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B1J0Z1 (PROA_ECOLC) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 46. 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:EcolC_3338
OrganismEscherichia coli (strain ATCC 8739 / DSM 1576 / Crooks) [Complete proteome] [HAMAP]
Taxonomic identifier481805 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length417 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-Rule MF_00412

Catalytic activity

L-glutamate 5-semialdehyde + phosphate + NADP+ = L-glutamyl 5-phosphate + NADPH. HAMAP-Rule MF_00412

Pathway

Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-glutamate: step 2/2. HAMAP-Rule MF_00412

Subcellular location

Cytoplasm By similarity HAMAP-Rule 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_processL-proline biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   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: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 417417Gamma-glutamyl phosphate reductase HAMAP-Rule MF_00412
PRO_1000080483

Sequences

Sequence LengthMass (Da)Tools
B1J0Z1 [UniParc].

Last modified April 29, 2008. Version 1.
Checksum: D9A4E3418EFEB488

FASTA41744,630
        10         20         30         40         50         60 
MLEQMGIAAK QASYKLAQLS SREKNRVLEK IADELEAQSE IILNANAQDV ADARANGLSE 

        70         80         90        100        110        120 
AMLDRLALTP ARLKGIADDV RQVCNLADPV GQVIDGGVLD SGLRLERRRV PLGVIGVIYE 

       130        140        150        160        170        180 
ARPNVTVDVA SLCLKTGNAV ILRGGKETCR TNAATVAVIQ DALKSCGLPA GAVQAIDNPD 

       190        200        210        220        230        240 
RALVSEMLRM DKYIDMLIPR GGAGLHKLCR EQSTIPVITG GIGVCHIYVD ESVEIAEALK 

       250        260        270        280        290        300 
VIVNAKTQRP STCNTVETLL VNKNIADSFL PALSKQMAES GVTLHADAAA LAQLQAGPAK 

       310        320        330        340        350        360 
VVAVKAEEYD DEFLSLDLNV KIVSDLDDAI AHIREHGTQH SDAILTRDMR NAQRFVNEVD 

       370        380        390        400        410 
SSAVYVNAST RFTDGGQFGL GAEVAVSTQK LHARGPMGLE ALTTYKWIGI GDYTIRA 

« Hide

References

[1]"Complete sequence of Escherichia coli C str. ATCC 8739."
Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L. expand/collapse author list , Kyrpides N., Mikhailova N., Ingram L., Richardson P.
Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 8739 / DSM 1576 / Crooks.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000946 Genomic DNA. Translation: ACA78959.1.
RefSeqYP_001726286.1. NC_010468.1.

3D structure databases

ProteinModelPortalB1J0Z1.
SMRB1J0Z1. Positions 16-416.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING481805.EcolC_3338.

Proteomic databases

PRIDEB1J0Z1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACA78959; ACA78959; EcolC_3338.
GeneID6067335.
KEGGecl:EcolC_3338.
PATRIC18229730. VBIEscCol82905_3566.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0014.
HOGENOMHOG000246356.
KOK00147.
OMACNAIETL.
OrthoDBEOG6FFSCX.
ProtClustDBPRK00197.

Enzyme and pathway databases

BioCycECOL481805:GI3G-3412-MONOMER.
UniPathwayUPA00098; UER00360.

Family and domain databases

Gene3D3.40.309.10. 1 hit.
3.40.605.10. 2 hits.
HAMAPMF_00412. ProA.
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]
PANTHERPTHR11063:SF1. PTHR11063:SF1. 1 hit.
PfamPF00171. Aldedh. 1 hit.
[Graphical view]
PIRSFPIRSF000151. GPR. 1 hit.
SUPFAMSSF53720. SSF53720. 1 hit.
TIGRFAMsTIGR00407. proA. 1 hit.
PROSITEPS01223. PROA. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePROA_ECOLC
AccessionPrimary (citable) accession number: B1J0Z1
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: April 29, 2008
Last modified: February 19, 2014
This is version 46 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways