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Q04KZ2 (PROA_STRP2) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 43. 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:SPD_0823
OrganismStreptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466) [Complete proteome] [HAMAP]
Taxonomic identifier373153 [NCBI]
Taxonomic lineageBacteriaFirmicutesLactobacillalesStreptococcaceaeStreptococcus

Protein attributes

Sequence length420 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 – 420420Gamma-glutamyl phosphate reductase HAMAP MF_00412
PRO_1000049995

Sequences

Sequence LengthMass (Da)Tools
Q04KZ2 [UniParc].

Last modified November 14, 2006. Version 1.
Checksum: C502599D319F7D94

FASTA42045,225
        10         20         30         40         50         60 
MVSRQEQFEQ VQAVKKSINT ASEEVKNQAL LAMADHLVAA TEEILAANAL DMAAAKGKIS 

        70         80         90        100        110        120 
DVMLDRLYLD ADRIEAMARG IREVVALPDP IGEVLETSQL ENGLVITKKR VAMGVIGIIY 

       130        140        150        160        170        180 
ESRPNVTSDA AALTLKSGNA VVLRSGKDAY QTTHAIVTAL KKGLETTTIH PNVIQLVEDT 

       190        200        210        220        230        240 
SRESSYAMMK AKGYLDLLIP RGGAGLINAV VENAIVPVIE TGTGIVHVYV DKDADEDKAL 

       250        260        270        280        290        300 
SIINNAKTSR PSVCNAMEVL LVHENKAASI LPRLDQMLVA ERKEAGLEPI QFRLDSKASQ 

       310        320        330        340        350        360 
FVSGQAAETQ DFDTEFLDYV LAVKVVSSLE EAVAHIESHS THHSDAIVTE NAEAAAYFTD 

       370        380        390        400        410        420 
QVDSAAVYVN ASTRFTDGGQ FGLGCEMGIS TQKLHARGPM GLKELTSYKY VVAGDGQIRE 

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References

[1]"Genome sequence of Avery's virulent serotype 2 strain D39 of Streptococcus pneumoniae and comparison with that of unencapsulated laboratory strain R6."
Lanie J.A., Ng W.-L., Kazmierczak K.M., Andrzejewski T.M., Davidsen T.M., Wayne K.J., Tettelin H., Glass J.I., Winkler M.E.
J. Bacteriol. 189:38-51(2007) [PubMed: 17041037] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: D39 / NCTC 7466.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000410 Genomic DNA. Translation: ABJ54450.1.
RefSeqYP_816306.1. NC_008533.1.

3D structure databases

ProteinModelPortalQ04KZ2.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ04KZ2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBSTRT00000018820; EBSTRP00000018060; EBSTRG00000018820.
GeneID4442516.
GenomeReviewsGene locus SPD_0823 in contig CP000410_GR.
KEGGspd:SPD_0823.
PATRIC19682782. VBIStrPne27904_0928.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0014.
GeneTreeEBGT00050000027638.
HOGENOMHBG318080.
OMAHRIEAMA.
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. 1 hit.
[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_STRP2
AccessionPrimary (citable) accession number: Q04KZ2
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: November 14, 2006
Last modified: January 25, 2012
This is version 43 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