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Reviewed, UniProtKB/Swiss-Prot A6VMV2 (PROA_ACTSZ)

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: Asuc_0931
OrganismActinobacillus succinogenes (strain ATCC 55618 / 130Z) [Complete proteome] [HAMAP]
Taxonomic identifier339671 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeActinobacillus

Protein attributes

Sequence length416 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 – 416416Gamma-glutamyl phosphate reductase
PRO_1000072277

Sequences

Sequence LengthMass (Da)Tools
A6VMV2-1 [UniParc].

Last modified August 21, 2007. Version 1.
Checksum: D11013433856BC4E

FASTA41645,186
        10         20         30         40         50         60 
MTNLEVMGKA ARQAAFELSQ LSAGDKNYAL QMIAEQLESQ QQQILAANAR DIDEARINGL 

        70         80         90        100        110        120 
NDAIIDRLLL TPERLRGIAN DVRHVISLAD PVGKLIDGGI LDSGLKLERI RVPVGVIGTI 

       130        140        150        160        170        180 
YEARPNVTID VASLCLKTGN AVILRGGKET RHSNRILVEV VQNALEKAGL PKTAVQAITD 

       190        200        210        220        230        240 
PDRALVMELL KLDRYVDMII PRGGAGLHAL CKQHATIPVI IGGIGVCHTF VEQSADQNRA 

       250        260        270        280        290        300 
ISVIKNAKTQ RPSTCNTLET LLIQESIAHE FLPKLAAELP VKYYADKTAY SILHHAGAEV 

       310        320        330        340        350        360 
LAVTEDDLRK EWLCTNLNVV IVQDIEAAVA HIREYGSQHS EAILTESLQL ARRFVAQVDS 

       370        380        390        400        410 
AAVYVNASTR FTDGGQFGLG AEVAVSTQKL HARGPMGLEA LTTYKWVATG DYTVRS 

« Hide

References

[1]"Complete sequence of Actinobacillus succinogenes 130Z."
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Lowry S., Clum A., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Vieille C., Richardson P.
Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000746 Genomic DNA. Translation: ABR74299.1.
RefSeqYP_001344234.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID5348169.
GenomeReviewsGene locus Asuc_0931 in contig CP000746_GR.
KEGGasu:Asuc_0931.

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. 2 hits.
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_ACTSZ
AccessionPrimary (citable) accession number: A6VMV2
Entry history
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: August 21, 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