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B9KW06 (PROA_RHOSK) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 26. 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:RSKD131_3150
OrganismRhodobacter sphaeroides (strain KD131 / KCTC 12085) [Complete proteome] [HAMAP]
Taxonomic identifier557760 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhodobacterales › Rhodobacteraceae › Rhodobacter

Protein attributes

Sequence length420 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 By similarity. 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 – 420420Gamma-glutamyl phosphate reductase HAMAP MF_00412
PRO_1000193642

Sequences

Sequence LengthMass (Da)Tools
B9KW06 [UniParc].

Last modified March 24, 2009. Version 1.
Checksum: 07C13935A12FD410

FASTA42044,643
        10         20         30         40         50         60 
MDGTDVTMLM REIGIRARAA AAELAFAEPS RKEEALNAAA EAMLARSDEI LEANGRDLAF 

        70         80         90        100        110        120 
GAEKGLTPAM MDRLKLDAAR IDGIVEGLRA VAGQPDPVGQ VIAEWDRPSG LHIRRVRTPL 

       130        140        150        160        170        180 
GVVGVIYESR PNVTADAGAL CLKSGNAVIL RGGSESFHSS GAIHAALQDG LRQAGLPVDA 

       190        200        210        220        230        240 
IQRVPTRDRA AVAEMLRMVE HIDVIVPRGG KGLVGLVQAE ARVPVFAHLE GICHVYADGD 

       250        260        270        280        290        300 
ADLEKARRVV LNAKTRRTGI CGSAECLLID RAFLAKHGPV LIEDLLKAGV EVRAEGELAE 

       310        320        330        340        350        360 
VPGTVPAQPE DFGREFLDMI IAAKVVGGVD EAIAHIRRYG SSHTESILTE NDATAERFFR 

       370        380        390        400        410        420 
RLDSAILMRN ASTQFADGGE FGMGAEIGIA TGKMHARGPV GAEQLTSFKY LVTGDGTIRA

« Hide

References

[1]"Complete genome sequence of Rhodobacter sphaeroides KD131."
Lim S.-K., Kim S.J., Cha S.H., Oh Y.-K., Rhee H.-J., Kim M.-S., Lee J.K.
J. Bacteriol. 191:1118-1119(2009) [PubMed: 19028901] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: KD131 / KCTC 12085.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001151 Genomic DNA. Translation: ACM03010.1.
RefSeqYP_002520083.1. NC_011958.1.

3D structure databases

ProteinModelPortalB9KW06.
ModBaseSearch...

Protein-protein interaction databases

STRINGB9KW06.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID7353146.
GenomeReviewsGene locus RSKD131_3150 in contig CP001151_GR.
KEGGrsk:RSKD131_3150.
PATRIC23176290. VBIRhoSph125910_0046.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAYGICGAM.
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_RHOSK
AccessionPrimary (citable) accession number: B9KW06
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 24, 2009
Last modified: January 25, 2012
This is version 26 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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