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A6V0A3 (PROA_PSEA7) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 37. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:PSPA7_1102
OrganismPseudomonas aeruginosa (strain PA7) [Complete proteome] [HAMAP]
Taxonomic identifier381754 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas

Protein attributes

Sequence length421 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. 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 HAMAP 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
Gene Ontology (GO)
   Biological processproline biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   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: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 421421Gamma-glutamyl phosphate reductase HAMAP MF_00412
PRO_1000049981

Sequences

Sequence LengthMass (Da)Tools
A6V0A3 [UniParc].

Last modified August 21, 2007. Version 1.
Checksum: 41D25361F5AAC0E1

FASTA42144,984
        10         20         30         40         50         60 
MTESVLDYMS RLGRDARAAS RLLARAATAQ KNRALLAAAD ALDAARAELS HANEQDLAAG 

        70         80         90        100        110        120 
RANGLEPAML DRLALTPARI DDMIEGLRQV ATLPDPIGEI RDMRYVPSGI QIGKMRVPLG 

       130        140        150        160        170        180 
VVGIIYESRP NVTIDAASLC LKSGNATILR GGSEAIHSNQ AIARCIQQGL AEAGLPAAAV 

       190        200        210        220        230        240 
QVVETTDRAA VGALISMPEY VDVIVPRGGK GLIERISREA RVPVIKHLDG ICHVYIDVAA 

       250        260        270        280        290        300 
DLDKAIRVAD NAKTQRYAPC NTMETLLVHA GIAERVLPPL AAIYREKGVE LRGDAATRAL 

       310        320        330        340        350        360 
LGADVLEATE EDWRTEYNAP ILSIRIVDGL GAAIEHINTY GSQHTDAIIT ENFSDARRFL 

       370        380        390        400        410        420 
AEVDSASVMV NASTRFADGF EYGLGAEIGI STDKLHARGP VGLEGLTSEK YVVFGDGHVR 


T

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References

[1]Dodson R.J., Harkins D., Paulsen I.T.
Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PA7.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000744 Genomic DNA. Translation: ABR81075.1.
RefSeqYP_001346488.1. NC_009656.1.

3D structure databases

ProteinModelPortalA6V0A3.
ModBaseSearch...

Protein-protein interaction databases

STRINGA6V0A3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5357649.
GenomeReviewsGene locus PSPA7_1102 in contig CP000744_GR.
KEGGpap:PSPA7_1102.
PATRIC19824020. VBIPseAer80442_1048.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0014.
HOGENOMHBG318080.
OMAYGICGAM.
PhylomeDBA6V0A3.
ProtClustDBPRK00197.

Family and domain databases

HAMAPMF_00412. ProA.
[Tree]
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]
Gene3DG3DSA:3.40.309.10. Aldehyde_dehydrogenase_C. 1 hit.
G3DSA:3.40.605.10. Aldehyde_dehydrogenase_N. 2 hits.
KOK00147.
PANTHERPTHR11063:SF1. GSA_DH. 1 hit.
PfamPF00171. Aldedh. 1 hit.
[Graphical view]
PIRSFPIRSF000151. GPR. 1 hit.
SUPFAMSSF53720. Aldehyde_DH/Histidinol_DH. 1 hit.
TIGRFAMsTIGR00407. ProA. 1 hit.
PROSITEPS01223. PROA. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePROA_PSEA7
AccessionPrimary (citable) accession number: A6V0A3
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: August 21, 2007
Last modified: December 14, 2011
This is version 37 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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