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Q820I7 (PROA_NITEU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 76. 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:NE2158
OrganismNitrosomonas europaea (strain ATCC 19718 / NBRC 14298) [Complete proteome] [HAMAP]
Taxonomic identifier228410 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaNitrosomonadalesNitrosomonadaceaeNitrosomonas

Protein attributes

Sequence length422 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: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 422422Gamma-glutamyl phosphate reductase HAMAP-Rule MF_00412
PRO_0000189757

Sequences

Sequence LengthMass (Da)Tools
Q820I7 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 96D624B0DAC10931

FASTA42245,013
        10         20         30         40         50         60 
MEKTEKIQAD MQALGRAARA AARIVAKADT AVKNHALIAM ARAIRCHEAS LLAANAADVA 

        70         80         90        100        110        120 
QARNKGLEPA MIDRLTLTPK GIASMAAGLE QIAALSDPIG AVTDLDYRPS GIQVGRMRVP 

       130        140        150        160        170        180 
LGVIAIIYEA RPNVTADAAG LCLKAGNAAI LRGGSEAIQS NQAIAACVQE GLRSAGLPEH 

       190        200        210        220        230        240 
AVQVVETTDR AAVGELITMS EYVDMVVPRG GKGLIERIAN EARVPVIKHL DGVCHVYVDL 

       250        260        270        280        290        300 
SADLEKAVRV ADNAKTQRYG TCNTMETLLV HAGIAERFLP RICKILLEKG VELRGDEAAR 

       310        320        330        340        350        360 
ALVAGIKPAV EEDWYAEYLA PVLSVRIVED IDQAITHIAT YGSQHTDAIV TEDYSRARQF 

       370        380        390        400        410        420 
LREVDSSSVM INASTRFADG FEYGLGAEIG ISTDKLHARG PVGLEGLTSQ KFIVLGDGHI 


RE 

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References

[1]"Complete genome sequence of the ammonia-oxidizing bacterium and obligate chemolithoautotroph Nitrosomonas europaea."
Chain P., Lamerdin J.E., Larimer F.W., Regala W., Lao V., Land M.L., Hauser L., Hooper A.B., Klotz M.G., Norton J., Sayavedra-Soto L.A., Arciero D.M., Hommes N.G., Whittaker M.M., Arp D.J.
J. Bacteriol. 185:2759-2773(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 19718 / NBRC 14298.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL954747 Genomic DNA. Translation: CAD86069.1.
RefSeqNP_842162.1. NC_004757.1.

3D structure databases

ProteinModelPortalQ820I7.
ModBaseSearch...

Protein-protein interaction databases

STRING228410.NE2158.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAD86069; CAD86069; NE2158.
GeneID1083120.
KEGGneu:NE2158.
PATRIC22715692. VBINitEur56163_2427.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0014.
HOGENOMHOG000246356.
KOK00147.
OMAISMPEYV.
ProtClustDBPRK00197.

Enzyme and pathway databases

BioCycNEUR228410:GJNO-2199-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. Aldehyde_DH/Histidinol_DH. 1 hit.
TIGRFAMsTIGR00407. proA. 1 hit.
PROSITEPS01223. PROA. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePROA_NITEU
AccessionPrimary (citable) accession number: Q820I7
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: June 1, 2003
Last modified: May 1, 2013
This is version 76 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