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Q3J7T1 (PROA_NITOC) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 51. 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:Noc_2662
OrganismNitrosococcus oceani (strain ATCC 19707 / NCIMB 11848) [Complete proteome] [HAMAP]
Taxonomic identifier323261 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaChromatialesChromatiaceaeNitrosococcus

Protein attributes

Sequence length418 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 – 418418Gamma-glutamyl phosphate reductase HAMAP MF_00412
PRO_0000230007

Sequences

Sequence LengthMass (Da)Tools
Q3J7T1 [UniParc].

Last modified November 8, 2005. Version 1.
Checksum: BA5710F927A2CF58

FASTA41845,326
        10         20         30         40         50         60 
MDIKDYMQNL GCRARKVSRV LARAGAEEKN QALEMAASFI EKESQALVEA NHKDLAAGRS 

        70         80         90        100        110        120 
KGLDEALLDR LTLTEARIAV MAEGLRQIAS LPDPVGAISE LSYRPSGIQV GRMRVPLGVI 

       130        140        150        160        170        180 
GIIYESRPNV TADAAGLCLK SGNAVILRGG SEAFHSNQAI ACCIHQGLEQ AGLPQEAVQV 

       190        200        210        220        230        240 
VETTDRLAVG ALITQEEHVD VIIPRGGRSL IERISQEAKI PVIKHLDGIC HVYIDDRADL 

       250        260        270        280        290        300 
DKAVAIAVNA KCQRYGVCNA METLLVAREI AAEILPMMGE HYCSAGVELR GCPETQGLLP 

       310        320        330        340        350        360 
HIEPATEEDW YTEYLAPLLA IRIVAGLDEA IEHITHYGSH HTETIVTEDF TRARRFLTEV 

       370        380        390        400        410 
DSSSVMVNAS TRFADGFEYG LGAEIGISTD KLHARGPVGL EGLTSQKWIV LGNGHIRE 

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References

[1]"Complete genome sequence of the marine, chemolithoautotrophic, ammonia-oxidizing bacterium Nitrosococcus oceani ATCC 19707."
Klotz M.G., Arp D.J., Chain P.S.G., El-Sheikh A.F., Hauser L.J., Hommes N.G., Larimer F.W., Malfatti S.A., Norton J.M., Poret-Peterson A.T., Vergez L.M., Ward B.B.
Appl. Environ. Microbiol. 72:6299-6315(2006) [PubMed: 16957257] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 19707 / NCIMB 11848.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000127 Genomic DNA. Translation: ABA59115.1.
RefSeqYP_344645.1. NC_007484.1.

3D structure databases

ProteinModelPortalQ3J7T1.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ3J7T1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3705159.
GenomeReviewsGene locus Noc_2662 in contig CP000127_GR.
KEGGnoc:Noc_2662.
NMPDRfig|323261.3.peg.2526.
PATRIC22709790. VBINitOce57959_3097.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0014.
HOGENOMHBG318080.
OMAYGICGAM.
PhylomeDBQ3J7T1.
ProtClustDBPRK00197.

Enzyme and pathway databases

BioCycNOCE323261:NOC_2662-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_NITOC
AccessionPrimary (citable) accession number: Q3J7T1
Entry history
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: November 8, 2005
Last modified: January 25, 2012
This is version 51 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