AADH1_PEA
ID AADH1_PEA Reviewed; 503 AA.
AC Q8VWZ1;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 04-NOV-2008, sequence version 2.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Aminoaldehyde dehydrogenase 1, peroxisomal {ECO:0000303|PubMed:20026072};
DE Short=PsAMADH1 {ECO:0000303|PubMed:20026072};
DE EC=1.2.1.- {ECO:0000269|PubMed:20026072};
DE AltName: Full=Aminobutyraldehyde dehydrogenase AMADH1 {ECO:0000305};
DE EC=1.2.1.19 {ECO:0000269|PubMed:20026072};
DE AltName: Full=Gamma-guanidinobutyraldehyde dehydrogenase AMADH1 {ECO:0000305};
DE EC=1.2.1.54 {ECO:0000269|PubMed:20026072};
GN Name=AMADH1 {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 X-RAY CRYSTALLOGRAPHY (2.40 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). Catalyzes the oxidation of 4-aminobutanal to 4-
CC aminobutanoate (PubMed:20026072). Catalyzes the oxidation of 4-
CC guanidinobutanal to 4-guanidinobutanoate (PubMed:20026072).
CC {ECO:0000269|PubMed:20026072, 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|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};
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=75 uM for 3-aminopropanal {ECO:0000269|PubMed:20026072};
CC KM=170 uM for 4-aminobutanal {ECO:0000269|PubMed:20026072};
CC KM=11 uM for 4-guanidinobutanal {ECO:0000269|PubMed:20026072};
CC KM=40 uM for NAD(+) with 3-aminopropanal as substrate
CC {ECO:0000269|PubMed:20026072};
CC Vmax=57 nmol/min/mg enzyme with 3-aminopropanal as substrate
CC {ECO:0000269|PubMed:20026072};
CC Vmax=50 nmol/min/mg enzyme with 4-aminobutanal as substrate
CC {ECO:0000269|PubMed:20026072};
CC Vmax=68 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}.
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DR EMBL; AJ315852; CAC48392.3; -; mRNA.
DR PDB; 3IWK; X-ray; 2.40 A; A/B/C/D/E/F/G/H/I/J/K/L=1-503.
DR PDBsum; 3IWK; -.
DR SMR; Q8VWZ1; -.
DR BRENDA; 1.2.1.19; 4872.
DR UniPathway; UPA00529; UER00386.
DR EvolutionaryTrace; Q8VWZ1; -.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
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: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 1, peroxisomal"
FT /id="PRO_0000454133"
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 27
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000269|PubMed:20026072,
FT ECO:0007744|PDB:3IWK"
FT BINDING 28
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000269|PubMed:20026072,
FT ECO:0007744|PDB:3IWK"
FT BINDING 99
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000269|PubMed:20026072,
FT ECO:0007744|PDB:3IWK"
FT BINDING 189
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000269|PubMed:20026072,
FT ECO:0007744|PDB:3IWK"
FT BINDING 238..245
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:20026072,
FT ECO:0007744|PDB:3IWK"
FT BINDING 294
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:20026072,
FT ECO:0007744|PDB:3IWK"
FT BINDING 393
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:20026072,
FT ECO:0007744|PDB:3IWK"
FT SITE 162
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P20000"
FT STRAND 10..12
FT /evidence="ECO:0007829|PDB:3IWK"
FT STRAND 15..17
FT /evidence="ECO:0007829|PDB:3IWK"
FT STRAND 24..28
FT /evidence="ECO:0007829|PDB:3IWK"
FT TURN 30..32
FT /evidence="ECO:0007829|PDB:3IWK"
FT STRAND 35..40
FT /evidence="ECO:0007829|PDB:3IWK"
FT HELIX 44..58
FT /evidence="ECO:0007829|PDB:3IWK"
FT TURN 66..68
FT /evidence="ECO:0007829|PDB:3IWK"
FT HELIX 71..100
FT /evidence="ECO:0007829|PDB:3IWK"
FT HELIX 104..131
FT /evidence="ECO:0007829|PDB:3IWK"
FT STRAND 141..151
FT /evidence="ECO:0007829|PDB:3IWK"
FT STRAND 154..158
FT /evidence="ECO:0007829|PDB:3IWK"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:3IWK"
FT HELIX 164..178
FT /evidence="ECO:0007829|PDB:3IWK"
FT STRAND 181..185
FT /evidence="ECO:0007829|PDB:3IWK"
FT HELIX 192..203
FT /evidence="ECO:0007829|PDB:3IWK"
FT STRAND 210..213
FT /evidence="ECO:0007829|PDB:3IWK"
FT TURN 218..220
FT /evidence="ECO:0007829|PDB:3IWK"
FT HELIX 221..227
FT /evidence="ECO:0007829|PDB:3IWK"
FT STRAND 233..238
FT /evidence="ECO:0007829|PDB:3IWK"
FT HELIX 240..252
FT /evidence="ECO:0007829|PDB:3IWK"
FT STRAND 257..260
FT /evidence="ECO:0007829|PDB:3IWK"
FT STRAND 265..269
FT /evidence="ECO:0007829|PDB:3IWK"
FT STRAND 271..273
FT /evidence="ECO:0007829|PDB:3IWK"
FT HELIX 275..287
FT /evidence="ECO:0007829|PDB:3IWK"
FT HELIX 288..291
FT /evidence="ECO:0007829|PDB:3IWK"
FT STRAND 297..303
FT /evidence="ECO:0007829|PDB:3IWK"
FT TURN 304..306
FT /evidence="ECO:0007829|PDB:3IWK"
FT HELIX 307..319
FT /evidence="ECO:0007829|PDB:3IWK"
FT HELIX 339..354
FT /evidence="ECO:0007829|PDB:3IWK"
FT STRAND 358..361
FT /evidence="ECO:0007829|PDB:3IWK"
FT STRAND 371..373
FT /evidence="ECO:0007829|PDB:3IWK"
FT STRAND 378..382
FT /evidence="ECO:0007829|PDB:3IWK"
FT HELIX 388..391
FT /evidence="ECO:0007829|PDB:3IWK"
FT STRAND 396..406
FT /evidence="ECO:0007829|PDB:3IWK"
FT HELIX 407..414
FT /evidence="ECO:0007829|PDB:3IWK"
FT STRAND 424..426
FT /evidence="ECO:0007829|PDB:3IWK"
FT HELIX 430..439
FT /evidence="ECO:0007829|PDB:3IWK"
FT STRAND 442..449
FT /evidence="ECO:0007829|PDB:3IWK"
FT HELIX 463..465
FT /evidence="ECO:0007829|PDB:3IWK"
FT HELIX 472..477
FT /evidence="ECO:0007829|PDB:3IWK"
FT STRAND 480..488
FT /evidence="ECO:0007829|PDB:3IWK"
SQ SEQUENCE 503 AA; 54809 MW; 159D913011D51697 CRC64;
MAITVSSRQL FIDGEWRVPI LNKRIPNINP STENIIGDIP AATKEDVDLA VDAAKRAISR
KNGRDWSAAS GSLRARYLRA IAAKIKEKKD ELGKLESIDC GKPLEEALAD LDDVVACFEY
YAGLAEELDS KQKAPISLPM DTFKSYILKE PIGVVALITP WNYPFLMATW KIAPALAAGC
AAILKPSELA SVTCLELGEI CKEVGLPRGV LNIVTGLGHE AGASLASHPD VDKISFTGSS
ATGSKIMTTA AQLVKPVSLE LGGKSPIVVF EDVDLDKVAE WTVFGCFFTN GQICSATSRL
IVHESIAVEF VDKLVKWAEN IKISDPLEEG CRLGPIVSEA QYKKVLNCIS SAKSEGATIL
TGGRRPEHLK KGYFVEPTII TDVTTSMQIW REEVFGPVLA VKTFSTEEEA INLANDTHYG
LGSAVMSNDL ERCERLSKAL QAGIVWINCA QPSFIQAPWG GIKRSGFGRE LGEWGLENYL
SVKQVTRYTS DEPWGWYQPP SKL
