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Q3IXX7 (PROA_RHOS4) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 50. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:RHOS4_30390
ORF Names:RSP_3824
OrganismRhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158)
Taxonomic identifier272943 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRhodobacter

Protein attributes

Sequence length420 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
Reference 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 – 420420Gamma-glutamyl phosphate reductase HAMAP MF_00412
PRO_0000230020

Sequences

Sequence LengthMass (Da)Tools
Q3IXX7 [UniParc].

Last modified November 8, 2005. Version 1.
Checksum: 14ECB68C72712616

FASTA42044,730
        10         20         30         40         50         60 
MDGTDVTMLM REIGVRARAA AAELAFAEPS RKEEALNAAA EAMLARSDEI LEANGRDLAF 

        70         80         90        100        110        120 
GAEKGLTPAM MDRLKLDAAR IDGIVEGLRA VAGQPDPVGQ VIAEWDRPSG LHIRRVRTPL 

       130        140        150        160        170        180 
GVVGVIYESR PNVTADAGAL CLKSGNAVIL RGGSESFHSS GAIHAALQDG LRQAGLPVDA 

       190        200        210        220        230        240 
IQRVPTRDRA AVAEMLRMVE HIDVIVPRGG KGLVGLVQAE ARVPVFAHLE GICHVYADGE 

       250        260        270        280        290        300 
ADLEKARRVV LNAKTRRTGI CGSAECLLID RAFLAKHGPV LIEDLLKAGV EVRAEGELAQ 

       310        320        330        340        350        360 
VPGTVPAQPE DFGREFLDMI IAAKVVDGVD EAIAHIRRYG SSHTESILTE NDATAERFFR 

       370        380        390        400        410        420 
RLDSAILMRN ASTQFADGGE FGMGAEIGIA TGKMHARGPV GAEQLTSFKY LVTGDGTIRT 

« Hide

References

[1]"Complete sequence of chromosome 2 of Rhodobacter sphaeroides 2.4.1."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C., Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J., Kaplan S.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000144 Genomic DNA. Translation: ABA80607.1.
RefSeqYP_354508.1. NC_007494.1.

3D structure databases

ProteinModelPortalQ3IXX7.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ3IXX7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3721405.
GenomeReviewsGene locus RHOS4_30390 in contig CP000144_GR.
KEGGrsp:RSP_3824.
NMPDRfig|272943.3.peg.3489.
PATRIC23156110. VBIRhoSph57909_3410.

Phylogenomic databases

eggNOGCOG0014.
HOGENOMHBG318080.
OMAYGICGAM.
PhylomeDBQ3IXX7.
ProtClustDBPRK00197.

Enzyme and pathway databases

BioCycRSPH272943:RSP_3824-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_RHOS4
AccessionPrimary (citable) accession number: Q3IXX7
Entry history
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: November 8, 2005
Last modified: January 25, 2012
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