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Q3IP72 (PROA_NATPD) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 50. 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:NP3978A
OrganismNatronomonas pharaonis (strain DSM 2160 / ATCC 35678) [Complete proteome] [HAMAP]
Taxonomic identifier348780 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaHalobacteriaHalobacterialesHalobacteriaceaeNatronomonas

Protein attributes

Sequence length438 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 – 438438Gamma-glutamyl phosphate reductase HAMAP MF_00412
PRO_0000230035

Sequences

Sequence LengthMass (Da)Tools
Q3IP72 [UniParc].

Last modified November 8, 2005. Version 1.
Checksum: BB01CE7C2483D92F

FASTA43847,559
        10         20         30         40         50         60 
MTETTEAKVD AAQTAALELA NESDEARQEN LQAIADAIDE RRAEVLEANE KDVEAAEEML 

        70         80         90        100        110        120 
EAGEYSQALV DRLKLSDAKL DSIIEMVRSV AGQEDPLGKT LTARELDDGL DLYKVSVPIG 

       130        140        150        160        170        180 
VIGTVFESRP DALVQIAALS LRSGNAVILK GGSEASHSNR VLYEIIREAT ADLPDGWAQL 

       190        200        210        220        230        240 
IEAREDVDRL LGMDDSVDLL MPRGSSAFVS YIQDNTSIPV LGHTEGVCHV YVDDAADLDM 

       250        260        270        280        290        300 
ATDIAYDAKV QYPAVCNAVE TLLVHEDVAE EYLPDIAARY AEADVEMRGD EATRSVLDRD 

       310        320        330        340        350        360 
IEAATDDDWT SEYGDLIVAI KVVDSLESAI DHINTNGSKH TESIVTEDDG RASTFMRRLD 

       370        380        390        400        410        420 
SASVFHNAST RFSDGYRFGL GAEVGISTGK IHARGPVGLK GLTTYKYHLE GDGHLVATYA 

       430 
GEDAKPFSHE EFDGEWSP 

« Hide

References

[1]"Living with two extremes: conclusions from the genome sequence of Natronomonas pharaonis."
Falb M., Pfeiffer F., Palm P., Rodewald K., Hickmann V., Tittor J., Oesterhelt D.
Genome Res. 15:1336-1343(2005) [PubMed: 16169924] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 2160 / ATCC 35678.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR936257 Genomic DNA. Translation: CAI50080.1.
RefSeqYP_327631.1. NC_007426.1.

3D structure databases

ProteinModelPortalQ3IP72.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ3IP72.

Proteomic databases

PRIDEQ3IP72.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3703054.
GenomeReviewsGene locus NP3978A in contig CR936257_GR.
KEGGnph:NP3978A.
NMPDRfig|348780.3.peg.2561.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGarNOG05521.
HOGENOMHBG318080.
OMAQYPAACN.
PhylomeDBQ3IP72.
ProtClustDBPRK00197.

Enzyme and pathway databases

BioCycNPHA348780:NP3978A-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.
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_NATPD
AccessionPrimary (citable) accession number: Q3IP72
Entry history
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: November 8, 2005
Last modified: November 16, 2011
This is version 50 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