ADH1A_MAIZE
ID ADH1A_MAIZE Reviewed; 505 AA.
AC C0P9J6;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Aminoaldehyde dehydrogenase 1a {ECO:0000303|PubMed:23408433};
DE Short=ZmAMADH1a {ECO:0000303|PubMed:23408433};
DE EC=1.2.1.- {ECO:0000269|PubMed:21740525, ECO:0000269|PubMed:23408433};
DE AltName: Full=4-trimethylammoniobutyraldehyde dehydrogenase AMADH1a {ECO:0000305};
DE EC=1.2.1.47 {ECO:0000269|PubMed:21740525};
DE AltName: Full=Aminobutyraldehyde dehydrogenase AMADH1a {ECO:0000305};
DE EC=1.2.1.19 {ECO:0000269|PubMed:23408433};
DE AltName: Full=Betaine aldehyde dehydrogenase AMADH1a {ECO:0000305};
DE EC=1.2.1.8 {ECO:0000269|PubMed:21740525, ECO:0000269|PubMed:23408433};
DE AltName: Full=Gamma-guanidinobutyraldehyde dehydrogenase AMADH1a {ECO:0000305};
DE EC=1.2.1.54 {ECO:0000269|PubMed:23408433};
GN Name=AMADH1A {ECO:0000303|PubMed:21740525};
GN Synonyms=ALDH10A8 {ECO:0000303|PubMed:23408433};
GN ORFNames=ZEAMMB73_Zm00001d050339 {ECO:0000312|EMBL:AQK52374.1};
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.
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 [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].
RC STRAIN=cv. B73;
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).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 2-505 IN COMPLEX WITH NAD AND
RP SODIUM ION, SUBUNIT, FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL
RP 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).
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 the
CC oxidation of betaine aldehyde to glycine betaine (PubMed:23408433).
CC {ECO:0000269|PubMed:23408433, ECO:0000305}.
CC -!- FUNCTION: Dehydrogenase that catalyzes the oxidation of several
CC aminoaldehydes (PubMed:21740525). Catalyzes the oxidation of betaine
CC aldehyde to glycine betaine (PubMed:21740525). Catalyzes the oxidation
CC of 4-(trimethylamino)butanal to 4-trimethylammoniobutanoate
CC (PubMed:21740525). {ECO:0000269|PubMed:21740525}.
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:21740525, 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; Evidence={ECO:0000269|PubMed:21740525,
CC ECO:0000269|PubMed:23408433};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15306;
CC Evidence={ECO:0000269|PubMed:21740525, ECO:0000269|PubMed:23408433};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=28 uM for 4-aminobutanal {ECO:0000269|PubMed:23408433};
CC KM=9 uM for 3-aminopropanal {ECO:0000269|PubMed:23408433};
CC KM=6 uM for 4-(trimethylamino)butanal {ECO:0000269|PubMed:23408433};
CC KM=3 uM for 4-guanidinobutanal {ECO:0000269|PubMed:23408433};
CC KM=14 uM for betaine aldehyde {ECO:0000269|PubMed:21740525,
CC ECO:0000269|PubMed:23408433};
CC KM=91 uM for NAD(+) with 3-aminopropanal as substrate
CC {ECO:0000269|PubMed:23408433};
CC Vmax=11 nmol/sec/mg enzyme with betaine aldehyde as substrate
CC {ECO:0000269|PubMed:21740525};
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}.
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DR EMBL; GQ184593; ACS74867.1; -; mRNA.
DR EMBL; CM000780; AQK52374.1; -; Genomic_DNA.
DR EMBL; BT064965; ACN30841.1; -; mRNA.
DR RefSeq; NP_001157807.1; NM_001164335.1.
DR PDB; 4I8P; X-ray; 1.95 A; A/B=2-505.
DR PDBsum; 4I8P; -.
DR AlphaFoldDB; C0P9J6; -.
DR SMR; C0P9J6; -.
DR PRIDE; C0P9J6; -.
DR EnsemblPlants; Zm00001eb179190_T004; Zm00001eb179190_P004; Zm00001eb179190.
DR GeneID; 100302679; -.
DR Gramene; Zm00001eb179190_T004; Zm00001eb179190_P004; Zm00001eb179190.
DR KEGG; zma:100302679; -.
DR OMA; REPKHIW; -.
DR OrthoDB; 153834at2759; -.
DR BRENDA; 1.2.1.19; 6752.
DR UniPathway; UPA00529; UER00386.
DR Proteomes; UP000007305; Chromosome 4.
DR ExpressionAtlas; C0P9J6; 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: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..505
FT /note="Aminoaldehyde dehydrogenase 1a"
FT /id="PRO_0000454135"
FT ACT_SITE 262
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007"
FT ACT_SITE 296
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:0000269|PubMed:23408433,
FT ECO:0007744|PDB:4I8P"
FT BINDING 161..163
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:23408433,
FT ECO:0007744|PDB:4I8P"
FT BINDING 187..190
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:23408433,
FT ECO:0007744|PDB:4I8P"
FT BINDING 191
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000269|PubMed:23408433,
FT ECO:0007744|PDB:4I8P"
FT BINDING 241..244
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:23408433,
FT ECO:0007744|PDB:4I8P"
FT BINDING 262
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:23408433,
FT ECO:0007744|PDB:4I8P"
FT BINDING 395
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:23408433,
FT ECO:0007744|PDB:4I8P"
FT BINDING 461
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:23408433,
FT ECO:0007744|PDB:4I8P"
FT SITE 164
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P20000"
FT STRAND 12..14
FT /evidence="ECO:0007829|PDB:4I8P"
FT STRAND 17..19
FT /evidence="ECO:0007829|PDB:4I8P"
FT STRAND 26..30
FT /evidence="ECO:0007829|PDB:4I8P"
FT TURN 32..34
FT /evidence="ECO:0007829|PDB:4I8P"
FT STRAND 37..42
FT /evidence="ECO:0007829|PDB:4I8P"
FT HELIX 46..61
FT /evidence="ECO:0007829|PDB:4I8P"
FT HELIX 62..65
FT /evidence="ECO:0007829|PDB:4I8P"
FT TURN 66..70
FT /evidence="ECO:0007829|PDB:4I8P"
FT HELIX 73..89
FT /evidence="ECO:0007829|PDB:4I8P"
FT HELIX 91..102
FT /evidence="ECO:0007829|PDB:4I8P"
FT HELIX 106..133
FT /evidence="ECO:0007829|PDB:4I8P"
FT STRAND 145..153
FT /evidence="ECO:0007829|PDB:4I8P"
FT STRAND 156..160
FT /evidence="ECO:0007829|PDB:4I8P"
FT STRAND 163..165
FT /evidence="ECO:0007829|PDB:4I8P"
FT HELIX 166..179
FT /evidence="ECO:0007829|PDB:4I8P"
FT STRAND 183..187
FT /evidence="ECO:0007829|PDB:4I8P"
FT HELIX 194..205
FT /evidence="ECO:0007829|PDB:4I8P"
FT STRAND 212..215
FT /evidence="ECO:0007829|PDB:4I8P"
FT TURN 220..223
FT /evidence="ECO:0007829|PDB:4I8P"
FT HELIX 224..228
FT /evidence="ECO:0007829|PDB:4I8P"
FT STRAND 234..240
FT /evidence="ECO:0007829|PDB:4I8P"
FT HELIX 242..252
FT /evidence="ECO:0007829|PDB:4I8P"
FT HELIX 253..255
FT /evidence="ECO:0007829|PDB:4I8P"
FT STRAND 259..262
FT /evidence="ECO:0007829|PDB:4I8P"
FT STRAND 268..271
FT /evidence="ECO:0007829|PDB:4I8P"
FT STRAND 273..275
FT /evidence="ECO:0007829|PDB:4I8P"
FT HELIX 277..289
FT /evidence="ECO:0007829|PDB:4I8P"
FT HELIX 290..293
FT /evidence="ECO:0007829|PDB:4I8P"
FT STRAND 301..305
FT /evidence="ECO:0007829|PDB:4I8P"
FT TURN 306..308
FT /evidence="ECO:0007829|PDB:4I8P"
FT HELIX 309..321
FT /evidence="ECO:0007829|PDB:4I8P"
FT HELIX 341..356
FT /evidence="ECO:0007829|PDB:4I8P"
FT STRAND 360..363
FT /evidence="ECO:0007829|PDB:4I8P"
FT STRAND 373..375
FT /evidence="ECO:0007829|PDB:4I8P"
FT STRAND 380..384
FT /evidence="ECO:0007829|PDB:4I8P"
FT HELIX 390..393
FT /evidence="ECO:0007829|PDB:4I8P"
FT STRAND 398..408
FT /evidence="ECO:0007829|PDB:4I8P"
FT HELIX 409..417
FT /evidence="ECO:0007829|PDB:4I8P"
FT STRAND 423..428
FT /evidence="ECO:0007829|PDB:4I8P"
FT HELIX 432..441
FT /evidence="ECO:0007829|PDB:4I8P"
FT STRAND 444..452
FT /evidence="ECO:0007829|PDB:4I8P"
FT HELIX 465..467
FT /evidence="ECO:0007829|PDB:4I8P"
FT STRAND 472..474
FT /evidence="ECO:0007829|PDB:4I8P"
FT HELIX 477..481
FT /evidence="ECO:0007829|PDB:4I8P"
FT STRAND 482..490
FT /evidence="ECO:0007829|PDB:4I8P"
SQ SEQUENCE 505 AA; 54913 MW; 5B3D693764642D8F CRC64;
MASPAMVPLR QLFVDGEWRP PAQGRRLPVV NPTTEAHIGE IPAGTAEDVD AAVAAARAAL
KRNRGRDWAR APGAVRAKYL RAIAAKVIER KPELAKLEAL DCGKPYDEAA WDMDDVAGCF
EYFADQAEAL DKRQNSPVSL PMETFKCHLR REPIGVVGLI TPWNYPLLMA TWKIAPALAA
GCTAVLKPSE LASVTCLELA DICKEVGLPS GVLNIVTGLG PDAGAPLSAH PDVDKVAFTG
SFETGKKIMA SAAPMVKPVT LELGGKSPIV VFDDVDIDKA VEWTLFGCFW TNGQICSATS
RLLIHTKIAK KFNERMVAWA KNIKVSDPLE EGCRLGPVVS EGQYEKIKKF ISNAKSQGAT
ILTGGVRPAH LEKGFFIEPT IITDITTSME IWREEVFGPV LCVKEFSTED EAIELANDTQ
YGLAGAVISG DRERCQRLSE EIDAGCIWVN CSQPCFCQAP WGGNKRSGFG RELGEGGIDN
YLSVKQVTEY ISDEPWGWYQ SPSKL
