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A1AVH0 (PROA_RUTMC) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 44. 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:Rmag_0133
OrganismRuthia magnifica subsp. Calyptogena magnifica [Complete proteome] [HAMAP]
Taxonomic identifier413404 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriasulfur-oxidizing symbionts

Protein attributes

Sequence length419 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 – 419419Gamma-glutamyl phosphate reductase HAMAP MF_00412
PRO_1000080490

Sequences

Sequence LengthMass (Da)Tools
A1AVH0 [UniParc].

Last modified January 23, 2007. Version 1.
Checksum: 1EBFFC5F0EB4C38E

FASTA41945,536
        10         20         30         40         50         60 
MDSIKNLIVT LGENAKNAAK TLRCATTVAK NNTLINIASQ IDQNRASIFK ANNQDLVNGK 

        70         80         90        100        110        120 
NKGLETTLLD RLMLDEERLN GVIESLNQII NLPDPIGEIT DLKYQPSGIQ VGKMRVPLGV 

       130        140        150        160        170        180 
LGIIYESRPN VTIDAAALCL KSGNSVILRG GSEAIHSNYA LYTCVRQGIK QAGLNENCAQ 

       190        200        210        220        230        240 
LINTQNHEAV IELVKASDYV DAIIPRGGKG LVEAISNSAK TPVIKHLNGI CHTYIDKDAD 

       250        260        270        280        290        300 
KKKAISIAFN AKTRRYGVCN ATETLLVHAC AVSRILPKLI AQYLTKGVEL RGCKETLKLS 

       310        320        330        340        350        360 
NKIIAATEKD WNTEYLDAIL SIRIVNSMSE AIKHIDKHGS GHTESIVSEN YTRSRRFITE 

       370        380        390        400        410 
VDSASVMINA STGFADGFEY GLGAEIGIST DKFHVRGPVG LEGLTSQKFI VLGDGHIRQ 

« Hide

References

[1]"The Calyptogena magnifica chemoautotrophic symbiont genome."
Newton I.L.G., Woyke T., Auchtung T.A., Dilly G.F., Dutton R.J., Fisher M.C., Fontanez K.M., Lau E., Stewart F.J., Richardson P.M., Barry K.W., Saunders E., Detter J.C., Wu D., Eisen J.A., Cavanaugh C.M.
Science 315:998-1000(2007) [PubMed: 17303757] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000488 Genomic DNA. Translation: ABL01927.1.
RefSeqYP_903398.1. NC_008610.1.

3D structure databases

ProteinModelPortalA1AVH0.
ModBaseSearch...

Protein-protein interaction databases

STRINGA1AVH0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4555381.
GenomeReviewsGene locus Rmag_0133 in contig CP000488_GR.
KEGGrma:Rmag_0133.
PATRIC31999851. VBICanRut45856_0157.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0014.
HOGENOMHBG318080.
OMAQYPAACN.
PhylomeDBA1AVH0.
ProtClustDBPRK00197.

Enzyme and pathway databases

BioCycCRUT413404:RMAG_0133-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.
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. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePROA_RUTMC
AccessionPrimary (citable) accession number: A1AVH0
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: January 23, 2007
Last modified: December 14, 2011
This is version 44 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