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Q89X85 (PROA_BRAJA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 66. 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:blr0429
OrganismBradyrhizobium japonicum
Taxonomic identifier375 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeBradyrhizobium

Protein attributes

Sequence length435 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
Reference 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 – 435435Gamma-glutamyl phosphate reductase HAMAP MF_00412
PRO_0000189704

Sequences

Sequence LengthMass (Da)Tools
Q89X85 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: C043AA17C4682B50

FASTA43545,636
        10         20         30         40         50         60 
MAAPLKAVDG NADRTGDLQA LMSDLAARAR AAARVLALAP PEQKNRALEA MERAIRSNAA 

        70         80         90        100        110        120 
AILAANAEDV AEARASSNMT ASFIDRLTLT PARVESMAEG IGIVRGIADP VGIVTESWQR 

       130        140        150        160        170        180 
PNGMTIERVR VPLGVVGVIF ESRPNVAADA GVLCLKSGNA VILRGGSDSF RSCRAIHECL 

       190        200        210        220        230        240 
VQGLREAGLP EAAITLVPTR DRAAVGMMLS GLNGAIDVIV PRGGKSLVAR VEQEARVPVF 

       250        260        270        280        290        300 
AHLEGVNHVY VDASADLAMA KSIVLNAKMR RTGVCGAAET LLVDRAAAAT SLKPLVEMLI 

       310        320        330        340        350        360 
EAGCEVRGDD VVQKTDARVK PANDDDWDTE YLDAIIAAKV VDGVDGAIAH IQNHGSHHTD 

       370        380        390        400        410        420 
AIVSENEAAA KKFLSEVDSA IVLHNASTQF ADGGEFGFGA EIGIATGRFH ARGPVGAEQL 

       430 
TSFKYRVHGT GQTRP 

« Hide

References

[1]"Complete genomic sequence of nitrogen-fixing symbiotic bacterium Bradyrhizobium japonicum USDA110."
Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S., Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M., Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.
DNA Res. 9:189-197(2002) [PubMed: 12597275] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: USDA 110.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000040 Genomic DNA. Translation: BAC45694.1.
RefSeqNP_767069.1. NC_004463.1.

3D structure databases

ProteinModelPortalQ89X85.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1054342.
GenomeReviewsGene locus blr0429 in contig BA000040_GR.
KEGGbja:blr0429.
NMPDRfig|224911.1.peg.429.
PATRIC21184319. VBIBraJap65052_0437.

Phylogenomic databases

HOGENOMHBG318080.
OMAITHINRY.
PhylomeDBQ89X85.
ProtClustDBPRK00197.

Enzyme and pathway databases

BioCycBJAP224911:BLR0429-MONOMER.

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_BRAJA
AccessionPrimary (citable) accession number: Q89X85
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: June 1, 2003
Last modified: January 25, 2012
This is version 66 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