Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q2SZ88 (PROA_BURTA) 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:BTH_I1214
OrganismBurkholderia thailandensis (strain E264 / ATCC 700388 / DSM 13276 / CIP 106301) [Complete proteome] [HAMAP]
Taxonomic identifier271848 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiapseudomallei group

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.

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_0000252566

Sequences

Sequence LengthMass (Da)Tools
Q2SZ88 [UniParc].

Last modified January 24, 2006. Version 1.
Checksum: BFC044A712674A8C

FASTA42345,309
        10         20         30         40         50         60 
MDIDQYMTDV GRRARRASRS IARASTAAKN AALEAVARAI ERDAGALKAA NARDVARAKD 

        70         80         90        100        110        120 
KGLDAAFVDR LTLSDKALKT MVEGLRQVAT LPDPIGEMSN LKYRPSGIQV GQMRVPLGVI 

       130        140        150        160        170        180 
GIIYESRPNV TIDAAALCLK SGNATILRGG SEALESNTAL AKLIGEGLAE AGLPQDTVQV 

       190        200        210        220        230        240 
VETADRAAVG RLITMTEYVD VIVPRGGKSL IERLINEARV PMIKHLDGIC HVYVDDRASV 

       250        260        270        280        290        300 
TKALTVCDNA KTHRYGTCNT METLLVARGI APAVLSPLGR LYREKGVELR VDADARAVLE 

       310        320        330        340        350        360 
AAGVGPLVDA TDEDWRTEYL APVLAIKIVD GIDAAIEHIN EYGSHHTDAI VTEDHDRAMR 

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


GRQ 

« Hide

References

[1]"Bacterial genome adaptation to niches: divergence of the potential virulence genes in three Burkholderia species of different survival strategies."
Kim H.S., Schell M.A., Yu Y., Ulrich R.L., Sarria S.H., Nierman W.C., DeShazer D.
BMC Genomics 6:174-174(2005) [PubMed: 16336651] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: E264 / ATCC 700388 / DSM 13276 / CIP 106301.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000086 Genomic DNA. Translation: ABC38329.1.
RefSeqYP_441761.1. NC_007651.1.

3D structure databases

HSSPHSSP built from PDB template 2H5G based on UniProtKB P54886.
ProteinModelPortalQ2SZ88.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ2SZ88.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3849726.
GenomeReviewsGene locus BTH_I1214 in contig CP000086_GR.
KEGGbte:BTH_I1214.
PATRIC19305322. VBIBurTha36512_3970.
TIGRBTH_I1214.

Phylogenomic databases

eggNOGCOG0014.
HOGENOMHBG318080.
OMAQYPAACN.
ProtClustDBPRK00197.

Enzyme and pathway databases

BioCycBTHA271848:BTH_I1214-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_BURTA
AccessionPrimary (citable) accession number: Q2SZ88
Entry history
Integrated into UniProtKB/Swiss-Prot: October 17, 2006
Last sequence update: January 24, 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