LOCUS       GQ184593                1518 bp    mRNA    linear   PLN 23-SEP-2011
DEFINITION  Zea mays aminoaldehyde dehydrogenase 1 (AMADH1) mRNA, complete cds.
ACCESSION   GQ184593
VERSION     GQ184593.1
KEYWORDS    .
SOURCE      Zea mays
  ORGANISM  Zea mays
            Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
            Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD
            clade; Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae;
            Zea.
REFERENCE   1  (bases 1 to 1518)
  AUTHORS   Kopecny,D., Tylichova,M., Snegaroff,J., Popelkova,H. and Sebela,M.
  TITLE     Carboxylate and aromatic active-site residues are determinants of
            high-affinity binding of omega-aminoaldehydes to plant
            aminoaldehyde dehydrogenases
  JOURNAL   FEBS J. 278 (17), 3130-3139 (2011)
   PUBMED   21740525
REFERENCE   2  (bases 1 to 1518)
  AUTHORS   Kopecny,D., Tylichova,M., Snegaroff,J. and Sebela,M.
  TITLE     Cloning, purification and characterization of Zea mays
            aminoaldehyde dehydrogenase
  JOURNAL   Unpublished
REFERENCE   3  (bases 1 to 1518)
  AUTHORS   Kopecny,D., Tylichova,M., Sebela,M. and Snegaroff,J.
  TITLE     Direct Submission
  JOURNAL   Submitted (22-MAY-2009) Department Of Biochemistry, Palacky
            University, Slechtitelu 11, Olomouc CZ-78371, Czech Republic
FEATURES             Location/Qualifiers
     source          1..1518
                     /organism="Zea mays"
                     /mol_type="mRNA"
                     /cultivar="Sachara"
                     /db_xref="taxon:4577"
                     /tissue_type="apical meristem"
                     /dev_stage="5-day old seedlings"
                     /geo_loc_name="Czech Republic"
     gene            1..1518
                     /gene="AMADH1"
                     /note="ZmAMADH1"
     CDS             1..1518
                     /gene="AMADH1"
                     /EC_number="1.2.1.19"
                     /note="betaine aldehyde dehydrogenase; BADH; involved in
                     oxidation of aminoaldehydes to corresponding amino acids
                     with NAD as a coenzyme"
                     /codon_start=1
                     /product="aminoaldehyde dehydrogenase 1"
                     /protein_id="ACS74867.1"
                     /translation="MASPAMVPLRQLFVDGEWRPPAQGRRLPVVNPTTEAHIGEIPAG
                     TAEDVDAAVAAARAALKRNRGRDWARAPGAVRAKYLRAIAAKVIERKPELAKLEALDC
                     GKPYDEAAWDMDDVAGCFEYFADQAEALDKRQNSPVSLPMETFKCHLRREPIGVVGLI
                     TPWNYPLLMATWKIAPALAAGCTAVLKPSELASVTCLELADICKEVGLPSGVLNIVTG
                     LGPDAGAPLSAHPDVDKVAFTGSFETGKKIMASAAPMVKPVTLELGGKSPIVVFDDVD
                     IDKAVEWTLFGCFWTNGQICSATSRLLIHTKIAKKFNERMVAWAKNIKVSDPLEEGCR
                     LGPVVSEGQYEKIKKFISNAKSQGATILTGGVRPAHLEKGFFIEPTIITDITTSMEIW
                     REEVFGPVLCVKEFSTEDEAIELANDTQYGLAGAVISGDRERCQRLSEEIDAGCIWVN
                     CSQPCFCQAPWGGNKRSGFGRELGEGGIDNYLSVKQVTEYISDEPWGWYQSPSKL"
BASE COUNT          355 a          347 c          443 g          373 t
ORIGIN      
        1 atggcctcgc cagcgatggt cccgctgcgg cagctcttcg tcgacggcga gtggcgcccg
       61 cccgcgcagg gccgccgcct ccccgtcgtc aaccccacca ccgaggctca catcggcgag
      121 atccctgcgg gcacagcgga ggacgtggac gccgcggtgg cggcggcgcg ggcggcgctc
      181 aagaggaacc gtggccgcga ctgggcgcgc gccccggggg ccgtccgggc caagtacctc
      241 cgcgctatcg ccgccaaggt gattgagagg aaacctgagc tggctaagct agaggcactt
      301 gattgtggga agccttatga tgaagcagca tgggacatgg atgatgttgc tgggtgcttt
      361 gagtactttg cggatcaggc agaagccttg gataaaaggc aaaattcccc agtttctctt
      421 ccaatggaaa cttttaaatg tcatctccga agagagccta ttggggtagt tgggctgata
      481 actccttgga actatcctct actgatggct acatggaaga tagcccctgc attggctgct
      541 ggttgtacag ctgtgctgaa gccatctgaa ctggcttctg tgacttgctt agagcttgct
      601 gatatctgta aagaagtcgg tctcccttct ggtgtcttga acattgtgac aggattaggt
      661 cctgatgctg gcgctccttt gtcagcacac ccagatgttg acaaggtcgc ttttactggg
      721 agttttgaaa ctggcaagaa aattatggca tcggcagctc ctatggtcaa gcctgttaca
      781 ctggaacttg gtggaaaaag tcctatagta gtatttgatg atgttgacat tgacaaagct
      841 gtcgagtgga ctctgtttgg gtgcttttgg accaatggtc agatttgcag cgcgacatct
      901 cgtcttctta tccatacaaa aattgctaaa aaatttaatg agaggatggt tgcatgggcc
      961 aaaaatatta aggtttcgga tccacttgaa gagggttgca ggcttgggcc agttgttagt
     1021 gaaggacagt atgagaagat taagaagttc atatcgaatg ccaaaagcca aggtgctact
     1081 attctgactg gaggtgttag acctgcgcat cttgagaagg ggttctttat tgaaccaact
     1141 attattactg atatcaccac atcaatggaa atctggaggg aggaagtctt tggtccagtc
     1201 ctgtgcgtta aagaatttag cactgaagat gaagccatcg aacttgccaa cgatacacag
     1261 tatggtttgg ctggtgctgt aatttctggt gatcgggagc gctgccagag gttatctgag
     1321 gagattgacg ctggatgcat ctgggtaaac tgctcgcaac cctgcttctg ccaagctccc
     1381 tggggcggga acaagcgcag tggatttgga cgtgagcttg gagaaggggg cattgataac
     1441 tacctgagcg tcaagcaagt cacggagtac atctctgatg agccgtgggg atggtaccaa
     1501 tccccctcca agctgtaa
//