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A1VYR7 (PROA_CAMJJ) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 45. 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:CJJ81176_0583
OrganismCampylobacter jejuni subsp. jejuni serotype O:23/36 (strain 81-176) [Complete proteome] [HAMAP]
Taxonomic identifier354242 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Campylobacteraceae › Campylobacter

Protein attributes

Sequence length410 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 – 410410Gamma-glutamyl phosphate reductase HAMAP MF_00412
PRO_1000049942

Sequences

Sequence LengthMass (Da)Tools
A1VYR7 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: EB2DA9A1E43DD068

FASTA41045,999
        10         20         30         40         50         60 
MRNLLENIKK NSQKLLNLTP KDKEKIILKL AQILRENFKI ILEANKKDMA NFTKSGAMKD 

        70         80         90        100        110        120 
RLLLDEKRIL ALCEGLEKIA YIEDPIGKIS KGWKNYAGLS IQKMSIPLGL ICVIYEARPS 

       130        140        150        160        170        180 
LSAEIAALMI KSSNACVFKG GSEAKFTNEA IFTLVNKVLK EFDLQDCFAM FTQRDEILQI 

       190        200        210        220        230        240 
LAFDDLIDVI IPRGSSNMIQ EIANNTKIPL IKQNKGLCHA FVDQSANLDM ALKIILNAKC 

       250        260        270        280        290        300 
QRVSVCNALE TLLIHEKIAK NFISLLIPEF KKFKVKIHAH ENALAYFNNS NLKIFKANEN 

       310        320        330        340        350        360 
TFDTEWLDFA LSVKLVKDCD EAIEHINKHS SLHSETIISN DASNIAKFQR LINSSCIYAN 

       370        380        390        400        410 
ASTRFSDGGE FGFGGEVGIS TSKLHARGPM GIEDICTYKY IINGEGQIRE

« Hide

References

[1]Fouts D.E., Nelson K.E., Sebastian Y.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 81-176.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000538 Genomic DNA. Translation: EAQ73086.1.
RefSeqYP_001000258.1. NC_008787.1.

3D structure databases

ProteinModelPortalA1VYR7.
ModBaseSearch...

Protein-protein interaction databases

STRINGA1VYR7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4682276.
GenomeReviewsGene locus CJJ81176_0583 in contig CP000538_GR.
KEGGcjj:CJJ81176_0583.
PATRIC20051119. VBICamJej103413_0591.
TIGRCJJ81176_0583.

Phylogenomic databases

eggNOGCOG0014.
HOGENOMHBG318080.
OMAYGICGAM.
ProtClustDBPRK00197.

Enzyme and pathway databases

BioCycCJEJ354242:CJJ81176_0583-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_CAMJJ
AccessionPrimary (citable) accession number: A1VYR7
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: February 6, 2007
Last modified: December 14, 2011
This is version 45 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

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