Identification
Name:N-succinylglutamate 5-semialdehyde dehydrogenase
Synonyms:
  • Succinylglutamic semialdehyde dehydrogenase
  • SGSD
Gene Name:astD
Enzyme Class:
Biological Properties
General Function:Involved in oxidoreductase activity
Specific Function:Catalyzes the NAD-dependent reduction of succinylglutamate semialdehyde into succinylglutamate. Also shows activity with decanal or succinic semialdehyde as the electron donor and NAD as the electron acceptor. No activity is detected with NADP as the electron acceptor. Therefore, is an aldehyde dehydrogenase with broad substrate specificity
Cellular Location:Not Available
SMPDB Pathways:
KEGG Pathways:
  • Arginine and proline metabolism ec00330
KEGG Reactions:
1.0Thumb+1.0Thumb+1.0Thumb2.0Thumb+1.0Thumb+1.0Thumb
1.0Thumb+1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb+1.0Thumb
SMPDB Reactions:
1.0Thumb+1.0Thumb+1.0Thumb2.0Thumb+1.0Thumb+1.0 N2-succinylglutamate+1.0Thumb
EcoCyc Reactions:
1.0Thumb+1.0Thumb+1.0Thumb1.0N2-succinylglutamate+1.0Thumb+1.0Thumb
1.0N2-Succinyl-L-glutamic acid 5-semialdehyde + 1.0NAD + 1.0Water → 1.0N2-succinylglutamate + 1.0NADH + 1.0Hydrogen ion
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb
Metabolites:
ECMDB IDNameView
ECMDB24191 N2-succinylglutamateMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB01437N-Succinyl-L-glutamateMetaboCard
ECMDB01180N2-Succinyl-L-glutamic acid 5-semialdehydeMetaboCard
ECMDB00902NADMetaboCard
ECMDB01487NADHMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Function
catalytic activity
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
succinylglutamate-semialdehyde dehydrogenase activity
Process
arginine catabolic process
arginine metabolic process
cellular amino acid and derivative metabolic process
cellular amino acid metabolic process
cellular metabolic process
glutamine family amino acid metabolic process
metabolic process
oxidation reduction
Gene Properties
Blattner:b1746
Gene OrientationCounterclockwise
Centisome Percentage:39.36
Left Sequence End1826280
Right Sequence End1827758
Gene Sequence:
>1479 bp
ATGACTTTATGGATTAACGGTGACTGGATAACGGGCCAGGGCGCATCGCGTGTGAAGCGT
AATCCGGTATCGGGCGAGGTGTTATGGCAAGGCAATGATGCCGATGCCGCTCAGGTCGAG
CAGGCTTGTCGGGCAGCCCGTGCGGCGTTTCCGCGCTGGGCGCGGCTTTCATTTGCTGAA
CGTCATGCCGTTGTCGAACGCTTTGCCGCACTGCTGGAAAGCAATAAAGCCGAATTAACC
GCGATTATTGCCAGAGAAACGGGTAAGCCGCGCTGGGAAGCGGCAACCGAAGTGACGGCG
ATGATCAATAAAATCGCGATATCAATTAAGGCGTATCACGTTCGTACCGGCGAGCAGCGT
AGTGAAATGCCGGACGGCGCGGCGAGCCTGCGACATCGCCCGCACGGCGTGCTGGCGGTG
TTTGGGCCGTATAATTTCCCTGGTCATTTGCCGAACGGACATATCGTTCCGGCATTGCTG
GCAGGTAACACCATTATCTTTAAACCCAGCGAACTGACACCGTGGAGTGGCGAAGCGGTA
ATGCGTTTATGGCAGCAGGCTGGCTTGCCGCCAGGCGTGCTGAACCTGGTGCAGGGCGGG
CGTGAAACGGGTCAGGCGCTGAGTGCGCTGGAGGATCTCGACGGTTTGCTGTTTACCGGT
AGCGCCAATACAGGCTACCAGTTGCATCGCCAGCTCTCCGGTCAGCCGGAGAAAATTCTC
GCCCTTGAGATGGGCGGTAATAATCCGCTAATTATCGATGAGGTGGCGGATATCGACGCG
GCTGTCCATCTGACCATTCAGTCGGCGTTTGTCACAGCCGGTCAACGCTGCACCTGCGCC
CGCCGTTTATTGCTGAAAAGCGGGGCGCAGGGCGATGCGTTTCTTGCTCGTCTGGTTGCC
GTCAGCCAGCGATTAACGCCGGGCAACTGGGATGACGAACCGCAGCCGTTTATTGGCGGG
CTGATTTCTGAACAGGCCGCACAGCAGGTGGTTACTGCATGGCAGCAACTGGAAGCGATG
GGCGGACGACCCCTGCTTGCGCCGCGCTTATTACAAGCAGGGACATCGTTGCTGACGCCG
GGGATCATTGAAATGACAGGCGTTGCTGGCGTACCAGATGAAGAGGTGTTCGGACCGTTA
TTGCGCGTCTGGCGTTATGATACTTTCGATGAAGCGATTCGAATGGCGAATAACACTCGC
TTCGGACTCTCTTGCGGTCTGGTTTCCCCCGAGCGGGAAAAGTTCGATCAACTGTTGCTG
GAGGCGCGGGCGGGGATTGTTAACTGGAACAAACCGCTTACCGGTGCTGCCAGTACCGCG
CCATTCGGCGGCATTGGTGCTTCCGGTAACCATCGCCCCAGCGCCTGGTATGCCGCAGAT
TACTGCGCATGGCCGATGGCGAGCCTGGAGTCGGACTCGTTAACATTGCCCGCCACGCTT
AACCCCGGGCTGGATTTTTCCGATGAGGTGGTGCGATGA
Protein Properties
Pfam Domain Function:
Protein Residues:492
Protein Molecular Weight:53026
Protein Theoretical pI:6
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>N-succinylglutamate 5-semialdehyde dehydrogenase
MTLWINGDWITGQGASRVKRNPVSGEVLWQGNDADAAQVEQACRAARAAFPRWARLSFAE
RHAVVERFAALLESNKAELTAIIARETGKPRWEAATEVTAMINKIAISIKAYHVRTGEQR
SEMPDGAASLRHRPHGVLAVFGPYNFPGHLPNGHIVPALLAGNTIIFKPSELTPWSGEAV
MRLWQQAGLPPGVLNLVQGGRETGQALSALEDLDGLLFTGSANTGYQLHRQLSGQPEKIL
ALEMGGNNPLIIDEVADIDAAVHLTIQSAFVTAGQRCTCARRLLLKSGAQGDAFLARLVA
VSQRLTPGNWDDEPQPFIGGLISEQAAQQVVTAWQQLEAMGGRPLLAPRLLQAGTSLLTP
GIIEMTGVAGVPDEEVFGPLLRVWRYDTFDEAIRMANNTRFGLSCGLVSPEREKFDQLLL
EARAGIVNWNKPLTGAASTAPFGGIGASGNHRPSAWYAADYCAWPMASLESDSLTLPATL
NPGLDFSDEVVR
References
External Links:
ResourceLink
Uniprot ID:P76217
Uniprot Name:ASTD_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85675101
Ecogene ID:EG13997
Ecocyc:EG13997
ColiBase:b1746
Kegg Gene:b1746
EchoBASE ID:EB3753
CCDB:ASTD_ECOLI
BacMap:16129700
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
  • Kiupakis, A. K., Reitzer, L. (2002). "ArgR-independent induction and ArgR-dependent superinduction of the astCADBE operon in Escherichia coli." J Bacteriol 184:2940-2950. Pubmed: 12003934
  • Kuznetsova, E., Proudfoot, M., Sanders, S. A., Reinking, J., Savchenko, A., Arrowsmith, C. H., Edwards, A. M., Yakunin, A. F. (2005). "Enzyme genomics: Application of general enzymatic screens to discover new enzymes." FEMS Microbiol Rev 29:263-279. Pubmed: 15808744
  • Schneider, B. L., Kiupakis, A. K., Reitzer, L. J. (1998). "Arginine catabolism and the arginine succinyltransferase pathway in Escherichia coli." J Bacteriol 180:4278-4286. Pubmed: 9696779