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Q8DVM9 (PROA_STRMU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 74. 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:SMU_450
OrganismStreptococcus mutans [Complete proteome] [HAMAP]
Taxonomic identifier1309 [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_0000189787

Sequences

Sequence LengthMass (Da)Tools
Q8DVM9 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 40EB07C1D5D68A79

FASTA41645,219
        10         20         30         40         50         60 
MAIIDNLGQN AKKASFLLAQ LGTEAKNTAL LKVAEALLAE LPYILEENAK DVALAQEHGI 

        70         80         90        100        110        120 
SAIMVDRLRL DEKRLQDIAS GVRDVAALGD PIGQVVRGYT NMVGLKIIQK RVPLGVIAMI 

       130        140        150        160        170        180 
FESRPNVSVD AFSLAFKTGN AIILRGGRDA ICSNTALVNV IRRTLASFGL DENAVQLVED 

       190        200        210        220        230        240 
TSHEVAKELM AAVDYVDVLI PRGGARLIQT VKKEAKVPVI ETGVGNVHIY VDEFADLDMA 

       250        260        270        280        290        300 
SKIVVNAKTQ RPSVCNAAEG LLVHEKVASD FLPKLEAAIN QIHPVEFRAD DRAQKILKNA 

       310        320        330        340        350        360 
QPASQEDYAT EFLDYIISVK IVNSLGEAID WINTYTSHHS ESIITRDIQA AERFQDEVDA 

       370        380        390        400        410 
AAVYVNASTR FTDGFVFGLG AEIGISTQKL HARGPMGLEA LTSTKFYING KGQIRE 

« Hide

References

[1]"Genome sequence of Streptococcus mutans UA159, a cariogenic dental pathogen."
Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B., Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S., Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.
Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002) [PubMed: 12397186] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700610 / UA159 / Serotype c.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE014133 Genomic DNA. Translation: AAN58200.1.
RefSeqNP_720894.1. NC_004350.2.

3D structure databases

ProteinModelPortalQ8DVM9.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBSTRT00000012492; EBSTRP00000011974; EBSTRG00000012492.
GeneID1029582.
GenomeReviewsGene locus SMU_450 in contig AE014133_GR.
KEGGsmu:SMU_450.
NMPDRfig|210007.1.peg.407.
PATRIC19663127. VBIStrMut61772_0396.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000027638.
HOGENOMHBG318080.
OMAYGICGAM.
ProtClustDBPRK00197.

Enzyme and pathway databases

BioCycSMUT210007:SMU_450-MONOMER.

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_STRMU
AccessionPrimary (citable) accession number: Q8DVM9
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: March 1, 2003
Last modified: January 25, 2012
This is version 74 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