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Reviewed, UniProtKB/Swiss-Prot Q2KXE0 (PROA_BORA1)

Last modified June 16, 2009. Version 27. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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: BAV2495
OrganismBordetella avium (strain 197N) [Complete proteome] [HAMAP]
Taxonomic identifier360910 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesAlcaligenaceaeBordetella

Protein attributes

Sequence length419 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

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 processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

proline biosynthetic process

Inferred from electronic annotation. Source: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionNADP or NADPH binding

Inferred from electronic annotation. Source: InterPro

glutamate-5-semialdehyde dehydrogenase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 419419Gamma-glutamyl phosphate reductase HAMAP MF_00412
PRO_0000252564

Sequences

Sequence LengthMass (Da)Tools
Q2KXE0-1 [UniParc].

Last modified March 7, 2006. Version 1.
Checksum: FD66A8A0D0A16518

FASTA41944,373
        10         20         30         40         50         60 
MSSIEQIMLT LGENARQASR AMMRASGTAK NRALLAMAEL IIDGKAALQA ANALDLEAAR 

        70         80         90        100        110        120 
ANGLEPALLD RLTLSDRSVQ LMAEGLRQIA ALPDPVGSLG PTQVRPNGMR VAQMRVPLGV 

       130        140        150        160        170        180 
IGIIYESRPN VTIDAAALCL KSGNATILRG GSEALHSNLA LGAIVQAGLA AAELPPAAVQ 

       190        200        210        220        230        240 
VVSTTDRAAV GKLVTMTEHI DVIVPRGGKG LIARLAQEAR VPLIKHLDGN CHVYIDAAAD 

       250        260        270        280        290        300 
PDRALEIAFN AKTYRYGVCG SMETLLVHRA IAPTQLPRIA RALIEHGVEL RGCERSQAIV 

       310        320        330        340        350        360 
PGMAAASEED WGTEYLGPVL AVRVVDDLDQ AMEHIARWGS GHTDAIVTEN LAAAQRFQRE 

       370        380        390        400        410 
VDSSSVYVNL PTVFADGFEY GLGAEIGIST NRLHARGPVG LEGLTTYKWV LTGEGQTRG 

« Hide

References

[1]"Comparison of the genome sequence of the poultry pathogen Bordetella avium with those of B. bronchiseptica, B. pertussis, and B. parapertussis reveals extensive diversity in surface structures associated with host interaction."
Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D., King N.D., Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D., Goble A., Lord A., Murphy L., Quail M.A., Rutter S., Squares R., Squares S., Woodward J., Parkhill J., Temple L.M.
J. Bacteriol. 188:6002-6015(2006) [PubMed: 16885469] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

AM167904 Genomic DNA. Translation: CAJ50105.1.
RefSeqYP_787007.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID6267189.
GenomeReviewsGene locus BAV2495 in contig AM167904_GR.
KEGGbav:BAV2495.
NMPDRfig|521.1.peg.3.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ2KXE0.
OMAQ2KXE0. FDTEWLD.

Family and domain databases

HAMAPMF_00412.
[Tree]
InterProIPR016163. Ald_DH_C.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH.
IPR000965. Gglut_pp_reduct.
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. 1 hit.
PANTHERPTHR11063:SF1. GSA_DH. 1 hit.
PfamPF00171. Aldedh. 1 hit.
[Graphical view]
PIRSFPIRSF000151. GPR. 1 hit.
TIGRFAMsTIGR00407. proA. 1 hit.
PROSITEPS01223. PROA. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePROA_BORA1
AccessionPrimary (citable) accession number: Q2KXE0
Entry history
Integrated into UniProtKB/Swiss-Prot: October 17, 2006
Last sequence update: March 7, 2006
Last modified: June 16, 2009
This is version 27 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents