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B0UMS9 (PROA_METS4) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 33. 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:M446_4218
OrganismMethylobacterium sp. (strain 4-46) [Complete proteome] [HAMAP]
Taxonomic identifier426117 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesMethylobacteriaceaeMethylobacterium

Protein attributes

Sequence length431 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 – 431431Gamma-glutamyl phosphate reductase HAMAP MF_00412
PRO_0000340895

Sequences

Sequence LengthMass (Da)Tools
B0UMS9 [UniParc].

Last modified April 8, 2008. Version 1.
Checksum: 0B4F622D081CCA6D

FASTA43144,656
        10         20         30         40         50         60 
MSVLSLKPRA GADDVDALMR EIGRRARAAS RRMALVPARA KDMALRAAAA AIRDAAPVIL 

        70         80         90        100        110        120 
EANAADLAEA RGANLPAATL DRLALTPGRV EAIAAAVEAI AGLPDPVGRQ LAAFERPNGL 

       130        140        150        160        170        180 
AIERISTPLG VVGVIYESRP NVTADAGALC LKAGNAAVLR AGSESLRSAA AIARAMADGL 

       190        200        210        220        230        240 
AAQGLPAEAI QLVPTRDRAA VGAMLAGLDG CIDVIVPRGG KSLVARVQSE ARVPVFAHLE 

       250        260        270        280        290        300 
GICHVFVHAR ADLAMAREIL RNSKLRRTGI CGAAETLLVD RACAGTHLAP LVADLLEAGC 

       310        320        330        340        350        360 
AVRGDAETQA VDPRVTPATE ADWRTEYLDA VIAVRVVDGL DAAIDHVETY GSHHTDAIVT 

       370        380        390        400        410        420 
ADEAAAERFL AEVDSAIVVH NASTQFADGG EFGFGAEIGI ATGRMHARGP VGVEQLTTFK 

       430 
YRVHGSGQVR P 

« Hide

References

[1]"Complete sequence of chromosome of Methylobacterium sp. 4-46."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L. expand/collapse author list , Kyrpides N., Ivanova N., Marx C.J., Richardson P.
Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 4-46.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000943 Genomic DNA. Translation: ACA18567.1.
RefSeqYP_001771001.1. NC_010511.1.

3D structure databases

ProteinModelPortalB0UMS9.
ModBaseSearch...

Protein-protein interaction databases

STRINGB0UMS9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6135420.
GenomeReviewsGene locus M446_4218 in contig CP000943_GR.
KEGGmet:M446_4218.
PATRIC22589604. VBIMetSp32184_4136.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG318080.
OMAYGICGAM.
ProtClustDBPRK00197.

Enzyme and pathway databases

BioCycMSP409:M446_4218-MONOMER.

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.
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. 1 hit.
[Graphical view]
PIRSFPIRSF000151. GPR. 1 hit.
SUPFAMSSF53720. Aldehyde_DH/Histidinol_DH. 1 hit.
TIGRFAMsTIGR00407. ProA. 1 hit.
PROSITEPS01223. PROA. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePROA_METS4
AccessionPrimary (citable) accession number: B0UMS9
Entry history
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: April 8, 2008
Last modified: January 25, 2012
This is version 33 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