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A2SCE2 (PROA_METPP) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 47. 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:Mpe_A0269
OrganismMethylibium petroleiphilum (strain PM1) [Complete proteome] [HAMAP]
Taxonomic identifier420662 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesMethylibium

Protein attributes

Sequence length429 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 – 429429Gamma-glutamyl phosphate reductase HAMAP MF_00412
PRO_0000340893

Sequences

Sequence LengthMass (Da)Tools
A2SCE2 [UniParc].

Last modified March 6, 2007. Version 1.
Checksum: 9012649954989C42

FASTA42944,948
        10         20         30         40         50         60 
MNAPDATPVI ALMDRLGSAA RSASTAMAAA STAAKNAALL ALAREIRAGA ARLAAENARD 

        70         80         90        100        110        120 
LDVATRAGLA APMVDRLRLT DKVIALMAEG CEQVAALPDP IGEMTNLRRR PSGITVGQMR 

       130        140        150        160        170        180 
VPLGVFGMVY ESRPNVTIDA ASLAIKSGNA AILRGGSEAL HSNTALMALV VRALAEAGLP 

       190        200        210        220        230        240 
GDAVQLVPTT DRAAVGRLIA MPQYVDVIIP RGGKGLIERI AAEATVPVIK HLDGNCHVYV 

       250        260        270        280        290        300 
DAGADLDLAV RVTDNAKTQK YSPCNAAESL LVHRDVAAAF LPRIGAVFAA KGVEMRCGPR 

       310        320        330        340        350        360 
AKALLAAVPG AKLVDATEAD WAEEYLAPVI SIKLVDSLDE AIARINRYGS HHTDAILTTN 

       370        380        390        400        410        420 
HPNAMRFLRE VDSASVMVNA STRFADGFEF GLGAEIGIST DKFHARGPVG LEGLTSMKWV 


VFGQGEVRT 

« Hide

References

[1]"Whole-genome analysis of the methyl tert-butyl ether-degrading beta-proteobacterium Methylibium petroleiphilum PM1."
Kane S.R., Chakicherla A.Y., Chain P.S.G., Schmidt R., Shin M.W., Legler T.C., Scow K.M., Larimer F.W., Lucas S.M., Richardson P.M., Hristova K.R.
J. Bacteriol. 189:1931-1945(2007) [PubMed: 17158667] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PM1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000555 Genomic DNA. Translation: ABM93231.1.
RefSeqYP_001019466.1. NC_008825.1.

3D structure databases

ProteinModelPortalA2SCE2.
ModBaseSearch...

Protein-protein interaction databases

STRINGA2SCE2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4786938.
GenomeReviewsGene locus Mpe_A0269 in contig CP000555_GR.
KEGGmpt:Mpe_A0269.
NMPDRfig|279263.3.peg.185.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0014.
HOGENOMHBG318080.
OMAYGICGAM.
PhylomeDBA2SCE2.
ProtClustDBPRK00197.

Enzyme and pathway databases

BioCycMPET420662:MPE_A0269-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. 2 hits.
[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_METPP
AccessionPrimary (citable) accession number: A2SCE2
Entry history
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: March 6, 2007
Last modified: November 16, 2011
This is version 47 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