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Q9RTD9 (PROA_DEIRA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Gamma-glutamyl phosphate reductase

Short name=GPR
EC=1.2.1.41
Alternative name(s):
Glutamate-5-semialdehyde dehydrogenase
Glutamyl-gamma-semialdehyde dehydrogenase
Short name=GSA dehydrogenase
Gene names
Name:proA
Ordered Locus Names:DR_1826
OrganismDeinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422) [Reference proteome] [HAMAP]
Taxonomic identifier243230 [NCBI]
Taxonomic lineageBacteriaDeinococcus-ThermusDeinococciDeinococcalesDeinococcaceaeDeinococcus

Protein attributes

Sequence length432 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

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 By similarity. HAMAP-Rule MF_00412

Catalytic activity

L-glutamate 5-semialdehyde + phosphate + NADP+ = L-glutamyl 5-phosphate + NADPH. HAMAP-Rule MF_00412

Pathway

Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-glutamate: step 2/2. HAMAP-Rule MF_00412

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00412.

Sequence similarities

Belongs to the gamma-glutamyl phosphate reductase family.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Proline biosynthesis
   Cellular componentCytoplasm
   LigandNADP
   Molecular functionOxidoreductase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processL-proline biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionNADP binding

Inferred from electronic annotation. Source: InterPro

glutamate-5-semialdehyde dehydrogenase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 432432Gamma-glutamyl phosphate reductase HAMAP-Rule MF_00412
PRO_0000189720

Sequences

Sequence LengthMass (Da)Tools
Q9RTD9 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 913FF295EAEAD1DB

FASTA43245,233
        10         20         30         40         50         60 
MTQTDSLPGV QATVQDMGER ARRAARVLRS LPTGRKVQAL RALAAELRAR EAGILAANAQ 

        70         80         90        100        110        120 
DVQAAEAAGL PAPLVDRLRL SAGALAAIAR DVEAVAALPD PVGEQTDEKT LPSGIRVSQR 

       130        140        150        160        170        180 
RVPLGVLGVI YESRPNVTVD VAALALMSGN AAILRGGKET VNSNAALEDA IHAALNREGL 

       190        200        210        220        230        240 
PADAVQVIRD PDRARMLELL RLDESVDAII PRGGAGLHRF CVENATVPVI VGGIGVVHIY 

       250        260        270        280        290        300 
LDGSFVQTPQ DVQIAAALIR NAKTQKPSAC NALDTLLIDR AALAALPDVV RPLLESGVEV 

       310        320        330        340        350        360 
RADAEAQAAL AGAGLNVTSA QLGDYGTEFL ALVASLRTVS GLDEALDFIA ERGGHTDVIL 

       370        380        390        400        410        420 
TRDPAQAERF VQDVDSAAVM VNVSPRFNDG GQLGLGAEVA ISTQKLHARG PMGLRELTTS 

       430 
KWVVRGEGQV RD 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE000513 Genomic DNA. Translation: AAF11380.1.
PIRD75348.
RefSeqNP_295549.1. NC_001263.1.

3D structure databases

ProteinModelPortalQ9RTD9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243230.DR_1826.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAF11380; AAF11380; DR_1826.
GeneID1799066.
KEGGdra:DR_1826.
PATRIC21631288. VBIDeiRad64572_2038.

Phylogenomic databases

eggNOGCOG0014.
HOGENOMHOG000246356.
KOK00147.
OMACNAIETL.
OrthoDBEOG6FFSCX.
ProtClustDBPRK00197.

Enzyme and pathway databases

BioCycDRAD243230:GH46-1858-MONOMER.
UniPathwayUPA00098; UER00360.

Family and domain databases

Gene3D3.40.309.10. 1 hit.
3.40.605.10. 2 hits.
HAMAPMF_00412. ProA.
InterProIPR016161. Ald_DH/histidinol_DH.
IPR016163. Ald_DH_C.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH_dom.
IPR000965. G-glutamylP_reductase.
IPR020593. G-glutamylP_reductase_CS.
IPR012134. Glu-5-SA_DH.
[Graphical view]
PANTHERPTHR11063:SF1. PTHR11063:SF1. 1 hit.
PfamPF00171. Aldedh. 1 hit.
[Graphical view]
PIRSFPIRSF000151. GPR. 1 hit.
SUPFAMSSF53720. SSF53720. 1 hit.
TIGRFAMsTIGR00407. proA. 1 hit.
PROSITEPS01223. PROA. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePROA_DEIRA
AccessionPrimary (citable) accession number: Q9RTD9
Entry history
Integrated into UniProtKB/Swiss-Prot: June 20, 2001
Last sequence update: May 1, 2000
Last modified: February 19, 2014
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways