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Q8PYP2 (PROA_METMA) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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:MM_0819
OrganismMethanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88) (Methanosarcina frisia) [Complete proteome] [HAMAP]
Taxonomic identifier192952 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanomicrobiaMethanosarcinalesMethanosarcinaceaeMethanosarcina

Protein attributes

Sequence length447 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. 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 – 447447Gamma-glutamyl phosphate reductase HAMAP MF_00412
PRO_0000189822

Sequences

Sequence LengthMass (Da)Tools
Q8PYP2 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: 6436403AF138FD4E

FASTA44749,255
        10         20         30         40         50         60 
MANDIESKVI KAKKASIELA SVSSEVKNRA LEAMAEALDK ERKIILEANL KDLEYAAQLK 

        70         80         90        100        110        120 
KAGKLTQALV DRLKVTDSKV DGMIAGIRDV IKLKDPVGET LSTLELDDDL ILYQVSCPIG 

       130        140        150        160        170        180 
LIGVIFESRP DVVPQVMSLC LKSGNATIFK GGSEARESNR TIFDILVRAI ESTGGMPEGA 

       190        200        210        220        230        240 
FQLMETREEI MSLLSLDAYV DLLIPRGSNE FVKFIQDNTK IPVLGHTSGI CHIYVDEFAD 

       250        260        270        280        290        300 
PDTAWQVCFD AKVQYPAVCN AIETLLVNRN IAEVFLPKMA EMYLKAGVEL RCDEGSYSLL 

       310        320        330        340        350        360 
SEKGLSPLSR ATDEDWSLEY NDLILSIKLV DTIKEAVDHI NTFGSHHTDG IITENASRRK 

       370        380        390        400        410        420 
EFIGLVDSSS VMVNASTRFA DGYRYGKGAE VGISTNKIHS RGPVGMEGLL IYKYILMGKG 

       430        440 
QVVADYAGKN AKPYTHRKLD LKFEDVN 

« Hide

References

[1]"The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea."
Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A., Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C., Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S., Bhattacharyya A., Lykidis A., Overbeek R. expand/collapse author list , Klenk H.-P., Gunsalus R.P., Fritz H.-J., Gottschalk G.
J. Mol. Microbiol. Biotechnol. 4:453-461(2002) [PubMed: 12125824] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE008384 Genomic DNA. Translation: AAM30515.1.
RefSeqNP_632843.1. NC_003901.1.

3D structure databases

ProteinModelPortalQ8PYP2.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1479161.
GenomeReviewsGene locus MM_0819 in contig AE008384_GR.
KEGGmma:MM_0819.
NMPDRfig|192952.1.peg.819.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG318080.
OMAQYPAACN.
PhylomeDBQ8PYP2.
ProtClustDBPRK00197.

Enzyme and pathway databases

BioCycMMAZ192952:MM0819-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.
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.
PfamPF00171. Aldedh. 1 hit.
[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_METMA
AccessionPrimary (citable) accession number: Q8PYP2
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 2002
Last sequence update: October 1, 2002
Last modified: December 14, 2011
This is version 76 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