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B9MH63 (PROA_ACIET) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 27. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:Dtpsy_3262
OrganismAcidovorax ebreus (strain TPSY) (Diaphorobacter sp. (strain TPSY)) [Complete proteome] [HAMAP]
Taxonomic identifier535289 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesComamonadaceaeAcidovorax

Protein attributes

Sequence length426 AA.
Sequence statusComplete.
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. HAMAP MF_00412

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 HAMAP MF_00412.

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 processproline biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionNADP binding

Inferred from electronic annotation. Source: InterPro

glutamate-5-semialdehyde dehydrogenase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 426426Gamma-glutamyl phosphate reductase HAMAP MF_00412
PRO_1000193598

Sequences

Sequence LengthMass (Da)Tools
B9MH63 [UniParc].

Last modified March 24, 2009. Version 1.
Checksum: 9BDD1FAE2DB5FCEB

FASTA42645,274
        10         20         30         40         50         60 
MNALNIAEYT HTLGLQAKTA SAQMARAPAA IKNKALLALA RLLRQNVDAL QGDNARDLER 

        70         80         90        100        110        120 
ARAAGLAEPM VDRLKLTPKV LETCAQGCEQ LAAMPDIIGE IQGMKQQPSG IRVGQMRVPI 

       130        140        150        160        170        180 
GVFGMIYESR PNVTIEAASL SIKSGNACIL RGGSEAIDSN KALARLVAQA LAEAGLPEHG 

       190        200        210        220        230        240 
VQLVQTTDRA AVGQLIAMPQ YVDVIIPRGG KGLIERISAE AKVPVIKHLD GNCHTYVDDP 

       250        260        270        280        290        300 
CDIVMAVQVA DNAKTQKYSP CNASEGLLVA RGVAAQFLPQ IGAVYAAKGV EMRGCPEALA 

       310        320        330        340        350        360 
ILRAVPGVQL AEATEADWSE EYLAPIISVK VVAGVDEAIA HINRYGSHHT DAILTRDHMH 

       370        380        390        400        410        420 
AQQFLRDVDS ASVMVNASTR FADGFEYGLG AEIGISTDKF HARGPVGIEG LTSLKWVVLG 


EGEVRT 

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References

[1]"Complete sequence of Diaphorobacter sp. TPSY."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Coates J.D.
Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: TPSY.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001392 Genomic DNA. Translation: ACM34691.1.
RefSeqYP_002554691.1. NC_011992.1.

3D structure databases

ProteinModelPortalB9MH63.
ModBaseSearch...

Protein-protein interaction databases

STRINGB9MH63.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID7383821.
GenomeReviewsGene locus Dtpsy_3262 in contig CP001392_GR.
KEGGdia:Dtpsy_3262.
PATRIC21783699. VBIDiaSp55748_3304.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAYGICGAM.
ProtClustDBPRK00197.

Family and domain databases

HAMAPMF_00412. ProA.
[Tree]
InterProIPR016161. Ald_DH/histidinol_DH.
IPR016163. Ald_DH_C.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH_dom.
IPR000965. G-glutamylP_reductase.
IPR020593. G-glutamylP_reductase_CS.
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. 2 hits.
KOK00147.
PANTHERPTHR11063:SF1. GSA_DH. 1 hit.
PfamPF00171. Aldedh. 2 hits.
[Graphical view]
PIRSFPIRSF000151. GPR. 1 hit.
SUPFAMSSF53720. Aldehyde_DH/Histidinol_DH. 1 hit.
TIGRFAMsTIGR00407. ProA. 1 hit.
PROSITEPS01223. PROA. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePROA_ACIET
AccessionPrimary (citable) accession number: B9MH63
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 24, 2009
Last modified: January 25, 2012
This is version 27 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families