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Q5KYA2 (PROA_GEOKA) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 71. 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:GK2049
OrganismGeobacillus kaustophilus (strain HTA426) [Complete proteome] [HAMAP]
Taxonomic identifier235909 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus

Protein attributes

Sequence length414 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 – 414414Gamma-glutamyl phosphate reductase HAMAP-Rule MF_00412
PRO_0000189728

Sequences

Sequence LengthMass (Da)Tools
Q5KYA2 [UniParc].

Last modified February 1, 2005. Version 1.
Checksum: D57558B51B02E565

FASTA41445,650
        10         20         30         40         50         60 
MSELLEKAER LKTASQTLAM LSAEEKNEAL EQIAQTLDRE RAFILQENEK DMAQGREQGL 

        70         80         90        100        110        120 
SPALLDRLQL TNERLDQIID GVRQVASLPD PVGEIIAEWT RPNGLRIQTV RVPLGVIGMV 

       130        140        150        160        170        180 
YEARPNVTVD AASLCLKTGN AVLLRGSTSA LHSNKALVAV MKEALRTTAI PETAIELLED 

       190        200        210        220        230        240 
TSRETAQRMF RLNNYLDVLI PRGGAGLIRS VVENATVPVL ETGVGNCHIF VDESAERQMA 

       250        260        270        280        290        300 
IEIVLNAKLQ RPSVCNAVET VLIHERWPYA ADLLETLHAR GVELRGDQRL ASAYPFISEA 

       310        320        330        340        350        360 
TEDDWYTEYL APILAVKLVA DVDEAIGHIR RYGTKHSEAI ITENEVNVRR FFQAVDAAVL 

       370        380        390        400        410 
YHNASTRFTD GEQFGYGAEI GISTQKLHAR GPMGLVAITT TKSLVYGTGQ IRTV 

« Hide

References

[1]"Thermoadaptation trait revealed by the genome sequence of thermophilic Geobacillus kaustophilus."
Takami H., Takaki Y., Chee G.-J., Nishi S., Shimamura S., Suzuki H., Matsui S., Uchiyama I.
Nucleic Acids Res. 32:6292-6303(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: HTA426.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000043 Genomic DNA. Translation: BAD76334.1.
RefSeqYP_147902.1. NC_006510.1.

3D structure databases

ProteinModelPortalQ5KYA2.
SMRQ5KYA2. Positions 3-413.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING235909.GK2049.

Proteomic databases

PRIDEQ5KYA2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAD76334; BAD76334; GK2049.
GeneID3186428.
KEGGgka:GK2049.
PATRIC21965487. VBIGeoKau81518_2199.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0014.
HOGENOMHOG000246356.
KOK00147.
OMAALTSYKW.
OrthoDBEOG6FFSCX.

Enzyme and pathway databases

BioCycGKAU235909:GJO7-2137-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_GEOKA
AccessionPrimary (citable) accession number: Q5KYA2
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: February 1, 2005
Last modified: June 11, 2014
This is version 71 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