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Reviewed, UniProtKB/Swiss-Prot A8EVN0 (PROA_ARCB4)

Last modified November 25, 2008. Version 13. 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: Abu_1757
OrganismArcobacter butzleri (strain RM4018) [Complete proteome] [HAMAP]
Taxonomic identifier367737 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesCampylobacteraceaeArcobacter

Protein attributes

Sequence length412 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 – 412412Gamma-glutamyl phosphate reductase
PRO_1000060837

Sequences

Sequence LengthMass (Da)Tools
A8EVN0-1 [UniParc].

Last modified November 13, 2007. Version 1.
Checksum: 1DB0933298630615

FASTA41245,081
        10         20         30         40         50         60 
MQEFLQEAKN SSRIIANLGS AQKNRVLNEM ADALIEHSSF ILSHNQKDMN DAKLNNLNDA 

        70         80         90        100        110        120 
LQDRLLLTEK RIQDMAIAIR QIASQQDPLG KILNGWVTKD GLNIQKVSIP IGVIGIIYES 

       130        140        150        160        170        180 
RPNVTSDTAA LCFKSGNVCV LKGGKEAENS NKAIATILRE VLRKNNLPEY AISLLPDSSR 

       190        200        210        220        230        240 
EGVAKLIKQD KYVDLIVPRG GEALIRFVSE NSSIPVIKHD KGICHIFIDQ DANITKIFDI 

       250        260        270        280        290        300 
VVNAKCQKPS ACNSIETLLI HTNIAALILS GLVETLSLHG TILKGCPETL QHINAIPATL 

       310        320        330        340        350        360 
EDFDTEYLAN VLNIKIVANV DEAITHIQRH GSGHSESILS ENYTTINKFL SEVDAACVYA 

       370        380        390        400        410 
NASTRFTDGG EFGLGAEVGI STNKLHSRGP MGIEDLTTFK YKIYGQGQIR KG 

« Hide

References

[1]"The complete genome sequence and analysis of the Epsilonproteobacterium Arcobacter butzleri."
Miller W.G., Parker C.T., Rubenfield M., Mendz G.L., Woesten M.M.S.M., Ussery D.W., Stolz J.F., Binnewies T.T., Hallin P.F., Wang G., Malek J.A., Rogosin A., Stanker L.H., Mandrell R.E.
PLoS ONE 2:E1358-E1358(2007) [PubMed: 18159241] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000361 Genomic DNA. Translation: ABV68003.1.
RefSeqYP_001490673.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID5624120.
GenomeReviewsGene locus Abu_1757 in contig CP000361_GR.
KEGGabu:Abu_1757.

Organism-specific databases

CMRSearch...

Family and domain databases

HAMAPMF_00412.
[Tree]
InterProIPR016163. Ald_DHase_C.
IPR016162. Ald_DHase_N.
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.
PIRSFPIRSF000151. GPR. 1 hit.
TIGRFAMsTIGR00407. proA. 1 hit.
PROSITEPS01223. PROA. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePROA_ARCB4
AccessionPrimary (citable) accession number: A8EVN0
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: November 13, 2007
Last modified: November 25, 2008
This is version 13 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