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B5XML5 (PROA_STRPZ) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 45. 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:Spy49_1295c
OrganismStreptococcus pyogenes serotype M49 (strain NZ131) [Complete proteome] [HAMAP]
Taxonomic identifier471876 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

Protein attributes

Sequence length416 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 – 416416Gamma-glutamyl phosphate reductase HAMAP-Rule MF_00412
PRO_1000193664

Sequences

Sequence LengthMass (Da)Tools
B5XML5 [UniParc].

Last modified November 25, 2008. Version 1.
Checksum: EA319F1B55B077E6

FASTA41645,528
        10         20         30         40         50         60 
MTDMRRLGQR AKQASLLIAP LSTQIKNRFL STLAKALVDD TQTLLAANQK DLANAKEHGI 

        70         80         90        100        110        120 
SDIMMDRLRL TSERIKAMAQ GVQQVADLAD PIGQVIKGYT NLDGLKILQK RVPLGVIAMI 

       130        140        150        160        170        180 
FESRPNVSVD AFSLAFKTNN AIILRGGKDA LHSNKALVKL IRQSLEKSGI TPDAVQLVED 

       190        200        210        220        230        240 
PSHAVAEELM QATDYVDVLI PRGGAKLIQT VKEKAKVPVI ETGVGNVHIY VDAQADLDMA 

       250        260        270        280        290        300 
TKIVINAKTK RPSVCNAAEG LVIHEAVAAR FIPMLEKAIN QVQPVEWRAD DKALPLFEQA 

       310        320        330        340        350        360 
VPAKAEDFET EFLDYIMSVK VVSSLEEAIF WINQHTSHHS EAIITRDIKV AETFQDLVDA 

       370        380        390        400        410 
AAVYVNASTR FTDGFVFGLG AEIGISTQKM HARGPMGLEA LTSTKFYING DGHIRE 

« Hide

References

[1]"Genome sequence of a nephritogenic and highly transformable M49 strain of Streptococcus pyogenes."
McShan W.M., Ferretti J.J., Karasawa T., Suvorov A.N., Lin S., Qin B., Jia H., Kenton S., Najar F., Wu H., Scott J., Roe B.A., Savic D.J.
J. Bacteriol. 190:7773-7785(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NZ131.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000829 Genomic DNA. Translation: ACI61577.1.
RefSeqYP_002286272.1. NC_011375.1.

3D structure databases

ProteinModelPortalB5XML5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING471876.Spy49_1295c.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACI61577; ACI61577; Spy49_1295c.
GeneID6984601.
KEGGsoz:Spy49_1295c.
PATRIC19757682. VBIStrPyo129711_1337.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0014.
HOGENOMHOG000246356.
KOK00147.
OMACNAIETL.
OrthoDBEOG6FFSCX.
ProtClustDBPRK00197.

Enzyme and pathway databases

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. 2 hits.
[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_STRPZ
AccessionPrimary (citable) accession number: B5XML5
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: November 25, 2008
Last modified: February 19, 2014
This is version 45 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