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C1EZ15 (PROA_BACC3) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 42. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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:BCA_3063
OrganismBacillus cereus (strain 03BB102) [Complete proteome] [HAMAP]
Taxonomic identifier572264 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group

Protein attributes

Sequence length415 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-Rule MF_00412

Catalytic activity

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

Pathway

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

Subcellular location

Cytoplasm By similarity HAMAP-Rule 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_processL-proline biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   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: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 415415Gamma-glutamyl phosphate reductase HAMAP-Rule MF_00412
PRO_1000193567

Sequences

Sequence LengthMass (Da)Tools
C1EZ15 [UniParc].

Last modified May 26, 2009. Version 1.
Checksum: B17A3959DEA104BD

FASTA41545,627
        10         20         30         40         50         60 
MNEVLAKGKR AKEVAMNLVL KSTSQKNEAL AAIAERLIVE TAYILEENKR GIEEGKAKGF 

        70         80         90        100        110        120 
SDSLLDRLML TEQRIVDMTE GIKQLIELRD PVGECVSAWE RPNGLSIQEM RVPLGVVGMI 

       130        140        150        160        170        180 
YEARPNVTVD AATICLKTGN AVILRGSSSA IHSNKAIVAV IHRALKQTSL PQESVQLIED 

       190        200        210        220        230        240 
TTRDSAKQLF TMNDYLDVLI PRGGKQLIDT VVREASVPVL ETGAGNCHVF IDETADKQMA 

       250        260        270        280        290        300 
FDIIINAKTQ RPSVCNAIET IVLHEKWAEQ YGSELFSSLK KRGVELRGDQ KALAMDSSIV 

       310        320        330        340        350        360 
LASEEDWWTE FLSLTLAVKL VSSIEEAIHH INTYGSMHSE AIISENEENV SKFFVSVDAA 

       370        380        390        400        410 
ALYHNASTRF TDGSEFGFGA EIGISTQKLH VRGPMGLPAL TSTKYVIRGN GQIRK 

« Hide

References

[1]"Genome sequence of Bacillus cereus 03BB102."
Dodson R.J., Jackson P., Munk A.C., Brettin T., Bruce D., Detter C., Tapia R., Han C., Sutton G., Sims D.
Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 03BB102.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001407 Genomic DNA. Translation: ACO27738.1.
RefSeqYP_002750334.1. NC_012472.1.

3D structure databases

ProteinModelPortalC1EZ15.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING572264.BCA_3063.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACO27738; ACO27738; BCA_3063.
GeneID7690946.
KEGGbcx:BCA_3063.
PATRIC18819277. VBIBacCer84800_2955.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0014.
HOGENOMHOG000246356.
KOK00147.
OMAHRIEAMA.
OrthoDBEOG6FFSCX.

Enzyme and pathway databases

BioCycBCER572264:GH22-3017-MONOMER.
UniPathwayUPA00098; UER00360.

Family and domain databases

Gene3D3.40.309.10. 1 hit.
3.40.605.10. 2 hits.
HAMAPMF_00412. ProA.
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]
PfamPF00171. Aldedh. 1 hit.
[Graphical view]
PIRSFPIRSF000151. GPR. 1 hit.
SUPFAMSSF53720. SSF53720. 1 hit.
TIGRFAMsTIGR00407. proA. 1 hit.
PROSITEPS01223. PROA. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePROA_BACC3
AccessionPrimary (citable) accession number: C1EZ15
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: May 26, 2009
Last modified: June 11, 2014
This is version 42 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways