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Reviewed, UniProtKB/Swiss-Prot A8MFQ5 (PROA_ALKOO)

Last modified November 25, 2008. Version 10. 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: Clos_0127
OrganismAlkaliphilus oremlandii (strain OhILAs) (Clostridium oremlandii (strain OhILAs)) [Complete proteome] [HAMAP]
Taxonomic identifier350688 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeAlkaliphilus

Protein attributes

Sequence length413 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 – 413413Gamma-glutamyl phosphate reductase
PRO_1000060836

Sequences

Sequence LengthMass (Da)Tools
A8MFQ5-1 [UniParc].

Last modified December 4, 2007. Version 1.
Checksum: 1972F76F31D71DBF

FASTA41345,572
        10         20         30         40         50         60 
MSYLIEQCKR LKEASYALGM ISTKDKDEAL RLIIDSIKRN KDDILAENDK DVLAAKEKGT 

        70         80         90        100        110        120 
KDSLIDRLKL TEDRIQGILE GIETIIGLKD PIWRSNDVWT LENGLTISKM TVPLGVIGII 

       130        140        150        160        170        180 
YESRPNVTVD AFSLALKSGN CILLRGSSSA IHSNKMIVSA IKEGLRRSKV SEDIIELIED 

       190        200        210        220        230        240 
TDRNVVKEML TLNEYIDVII PRGGADLIRF VVDHATVPTI ETGIGNCHIY VDESANLENA 

       250        260        270        280        290        300 
IQIITNAKIQ RPGVCNACET TLIHEDIAPK FLPMLAAALK DKVELKGCPR TREIIQAAEA 

       310        320        330        340        350        360 
TDMDWAEEYL DYILAVKVVS NVDEAIGHIQ AYGTKHSEAI ITENYTNANY FLRRVDAAAV 

       370        380        390        400        410 
YVNASTRFTD GGAFGFGGEM GISTQKTHAR GPMGLNELVT MKYTVVGNGQ IRQ 

« Hide

References

[1]"Complete genome of Alkaliphilus oremlandii OhILAs."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Mikhailova N., Stolz J.F., Dawson A., Fisher E., Crable B., Perera E., Lisak J., Ranganathan M., Basu P., Richardson P.
Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000853 Genomic DNA. Translation: ABW17694.1.
RefSeqYP_001511690.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID5677906.
GenomeReviewsGene locus Clos_0127 in contig CP000853_GR.
KEGGaoe:Clos_0127.

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_ALKOO
AccessionPrimary (citable) accession number: A8MFQ5
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: December 4, 2007
Last modified: November 25, 2008
This is version 10 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