Q3MH53 · PROA_TRIV2

Function

function

Catalyzes the NADPH-dependent reduction of L-glutamate 5-phosphate into L-glutamate 5-semialdehyde and phosphate. The product spontaneously undergoes cyclization to form 1-pyrroline-5-carboxylate.

Catalytic activity

Pathway

Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-glutamate: step 2/2.

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcytoplasm
Molecular Functionglutamate-5-semialdehyde dehydrogenase activity
Molecular FunctionNADP binding
Biological ProcessL-proline biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Gamma-glutamyl phosphate reductase
  • EC number
  • Short names
    GPR
  • Alternative names
    • Glutamate-5-semialdehyde dehydrogenase
    • Glutamyl-gamma-semialdehyde dehydrogenase
      (GSA dehydrogenase
      )

Gene names

    • Name
      proA
    • Ordered locus names
      Ava_0057

Organism names

Accessions

  • Primary accession
    Q3MH53

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00002299921-434Gamma-glutamyl phosphate reductase

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Sequence similarities

Belongs to the gamma-glutamyl phosphate reductase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    434
  • Mass (Da)
    46,945
  • Last updated
    2006-04-04 v2
  • Checksum
    3393756F7C3684DA
MTTLQVASSLNDIAQQTRQAASLLAMLSTEAKNQAIAAVAQALESAKEEILQANIADCEAATAEGIAKPLYKRLQLDEHKLRDAIAGVRDVGKLADPIGQVQIQRELDTGLVLKRITCPLGVLGIIFEARPEAAIQIISLAIKSGNGVILKCGKEAVRSCEAIVKAVKQGLSTTDVNPDVVQLLTTREETLELLRLDKYVDLIIPRGSNSFVRFVQENTRIPVLGHADGICHVYIDKSADIEKAIAVSVDAKVQYPAACNAIETLLVHHSIAAEFLPKVAQALAERQVELKGDERTLQILPEIAAATAIDWETEYSDFILSIKIVDSLTEAIAHINQYGSRHTDAIITEDVAAVETFFGLVNSAGVFHNCSTRFADGFRYGFGAEVGISTQQMPPRGPVGLEGLVTYKYQMTGTGHIVATYTGENAKPFTHQDF

Sequence caution

The sequence ABA19683.1 differs from that shown. Reason: Erroneous initiation

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP000117
EMBL· GenBank· DDBJ
ABA19683.1
EMBL· GenBank· DDBJ
Genomic DNA Different initiation

Genome annotation databases

Similar Proteins

Disclaimer

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