Gamma-glutamyl phosphate reductase (P07004)

Identification
Name:Gamma-glutamyl phosphate reductase
Synonyms:
  • GPR
  • Glutamate-5-semialdehyde dehydrogenase
  • Glutamyl-gamma-semialdehyde dehydrogenase
  • GSA dehydrogenase
Gene Name:proA
Enzyme Class:
Biological Properties
General Function:Involved in oxidoreductase activity
Specific Function:Catalyzes the NADPH dependent reduction of L-gamma- glutamyl 5-phosphate into L-glutamate 5-semialdehyde and phosphate. The product spontaneously undergoes cyclization to form 1-pyrroline-5-carboxylate
Cellular Location:Cytoplasm
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0L-Glutamyl 5-phosphate+1.0Thumb+1.0Thumb+1.0Thumb
1.0L-Glutamic-gamma-semialdehyde + 1.0Phosphate + 1.0NADP ↔ 1.0L-Glutamyl 5-phosphate + 1.0NADPH + 1.0Hydrogen ion + 1.0L-Glutamic acid 5-phosphate
ReactionCard
SMPDB Reactions:
1.0Thumb+1.0Thumb+1.0NADPH+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb
1.0L-Glutamic acid 5-phosphate + 1.0Hydrogen ion + 1.0NADPH + 1.0NADPH → 1.0L-Glutamic-gamma-semialdehyde + 1.0NADP + 1.0Phosphate
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb
1.0L-Glutamic acid 5-phosphate + 1.0Hydrogen ion + 1.0NADPH → 1.0L-Glutamic-gamma-semialdehyde + 1.0NADP + 1.0Phosphate
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0L-Glutamic-gamma-semialdehyde + 1.0Inorganic phosphate + 1.0NADP → 1.0L-Glutamic acid 5-phosphate + 1.0NADPH
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB21225Hydrogen ionMetaboCard
ECMDB21380Inorganic phosphateMetaboCard
ECMDB01228L-Glutamic acid 5-phosphateMetaboCard
ECMDB01305L-Glutamic-gamma-semialdehydeMetaboCard
ECMDB00217NADPMetaboCard
ECMDB04111NADPHMetaboCard
ECMDB01429PhosphateMetaboCard
ECMDB00805Pyrrolidonecarboxylic acidMetaboCard
GO Classification:
Function
binding
catalytic activity
glutamate-5-semialdehyde dehydrogenase activity
NADP or NADPH 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 metabolic process
cellular metabolic process
glutamine family amino acid metabolic process
metabolic process
oxidation reduction
proline biosynthetic process
proline metabolic process
Gene Properties
Blattner:b0243
Gene OrientationClockwise
Centisome Percentage:5.62
Left Sequence End260727
Right Sequence End261980
Gene Sequence:
>1254 bp
ATGCTGGAACAAATGGGCATTGCCGCGAAGCAAGCCTCGTATAAATTAGCGCAACTCTCC
AGCCGCGAAAAAAATCGCGTGCTGGAAAAAATCGCCGATGAACTGGAAGCACAAAGCGAA
ATCATCCTCAACGCTAACGCCCAGGATGTTGCTGACGCGCGAGCCAATGGCCTTAGCGAA
GCGATGCTTGACCGTCTGGCACTGACGCCCGCACGGCTGAAAGGCATTGCCGACGATGTA
CGTCAGGTGTGCAACCTCGCCGATCCGGTGGGGCAGGTAATCGATGGCGGCGTACTGGAC
AGCGGCCTGCGTCTTGAGCGTCGTCGCGTACCGCTGGGGGTTATTGGCGTGATTTATGAA
GCGCGCCCGAACGTGACGGTTGATGTCGCTTCGCTGTGCCTGAAAACCGGTAATGCGGTG
ATCCTGCGCGGTGGCAAAGAAACGTGTCGCACTAACGCTGCAACGGTGGCGGTGATTCAG
GACGCCCTGAAATCCTGCGGCTTACCGGCGGGTGCCGTGCAGGCGATTGATAATCCTGAC
CGTGCGCTGGTCAGTGAAATGCTGCGTATGGATAAATACATCGACATGCTGATCCCGCGT
GGTGGCGCTGGTTTGCATAAACTGTGCCGTGAACAGTCGACAATCCCGGTGATCACAGGT
GGTATAGGCGTATGCCATATTTACGTTGATGAAAGTGTAGAGATCGCTGAAGCATTAAAA
GTGATCGTCAACGCGAAAACTCAGCGTCCGAGCACATGTAATACGGTTGAAACGTTGCTG
GTGAATAAAAACATCGCCGATAGCTTCCTGCCCGCATTAAGCAAACAAATGGCGGAAAGC
GGCGTGACATTACACGCAGATGCAGCTGCACTGGCGCAGTTGCAGGCAGGCCCTGCGAAG
GTGGTTGCTGTTAAAGCCGAAGAGTATGACGATGAGTTTCTGTCATTAGATTTGAACGTC
AAAATCGTCAGCGATCTTGACGATGCCATCGCCCATATTCGTGAACACGGCACACAACAC
TCCGATGCGATCCTGACCCGCGATATGCGCAACGCCCAGCGTTTTGTTAACGAAGTGGAT
TCGTCCGCTGTTTACGTTAACGCCTCTACGCGTTTTACCGACGGCGGCCAGTTTGGTCTG
GGTGCGGAAGTGGCGGTAAGCACACAAAAACTCCACGCGCGTGGCCCAATGGGGCTGGAA
GCACTGACCACTTACAAGTGGATCGGCATTGGTGATTACACCATTCGTGCGTAA
Protein Properties
Pfam Domain Function:
Protein Residues:417
Protein Molecular Weight:44630
Protein Theoretical pI:5
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Gamma-glutamyl phosphate reductase
MLEQMGIAAKQASYKLAQLSSREKNRVLEKIADELEAQSEIILNANAQDVADARANGLSE
AMLDRLALTPARLKGIADDVRQVCNLADPVGQVIDGGVLDSGLRLERRRVPLGVIGVIYE
ARPNVTVDVASLCLKTGNAVILRGGKETCRTNAATVAVIQDALKSCGLPAGAVQAIDNPD
RALVSEMLRMDKYIDMLIPRGGAGLHKLCREQSTIPVITGGIGVCHIYVDESVEIAEALK
VIVNAKTQRPSTCNTVETLLVNKNIADSFLPALSKQMAESGVTLHADAAALAQLQAGPAK
VVAVKAEEYDDEFLSLDLNVKIVSDLDDAIAHIREHGTQHSDAILTRDMRNAQRFVNEVD
SSAVYVNASTRFTDGGQFGLGAEVAVSTQKLHARGPMGLEALTTYKWIGIGDYTIRA
References
External Links:
ResourceLink
Uniprot ID:P07004
Uniprot Name:PROA_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674395
Ecogene ID:EG10767
Ecocyc:EG10767
ColiBase:b0243
Kegg Gene:b0243
EchoBASE ID:EB0760
CCDB:PROA_ECOLI
BacMap:16128229
General Reference:
  • 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
  • Deutch, A. H., Rushlow, K. E., Smith, C. J. (1984). "Analysis of the Escherichia coli proBA locus by DNA and protein sequencing." Nucleic Acids Res 12:6337-6355. Pubmed: 6089111
  • 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
  • Lim, D. (1992). "Structure and biosynthesis of unbranched multicopy single-stranded DNA by reverse transcriptase in a clinical Escherichia coli isolate." Mol Microbiol 6:3531-3542. Pubmed: 1282191