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Q12TF9 (PROA_METBU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 46. 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:Mbur_2416
OrganismMethanococcoides burtonii (strain DSM 6242) [Complete proteome] [HAMAP]
Taxonomic identifier259564 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanomicrobiaMethanosarcinalesMethanosarcinaceaeMethanococcoides

Protein attributes

Sequence length449 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 – 449449Gamma-glutamyl phosphate reductase HAMAP MF_00412
PRO_1000049963

Sequences

Sequence LengthMass (Da)Tools
Q12TF9 [UniParc].

Last modified August 22, 2006. Version 1.
Checksum: C5A2E1B00FACE5FC

FASTA44949,610
        10         20         30         40         50         60 
MATDIEQKVM EAKMASIVLA SVDTQTKDNA LEAMAKALDA NRNKILEANK ADLEEAERMK 

        70         80         90        100        110        120 
NEGKLSQALV DRLKVTDPKI DGMISGIRDV IKLEDPSGRT INTLELDKGL ELYQVSSPIG 

       130        140        150        160        170        180 
LIGVIFESRP DVVPQVMSLC LKSGNATVFK GGSEALNSNR VIFNILVEAL EDTPGIPKGA 

       190        200        210        220        230        240 
FQLMETREEV MDILALDEYI DLLIPRGSND FVKFIQDNTK ISVLGHADGI CHVYVDTNAD 

       250        260        270        280        290        300 
LNKAYDVCFD SKVQYPAVCN AMETLLINRE IAEEFLPEMV RRYEEVGVEL RFDEGSYAIA 

       310        320        330        340        350        360 
EKLGSANIAK ATEDDWKTEY NDFILSIKLV DSIEEAIDHI NKYGSHHTDA IITENKTKRK 

       370        380        390        400        410        420 
QFIALVDSSS VMVNASTRFA DGFRYGKGAE VGISTNKIHA RGPVGMEGLV IYKYVLLGNG 

       430        440 
DKVATYAGDT PRPFTHKELD SKLSDIINE 

« Hide

References

[1]"Complete sequence of Methanococcoides burtonii DSM 6242."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Kadner K., Aerts A., Dehal P., Pitluck S., Martinez M., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Anderson I., Franzmann P., Thomas T., Saunders N., Cavicchioli R., Sowers K., Richardson P.
Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 6242.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000300 Genomic DNA. Translation: ABE53267.1.
RefSeqYP_567017.1. NC_007955.1.

3D structure databases

ProteinModelPortalQ12TF9.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ12TF9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3999006.
GenomeReviewsGene locus Mbur_2416 in contig CP000300_GR.
KEGGmbu:Mbur_2416.
NMPDRfig|259564.8.peg.2320.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGarNOG05521.
HOGENOMHBG318080.
OMAQYPAACN.
PhylomeDBQ12TF9.
ProtClustDBPRK00197.

Enzyme and pathway databases

BioCycMBUR259564:MBUR_2416-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_METBU
AccessionPrimary (citable) accession number: Q12TF9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: August 22, 2006
Last modified: January 25, 2012
This is version 46 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