AADH2_SOLLC
ID AADH2_SOLLC Reviewed; 505 AA.
AC B6ECN9; A0A3Q7FS73;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 2.
DT 03-AUG-2022, entry version 55.
DE RecName: Full=Aminoaldehyde dehydrogenase 2 {ECO:0000303|PubMed:23408433};
DE Short=SlAMADH2 {ECO:0000303|PubMed:23408433};
DE EC=1.2.1.- {ECO:0000269|PubMed:23408433};
DE AltName: Full=4-trimethylammoniobutyraldehyde dehydrogenase AMADH2 {ECO:0000305};
DE EC=1.2.1.47 {ECO:0000269|PubMed:23408433};
DE AltName: Full=Aminobutyraldehyde dehydrogenase AMADH2 {ECO:0000305};
DE EC=1.2.1.19 {ECO:0000269|PubMed:23408433};
DE AltName: Full=Gamma-guanidinobutyraldehyde dehydrogenase AMADH2 {ECO:0000305};
DE EC=1.2.1.54 {ECO:0000269|PubMed:23408433};
GN Name=AMADH2 {ECO:0000303|PubMed:23408433};
GN Synonyms=ALDH10A13 {ECO:0000303|PubMed:23408433};
GN OrderedLocusNames=Solyc03g113800 {ECO:0000305};
OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC Solanum subgen. Lycopersicon.
OX NCBI_TaxID=4081;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=23408433; DOI=10.1074/jbc.m112.443952;
RA Kopecny D., Koncitikova R., Tylichova M., Vigouroux A., Moskalikova H.,
RA Soural M., Sebela M., Morera S.;
RT "Plant ALDH10 family: identifying critical residues for substrate
RT specificity and trapping a thiohemiacetal intermediate.";
RL J. Biol. Chem. 288:9491-9507(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Heinz 1706;
RX PubMed=22660326; DOI=10.1038/nature11119;
RG Tomato Genome Consortium;
RT "The tomato genome sequence provides insights into fleshy fruit
RT evolution.";
RL Nature 485:635-641(2012).
CC -!- FUNCTION: Dehydrogenase that catalyzes the oxidation of several
CC aminoaldehydes (PubMed:23408433). 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:23408433).
CC Catalyzes the oxidation of 4-(trimethylamino)butanal and 4-
CC guanidinobutanal to 4-trimethylammoniobutanoate and 4-
CC guanidinobutanoate, respectively (PubMed:23408433).
CC {ECO:0000269|PubMed:23408433, 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:23408433};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19106;
CC Evidence={ECO:0000269|PubMed:23408433};
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:23408433};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30696;
CC Evidence={ECO:0000269|PubMed:23408433};
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:23408433};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17986;
CC Evidence={ECO:0000269|PubMed:23408433};
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:23408433};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14382;
CC Evidence={ECO:0000269|PubMed:23408433};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=54 uM for 4-aminobutanal {ECO:0000269|PubMed:23408433};
CC KM=9 uM for 3-aminopropanal {ECO:0000269|PubMed:23408433};
CC KM=141 uM for 4-(trimethylamino)butanal
CC {ECO:0000269|PubMed:23408433};
CC KM=22 uM for 4-guanidinobutanal {ECO:0000269|PubMed:23408433};
CC KM=89 uM for NAD(+) with 3-aminopropanal as substrate
CC {ECO:0000269|PubMed:23408433};
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:0000250|UniProtKB:Q56R04}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; FJ228482; ACI43573.1; -; mRNA.
DR RefSeq; NP_001234235.2; NM_001247306.2.
DR STRING; 4081.Solyc03g113800.2.1; -.
DR GeneID; 100301929; -.
DR KEGG; sly:100301929; -.
DR OMA; AFTASMH; -.
DR BRENDA; 1.2.1.19; 3101.
DR UniPathway; UPA00529; UER00386.
DR Proteomes; UP000004994; Chromosome 3.
DR ExpressionAtlas; B6ECN9; baseline and differential.
DR GO; GO:0033737; F:1-pyrroline dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0047105; F:4-trimethylammoniobutyraldehyde dehydrogenase activity; IDA:UniProtKB.
DR GO; GO:0019145; F:aminobutyraldehyde dehydrogenase activity; IDA:UniProtKB.
DR GO; GO:0008802; F:betaine-aldehyde dehydrogenase activity; IDA:UniProtKB.
DR GO; GO:0047107; F:gamma-guanidinobutyraldehyde dehydrogenase activity; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0031402; F:sodium ion binding; ISS: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 Metal-binding; NAD; Oxidoreductase; Reference proteome; Sodium.
FT CHAIN 1..505
FT /note="Aminoaldehyde dehydrogenase 2"
FT /id="PRO_0000454139"
FT ACT_SITE 260
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007"
FT ACT_SITE 295
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10008"
FT BINDING 31
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000250|UniProtKB:Q56R04"
FT BINDING 99
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000250|UniProtKB:Q56R04"
FT BINDING 159..161
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q56R04"
FT BINDING 185..188
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q56R04"
FT BINDING 189
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000250|UniProtKB:Q56R04"
FT BINDING 238..242
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q56R04"
FT BINDING 261
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q56R04"
FT BINDING 394
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q56R04"
FT BINDING 460
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q56R04"
FT SITE 162
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P20000"
FT CONFLICT 407
FT /note="I -> T (in Ref. 1; ACI43573)"
SQ SEQUENCE 505 AA; 55952 MW; 01B3F0AC37CD10E7 CRC64;
MAIPNIRIPC RQLFIDGEWR EPLKKNRLPI INPANEEIIG YIPAATEEDV DMAVKAARSA
LRRDDWGSTT GAQRAKYLRA IAAKVLEKKP ELATLETIDN GKPWFEAASD IDDVVACFEY
YADLAEALDS KKQTEVKLHL DSFKTHVLRE PLGVVGLITP WNYPLLMTTW KVAPALAAGC
AAILKPSELA SITSLELGEI CREVGLPPGA LSILTGLGHE AGSPLVSHPD VDKIAFTGSG
PTGVKIMTAA AQLVKPVTLE LGGKSPIVVF DDIHNLDTAV EWTLFGCFWT NGQICSATSR
LIIQETIAPQ FLARLLEWTK NIKISDPLEE DCKLGPVISR GQYEKILKFI STAKDEGATI
LYGGDRPEHL KKGYYIQPTI ITDVDTSMEI WKEEVFGPVL CVKTFKIEEE AIELANDTKF
GLGAAILSKD LERCERFTKA FQSGIVWINC SQPCFWQPPW GGKKRSGFGR ELGEWSLENY
LNIKQVTQYV TPDEPWAFYK SPSKL
