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A2RD38 (PROA_STRPG) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. 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:SpyM50421
OrganismStreptococcus pyogenes serotype M5 (strain Manfredo) [Complete proteome] [HAMAP]
Taxonomic identifier160491 [NCBI]
Taxonomic lineageBacteriaFirmicutesLactobacillalesStreptococcaceaeStreptococcus

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. HAMAP MF_00412

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 HAMAP 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 processproline biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   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: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 416416Gamma-glutamyl phosphate reductase HAMAP MF_00412
PRO_1000049996

Sequences

Sequence LengthMass (Da)Tools
A2RD38 [UniParc].

Last modified March 6, 2007. Version 1.
Checksum: DDDDE9DF33D9D4BD

FASTA41645,407
        10         20         30         40         50         60 
MTDMRRLGQR AKQASLLIAP LSTQIKNRFL STLAKALVDD TQTLLAANQK DLANAKEHGI 

        70         80         90        100        110        120 
SDIMMDRLRL TSERIKAIAQ 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 
TNIVINAKTK RPSVCNAAEG LVIHEAVAAR FIPMLEKAIN QVQPVEWRAD DKALPLFEQA 

       310        320        330        340        350        360 
VPAKAEDFET EFLDYIMSVK VVSSLEEAIS WINQHTSHHS EAIITRDIKA AETFQDLVDA 

       370        380        390        400        410 
AAVYVNASTR FTDGFVFGLG AEIGISTQKM HARGPMGLEA LTSTKFYING DGHIRE 

« Hide

References

[1]"Complete genome of acute rheumatic fever-associated serotype M5 Streptococcus pyogenes strain Manfredo."
Holden M.T.G., Scott A., Cherevach I., Chillingworth T., Churcher C., Cronin A., Dowd L., Feltwell T., Hamlin N., Holroyd S., Jagels K., Moule S., Mungall K., Quail M.A., Price C., Rabbinowitsch E., Sharp S., Skelton J. expand/collapse author list , Whitehead S., Barrell B.G., Kehoe M., Parkhill J.
J. Bacteriol. 189:1473-1477(2007) [PubMed: 17012393] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Manfredo.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM295007 Genomic DNA. Translation: CAM29763.1.
RefSeqYP_001128008.1. NC_009332.1.

3D structure databases

ProteinModelPortalA2RD38.
ModBaseSearch...

Protein-protein interaction databases

STRINGA2RD38.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBSTRT00000047818; EBSTRP00000045946; EBSTRG00000047810.
GeneID4963003.
GenomeReviewsGene locus SpyM50421 in contig AM295007_GR.
KEGGspf:SpyM50421.
PATRIC19763968. VBIStrPyo41547_0451.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0014.
GeneTreeEBGT00050000027638.
HOGENOMHBG318080.
OMAQYPAACN.
ProtClustDBPRK00197.

Family and domain databases

HAMAPMF_00412. ProA.
[Tree]
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]
Gene3DG3DSA:3.40.309.10. Aldehyde_dehydrogenase_C. 1 hit.
G3DSA:3.40.605.10. Aldehyde_dehydrogenase_N. 2 hits.
KOK00147.
PANTHERPTHR11063:SF1. GSA_DH. 1 hit.
PfamPF00171. Aldedh. 2 hits.
[Graphical view]
PIRSFPIRSF000151. GPR. 1 hit.
SUPFAMSSF53720. Aldehyde_DH/Histidinol_DH. 1 hit.
TIGRFAMsTIGR00407. ProA. 1 hit.
PROSITEPS01223. PROA. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePROA_STRPG
AccessionPrimary (citable) accession number: A2RD38
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: March 6, 2007
Last modified: December 14, 2011
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

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families