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Reviewed, UniProtKB/Swiss-Prot A0KNQ8 (PROA_AERHH)

Last modified June 16, 2009. Version 21. 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: AHA_3420
OrganismAeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / NCIB 9240) [Complete proteome] [HAMAP]
Taxonomic identifier380703 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAeromonadalesAeromonadaceaeAeromonas

Protein attributes

Sequence length417 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. HAMAP MF_00412

Catalytic activity

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

Pathway

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

Subcellular location

Cytoplasm By 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: UniProtKB-SubCell

   Molecular functionNADP or NADPH 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 – 417417Gamma-glutamyl phosphate reductase HAMAP MF_00412
PRO_1000049932

Sequences

Sequence LengthMass (Da)Tools
A0KNQ8-1 [UniParc].

Last modified December 12, 2006. Version 1.
Checksum: 3D9241D61B0E51CF

FASTA41744,328
        10         20         30         40         50         60 
MSLEKMGQAA REAAYQLATV STAQKNRALA AIADELEARS HQILAANEKD IAAGRAAGLS 

        70         80         90        100        110        120 
DAMLDRLLLN PARLAGIVAD VRKVISLDDP VGAEIDSRVL ENGLRLSRRR VPIGVIGVIY 

       130        140        150        160        170        180 
EARPNVTIDI ASLCLKTGNA SILRGGRETF HSNLELVRVI QSALAASGLP RDAVQYIDNP 

       190        200        210        220        230        240 
DRALVGELLR LDRYVDMIIP RGGAGLHKMC KENSSIPVII GGFGISHIFV DESADLARSL 

       250        260        270        280        290        300 
AVIDNAKVQR PSACNALDSL LVHEKVAATL LPQLVGLMNE RKVALVATPE AMPLLAGADS 

       310        320        330        340        350        360 
LRAAGPEDFD TEWLSLTLGV KLVADVNEAL AHMREHNAGH SDAILTNDLA NAERFVNGAG 

       370        380        390        400        410 
SAAVYVNAST RFTDGGQFGL GAEVAVSTQM LHARGPMGLT ELTSYKWVGL ADYLSRA 

« Hide

References

[1]"Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all trades."
Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J., Haft D.H., Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M., Jin S., Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.
J. Bacteriol. 188:8272-8282(2006) [PubMed: 16980456] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000462 Genomic DNA. Translation: ABK38804.1.
RefSeqYP_857909.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID4487146.
GenomeReviewsGene locus AHA_3420 in contig CP000462_GR.
KEGGaha:AHA_3420.
TIGRAHA_3420.

Phylogenomic databases

OMAA0KNQ8. QYPAACN.

Family and domain databases

HAMAPMF_00412.
[Tree]
InterProIPR016163. Ald_DH_C.
IPR000965. Gglut_pp_reduct.
IPR012134. Glu-5-SA_DH.
[Graphical view]
Gene3DG3DSA:3.40.309.10. Aldehyde_dehydrogenase_C. 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_AERHH
AccessionPrimary (citable) accession number: A0KNQ8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: December 12, 2006
Last modified: June 16, 2009
This is version 21 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