Identification
Name:Gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase
Synonyms:
  • Gamma-Glu-gamma-aminobutyraldehyde dehydrogenase
Gene Name:puuC
Enzyme Class:Not Available
Biological Properties
General Function:Involved in oxidoreductase activity
Specific Function:Involved in the breakdown of putrescine. Was previously shown to have a weak but measurable ALDH enzyme activity that prefers NADP over NAD as coenzyme
Cellular Location:Not Available
SMPDB Pathways:
KEGG Pathways:
  • Arginine and proline metabolism ec00330
KEGG Reactions:
Thumb+Thumb+ThumbThumb+2 Thumb+Thumb
Thumb+Thumb+ThumbThumb+Thumb+Thumb
Thumb+Thumb+ThumbThumb+Thumb+Thumb
SMPDB Reactions:
Thumb+Thumb+ThumbThumb+2 Thumb+NADPH+Thumb
Thumb+Thumb+Thumbgamma-glutamyl-gamma-aminobutyrate+Thumb+2 Thumb
gamma-Glutamyl-gamma-butyraldehyde + NADP + Water → gamma-glutamyl-gamma-aminobutyrate + NADPH + 2 Hydrogen ion
ReactionCard
EcoCyc Reactions:
NAD(P)++Thumb+ThumbThumb+NAD(P)H+Thumb
3-hydroxypropionaldehyde+Thumb+ThumbThumb+Thumb+Thumb
3-hydroxypropionaldehyde + NAD + WaterHydrogen ion + 3-Hydroxypropanoate + NADH
ReactionCard
Complex Reactions:
Thumb+Thumb+ThumbThumb+2 Thumb+Thumb
Thumb+NAD(P)(+)+Thumba carboxylate+NAD(P)H
Aldehyde + NAD(P)(+) + Water → a carboxylate + NAD(P)H
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB211683-HydroxypropanoateMetaboCard
ECMDB121614-(Glutamylamino) butanoateMetaboCard
ECMDB241924-(γ-glutamylamino)butanalMetaboCard
ECMDB00990AcetaldehydeMetaboCard
ECMDB00042Acetic acidMetaboCard
ECMDB21646AldehydeMetaboCard
ECMDB21337gamma-Glutamyl-gamma-butyraldehydeMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB00902NADMetaboCard
ECMDB01487NADHMetaboCard
ECMDB00217NADPMetaboCard
ECMDB04111NADPHMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Function
catalytic activity
oxidoreductase activity
Process
metabolic process
oxidation reduction
Gene Properties
Blattner:b1300
Gene OrientationClockwise
Centisome Percentage:29.33
Left Sequence End1360767
Right Sequence End1362254
Gene Sequence:
>1488 bp
ATGAATTTTCATCATCTGGCTTACTGGCAGGATAAAGCGTTAAGTCTCGCCATTGAAAAC
CGCTTATTTATTAACGGTGAATATACTGCTGCGGCGGAAAATGAAACCTTTGAAACCGTT
GATCCGGTCACCCAGGCACCGCTGGCGAAAATTGCCCGCGGCAAGAGCGTCGATATCGAC
CGTGCGATGAGCGCAGCACGCGGCGTATTTGAACGCGGCGACTGGTCACTCTCTTCTCCG
GCTAAACGTAAAGCGGTACTGAATAAACTCGCCGATTTAATGGAAGCCCACGCCGAAGAG
CTGGCACTGCTGGAAACTCTCGACACCGGCAAACCGATTCGTCACAGTCTGCGTGATGAT
ATTCCCGGCGCGGCGCGCGCCATTCGCTGGTACGCCGAAGCGATCGACAAAGTGTATGGC
GAAGTGGCGACCACCAGTAGCCATGAGCTGGCGATGATCGTGCGTGAACCGGTCGGCGTG
ATTGCCGCCATCGTGCCGTGGAACTTCCCGCTGTTGCTGACTTGCTGGAAACTCGGCCCG
GCGCTGGCGGCGGGAAACAGCGTGATTCTAAAACCGTCTGAAAAATCACCGCTCAGTGCG
ATTCGTCTCGCGGGGCTGGCGAAAGAAGCAGGCTTGCCGGATGGTGTGTTGAACGTGGTG
ACGGGTTTTGGTCATGAAGCCGGGCAGGCGCTGTCGCGTCATAACGATATCGACGCCATT
GCCTTTACCGGTTCAACCCGTACCGGGAAACAGCTGCTGAAAGATGCGGGCGACAGCAAC
ATGAAACGCGTCTGGCTGGAAGCGGGCGGCAAAAGCGCCAACATCGTTTTCGCTGACTGC
CCGGATTTGCAACAGGCGGCAAGCGCCACCGCAGCAGGCATTTTCTACAACCAGGGACAG
GTGTGCATCGCCGGAACGCGCCTGTTGCTGGAAGAGAGCATCGCCGATGAATTCTTAGCC
CTGTTAAAACAGCAGGCGCAAAACTGGCAGCCGGGCCATCCACTTGATCCCGCAACCACC
ATGGGCACCTTAATCGACTGCGCCCACGCCGACTCGGTCCATAGCTTTATTCGGGAAGGC
GAAAGCAAAGGGCAACTGTTGTTGGATGGCCGTAACGCCGGGCTGGCTGCCGCCATCGGC
CCGACCATCTTTGTGGATGTGGACCCGAATGCGTCCTTAAGTCGCGAAGAGATTTTCGGT
CCGGTGCTGGTGGTCACGCGTTTCACATCAGAAGAACAGGCGCTACAGCTTGCCAACGAC
AGCCAGTACGGCCTTGGCGCGGCGGTATGGACGCGCGACCTCTCCCGCGCGCACCGCATG
AGCCGACGCCTGAAAGCCGGTTCCGTCTTCGTCAATAACTACAACGACGGCGATATGACC
GTGCCGTTTGGCGGCTATAAGCAGAGCGGCAACGGTCGCGACAAATCCCTGCATGCCCTT
GAAAAATTCACTGAACTGAAAACCATCTGGATAAGCCTGGAGGCCTGA
Protein Properties
Pfam Domain Function:
Protein Residues:495
Protein Molecular Weight:53418
Protein Theoretical pI:6
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase
MNFHHLAYWQDKALSLAIENRLFINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDID
RAMSAARGVFERGDWSLSSPAKRKAVLNKLADLMEAHAEELALLETLDTGKPIRHSLRDD
IPGAARAIRWYAEAIDKVYGEVATTSSHELAMIVREPVGVIAAIVPWNFPLLLTCWKLGP
ALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAI
AFTGSTRTGKQLLKDAGDSNMKRVWLEAGGKSANIVFADCPDLQQAASATAAGIFYNQGQ
VCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATTMGTLIDCAHADSVHSFIREG
ESKGQLLLDGRNAGLAAAIGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQLAND
SQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHAL
EKFTELKTIWISLEA
References
External Links:
ResourceLink
Uniprot ID:P23883
Uniprot Name:PUUC_ECOLI
GenBank Gene ID:AB200319
Genebank Protein ID:58197517
Ecogene ID:EG10036
Ecocyc:EG10036
ColiBase:b1300
Kegg Gene:b1300
EchoBASE ID:EB0035
CCDB:PUUC_ECOLI
BacMap:16129261
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
  • 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
  • Heim, R., Strehler, E. E. (1991). "Cloning an Escherichia coli gene encoding a protein remarkably similar to mammalian aldehyde dehydrogenases." Gene 99:15-23. Pubmed: 1840553
  • Kurihara, S., Oda, S., Kato, K., Kim, H. G., Koyanagi, T., Kumagai, H., Suzuki, H. (2005). "A novel putrescine utilization pathway involves gamma-glutamylated intermediates of Escherichia coli K-12." J Biol Chem 280:4602-4608. Pubmed: 15590624