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Q220P2 (PROA_RHOFD) 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
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:Rfer_0761
OrganismRhodoferax ferrireducens (strain DSM 15236 / ATCC BAA-621 / T118) [Complete proteome] [HAMAP]
Taxonomic identifier338969 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesComamonadaceaeAlbidiferax

Protein attributes

Sequence length444 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 – 444444Gamma-glutamyl phosphate reductase HAMAP MF_00412
PRO_0000252587

Sequences

Sequence LengthMass (Da)Tools
Q220P2 [UniParc].

Last modified April 18, 2006. Version 1.
Checksum: 29E355694790C5D6

FASTA44447,463
        10         20         30         40         50         60 
MIPLNTTDYA NALGLKAKQA SALMARAPTA TKNAALRKLA GLLRANVNAL QIDNARDIER 

        70         80         90        100        110        120 
AVQSGLAAPM VDRLKLSPQV IETCAQGCEQ LAGMADVIGE IIGMKQQPSG IRVGQMRVPI 

       130        140        150        160        170        180 
GVFGMIFESR PNVTIEAASL SIKSGNACIL RGGSEAIESN KALARLVQQA LTESGLPAEA 

       190        200        210        220        230        240 
VQLVQTTDRA VVGQLITMPQ YVDVIIPRGG KGLIERISRD AKVPVIKHLD GNCHTYVDDP 

       250        260        270        280        290        300 
CDIAMAVKVA DNAKTNKYSP CNATESLLVA RAVAAEFLPS IGRVYAAKGV EMRCDPQALA 

       310        320        330        340        350        360 
IFKENQPVAP VNIGHDAIDS AVELKPVLVL AQESDWFEEY LAPIISIKVV AGVDEAIAHI 

       370        380        390        400        410        420 
NRYSSHHTDA ILTRDHMHAQ QFLREVDSAS VMVNTSTRFA DGFEYGLGAE IGISTDKFHA 

       430        440 
RGPVGIEGLT SLKYVVLGDG EIRA 

« Hide

References

[1]"Complete sequence of chromosome of Rhodoferax ferrireducens DSM 15236."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M. expand/collapse author list , Kyrpides N., Ivanova N., Richardson P.
Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 15236 / ATCC BAA-621 / T118.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000267 Genomic DNA. Translation: ABD68511.1.
RefSeqYP_522042.1. NC_007908.1.

3D structure databases

ProteinModelPortalQ220P2.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ220P2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3964139.
GenomeReviewsGene locus Rfer_0761 in contig CP000267_GR.
KEGGrfr:Rfer_0761.
NMPDRfig|338969.3.peg.971.
PATRIC23234039. VBIRhoFer131161_1044.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0014.
HOGENOMHBG318080.
OMAYGICGAM.
PhylomeDBQ220P2.
ProtClustDBPRK00197.

Enzyme and pathway databases

BioCycRFER338969:RFER_0761-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. 2 hits.
[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_RHOFD
AccessionPrimary (citable) accession number: Q220P2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 17, 2006
Last sequence update: April 18, 2006
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