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A9VK31 (PROA_BACWK) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 42. 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:BcerKBAB4_2789
OrganismBacillus weihenstephanensis (strain KBAB4) [Complete proteome] [HAMAP]
Taxonomic identifier315730 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillusBacillus cereus group

Protein attributes

Sequence length415 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 By similarity. 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 – 415415Gamma-glutamyl phosphate reductase HAMAP MF_00412
PRO_1000193571

Sequences

Sequence LengthMass (Da)Tools
A9VK31 [UniParc].

Last modified February 5, 2008. Version 1.
Checksum: 0F1DA130039F4277

FASTA41545,556
        10         20         30         40         50         60 
MNEVVAKGKK AKEIARELVL KSTNQKNEAL AAIADQMIVE TAYILEENKR DIEEGKAKGF 

        70         80         90        100        110        120 
SDSLLDRLML NEQRIIDMAE GIKQLIELRD PVGECVSAWE RPNGLSIQEM RVPLGVVGMI 

       130        140        150        160        170        180 
YEARPNVTVD AATICLKTGN AVILRGSSSA INSNKAIVSV IHRALKQTSL PPESVQLIED 

       190        200        210        220        230        240 
TTRDSAKQLF TLNEYLDVLI PRGGKQLIDT VVREASVPVL ETGAGNCHIF IDETADKQMA 

       250        260        270        280        290        300 
FNIIINAKTQ RPSVCNAIET IVLHEKWAQQ FGSELFSSLK ERGVELRGDS KSLAIDSSIA 

       310        320        330        340        350        360 
LASEEDWETE FLSLTLAVKV VSTTEEAIHH INTYGSMHSE AIITENEENV SKFFTSVDAA 

       370        380        390        400        410 
ALYHNASTRF TDGSEFGFGA EIGISTQKLH VRGPMGLPAL TSTKYVIRGN GQIRR 

« Hide

References

[1]"Extending the Bacillus cereus group genomics to putative food-borne pathogens of different toxicity."
Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., Dossat C., Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H., Sanchis V., Nguen-the C., Lereclus D., Richardson P., Wincker P., Weissenbach J., Ehrlich S.D., Sorokin A.
Chem. Biol. Interact. 171:236-249(2008) [PubMed: 17434157] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: KBAB4.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000903 Genomic DNA. Translation: ABY43986.1.
RefSeqYP_001645614.1. NC_010184.1.

3D structure databases

ProteinModelPortalA9VK31.
SMRA9VK31. Positions 3-415.
ModBaseSearch...

Protein-protein interaction databases

STRINGA9VK31.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000079313; EBBACP00000077247; EBBACG00000079304.
GeneID5843001.
GenomeReviewsGene locus BcerKBAB4_2789 in contig CP000903_GR.
KEGGbwe:BcerKBAB4_2789.
PATRIC19010189. VBIBacWei55973_3411.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000000020.
HOGENOMHBG318080.
OMAQYPAACN.
ProtClustDBPRK00197.

Enzyme and pathway databases

BioCycBWEI315730:BCERKBAB4_2789-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_BACWK
AccessionPrimary (citable) accession number: A9VK31
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: February 5, 2008
Last modified: January 25, 2012
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