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C0QLF1 (PROA_DESAH) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 39. 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:HRM2_31740
OrganismDesulfobacterium autotrophicum (strain ATCC 43914 / DSM 3382 / HRM2) [Complete proteome] [HAMAP]
Taxonomic identifier177437 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaDesulfobacteralesDesulfobacteraceaeDesulfobacterium

Protein attributes

Sequence length418 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 – 418418Gamma-glutamyl phosphate reductase HAMAP-Rule MF_00412
PRO_1000205992

Sequences

Sequence LengthMass (Da)Tools
C0QLF1 [UniParc].

Last modified May 5, 2009. Version 1.
Checksum: 51CDA5FDD7AC0651

FASTA41845,025
        10         20         30         40         50         60 
MTLASMIEDI ARRARTAARP LATASADTKN TVLAEIARGL AHGKREIEAE NQKDLKAARD 

        70         80         90        100        110        120 
SGMSAAMIDR LTISDQTLES MIKGLNQVIA LPDPVGRITG AWTRPNGLEI SKRRIPLGVI 

       130        140        150        160        170        180 
AMIYESRPNV TVDAAALCLK AGNAAILRGG SEAFFSNTIL ARIIGNALET VGISRDSVQV 

       190        200        210        220        230        240 
LPVKDRQAIT ELLQQEAYID LVIPRGGESL IRFVVKHSTI PVLKHYKGVC HVYVDETCNM 

       250        260        270        280        290        300 
DEAVDICINA KTQRPGVCNA METLLVHERI APLFLPRMAQ AFSAAKVEMR GCPATLAMVP 

       310        320        330        340        350        360 
QALPADETDW STEYLDLIVS VKIVKDLAQA MAHIAVFGSD HTDVIVTDIP ENAETFINTV 

       370        380        390        400        410 
SSSMVGVNVS TRFNDGGELG LGAEIGISTS RLHAFGPMGL EELTSTKFVV VGKGQTRQ 

« Hide

References

[1]"Genome sequence of Desulfobacterium autotrophicum HRM2, a marine sulfate reducer oxidizing organic carbon completely to carbon dioxide."
Strittmatter A.W., Liesegang H., Rabus R., Decker I., Amann J., Andres S., Henne A., Fricke W.F., Martinez-Arias R., Bartels D., Goesmann A., Krause L., Puehler A., Klenk H.P., Richter M., Schuler M., Gloeckner F.O., Meyerdierks A., Gottschalk G., Amann R.
Environ. Microbiol. 11:1038-1055(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43914 / DSM 3382 / HRM2.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001087 Genomic DNA. Translation: ACN16255.1.
RefSeqYP_002604419.1. NC_012108.1.

3D structure databases

ProteinModelPortalC0QLF1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING177437.HRM2_31740.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACN16255; ACN16255; HRM2_31740.
GeneID7502638.
KEGGdat:HRM2_31740.
PATRIC21686057. VBIDesAut25181_3280.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0014.
HOGENOMHOG000246356.
KOK00147.
OMACNAIETL.
OrthoDBEOG6FFSCX.

Enzyme and pathway databases

BioCycDAUT177437:GHLR-3172-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]
PANTHERPTHR11063:SF1. PTHR11063:SF1. 1 hit.
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_DESAH
AccessionPrimary (citable) accession number: C0QLF1
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: May 5, 2009
Last modified: February 19, 2014
This is version 39 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