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Reviewed, UniProtKB/Swiss-Prot Q1IS80 (PROA_ACIBL)

Last modified November 25, 2008. Version 19. 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: Acid345_1268
OrganismAcidobacteria bacterium (strain Ellin345) [Complete proteome] [HAMAP]
Taxonomic identifier204669 [NCBI]
Taxonomic lineageBacteriaAcidobacteriaAcidobacterialesAcidobacteriaceae

Protein attributes

Sequence length409 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 – 409409Gamma-glutamyl phosphate reductase
PRO_0000252561

Sequences

Sequence LengthMass (Da)Tools
Q1IS80-1 [UniParc].

Last modified June 13, 2006. Version 1.
Checksum: 7F51E3D1C2D9298A

FASTA40943,990
        10         20         30         40         50         60 
MTTREKLEAA RRAAPVVAEL STESKNALLL ALARTIDERT EEILAANRAD LEASGLDGSL 

        70         80         90        100        110        120 
RDRLLLTPER IATMAEGLRE VAALADPVGE TLAEWERPNG LRIRKVRVPL GVVAIIYEAR 

       130        140        150        160        170        180 
PNVTIDVIGL ALKSGNAVVL RGGKEAVRSN ECLVKIAGAT PGMPDGAIQL LDASNRESVQ 

       190        200        210        220        230        240 
QLMKARGLVD VIVPRGGAGL IQFVVENSTV PVIETGAGNC HIFVDESANL DMADRIVINA 

       250        260        270        280        290        300 
KTQRPSVCNA AEKLLVHRAI AKEYVPRIVK LLLDHGVEVR GDAETLALAQ GMQVAEATSA 

       310        320        330        340        350        360 
DWDEEYLRLC MAVKVVADVD EAIAHINQHS TKHSESIITA NDAHARRFLR AADSAAVYWN 

       370        380        390        400 
ASTRFTDGAE FGFGAEMGIS TQKLHCRGPF ALAELTSSKY EVIGSGQVR 

« Hide

References

[1]"Complete sequence of Acidobacteria bacterium Ellin345."
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., Brettin T., Bruce D., Han C., Tapia R., Kiss H., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Kuske C., Janssen P.H., Richardson P.
Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000360 Genomic DNA. Translation: ABF40270.1.
RefSeqYP_590344.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID4073238.
GenomeReviewsGene locus Acid345_1268 in contig CP000360_GR.
KEGGaba:Acid345_1268.
NMPDRfig|204669.6.peg.1255.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ1IS80.

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_ACIBL
AccessionPrimary (citable) accession number: Q1IS80
Entry history
Integrated into UniProtKB/Swiss-Prot: October 17, 2006
Last sequence update: June 13, 2006
Last modified: November 25, 2008
This is version 19 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