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B1J133 (PROA_PSEPW) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 36. 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:PputW619_0610
OrganismPseudomonas putida (strain W619) [Complete proteome] [HAMAP]
Taxonomic identifier390235 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas

Protein attributes

Sequence length423 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 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 – 423423Gamma-glutamyl phosphate reductase HAMAP MF_00412
PRO_1000193638

Sequences

Sequence LengthMass (Da)Tools
B1J133 [UniParc].

Last modified April 29, 2008. Version 1.
Checksum: 544CA8F8DF9099F4

FASTA42345,584
        10         20         30         40         50         60 
MTESVLDYMT RLGRAARQAS RVIARASTAQ KNRALQAAAD ALDAARAELA AANEQDLAAG 

        70         80         90        100        110        120 
RANGLEPALL DRLALTPARI DGMITGLRQV ASLPDPVGAI RDMSYRPSGI QVGKMRVPLG 

       130        140        150        160        170        180 
VIGIIYESRP NVTIDAASLC LKSGNATILR GGSEAIHSNR AIATCIQRGL AEAGLPAAVV 

       190        200        210        220        230        240 
QVVETTDREA VGALISMPEF VDVIVPRGGR GLIERISRDA RVPVIKHLDG ICHVYVAEHA 

       250        260        270        280        290        300 
DLDKGWRVAF NAKTYRYGIC GAMETLLVDQ RVAEGFLPEM ARRFQEKGVE LRGCERTRAL 

       310        320        330        340        350        360 
IEAKPASEDD WHTEYLDAIL SIRVVDGLDQ AIEHINHYGS HHTDSIITEH QGQARQFMAE 

       370        380        390        400        410        420 
VDSASVMLNT PTCFADGFEY GLGAEIGIST DKLHARGPVG LEGLTCEKYV VIGDGQLRGQ 


ESC

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References

[1]"Complete sequence of Pseudomonas putida W619."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N. expand/collapse author list , Kim E., Taghavi S., Vangronsveld D., van der Lelie D., Richardson P.
Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: W619.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000949 Genomic DNA. Translation: ACA71115.1.
RefSeqYP_001747484.1. NC_010501.1.

3D structure databases

ProteinModelPortalB1J133.
ModBaseSearch...

Protein-protein interaction databases

STRINGB1J133.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6109519.
GenomeReviewsGene locus PputW619_0610 in contig CP000949_GR.
KEGGppw:PputW619_0610.
PATRIC19950951. VBIPsePut93764_0616.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG318080.
OMAYGICGAM.
ProtClustDBPRK00197.

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_PSEPW
AccessionPrimary (citable) accession number: B1J133
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: April 29, 2008
Last modified: January 25, 2012
This is version 36 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

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