Gamma-aminobutyraldehyde dehydrogenase (P77674)

Identification
Name:Gamma-aminobutyraldehyde dehydrogenase
Synonyms:
  • 1-pyrroline dehydrogenase
  • 4-aminobutanal dehydrogenase
  • ABALDH
Gene Name:ydcW
Enzyme Class:
Biological Properties
General Function:Involved in aminobutyraldehyde dehydrogenase activity
Specific Function:Catalyzes the oxidation of 1-pyrroline, which is spontaneously formed from 4-aminobutanal, leading to 4- aminobutanoate (GABA). Can also oxidize n-alkyl medium-chain aldehydes, but with a lower catalytic efficiency
Cellular Location:Not Available
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+2.0Thumb+1.0Thumb
1.04-Aminobutyraldehyde + 1.0Water + 1.0NAD ↔ 1.0gamma-Aminobutyric acid + 2.0Hydrogen ion + 1.0NADH
ReactionCard
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.04-Aminobutyraldehyde + 1.0NAD + 1.0Water ↔ 1.0gamma-Aminobutyric acid + 1.0NADH + 1.0Hydrogen ion
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+2.0Thumb+1.0Thumb
1.04-Aminobutyraldehyde + 1.0Water + 1.0NAD ↔ 1.0gamma-Aminobutyric acid + 2.0Hydrogen ion + 1.0NADH
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.04-Aminobutyraldehyde + 1.0NAD + 1.0Water → 1.0gamma-Aminobutyric acid + 1.0NADH
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB010804-AminobutyraldehydeMetaboCard
ECMDB04017gamma-Aminobutyric acidMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB00902NADMetaboCard
ECMDB01487NADHMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Function
aminobutyraldehyde dehydrogenase activity
binding
catalytic activity
NAD or NADH binding
nucleotide binding
oxidoreductase activity
oxidoreductase activity, acting on the aldehyde or oxo group of donors
oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
Process
cellular amino acid and derivative metabolic process
cellular amino acid derivative metabolic process
cellular biogenic amine metabolic process
cellular metabolic process
metabolic process
oxidation reduction
polyamine catabolic process
polyamine metabolic process
putrescine catabolic process
Gene Properties
Blattner:b1444
Gene OrientationClockwise
Centisome Percentage:32.62
Left Sequence End1513602
Right Sequence End1515026
Gene Sequence:
>1425 bp
ATGAGTACTGAAATCAAAACTCAGGTCGTGGTACTTGGGGCAGGCCCCGCAGGTTACTCC
GCTGCCTTCCGTTGCGCTGATTTAGGTCTGGAAACCGTAATCGTAGAACGTTACAACACC
CTTGGCGGTGTTTGCCTGAACGTCGGCTGTATCCCTTCTAAAGCACTGCTGCACGTAGCA
AAAGTTATCGAAGAAGCCAAAGCGCTGGCTGAACACGGTATCGTCTTCGGCGAACCGAAA
ACCGATATCGACAAGATTCGTACCTGGAAAGAGAAAGTGATCAATCAGCTGACCGGTGGT
CTGGCTGGTATGGCGAAAGGCCGCAAAGTCAAAGTGGTCAACGGTCTGGGTAAATTCACC
GGGGCTAACACCCTGGAAGTTGAAGGTGAGAACGGCAAAACCGTGATCAACTTCGACAAC
GCGATCATTGCAGCGGGTTCTCGCCCGATCCAACTGCCGTTTATTCCGCATGAAGATCCG
CGTATCTGGGACTCCACTGACGCGCTGGAACTGAAAGAAGTACCAGAACGCCTGCTGGTA
ATGGGTGGCGGTATCATCGGTCTGGAAATGGGCACCGTTTACCACGCGCTGGGTTCACAG
ATTGACGTGGTTGAAATGTTCGACCAGGTTATCCCGGCAGCTGACAAAGACATCGTTAAA
GTCTTCACCAAGCGTATCAGCAAGAAATTCAACCTGATGCTGGAAACCAAAGTTACCGCC
GTTGAAGCGAAAGAAGACGGCATTTATGTGACGATGGAAGGCAAAAAAGCACCCGCTGAA
CCGCAGCGTTACGACGCCGTGCTGGTAGCGATTGGTCGTGTGCCGAACGGTAAAAACCTC
GACGCAGGCAAAGCAGGCGTGGAAGTTGACGACCGTGGTTTCATCCGCGTTGACAAACAG
CTGCGTACCAACGTACCGCACATCTTTGCTATCGGCGATATCGTCGGTCAACCGATGCTG
GCACACAAAGGTGTTCACGAAGGTCACGTTGCCGCTGAAGTTATCGCCGGTAAGAAACAC
TACTTCGATCCGAAAGTTATCCCGTCCATCGCCTATACCGAACCAGAAGTTGCATGGGTG
GGTCTGACTGAGAAAGAAGCGAAAGAGAAAGGCATCAGCTATGAAACCGCCACCTTCCCG
TGGGCTGCTTCTGGTCGTGCTATCGCTTCCGACTGCGCAGACGGTATGACCAAGCTGATT
TTCGACAAAGAATCTCACCGTGTGATCGGTGGTGCGATTGTCGGTACTAACGGCGGCGAG
CTGCTGGGTGAAATCGGCCTGGCAATCGAAATGGGTTGTGATGCTGAAGACATCGCACTG
ACCATCCACGCGCACCCGACTCTGCACGAGTCTGTGGGCCTGGCGGCAGAAGTGTTCGAA
GGTAGCATTACCGACCTGCCGAACCCGAAAGCGAAGAAGAAGTAA
Protein Properties
Pfam Domain Function:
Protein Residues:474
Protein Molecular Weight:50830
Protein Theoretical pI:6
PDB File:1WND
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Gamma-aminobutyraldehyde dehydrogenase
MQHKLLINGELVSGEGEKQPVYNPATGDVLLEIAEASAEQVDAAVRAADAAFAEWGQTTP
KVRAECLLKLADVIEENGQVFAELESRNCGKPLHSAFNDEIPAIVDVFRFFAGAARCLNG
LAAGEYLEGHTSMIRRDPLGVVASIAPWNYPLMMAAWKLAPALAAGNCVVLKPSEITPLT
ALKLAELAKDIFPAGVINILFGRGKTVGDPLTGHPKVRMVSLTGSIATGEHIISHTASSI
KRTHMELGGKAPVIVFDDADIEAVVEGVRTFGYYNAGQDCTAACRIYAQKGIYDTLVEKL
GAAVATLKSGAPDDESTELGPLSSLAHLERVGKAVEEAKATGHIKVITGGEKRKGNGYYY
APTLLAGALQDDAIVQKEVFGPVVSVTPFDNEEQVVNWANDSQYGLASSVWTKDVGRAHR
VSARLQYGCTWVNTHFMLVSEMPHGGQKLSGYGKDMSLYGLEDYTVVRHVMVKH
References
External Links:
ResourceLink
Uniprot ID:P77674
Uniprot Name:ABDH_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674337
PDB ID:1WND
Ecogene ID:EG13766
Ecocyc:EG13766
ColiBase:b1444
Kegg Gene:b1444
EchoBASE ID:EB3529
CCDB:ABDH_ECOLI
BacMap:16129403
General Reference:
  • Aiba, H., Baba, T., Hayashi, K., Inada, T., Isono, K., Itoh, T., Kasai, H., Kashimoto, K., Kimura, S., Kitakawa, M., Kitagawa, M., Makino, K., Miki, T., Mizobuchi, K., Mori, H., Mori, T., Motomura, K., Nakade, S., Nakamura, Y., Nashimoto, H., Nishio, Y., Oshima, T., Saito, N., Sampei, G., Horiuchi, T., et, a. l. .. (1996). "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map." DNA Res 3:363-377. Pubmed: 9097039
  • Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Gruez, A., Roig-Zamboni, V., Grisel, S., Salomoni, A., Valencia, C., Campanacci, V., Tegoni, M., Cambillau, C. (2004). "Crystal structure and kinetics identify Escherichia coli YdcW gene product as a medium-chain aldehyde dehydrogenase." J Mol Biol 343:29-41. Pubmed: 15381418
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Samsonova, N. N., Smirnov, S. V., Novikova, A. E., Ptitsyn, L. R. (2005). "Identification of Escherichia coli K12 YdcW protein as a gamma-aminobutyraldehyde dehydrogenase." FEBS Lett 579:4107-4112. Pubmed: 16023116