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A0KNQ8 (PROA_AERHH) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 42. 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:AHA_3420
OrganismAeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / NCIB 9240) [Complete proteome] [HAMAP]
Taxonomic identifier380703 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAeromonadalesAeromonadaceaeAeromonas

Protein attributes

Sequence length417 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 – 417417Gamma-glutamyl phosphate reductase HAMAP MF_00412
PRO_1000049932

Sequences

Sequence LengthMass (Da)Tools
A0KNQ8 [UniParc].

Last modified December 12, 2006. Version 1.
Checksum: 3D9241D61B0E51CF

FASTA41744,328
        10         20         30         40         50         60 
MSLEKMGQAA REAAYQLATV STAQKNRALA AIADELEARS HQILAANEKD IAAGRAAGLS 

        70         80         90        100        110        120 
DAMLDRLLLN PARLAGIVAD VRKVISLDDP VGAEIDSRVL ENGLRLSRRR VPIGVIGVIY 

       130        140        150        160        170        180 
EARPNVTIDI ASLCLKTGNA SILRGGRETF HSNLELVRVI QSALAASGLP RDAVQYIDNP 

       190        200        210        220        230        240 
DRALVGELLR LDRYVDMIIP RGGAGLHKMC KENSSIPVII GGFGISHIFV DESADLARSL 

       250        260        270        280        290        300 
AVIDNAKVQR PSACNALDSL LVHEKVAATL LPQLVGLMNE RKVALVATPE AMPLLAGADS 

       310        320        330        340        350        360 
LRAAGPEDFD TEWLSLTLGV KLVADVNEAL AHMREHNAGH SDAILTNDLA NAERFVNGAG 

       370        380        390        400        410 
SAAVYVNAST RFTDGGQFGL GAEVAVSTQM LHARGPMGLT ELTSYKWVGL ADYLSRA 

« Hide

References

[1]"Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all trades."
Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J., Haft D.H., Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M., Jin S., Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.
J. Bacteriol. 188:8272-8282(2006) [PubMed: 16980456] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 7966 / NCIB 9240.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000462 Genomic DNA. Translation: ABK38804.1.
RefSeqYP_857909.1. NC_008570.1.

3D structure databases

ProteinModelPortalA0KNQ8.
ModBaseSearch...

Protein-protein interaction databases

STRINGA0KNQ8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4487146.
GenomeReviewsGene locus AHA_3420 in contig CP000462_GR.
KEGGaha:AHA_3420.
PATRIC20784478. VBIAerHyd135212_3421.
TIGRAHA_3420.

Phylogenomic databases

eggNOGCOG0014.
HOGENOMHBG318080.
OMAQYPAACN.
PhylomeDBA0KNQ8.
ProtClustDBPRK00197.

Enzyme and pathway databases

BioCycAHYD196024:AHA_3420-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_AERHH
AccessionPrimary (citable) accession number: A0KNQ8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: December 12, 2006
Last modified: December 14, 2011
This is version 42 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