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B2IE42 (PROA_BEII9) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 33. 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:Bind_0413
OrganismBeijerinckia indica subsp. indica (strain ATCC 9039 / DSM 1715 / NCIB 8712) [Complete proteome] [HAMAP]
Taxonomic identifier395963 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBeijerinckiaceaeBeijerinckia

Protein attributes

Sequence length431 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 – 431431Gamma-glutamyl phosphate reductase HAMAP MF_00412
PRO_1000193573

Sequences

Sequence LengthMass (Da)Tools
B2IE42 [UniParc].

Last modified June 10, 2008. Version 1.
Checksum: 62338784C47E6F61

FASTA43145,789
        10         20         30         40         50         60 
MDALQLVSNR SETDVPALMH ALGQQARASA HALSLASTEA KNLALRVAAE QLRKRTQDLL 

        70         80         90        100        110        120 
LANARDLEGA KAQDANAAFL DRLTLDDKRI EAIARGLDEI AALPDPVGRM LARYERPNGL 

       130        140        150        160        170        180 
VIERVATPLG VIGIIYESRP AVTADAGALC LKAGNAAILR GGSESFFSAT IIHACLTEGL 

       190        200        210        220        230        240 
RAAGLPEAAV SLVPTRDRAA VGEMLKGLDG TIDVIVPRGG KSLVARVQAE ARVPVFAHLE 

       250        260        270        280        290        300 
GVNHIFVHRA ADLEKAAIII RNAKLRRPGV CGAAEILLVD EACMATHLAP LTRMLLDAGC 

       310        320        330        340        350        360 
AIRGDAATQT IDPRVTAAME SDWRTEYSDA IIAVRVIDGL NKAIAHIETH GSHHTDCIIT 

       370        380        390        400        410        420 
EDQEAADRFL AEVDSAIVMH NASTQFADGG EFGFGAEIGI ATGRLHARGP VGLEQLTSFK 

       430 
YRVHGNGQIR P 

« Hide

References

[1]"Complete sequence of chromosome of Beijerinckia indica subsp. indica ATCC 9039."
Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., LaButti K., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Dunfield P.F., Dedysh S.N. expand/collapse author list , Liesack W., Saw J.H., Alam M., Chen Y., Murrell J.C., Richardson P.
Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 9039 / DSM 1715 / NCIB 8712.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001016 Genomic DNA. Translation: ACB94066.1.
RefSeqYP_001831555.1. NC_010581.1.

3D structure databases

ProteinModelPortalB2IE42.
ModBaseSearch...

Protein-protein interaction databases

STRINGB2IE42.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6200008.
GenomeReviewsGene locus Bind_0413 in contig CP001016_GR.
KEGGbid:Bind_0413.
PATRIC21083435. VBIBeiInd21058_0675.

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.
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. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePROA_BEII9
AccessionPrimary (citable) accession number: B2IE42
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: June 10, 2008
Last modified: January 25, 2012
This is version 33 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