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Q39JM2 (PROA_BURS3) 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:Bcep18194_A3743
OrganismBurkholderia sp. (strain 383) (Burkholderia cepacia (strain ATCC 17760 / NCIB 9086 / R18194)) [Complete proteome] [HAMAP]
Taxonomic identifier269483 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiaBurkholderia cepacia complex

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. 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.

Sequence caution

The sequence ABB07344.1 differs from that shown. Reason: Erroneous initiation.

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_0000229995

Sequences

Sequence LengthMass (Da)Tools
Q39JM2 [UniParc].

Last modified April 4, 2006. Version 2.
Checksum: 1ED5D01D489288BD

FASTA42345,279
        10         20         30         40         50         60 
MDIDQYMTDL GRRARHASRA MARASTAAKN AALDAVARAI ERDAQVLKDA NARDVARARE 

        70         80         90        100        110        120 
KGLDAAFVDR LTLSDKALNT MVEGLRQVAS LADPIGEISN LKYRPSGIQV GQMRVPLGVI 

       130        140        150        160        170        180 
GIIYESRPNV TIDAAALCLK SGNATILRGG SEALESNTAL AKLIGEGLEA AGLPQDAVQV 

       190        200        210        220        230        240 
VATADRAAVG KLITMTEYVD VIVPRGGKSL IERLINEARV PMIKHLDGIC HVYVDDRADL 

       250        260        270        280        290        300 
AKALTVCDNA KTHRYGTCNT METLLVSSGV AAKLLPPLGK LYRDKQVELR VDAAARTVLA 

       310        320        330        340        350        360 
DAGVGPLVDA TEEDWHTEYL APVLAIKVVD GLDAAIEHIN HYGSHHTDAI VTEDHDRAMR 

       370        380        390        400        410        420 
FLREVDSASV MVNASTRFAD GFEFGLGAEI GISNDKLHAR GPVGLEGLTS LKYVVLGHGE 


GRQ 

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References

[1]"Complete sequence of chromosome 1 of Burkholderia sp. 383."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A., Richardson P.
Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 383.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000151 Genomic DNA. Translation: ABB07344.1. Different initiation.
RefSeqYP_367988.2. NC_007510.1.

3D structure databases

ProteinModelPortalQ39JM2.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ39JM2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3748927.
GenomeReviewsGene locus Bcep18194_A3743 in contig CP000151_GR.
KEGGbur:Bcep18194_A3743.
NMPDRfig|269483.3.peg.5384.
PATRIC19284789. VBIBurSp120713_1827.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0014.
HOGENOMHBG318080.
ProtClustDBPRK00197.

Enzyme and pathway databases

BioCycBSP36773:BCEP18194_A3743-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_BURS3
AccessionPrimary (citable) accession number: Q39JM2
Entry history
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: April 4, 2006
Last modified: January 25, 2012
This is version 50 of the entry and version 2 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