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Reviewed, UniProtKB/Swiss-Prot O67166 (PROA_AQUAE)

Last modified November 25, 2008. Version 62. 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: aq_1071
OrganismAquifex aeolicus [Complete proteome] [HAMAP]
Taxonomic identifier63363 [NCBI]
Taxonomic lineageBacteriaAquificaeAquificalesAquificaceaeAquifex

Protein attributes

Sequence length435 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 – 435435Gamma-glutamyl phosphate reductase
PRO_0000189684

Sequences

Sequence LengthMass (Da)Tools
O67166-1 [UniParc].

Last modified June 20, 2001. Version 2.
Checksum: BE6500C58A2B2D61

FASTA43549,119
        10         20         30         40         50         60 
MNYIEEKVNR ARSVLRELTS LKTSVKNETL LKVAELIDKN RDYIKEENRK DVEKAKEMGL 

        70         80         90        100        110        120 
RPAVVDRLVL NDKRIDGMVK VLKDVASLPD PVGEIIKMWN LPNGLKVGRM RVPLGVIFIV 

       130        140        150        160        170        180 
YESRPNVTIE ASSLCMKSSN AVILRGGKEA INSNKALVNL IKEACRETGF PEDAVQFIDR 

       190        200        210        220        230        240 
SEREIVWEIL KMEGKIDVAI PRGGESLIRA VVEHAKVPVI KHYKGVCNIY VDDEADLEKA 

       250        260        270        280        290        300 
YHIVYNAKVQ RPSVCNAVEN LVINRKILKE FFPKMAYYLG KAGVELRCDE ESLQVIKENP 

       310        320        330        340        350        360 
KLSFVNAKPA TEEDYYEEFL DLILAVKVVD DVDEAIAFIE KYGSKHSDAI ITENYTKAMK 

       370        380        390        400        410        420 
FLREVDSAAV YVNASTRFTD GNEFGLGAEM GISTDKIHAR GPMALEELTI PKFVILGEGQ 

       430 
VRDNFGVPEE WMKEF 

« Hide

References

[1]"The complete genome of the hyperthermophilic bacterium Aquifex aeolicus."
Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L., Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R., Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.
Nature 392:353-358(1998) [PubMed: 9537320] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: VF5.

Cross-references

Sequence databases

AE000657 Genomic DNA. Translation: AAC07119.1. Different initiation.
PIRC70392.
RefSeqNP_213729.1.

3D structure databases

HSSPHSSP built from PDB template 1O20 based on UniProtKB Q9WYC9.
ModBaseSearch...

Genome annotation databases

GeneID1193800.
GenomeReviewsGene locus aq_1071 in contig AE000657_GR.
KEGGaae:aq_1071.
NMPDRfig|224324.1.peg.744.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMO67166.

Enzyme and pathway databases

BioCycAAEO224324:AQ_1071-MON.

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_AQUAE
AccessionPrimary (citable) accession number: O67166
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: June 20, 2001
Last modified: November 25, 2008
This is version 62 of the entry and version 2 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