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A4W028 (PROA_STRS2) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 57. 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:SSU98_0559
OrganismStreptococcus suis (strain 98HAH33) [Complete proteome] [HAMAP]
Taxonomic identifier391296 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

Protein attributes

Sequence length412 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 – 412412Gamma-glutamyl phosphate reductase HAMAP-Rule MF_00412
PRO_1000049997

Sequences

Sequence LengthMass (Da)Tools
A4W028 [UniParc].

Last modified May 29, 2007. Version 1.
Checksum: C688B33D7A3CFB64

FASTA41243,863
        10         20         30         40         50         60 
MTTTQVLLDS LLANKASINL ATTEQKNQAL SAMADQLVAQ TEAILAGNAI DMEHAQGKIS 

        70         80         90        100        110        120 
QVMQDRLLLT EERIEAMADG IRALIGLPDP VGLVLEESTR ADGLNICKKS IPFGLVGMIY 

       130        140        150        160        170        180 
ESRPNVTSDA AALAIKSGNA VILRGGKEAF HSAKAIVTAL KSGLEEAGVS PKVIELVQDT 

       190        200        210        220        230        240 
SRVSATELMT AKGKIDLLVP RGGAGLIQAV VENATVPVIE TGTGICHVYV DKDADLDKAL 

       250        260        270        280        290        300 
RIVVNAKTSR PSVCNAAEVL LVHEEIASQF LPRLEEALSG QVELRADSQA QALLNQARPA 

       310        320        330        340        350        360 
GDQDFDTEFL DYIMAVKVVS SVEEAISHIA QHSTGHSEAI VTENSQTAEH FTLHVDSAAV 

       370        380        390        400        410 
YVNASTRFTD GGEFGLGCEL GISTQKMHAR GPMGLREMTT YKYIITGDGH IR 

« Hide

References

[1]"A glimpse of streptococcal toxic shock syndrome from comparative genomics of S. suis 2 Chinese isolates."
Chen C., Tang J., Dong W., Wang C., Feng Y., Wang J., Zheng F., Pan X., Liu D., Li M., Song Y., Zhu X., Sun H., Feng T., Guo Z., Ju A., Ge J., Dong Y. expand/collapse author list , Sun W., Jiang Y., Wang J., Yan J., Yang H., Wang X., Gao G.F., Yang R., Wang J., Yu J.
PLoS ONE 2:E315-E315(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 98HAH33.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000408 Genomic DNA. Translation: ABP91717.1.
RefSeqYP_001200117.1. NC_009443.1.

3D structure databases

ProteinModelPortalA4W028.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING391296.SSU98_0559.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABP91717; ABP91717; SSU98_0559.
GeneID5103016.
KEGGssv:SSU98_0559.
PATRIC19777351. VBIStrSui72275_0545.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycSSUI391296:GI2E-609-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_STRS2
AccessionPrimary (citable) accession number: A4W028
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: May 29, 2007
Last modified: February 19, 2014
This is version 57 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