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Reviewed, UniProtKB/Swiss-Prot A5FYS4 (PROA_ACICJ)

Last modified November 25, 2008. Version 15. 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: Acry_1548
OrganismAcidiphilium cryptum (strain JF-5) [Complete proteome] [HAMAP]
Taxonomic identifier349163 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesAcetobacteraceaeAcidiphilium

Protein attributes

Sequence length420 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 By similarity.

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 – 420420Gamma-glutamyl phosphate reductase
PRO_0000340869

Sequences

Sequence LengthMass (Da)Tools
A5FYS4-1 [UniParc].

Last modified June 12, 2007. Version 1.
Checksum: F8347D4E4DC3D2A0

FASTA42043,953
        10         20         30         40         50         60 
MDTATPSAEA ILRTAAGRAR AAMRSLAAMP AARRDGALRA AAAELRIHAV NILAANARDL 

        70         80         90        100        110        120 
DSFEGPPAMR DRLLLNEARI EAIAAGIDAI ADLPDPLAGS LAEWTRPNGL VIRRVPQPLG 

       130        140        150        160        170        180 
VIGMIYESRP NVGADAAAIC IKSGNAVILR GGSESYHSNT AIYLAMTKGL RQAGFPDGTV 

       190        200        210        220        230        240 
QIAPNIDRAF VAAMLGASGQ IDLIIPRGGK SLVERVQREA RVPVLAHAEG LNHTYIHAEA 

       250        260        270        280        290        300 
DAEMARTVLA NAKMRRTGIC GATETLLIDA AIAPALLPRL IEDLAALGCG FRADDRARAI 

       310        320        330        340        350        360 
VPSLPAAGPA DFDTEWLDAM LSVSVVDDLD AALDHIARHG SSHTEAIVTE NADAAARFLA 

       370        380        390        400        410        420 
GTDSAVAMWN ASTQFCDGGE FGFGAEIGIA TGRIHARGPI GPAQLTTFRY HVVGTGQVRP 

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References

[1]"Complete sequence of chromosome of Acidiphilium cryptum JF-5."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Kim E., Magnuson T., Richardson P.
Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000697 Genomic DNA. Translation: ABQ30756.1.
RefSeqYP_001234675.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID5161093.
GenomeReviewsGene locus Acry_1548 in contig CP000697_GR.
KEGGacr:Acry_1548.

Organism-specific databases

CMRSearch...

Family and domain databases

HAMAPMF_00412.
[Tree]
InterProIPR016162. Ald_DHase_N.
IPR000965. Gglut_pp_reduct.
IPR012134. Glu-5-SA_DHase.
[Graphical view]
Gene3DG3DSA: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_ACICJ
AccessionPrimary (citable) accession number: A5FYS4
Entry history
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: June 12, 2007
Last modified: November 25, 2008
This is version 15 of the entry and version 1 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