Skip Header

 
Contribute Send feedback

Reviewed, UniProtKB/Swiss-Prot Q1QXB4 (PROA_CHRSD)

Last modified November 25, 2008. Version 25. 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: Csal_1541
OrganismChromohalobacter salexigens (strain DSM 3043 / ATCC BAA-138 / NCIMB 13768) [Complete proteome] [HAMAP]
Taxonomic identifier290398 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaOceanospirillalesHalomonadaceaeChromohalobacter

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_0000252568

Sequences

Sequence LengthMass (Da)Tools
Q1QXB4-1 [UniParc].

Last modified May 16, 2006. Version 1.
Checksum: 0CDA35B24B1C3070

FASTA42845,827
        10         20         30         40         50         60 
MALETSAPEI ADVEAYMRAL GERARDASRM LARATTAQKN RALHAMAEAL DAARETLETA 

        70         80         90        100        110        120 
NRRDLEAGRA NGLDEALLDR LALTPARIDS MIEGLRQVAA LPDPVGEIRD MRYLPSGIQV 

       130        140        150        160        170        180 
GKMRVALGVV GIVYESRPNV TVDAASLCLK SGNATILRGG SEAIQSNRAI ADCIRQGLAA 

       190        200        210        220        230        240 
ADLDAACVQV VATTDRAAVG ALIAMPEYVD VIVPRGGKGL IERISRDARV PVIKHLDGVC 

       250        260        270        280        290        300 
HVYVDRAADD AKAVAIADNA KTQRYSPCNT METLLVHVDA APRVLPELAR LYASKGVELR 

       310        320        330        340        350        360 
ACERARAWLA DAVAATEDDW HAEYLAPILA VRVVDSLEEA IAHINTYGSH HTDAIVTESV 

       370        380        390        400        410        420 
TDARRFLAEV DSSSVMVNAS TRFADGFEYG LGAEIGISTD KLHARGPVGL EGLTSEKYIV 


YGDGHVRS 

« Hide

References

[1]"Complete sequence of Chromohalobacter salexigens DSM 3043."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Saunders E., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Csonka L.N., O'Conner K., Vreeland R.H., Oren A., Vargas C., Nieto J., Arahal D.R., Goodner B., Wheeler C., Hall P., Ewing A., Benson L., McBeath D., Canovas D., Richardson P.
Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000285 Genomic DNA. Translation: ABE58894.1.
RefSeqYP_573593.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID4027639.
GenomeReviewsGene locus Csal_1541 in contig CP000285_GR.
KEGGcsa:Csal_1541.
NMPDRfig|290398.4.peg.2596.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ1QXB4.

Enzyme and pathway databases

BioCycCSAL290398:CSAL_1541-MON.

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_CHRSD
AccessionPrimary (citable) accession number: Q1QXB4
Entry history
Integrated into UniProtKB/Swiss-Prot: October 17, 2006
Last sequence update: May 16, 2006
Last modified: November 25, 2008
This is version 25 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