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Q57B47 (PROA_BRUAB) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 52. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:BruAb1_1822
OrganismBrucella abortus biovar 1 (strain 9-941) [Complete proteome] [HAMAP]
Taxonomic identifier262698 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella

Protein attributes

Sequence length421 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 – 421421Gamma-glutamyl phosphate reductase HAMAP MF_00412
PRO_0000189705

Sequences

Sequence LengthMass (Da)Tools
Q57B47 [UniParc].

Last modified May 10, 2005. Version 1.
Checksum: 86B9B722DFDEE431

FASTA42144,041
        10         20         30         40         50         60 
MTKDIAQVMA EVGRKAKAAA APLSIATSEQ KNKALNAAAD AILEARADIL EANRLDLANA 

        70         80         90        100        110        120 
EKNGMAASFV DRLTLNEARI DAIAEGIRAI ATLPDPVGEV IAEWDRPNGL HIERVRTPLG 

       130        140        150        160        170        180 
VIGVIYESRP NVTADAGALC LKAGNAVILR GGSDSAHSSA AIHKALVKGL EAANLPADAI 

       190        200        210        220        230        240 
QIVPVTDRAA VGEMLKGLGG AIDVIVPRGG KSLVARVQSE ARVPVFAHLE GICHLYIDKS 

       250        260        270        280        290        300 
ADLDMARRIA LDAKMRRTGI CGAAETLLVD RAVASTHLAP ILGDLAAGGC EIRGSAEVLA 

       310        320        330        340        350        360 
LYPAAKPATE EDWSTEYLDA IISVALVDGI SGAIDHINRY SSHHTEAIVA EDAQTVARFF 

       370        380        390        400        410        420 
NEIDSAILLH NASTQFADGG EFGMGAEIGI ATGKMHARGP VGVEQLTSFK YRVRGSGQVR 


G 

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References

[1]"Completion of the genome sequence of Brucella abortus and comparison to the highly similar genomes of Brucella melitensis and Brucella suis."
Halling S.M., Peterson-Burch B.D., Bricker B.J., Zuerner R.L., Qing Z., Li L.-L., Kapur V., Alt D.P., Olsen S.C.
J. Bacteriol. 187:2715-2726(2005) [PubMed: 15805518] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 9-941.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017223 Genomic DNA. Translation: AAX75137.1.
RefSeqYP_222498.1. NC_006932.1.

3D structure databases

ProteinModelPortalQ57B47.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3340400.
GenomeReviewsGene locus BruAb1_1822 in contig AE017223_GR.
KEGGbmb:BruAb1_1822.
PATRIC17825449. VBIBruAbo15061_1926.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG318080.
OMAITHINRY.
PhylomeDBQ57B47.
ProtClustDBPRK00197.

Enzyme and pathway databases

BioCycBABO262698:BRUAB1_1822-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. 1 hit.
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_BRUAB
AccessionPrimary (citable) accession number: Q57B47
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: May 10, 2005
Last modified: January 25, 2012
This is version 52 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Brucella abortus strain 9-941

Brucella abortus (strain 9-941): entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families