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Q2P2G1 (PROA_XANOM) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 64. 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:XOO2511
OrganismXanthomonas oryzae pv. oryzae (strain MAFF 311018) [Complete proteome] [HAMAP]
Taxonomic identifier342109 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeXanthomonas

Protein attributes

Sequence length414 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: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 414414Gamma-glutamyl phosphate reductase HAMAP-Rule MF_00412
PRO_0000230033

Sequences

Sequence LengthMass (Da)Tools
Q2P2G1 [UniParc].

Last modified February 7, 2006. Version 1.
Checksum: 60E50F02859F76B5

FASTA41444,359
        10         20         30         40         50         60 
MTIKTLALQC RDAAQVVSQL SSQAKCALLQ AMAAALEADA GTILAANARD LEAARAKGTA 

        70         80         90        100        110        120 
SAMLDRLALD DKRLAGIAAA LREVALLPDP VGRITREDVR PNGIRVQKVR VPLGVIAMIY 

       130        140        150        160        170        180 
EARPNVTADA AALCIKAGNG VILRGGSEAI HSNIAIARAL QRALREANVP EAALTLVEDL 

       190        200        210        220        230        240 
RRETMLELLQ LNDIVDLAIP RGGEGLIRFV AEHARVPVIK HYKGVCHLFV DASAEMELAL 

       250        260        270        280        290        300 
RLLIDGKATR PSACNSLETL LVHADIAERF LPLAAQALRE RKVELRGDAA TRAVLPEIAP 

       310        320        330        340        350        360 
ASDDDYAAEF LDLILAMRVV ADLDTALAHI RQYGSDHTEV IATQDPDNAE RFVQSLRSAV 

       370        380        390        400        410 
VMVNASSRFS DGGELGLGAE IGISTTRLHS YGPMGLEALT VERFVVRGEG QVRH 

« Hide

References

[1]"Genome sequence of Xanthomonas oryzae pv. oryzae suggests contribution of large numbers of effector genes and insertion sequences to its race diversity."
Ochiai H., Inoue Y., Takeya M., Sasaki A., Kaku H.
Jpn. Agric. Res. Q. 39:275-287(2005)
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MAFF 311018.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP008229 Genomic DNA. Translation: BAE69266.1.
RefSeqYP_451540.1. NC_007705.1.

3D structure databases

ProteinModelPortalQ2P2G1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING342109.XOO_2511.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAE69266; BAE69266; BAE69266.
GeneID3856967.
KEGGxom:XOO_2511.
PATRIC24114866. VBIXanOry49434_2850.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0014.
KOK00147.
OMAICHVYVS.
OrthoDBEOG6FFSCX.
ProtClustDBPRK00197.

Enzyme and pathway databases

BioCycXORY342109:GIX9-2551-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. SSF53720. 1 hit.
TIGRFAMsTIGR00407. proA. 1 hit.
PROSITEPS01223. PROA. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePROA_XANOM
AccessionPrimary (citable) accession number: Q2P2G1
Entry history
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: February 7, 2006
Last modified: February 19, 2014
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways