Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot A1KAH8 (PROA_AZOSB)

Last modified June 16, 2009. Version 23. 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: azo3218
OrganismAzoarcus sp. (strain BH72) [Complete proteome] [HAMAP]
Taxonomic identifier62928 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaRhodocyclalesRhodocyclaceaeAzoarcus

Protein attributes

Sequence length419 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 By similarity.

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.

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: UniProtKB-SubCell

   Molecular functionNADP or NADPH 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 – 419419Gamma-glutamyl phosphate reductase HAMAP MF_00412
PRO_0000340871

Sequences

Sequence LengthMass (Da)Tools
A1KAH8-1 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: 28F270332CA1E276

FASTA41944,257
        10         20         30         40         50         60 
MQTVGREARA ASRTLAAAST DAKNSALVAM AQAIRDSRDA LLAANAADLA EARAAGLDEA 

        70         80         90        100        110        120 
LIDRLTLSAK GVEGMAAGLE QVAALPDPVG EITDVKRRPS GIQVGKMRVP LGVVGIIYEA 

       130        140        150        160        170        180 
RPNVTADAAA LCLKSGNAAI LRGGKEALRS NQAIASCVRT GLAAAGLPQT AVQVLETTDR 

       190        200        210        220        230        240 
AAVGALITMP EFVDVIVPRG GKGLIERISS EARVPVIKHL DGNCHVYVDD HADPAKVLPI 

       250        260        270        280        290        300 
VENAKTQRYG TCNTTESLLV ARAVAPRFLS DIGRMLAARN VEMRACPEAL ALLREAGIEG 

       310        320        330        340        350        360 
ARLSPATEQD WHEEYLAPII AIRVVAGLDE AIAHINTYSS GHTEAILTEH YTHAMRFLRE 

       370        380        390        400        410 
VDSASVMVNA STRFADGFEY GLGAEIGIST DKIHARGPVG LEGLTSQKWI VFGNGEIRR 

« Hide

References

[1]"Complete genome of the mutualistic, N2-fixing grass endophyte Azoarcus sp. strain BH72."
Krause A., Ramakumar A., Bartels D., Battistoni F., Bekel T., Boch J., Boehm M., Friedrich F., Hurek T., Krause L., Linke B., McHardy A.C., Sarkar A., Schneiker S., Syed A.A., Thauer R., Vorhoelter F.-J., Weidner S. expand/collapse author list , Puehler A., Reinhold-Hurek B., Kaiser O., Goesmann A.
Nat. Biotechnol. 24:1385-1391(2006) [PubMed: 17057704] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

AM406670 Genomic DNA. Translation: CAL95834.1.
RefSeqYP_934720.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID4609012.
GenomeReviewsGene locus azo3218 in contig AM406670_GR.
KEGGazo:azo3218.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAA1KAH8. FDTEWLD.

Family and domain databases

HAMAPMF_00412.
[Tree]
InterProIPR016163. Ald_DH_C.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH.
IPR000965. Gglut_pp_reduct.
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. 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_AZOSB
AccessionPrimary (citable) accession number: A1KAH8
Entry history
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: February 6, 2007
Last modified: June 16, 2009
This is version 23 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