Skip Header

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

A6LE74 (PROA_PARD8) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 42. 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:BDI_2257
OrganismParabacteroides distasonis (strain ATCC 8503 / DSM 20701 / NCTC 11152) [Complete proteome] [HAMAP]
Taxonomic identifier435591 [NCBI]
Taxonomic lineageBacteriaBacteroidetesBacteroidiaBacteroidalesPorphyromonadaceaeParabacteroides

Protein attributes

Sequence length415 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 – 415415Gamma-glutamyl phosphate reductase HAMAP MF_00412
PRO_0000340900

Sequences

Sequence LengthMass (Da)Tools
A6LE74 [UniParc].

Last modified July 24, 2007. Version 1.
Checksum: 99DF1DED71ECCC1C

FASTA41545,817
        10         20         30         40         50         60 
MNVKDMLRQA SDAAKQLITL SDQTIIGILK ETAQVLRTHT EEVLAANRQD LERMDPANPK 

        70         80         90        100        110        120 
YDRLKLTEER LQGIAADMEN VSTLPSPLNK VLSETIRPNG MVIRKVTVPF GVIGVIYEAR 

       130        140        150        160        170        180 
PNVTFDVFSL CFRSGNACVL KGGSDADFSN RALVRIIHSV LERQGINPAV CTLLPPDREA 

       190        200        210        220        230        240 
TAELLGAVGL VDLIIPRGSS SLIHFVREHA KVPVIETGAG ICHTYFDRSG DKGKGREIVN 

       250        260        270        280        290        300 
NAKTRRVSVC NALDCLIIHR ERLSDLPYIC EKLPDSNVII YADEPAYAAL SEHYPETLLQ 

       310        320        330        340        350        360 
QANENSFGTE FLDYKMSIRT VSSLDEVLSH IARYSSKHSE SIISEDPETI RRFQQLVDAA 

       370        380        390        400        410 
CVYANVSTAF TDGAQFGFGA EIGISTQKLH ARGPMALPEL TTYKYIIEGD GQTRI 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000140 Genomic DNA. Translation: ABR43988.1.
RefSeqYP_001303610.1. NC_009615.1.

3D structure databases

ProteinModelPortalA6LE74.
ModBaseSearch...

Protein-protein interaction databases

STRINGA6LE74.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5307406.
GenomeReviewsGene locus BDI_2257 in contig CP000140_GR.
KEGGpdi:BDI_2257.
PATRIC22847722. VBIParDis29947_2242.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0014.
HOGENOMHBG318080.
OMAYGICGAM.
ProtClustDBPRK00197.

Enzyme and pathway databases

BioCycPDIS435591:BDI_2257-MONOMER.

Family and domain databases

HAMAPMF_00412. ProA.
[Tree]
InterProIPR016161. Ald_DH/histidinol_DH.
IPR016163. Ald_DH_C.
IPR016162. Ald_DH_N.
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.
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_PARD8
AccessionPrimary (citable) accession number: A6LE74
Entry history
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: July 24, 2007
Last modified: December 14, 2011
This is version 42 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