AADH2_MAIZE
ID AADH2_MAIZE Reviewed; 506 AA.
AC C6KEM4; A0A1D6J865; B4G044; B6SWI7;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 2.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=Aminoaldehyde dehydrogenase 2 {ECO:0000303|PubMed:23408433};
DE Short=ZmAMADH2 {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=ALDH10A5 {ECO:0000303|PubMed:23408433};
GN ORFNames=ZEAMMB73_Zm00001d025626 {ECO:0000312|EMBL:AQK44109.1};
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC TISSUE=Meristem;
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. B73;
RX PubMed=19965430; DOI=10.1126/science.1178534;
RA Schnable P.S., Ware D., Fulton R.S., Stein J.C., Wei F., Pasternak S.,
RA Liang C., Zhang J., Fulton L., Graves T.A., Minx P., Reily A.D.,
RA Courtney L., Kruchowski S.S., Tomlinson C., Strong C., Delehaunty K.,
RA Fronick C., Courtney B., Rock S.M., Belter E., Du F., Kim K., Abbott R.M.,
RA Cotton M., Levy A., Marchetto P., Ochoa K., Jackson S.M., Gillam B.,
RA Chen W., Yan L., Higginbotham J., Cardenas M., Waligorski J., Applebaum E.,
RA Phelps L., Falcone J., Kanchi K., Thane T., Scimone A., Thane N., Henke J.,
RA Wang T., Ruppert J., Shah N., Rotter K., Hodges J., Ingenthron E.,
RA Cordes M., Kohlberg S., Sgro J., Delgado B., Mead K., Chinwalla A.,
RA Leonard S., Crouse K., Collura K., Kudrna D., Currie J., He R.,
RA Angelova A., Rajasekar S., Mueller T., Lomeli R., Scara G., Ko A.,
RA Delaney K., Wissotski M., Lopez G., Campos D., Braidotti M., Ashley E.,
RA Golser W., Kim H., Lee S., Lin J., Dujmic Z., Kim W., Talag J., Zuccolo A.,
RA Fan C., Sebastian A., Kramer M., Spiegel L., Nascimento L., Zutavern T.,
RA Miller B., Ambroise C., Muller S., Spooner W., Narechania A., Ren L.,
RA Wei S., Kumari S., Faga B., Levy M.J., McMahan L., Van Buren P.,
RA Vaughn M.W., Ying K., Yeh C.-T., Emrich S.J., Jia Y., Kalyanaraman A.,
RA Hsia A.-P., Barbazuk W.B., Baucom R.S., Brutnell T.P., Carpita N.C.,
RA Chaparro C., Chia J.-M., Deragon J.-M., Estill J.C., Fu Y., Jeddeloh J.A.,
RA Han Y., Lee H., Li P., Lisch D.R., Liu S., Liu Z., Nagel D.H., McCann M.C.,
RA SanMiguel P., Myers A.M., Nettleton D., Nguyen J., Penning B.W.,
RA Ponnala L., Schneider K.L., Schwartz D.C., Sharma A., Soderlund C.,
RA Springer N.M., Sun Q., Wang H., Waterman M., Westerman R., Wolfgruber T.K.,
RA Yang L., Yu Y., Zhang L., Zhou S., Zhu Q., Bennetzen J.L., Dawe R.K.,
RA Jiang J., Jiang N., Presting G.G., Wessler S.R., Aluru S.,
RA Martienssen R.A., Clifton S.W., McCombie W.R., Wing R.A., Wilson R.K.;
RT "The B73 maize genome: complexity, diversity, and dynamics.";
RL Science 326:1112-1115(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=18937034; DOI=10.1007/s11103-008-9415-4;
RA Alexandrov N.N., Brover V.V., Freidin S., Troukhan M.E., Tatarinova T.V.,
RA Zhang H., Swaller T.J., Lu Y.-P., Bouck J., Flavell R.B., Feldmann K.A.;
RT "Insights into corn genes derived from large-scale cDNA sequencing.";
RL Plant Mol. Biol. 69:179-194(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. B73; TISSUE=Seedling;
RX PubMed=19936069; DOI=10.1371/journal.pgen.1000740;
RA Soderlund C., Descour A., Kudrna D., Bomhoff M., Boyd L., Currie J.,
RA Angelova A., Collura K., Wissotski M., Ashley E., Morrow D., Fernandes J.,
RA Walbot V., Yu Y.;
RT "Sequencing, mapping, and analysis of 27,455 maize full-length cDNAs.";
RL PLoS Genet. 5:E1000740-E1000740(2009).
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=59 uM for 4-aminobutanal {ECO:0000269|PubMed:23408433};
CC KM=98 uM for 3-aminopropanal {ECO:0000269|PubMed:23408433};
CC KM=16 uM for 4-(trimethylamino)butanal {ECO:0000269|PubMed:23408433};
CC KM=11 uM for 4-guanidinobutanal {ECO:0000269|PubMed:23408433};
CC KM=86 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 -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AQK44109.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; GQ184594; ACS74868.1; -; mRNA.
DR EMBL; CM000786; AQK44108.1; -; Genomic_DNA.
DR EMBL; CM000786; AQK44109.1; ALT_INIT; Genomic_DNA.
DR EMBL; EU957102; ACG29220.1; -; mRNA.
DR EMBL; BT042732; ACF87737.1; -; mRNA.
DR EMBL; BT067636; ACN34533.1; -; mRNA.
DR RefSeq; NP_001157804.1; NM_001164332.1.
DR SMR; C6KEM4; -.
DR STRING; 4577.GRMZM2G135470_P01; -.
DR EnsemblPlants; Zm00001eb424410_T001; Zm00001eb424410_P001; Zm00001eb424410.
DR GeneID; 541949; -.
DR Gramene; Zm00001eb424410_T001; Zm00001eb424410_P001; Zm00001eb424410.
DR KEGG; zma:541949; -.
DR eggNOG; KOG2450; Eukaryota.
DR HOGENOM; CLU_005391_0_1_1; -.
DR OMA; AFTASMH; -.
DR OrthoDB; 153834at2759; -.
DR BRENDA; 1.2.1.19; 6752.
DR UniPathway; UPA00529; UER00386.
DR Proteomes; UP000007305; Chromosome 10.
DR ExpressionAtlas; C6KEM4; baseline and differential.
DR GO; GO:0005777; C:peroxisome; IEA:EnsemblPlants.
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; IEA:EnsemblPlants.
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:0071454; P:cellular response to anoxia; IEA:EnsemblPlants.
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..506
FT /note="Aminoaldehyde dehydrogenase 2"
FT /id="PRO_0000454137"
FT ACT_SITE 262
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007"
FT ACT_SITE 297
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10008"
FT BINDING 101
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000250|UniProtKB:C0P9J6"
FT BINDING 161..163
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:C0P9J6"
FT BINDING 187..190
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:C0P9J6"
FT BINDING 191
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000250|UniProtKB:C0P9J6"
FT BINDING 241..244
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:C0P9J6"
FT BINDING 262
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:C0P9J6"
FT BINDING 396
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:C0P9J6"
FT BINDING 462
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:C0P9J6"
FT SITE 164
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P20000"
FT CONFLICT 67
FT /note="H -> Q (in Ref. 1; ACS74868)"
FT CONFLICT 135
FT /note="Q -> R (in Ref. 1; ACS74868)"
FT /evidence="ECO:0000305"
FT CONFLICT 202
FT /note="I -> T (in Ref. 3; ACG29220)"
FT /evidence="ECO:0000305"
FT CONFLICT 250
FT /note="I -> T (in Ref. 1; ACS74868 and 3; ACG29220)"
FT /evidence="ECO:0000305"
FT CONFLICT 274
FT /note="D -> G (in Ref. 3; ACG29220)"
FT /evidence="ECO:0000305"
FT CONFLICT 410
FT /note="E -> D (in Ref. 1; ACS74868)"
FT /evidence="ECO:0000305"
FT CONFLICT 442
FT /note="A -> P (in Ref. 3; ACG29220)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 506 AA; 54862 MW; 8033CB10EF67B5A3 CRC64;
MAPPQTIPRR GLFIGGAWRE PCLGRRLPVV NPATEATIGD IPAGTAEDVE IAVAAARDAF
SRDGGRHWSR APGAVRANFL RAIAAKIKDR KSELALLETL DSGKPLDEAS GDMDDVAACF
EYYADLAEAL DGKQQSPISL PMENFKSYVL KEPIGVVGLI TPWNYPLLMA TWKVAPALAA
GCTTILKPSE LASVSCLELG AICMEIGLPP GVLNIITGLG PEAGAPLSSH SHVDKVAFTG
STETGKRIMI SAAQMVKPVS LELGGKSPLI VFDDIGDIDK AVEWTMFGIF ANAGQVCSAT
SRLLLHEKIA KKFLDRLVAW AKNIKVSDPL EEGCRLGSVI SEGQYEKIKK FISTARSEGA
TILYGGGRPQ HLRRGFFLEP TIITDVSTSM QIWQEEVFGP VICVKEFRTE SEAVELANDT
HYGLAGAVIS NDQERCERIS KALHSGIIWI NCSQPCFVQA PWGGNKRSGF GRELGEWGLD
NYLTVKQVTK YCSDEPWGWY QPPSKL
