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Reviewed, UniProtKB/Swiss-Prot Q8UBS1 (PROA_AGRT5)

Last modified November 25, 2008. Version 53. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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: Atu2779
ORF Names: AGR_C_5042
OrganismAgrobacterium tumefaciens (strain C58 / ATCC 33970) [Complete proteome] [HAMAP]
Taxonomic identifier176299 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeRhizobium/Agrobacterium groupAgrobacterium

Protein attributes

Sequence length428 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

Catalytic activity

L-glutamate 5-semialdehyde + phosphate + NADP(+) = L-glutamyl 5-phosphate + NADPH.

Pathway

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

Subcellular location

CytoplasmBy similarity.

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

Gene Ontology (GO)

   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

proline biosynthetic process

Inferred from electronic annotation. Source: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: HAMAP

   Molecular functionNADP binding

Inferred from electronic annotation. Source: InterPro

glutamate-5-semialdehyde dehydrogenase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 428428Gamma-glutamyl phosphate reductase
PRO_0000189682

Sequences

Sequence LengthMass (Da)Tools
Q8UBS1-1 [UniParc].

Last modified September 13, 2004. Version 2.
Checksum: 33266C27681C1F9B

FASTA42844,630
        10         20         30         40         50         60 
MPEQAVKQSH DIDALMMTIG AQAKAASRPL SIAGTDQKNR ALLAMASAIE ASKEAILAAN 

        70         80         90        100        110        120 
RKDLAAAESA GLAASFVDRL TLNDARIAGI AEGIRSVAAL ADPVGEVIAA WDRPNGLKIE 

       130        140        150        160        170        180 
RVRTPLGVIG VIYESRPNVT ADAGALCLKA GNAVILRGGS DSQHSSRAIH ACLVQGLRIA 

       190        200        210        220        230        240 
GLPENAIQLV PVTDRAAVGA LLSGLKGTVD VIVPRGGKSL VARVQSEARV PVFAHLEGIC 

       250        260        270        280        290        300 
HIYVDKSADL DMAKAIVVNA KMRRTGICGA AETLLVDASA VSSHLEPVVK ALLDAGCEVR 

       310        320        330        340        350        360 
GSQPVRNVVE GLEAATEEDW RTEYLDAIIS VAVVDGISGA IEHIGTYSSN HTEAVIAEDP 

       370        380        390        400        410        420 
DVVARFFNEL DSAILLHNAS TQFADGGEFG MGAEIGIATG KMHARGPVGV EQLTSFKYRV 


HGTGQTRT 

« Hide

Cross-references

Sequence databases

AE007869 Genomic DNA. Translation: AAK88494.2. Different initiation.
PIRAB2918.
E97692.
RefSeqNP_355709.2.

3D structure databases

HSSPHSSP built from PDB template 1O20 based on UniProtKB Q9WYC9.
ModBaseSearch...

Genome annotation databases

GeneID1134817.
GenomeReviewsGene locus Atu2779 in contig AE007869_GR.
KEGGatc:AGR_C_5042.
atu:Atu2779.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ8UBS1.

Family and domain databases

HAMAPMF_00412.
[Tree]
InterProIPR016163. Ald_DHase_C.
IPR016162. Ald_DHase_N.
IPR000965. Gglut_pp_reduct.
IPR012134. Glu-5-SA_DHase.
[Graphical view]
Gene3DG3DSA:3.40.309.10. Aldehyde_dehydrogenase_C. 1 hit.
G3DSA:3.40.605.10. Aldehyde_dehydrogenase_N. 1 hit.
PANTHERPTHR11063:SF1. GSA_DH. 1 hit.
PIRSFPIRSF000151. GPR. 1 hit.
TIGRFAMsTIGR00407. proA. 1 hit.
PROSITEPS01223. PROA. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePROA_AGRT5
AccessionPrimary (citable) accession number: Q8UBS1
Entry history
Integrated into UniProtKB/Swiss-Prot: August 2, 2002
Last sequence update: September 13, 2004
Last modified: November 25, 2008
This is version 53 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents