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Reviewed, UniProtKB/Swiss-Prot B0T315 (PROA_CAUSK)

Last modified June 16, 2009. Version 11. 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: Caul_4717
OrganismCaulobacter sp. (strain K31) [Complete proteome] [HAMAP]
Taxonomic identifier366602 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaCaulobacteralesCaulobacteraceaeCaulobacter

Protein attributes

Sequence length419 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 By similarity.

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 – 419419Gamma-glutamyl phosphate reductase HAMAP MF_00412
PRO_0000340876

Sequences

Sequence LengthMass (Da)Tools
B0T315-1 [UniParc].

Last modified June 10, 2008. Version 2.
Checksum: D91003013D3509AB

FASTA41943,111
        10         20         30         40         50         60 
MSLQATMTAM GQAARQGASA LRVATPAQRT AALHAMAAAI RADAPAILAA NAKDLEKAGA 

        70         80         90        100        110        120 
GGLTAPMVER LMLNPERLED VAAGVEAVAA IPDPLGVETA RWTRPNGLDI ARVRTPIGVI 

       130        140        150        160        170        180 
AMIFESRPNV TADAAALCVR SGNAVILRGG SECIHSNLAI HAAIAKGLKA AGISSDAVQI 

       190        200        210        220        230        240 
VRTPDRDAVG AILGGLNRTI DLIIPRGGKS LVARVQAEAR VAVLGHLEGL NHVFVHAAAD 

       250        260        270        280        290        300 
PRKAVEIVLN AKMRRVSVCG SAETLLVDRA AAERLLPPIA DALIKAGCEL RGDGPSRAIE 

       310        320        330        340        350        360 
PTMKPAVEAD WSTEYLAPVI SVAVVDGVEG AAAHIAAYGS GHTDAIVTED VAAAERFIAL 

       370        380        390        400        410 
VDSAIVLVNA STQFADGGEF GFGAEIGIAT DKLHARGPVG AEQLTTFKYV VRGTGQTRP 

« Hide

References

[1]"Complete sequence of chromosome of Caulobacter sp. K31."
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Bruce D., Goodwin L., Thompson L.S., Brettin T., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L. expand/collapse author list , Kyrpides N., Kim E., Stephens C., Richardson P.
Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000927 Genomic DNA. Translation: ABZ73837.1. Different initiation.
RefSeqYP_001686335.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID5902179.
GenomeReviewsGene locus Caul_4717 in contig CP000927_GR.
KEGGcak:Caul_4717.

Organism-specific databases

CMRSearch...

Family and domain databases

HAMAPMF_00412.
[Tree]
InterProIPR016163. Ald_DH_C.
IPR016162. Ald_DH_N.
IPR000965. Gglut_pp_reduct.
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. 1 hit.
PIRSFPIRSF000151. GPR. 1 hit.
TIGRFAMsTIGR00407. proA. 1 hit.
PROSITEPS01223. PROA. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePROA_CAUSK
AccessionPrimary (citable) accession number: B0T315
Entry history
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: June 10, 2008
Last modified: June 16, 2009
This is version 11 of the entry and version 2 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