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Reviewed, UniProtKB/Swiss-Prot A8AKP4 (PROA_CITK8)

Last modified November 25, 2008. Version 12. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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: CKO_02952
OrganismCitrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696) [Complete proteome] [HAMAP]
Taxonomic identifier290338 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeCitrobacter

Protein attributes

Sequence length417 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

Catalytic activity

L-glutamate 5-semialdehyde + phosphate + NADP(+) = L-glutamyl 5-phosphate + NADPH.

Pathway

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

Subcellular location

CytoplasmBy similarity.

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 processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

proline biosynthetic process

Inferred from electronic annotation. Source: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: HAMAP

   Molecular functionNADP binding

Inferred from electronic annotation. Source: InterPro

glutamate-5-semialdehyde dehydrogenase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 417417Gamma-glutamyl phosphate reductase
PRO_1000049943

Sequences

Sequence LengthMass (Da)Tools
A8AKP4-1 [UniParc].

Last modified October 23, 2007. Version 1.
Checksum: B93B15BDEFE838D5

FASTA41744,559
        10         20         30         40         50         60 
MLEQMGIAAK AASYKLALLS SREKNRVLEK IADELEAQTE SILSANAQDV AEARENGLSE 

        70         80         90        100        110        120 
AMLDRLALTP ARLKAIADDV RQVCNLADPV GQVIDGGLLD SGLRLERRRV PLGVIGVIYE 

       130        140        150        160        170        180 
ARPNVTVDVA SLCLKTGNAA ILRGGKETYR TNAATVAVIQ QALEACGLPA GAVQAIDSPD 

       190        200        210        220        230        240 
RALVNEMLRM DKYIDMLIPR GGAGLHKLCR EQSTIPVITG GIGVCHIFVD DSAEIEPALK 

       250        260        270        280        290        300 
IIVNAKTQRP STCNTVETLL VHQDIAARFL PALSKQMAES GVTLHADDAA LAQLKSGPAN 

       310        320        330        340        350        360 
VVAVKAEEYD DEFLSLDLNV KIVAGLDDAI AHIREHGTQH SDAILTRTLR NADRFVNEVD 

       370        380        390        400        410 
SSAVYVNAST RFTDGGQFGL GAEVAVSTQK LHARGPMGLE ALTTYKWIGI GDDTIRA 

« Hide

References

[1]McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S., Latreille P., Courtney L., Wang C., Pepin K., Bhonagiri V., Nash W., Johnson M., Thiruvilangam P., Wilson R.
Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000822 Genomic DNA. Translation: ABV14057.1.
RefSeqYP_001454493.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID5581896.
GenomeReviewsGene locus CKO_02952 in contig CP000822_GR.
KEGGcko:CKO_02952.

Organism-specific databases

CMRSearch...

Family and domain databases

HAMAPMF_00412.
[Tree]
InterProIPR016163. Ald_DHase_C.
IPR016162. Ald_DHase_N.
IPR015590. Aldehyde_DHase.
IPR000965. Gglut_pp_reduct.
IPR012134. Glu-5-SA_DHase.
[Graphical view]
Gene3DG3DSA:3.40.309.10. Aldehyde_dehydrogenase_C. 1 hit.
G3DSA:3.40.605.10. Aldehyde_dehydrogenase_N. 1 hit.
PANTHERPTHR11063:SF1. GSA_DH. 1 hit.
PfamPF00171. Aldedh. 1 hit.
[Graphical view]
PIRSFPIRSF000151. GPR. 1 hit.
TIGRFAMsTIGR00407. proA. 1 hit.
PROSITEPS01223. PROA. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePROA_CITK8
AccessionPrimary (citable) accession number: A8AKP4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 23, 2007
Last modified: November 25, 2008
This is version 12 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents