amine and polyamine biosynthesis; betaine biosynthesis via
CC choline pathway; betaine from betaine aldehyde: step 1/1.
CC {ECO:0000305}.
CC -!- SUBUNIT: Forms homodimers. {ECO:0000269|PubMed:20026072}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000255}.
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; AJ315853; CAC48393.2; -; mRNA.
DR PDB; 3IWJ; X-ray; 2.15 A; A/B=1-503.
DR PDBsum; 3IWJ; -.
DR SMR; Q93YB2; -.
DR BRENDA; 1.2.1.19; 4872.
DR UniPathway; UPA00529; UER00386.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR GO; GO:0019145; F:aminobutyraldehyde dehydrogenase activity; IDA:UniProtKB.
DR GO; GO:0047107; F:gamma-guanidinobutyraldehyde dehydrogenase activity; IDA:UniProtKB.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0031402; F:sodium ion binding; IDA:UniProtKB.
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 3D-structure; Direct protein sequencing; Metal-binding; NAD;
KW Nucleotide-binding; Oxidoreductase; Peroxisome; Sodium.
FT CHAIN 1..503
FT /note="Aminoaldehyde dehydrogenase 2, peroxisomal"
FT /id="PRO_0000454134"
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:0000269|PubMed:20026072,
FT ECO:0007744|PDB:3IWJ"
FT BINDING 99
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000269|PubMed:20026072,
FT ECO:0007744|PDB:3IWJ"
FT BINDING 161
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:20026072,
FT ECO:0007744|PDB:3IWJ"
FT BINDING 185
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:20026072,
FT ECO:0007744|PDB:3IWJ"
FT BINDING 189
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000269|PubMed:20026072,
FT ECO:0007744|PDB:3IWJ"
FT BINDING 239
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:20026072,
FT ECO:0007744|PDB:3IWJ"
FT SITE 162
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P20000"
FT STRAND 10..12
FT /evidence="ECO:0007829|PDB:3IWJ"
FT STRAND 15..17
FT /evidence="ECO:0007829|PDB:3IWJ"
FT STRAND 24..28
FT /evidence="ECO:0007829|PDB:3IWJ"
FT TURN 30..32
FT /evidence="ECO:0007829|PDB:3IWJ"
FT STRAND 35..40
FT /evidence="ECO:0007829|PDB:3IWJ"
FT HELIX 44..59
FT /evidence="ECO:0007829|PDB:3IWJ"
FT HELIX 60..63
FT /evidence="ECO:0007829|PDB:3IWJ"
FT TURN 64..67
FT /evidence="ECO:0007829|PDB:3IWJ"
FT HELIX 71..87
FT /evidence="ECO:0007829|PDB:3IWJ"
FT HELIX 89..100
FT /evidence="ECO:0007829|PDB:3IWJ"
FT HELIX 104..131
FT /evidence="ECO:0007829|PDB:3IWJ"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:3IWJ"
FT STRAND 143..151
FT /evidence="ECO:0007829|PDB:3IWJ"
FT STRAND 154..158
FT /evidence="ECO:0007829|PDB:3IWJ"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:3IWJ"
FT HELIX 164..177
FT /evidence="ECO:0007829|PDB:3IWJ"
FT STRAND 181..185
FT /evidence="ECO:0007829|PDB:3IWJ"
FT HELIX 192..204
FT /evidence="ECO:0007829|PDB:3IWJ"
FT STRAND 210..213
FT /evidence="ECO:0007829|PDB:3IWJ"
FT HELIX 218..221
FT /evidence="ECO:0007829|PDB:3IWJ"
FT HELIX 223..226
FT /evidence="ECO:0007829|PDB:3IWJ"
FT STRAND 233..238
FT /evidence="ECO:0007829|PDB:3IWJ"
FT HELIX 240..250
FT /evidence="ECO:0007829|PDB:3IWJ"
FT HELIX 251..253
FT /evidence="ECO:0007829|PDB:3IWJ"
FT STRAND 257..260
FT /evidence="ECO:0007829|PDB:3IWJ"
FT STRAND 265..269
FT /evidence="ECO:0007829|PDB:3IWJ"
FT STRAND 271..273
FT /evidence="ECO:0007829|PDB:3IWJ"
FT HELIX 275..286
FT /evidence="ECO:0007829|PDB:3IWJ"
FT HELIX 288..291
FT /evidence="ECO:0007829|PDB:3IWJ"
FT STRAND 297..303
FT /evidence="ECO:0007829|PDB:3IWJ"
FT TURN 304..306
FT /evidence="ECO:0007829|PDB:3IWJ"
FT HELIX 307..319
FT /evidence="ECO:0007829|PDB:3IWJ"
FT HELIX 339..354
FT /evidence="ECO:0007829|PDB:3IWJ"
FT STRAND 358..361
FT /evidence="ECO:0007829|PDB:3IWJ"
FT STRAND 371..373
FT /evidence="ECO:0007829|PDB:3IWJ"
FT STRAND 378..382
FT /evidence="ECO:0007829|PDB:3IWJ"
FT HELIX 388..391
FT /evidence="ECO:0007829|PDB:3IWJ"
FT STRAND 396..406
FT /evidence="ECO:0007829|PDB:3IWJ"
FT HELIX 407..414
FT /evidence="ECO:0007829|PDB:3IWJ"
FT STRAND 421..426
FT /evidence="ECO:0007829|PDB:3IWJ"
FT HELIX 430..439
FT /evidence="ECO:0007829|PDB:3IWJ"
FT STRAND 442..450
FT /evidence="ECO:0007829|PDB:3IWJ"
FT HELIX 463..465
FT /evidence="ECO:0007829|PDB:3IWJ"
FT HELIX 472..477
FT /evidence="ECO:0007829|PDB:3IWJ"
FT STRAND 480..488
FT /evidence="ECO:0007829|PDB:3IWJ"
SQ SEQUENCE 503 AA; 54496 MW; EA924DC4859F3C80 CRC64;
MDIPIPTRQL FINGDWKAPV LNKRIPVINP ATQNIIGDIP AATKEDVDVA VAAAKTALTR
NKGADWATAS GAVRARYLRA IAAKVTEKKP ELAKLESIDC GKPLDEAAWD IDDVAGCFEY
YADLAEKLDA RQKAPVSLPM DTFKSHVLRE PIGVVGLITP WNYPMLMATW KVAPALAAGC
AAILKPSELA SLTCLELGEI CKEVGLPPGV LNILTGLGPE AGAPLATHPD VDKVAFTGSS
ATGSKIMTAA AQLVKPVSLE LGGKSPLVVF EDVDLDKAAE WAIFGCFWTN GQICSATSRL
ILHESIATEF LNRIVKWIKN IKISDPLEEG CRLGPVVSEG QYEKILKFVS NAKSEGATIL
TGGSRPEHLK KGFFIEPTII TDVTTNMQIW REEVFGPVLC VKTFSTEEEA IDLANDTVYG
LGAAVISNDL ERCERVTKAF KAGIVWVNCS QPCFTQAPWG GVKRSGFGRE LGEWGLDNYL
SVKQVTQYIS EEPWGWYQPP AKL
