AADH1_SOLLC
ID AADH1_SOLLC Reviewed; 504 AA.
AC Q56R04;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Aminoaldehyde dehydrogenase 1 {ECO:0000303|PubMed:23408433};
DE Short=SlAMADH1 {ECO:0000303|PubMed:23408433};
DE EC=1.2.1.- {ECO:0000269|PubMed:23408433};
DE AltName: Full=4-trimethylammoniobutyraldehyde dehydrogenase AMADH1 {ECO:0000305};
DE EC=1.2.1.47 {ECO:0000269|PubMed:23408433};
DE AltName: Full=Aminobutyraldehyde dehydrogenase AMADH1 {ECO:0000305};
DE EC=1.2.1.19 {ECO:0000269|PubMed:23408433};
DE AltName: Full=Betaine aldehyde dehydrogenase AMADH1 {ECO:0000305};
DE EC=1.2.1.8 {ECO:0000269|PubMed:23408433};
DE AltName: Full=Gamma-guanidinobutyraldehyde dehydrogenase AMADH1 {ECO:0000305};
DE EC=1.2.1.54 {ECO:0000269|PubMed:23408433};
GN Name=AMADH1 {ECO:0000303|PubMed:23408433};
GN Synonyms=ALDH10A12 {ECO:0000303|PubMed:23408433};
GN OrderedLocusNames=Solyc06g071290 {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 [GENOMIC DNA].
RX PubMed=15842623; DOI=10.1111/j.1365-313x.2005.02380.x;
RA Hu G., deHart A.K., Li Y., Ustach C., Handley V., Navarre R., Hwang C.F.,
RA Aegerter B.J., Williamson V.M., Baker B.;
RT "EDS1 in tomato is required for resistance mediated by TIR-class R genes
RT and the receptor-like R gene Ve.";
RL Plant J. 42:376-391(2005).
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).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 2-504 IN COMPLEX WITH NAD AND
RP SODIUM ION, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES,
RP SUBUNIT, AND ACTIVE SITE.
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).
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). Catalyzes with low
CC efficiency the oxidation of betaine aldehyde to glycine betaine
CC (PubMed:23408433). {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 -!- CATALYTIC ACTIVITY:
CC Reaction=betaine aldehyde + H2O + NAD(+) = glycine betaine + 2 H(+) +
CC NADH; Xref=Rhea:RHEA:15305, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15710, ChEBI:CHEBI:17750, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.2.1.8;
CC Evidence={ECO:0000269|PubMed:23408433};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15306;
CC Evidence={ECO:0000269|PubMed:23408433};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=278 uM for 4-aminobutanal {ECO:0000269|PubMed:23408433};
CC KM=41 uM for 3-aminopropanal {ECO:0000269|PubMed:23408433};
CC KM=17 uM for 4-(trimethylamino)butanal {ECO:0000269|PubMed:23408433};
CC KM=85 uM for 4-guanidinobutanal {ECO:0000269|PubMed:23408433};
CC KM=2.1 mM for betaine aldehyde {ECO:0000269|PubMed:23408433};
CC KM=72 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:0000269|PubMed:23408433}.
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; AY796114; AAX73303.1; -; Genomic_DNA.
DR RefSeq; NP_001333606.1; NM_001346677.1.
DR PDB; 4I8Q; X-ray; 2.65 A; A=2-501.
DR PDB; 4I9B; X-ray; 1.90 A; A/B=2-504.
DR PDBsum; 4I8Q; -.
DR PDBsum; 4I9B; -.
DR SMR; Q56R04; -.
DR STRING; 4081.Solyc06g071290.2.1; -.
DR PaxDb; Q56R04; -.
DR PRIDE; Q56R04; -.
DR EnsemblPlants; Solyc06g071290.3.1; Solyc06g071290.3.1; Solyc06g071290.3.
DR GeneID; 101253497; -.
DR Gramene; Solyc06g071290.3.1; Solyc06g071290.3.1; Solyc06g071290.3.
DR KEGG; sly:101253497; -.
DR eggNOG; KOG2450; Eukaryota.
DR HOGENOM; CLU_005391_0_1_1; -.
DR InParanoid; Q56R04; -.
DR OMA; EGGHYSF; -.
DR OrthoDB; 153834at2759; -.
DR PhylomeDB; Q56R04; -.
DR UniPathway; UPA00529; UER00386.
DR Proteomes; UP000004994; Chromosome 6.
DR ExpressionAtlas; Q56R04; baseline and differential.
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: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; Metal-binding; NAD; Nucleotide-binding; Oxidoreductase;
KW Reference proteome; Sodium.
FT CHAIN 1..504
FT /note="Aminoaldehyde dehydrogenase 1"
FT /id="PRO_0000454138"
FT ACT_SITE 260
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007,
FT ECO:0000269|PubMed:23408433"
FT ACT_SITE 295
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10008,
FT ECO:0000269|PubMed:23408433"
FT BINDING 31
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000269|PubMed:23408433,
FT ECO:0007744|PDB:4I8Q, ECO:0007744|PDB:4I9B"
FT BINDING 99
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000269|PubMed:23408433,
FT ECO:0007744|PDB:4I8Q, ECO:0007744|PDB:4I9B"
FT BINDING 159..161
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:23408433,
FT ECO:0007744|PDB:4I8Q, ECO:0007744|PDB:4I9B"
FT BINDING 185..188
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:23408433,
FT ECO:0007744|PDB:4I8Q, ECO:0007744|PDB:4I9B"
FT BINDING 189
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000269|PubMed:23408433,
FT ECO:0007744|PDB:4I8Q, ECO:0007744|PDB:4I9B"
FT BINDING 238..242
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:23408433,
FT ECO:0007744|PDB:4I8Q, ECO:0007744|PDB:4I9B"
FT BINDING 261
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:23408433,
FT ECO:0007744|PDB:4I8Q"
FT BINDING 394
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:23408433,
FT ECO:0007744|PDB:4I8Q"
FT BINDING 460
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:23408433,
FT ECO:0007744|PDB:4I8Q"
FT SITE 162
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P20000"
FT STRAND 13..15
FT /evidence="ECO:0007829|PDB:4I9B"
FT STRAND 18..20
FT /evidence="ECO:0007829|PDB:4I9B"
FT STRAND 27..31
FT /evidence="ECO:0007829|PDB:4I9B"
FT TURN 33..35
FT /evidence="ECO:0007829|PDB:4I9B"
FT STRAND 38..43
FT /evidence="ECO:0007829|PDB:4I9B"
FT HELIX 47..62
FT /evidence="ECO:0007829|PDB:4I9B"
FT HELIX 64..67
FT /evidence="ECO:0007829|PDB:4I9B"
FT HELIX 71..87
FT /evidence="ECO:0007829|PDB:4I9B"
FT HELIX 89..100
FT /evidence="ECO:0007829|PDB:4I9B"
FT HELIX 104..128
FT /evidence="ECO:0007829|PDB:4I9B"
FT HELIX 129..131
FT /evidence="ECO:0007829|PDB:4I9B"
FT STRAND 132..136
FT /evidence="ECO:0007829|PDB:4I9B"
FT STRAND 141..151
FT /evidence="ECO:0007829|PDB:4I9B"
FT STRAND 154..158
FT /evidence="ECO:0007829|PDB:4I9B"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:4I8Q"
FT HELIX 164..177
FT /evidence="ECO:0007829|PDB:4I9B"
FT STRAND 181..185
FT /evidence="ECO:0007829|PDB:4I9B"
FT HELIX 192..204
FT /evidence="ECO:0007829|PDB:4I9B"
FT STRAND 210..213
FT /evidence="ECO:0007829|PDB:4I9B"
FT HELIX 218..226
FT /evidence="ECO:0007829|PDB:4I9B"
FT STRAND 233..238
FT /evidence="ECO:0007829|PDB:4I9B"
FT HELIX 240..251
FT /evidence="ECO:0007829|PDB:4I9B"
FT TURN 252..254
FT /evidence="ECO:0007829|PDB:4I9B"
FT STRAND 257..260
FT /evidence="ECO:0007829|PDB:4I9B"
FT STRAND 265..269
FT /evidence="ECO:0007829|PDB:4I9B"
FT HELIX 276..288
FT /evidence="ECO:0007829|PDB:4I9B"
FT HELIX 289..292
FT /evidence="ECO:0007829|PDB:4I9B"
FT STRAND 298..304
FT /evidence="ECO:0007829|PDB:4I9B"
FT TURN 305..307
FT /evidence="ECO:0007829|PDB:4I9B"
FT HELIX 308..320
FT /evidence="ECO:0007829|PDB:4I9B"
FT HELIX 340..355
FT /evidence="ECO:0007829|PDB:4I9B"
FT STRAND 359..362
FT /evidence="ECO:0007829|PDB:4I9B"
FT STRAND 379..383
FT /evidence="ECO:0007829|PDB:4I9B"
FT HELIX 389..392
FT /evidence="ECO:0007829|PDB:4I9B"
FT STRAND 397..407
FT /evidence="ECO:0007829|PDB:4I9B"
FT HELIX 408..415
FT /evidence="ECO:0007829|PDB:4I9B"
FT STRAND 425..427
FT /evidence="ECO:0007829|PDB:4I9B"
FT HELIX 431..440
FT /evidence="ECO:0007829|PDB:4I9B"
FT STRAND 443..452
FT /evidence="ECO:0007829|PDB:4I9B"
FT HELIX 464..466
FT /evidence="ECO:0007829|PDB:4I9B"
FT HELIX 473..478
FT /evidence="ECO:0007829|PDB:4I9B"
FT STRAND 481..489
FT /evidence="ECO:0007829|PDB:4I9B"
SQ SEQUENCE 504 AA; 54798 MW; 680F8FCA857B7ABC CRC64;
MANRNVPIPR RQLYIGGEWR EPVKKNRIPI INPATEEIIG DIPAATAEDV DIAVEAARKA
IARDDWGSTT GAQRAKYLRA IAAKVLEKKS VLATLESLDS GKTLYESAAD MDDVAGCFEY
YAGLAEALDS RRMTPVNLNS DSYKSYVLRE PLGVVGLITP WNYPLLMAIW KVAPALAAGC
AAILKPSELA SITCLELGEI CREIGLPSGA LNILTGLGPE AGGPLASHPH VDKISFTGSG
PTGSKIMTAA AQLVKPVSLE LGGKSPIVVF DDIDNLDIAA EWTLFGIFAN TGQVCSATSR
LIVQENIASA FMDRLLKWTK NIKISDPLEE DCKLGPVVSA GQYEKVLKFI SNAKSEGATI
LCGGERPQHL KKGYYVQPTI ITDVNTSMEI WKEEVFGPVL CVKTFKTEEQ AIELANDTKY
GLGAAVMSKD VKRCERFTKA FQTGIIWINC SQPTFNELPW GGKKRSGFGR DLGKWGLENF
LNIKQVTEYT SAEPLAFYKS PSKN
