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Q5P255 (PROA_AROAE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 57. 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:AZOSEA24840
ORF Names:ebA4380
OrganismAromatoleum aromaticum (strain EbN1) (Azoarcus sp. (strain EbN1)) [Complete proteome] [HAMAP]
Taxonomic identifier76114 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaRhodocyclalesRhodocyclaceaeAromatoleum

Protein attributes

Sequence length425 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 – 425425Gamma-glutamyl phosphate reductase HAMAP MF_00412
PRO_0000189685

Sequences

Sequence LengthMass (Da)Tools
Q5P255 [UniParc].

Last modified January 4, 2005. Version 1.
Checksum: 823329058BA020C3

FASTA42545,075
        10         20         30         40         50         60 
MDIHDYMQTL GRQARAASRV LATASTADKN AALVAMAAAI REQTGELLAA NARDLDEARA 

        70         80         90        100        110        120 
AGLEAALIDR LTLTAKGIEA MAEGLEQVAG LPDPIGEITD VKRRPSGIQV GKMRVPLGVI 

       130        140        150        160        170        180 
GIIYEARPNV TADAAALCLK SGNAAILRGG KEALHCNQAI AQCVRTGLAA AGLPETSVQV 

       190        200        210        220        230        240 
VETTDRAAVG HLITMPEFVD VIVPRGGKGL IERISKEARV PVIKHLDGNC HVYIDRDADV 

       250        260        270        280        290        300 
AKVVPIVENA KTQRYGTCNT AESLLVAREV APRLLPEIGR MLATKGVEMR GCEQSLAILR 

       310        320        330        340        350        360 
AAGIAADKLR AASEQDWSEE YLAPVIAVKV VADLDEAIAH INTYSSGHTE AIVTENYTSA 

       370        380        390        400        410        420 
MRFLREVDSS SVMVNASTRF ADGFEYGLGA EIGISTDKIH ARGPVGLDGL TSQKWIVFGN 


GEIRG 

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References

[1]"The genome sequence of an anaerobic aromatic-degrading denitrifying bacterium, strain EbN1."
Rabus R., Kube M., Heider J., Beck A., Heitmann K., Widdel F., Reinhardt R.
Arch. Microbiol. 183:27-36(2005) [PubMed: 15551059] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: EbN1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR555306 Genomic DNA. Translation: CAI08609.1.
RefSeqYP_159510.1. NC_006513.1.

3D structure databases

ProteinModelPortalQ5P255.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ5P255.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3179697.
GenomeReviewsGene locus AZOSEA24840 in contig CR555306_GR.
KEGGeba:ebA4380.
NMPDRfig|76114.4.peg.2782.
PATRIC20971140. VBIAroAro98752_2513.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0014.
HOGENOMHBG318080.
OMAYGICGAM.
ProtClustDBPRK00197.

Enzyme and pathway databases

BioCycASP76114:EBA4380-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. 2 hits.
[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_AROAE
AccessionPrimary (citable) accession number: Q5P255
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: January 4, 2005
Last modified: January 25, 2012
This is version 57 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