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Q0BRE6 (Q0BRE6_GRABC) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 48. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Gamma-glutamyl phosphate reductase HAMAP MF_00412
Short name=GPR HAMAP MF_00412
EC=1.2.1.41 HAMAP MF_00412
Alternative name(s):
Glutamate-5-semialdehyde dehydrogenase HAMAP MF_00412
Glutamyl-gamma-semialdehyde dehydrogenase HAMAP MF_00412
Gene names
Name:proA HAMAP MF_00412
Ordered Locus Names:GbCGDNIH1_1708
OrganismGranulibacter bethesdensis (strain ATCC BAA-1260 / CGDNIH1) [Complete proteome] [HAMAP] EMBL ABI62606.1
Taxonomic identifier391165 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhodospirillales › Acetobacteraceae › Granulibacter

Protein attributes

Sequence length446 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. HAMAP MF_00412

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Proline biosynthesis HAMAP MF_00412
   Cellular componentCytoplasm HAMAP MF_00412
   LigandNADP HAMAP MF_00412
   Molecular functionOxidoreductase HAMAP MF_00412 EMBL ABI62606.1
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processproline biosynthetic process

Inferred from electronic annotation. Source: HAMAP

   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: HAMAP

Complete GO annotation...

Sequences

Sequence LengthMass (Da)Tools
Q0BRE6 [UniParc].

Last modified October 17, 2006. Version 1.
Checksum: FA2CA60513750BA3

FASTA44647,516
        10         20         30         40         50         60 
MLCILATEQK NELNITSRCI TELEAMLDGV SETAQQWIAQ AGRSARMASS VLARVPHEAR 

        70         80         90        100        110        120 
QNALRQAASA LRDEEAAILA ANAIDLERSN ASAAFRDRLT LTRSRVAAMA DGLEQIADLP 

       130        140        150        160        170        180 
DPLSRVLSEW ERPNGLRIRR IAAPIGVIGM IYESRPNVGA DAAGIAIKSG NAVLLRGGSE 

       190        200        210        220        230        240 
SQHSARAIHK AMQAGLRKAG LPEEAVQIAP DTDRAYVAAM LAGNQVLDLI IPRGGKSLVE 

       250        260        270        280        290        300 
RVQKEARVPV LAHAEGLCHT YIHKAADREK ARSILANAKM RRTGICGATE TLLIDAAIAG 

       310        320        330        340        350        360 
SLLPVLVEDL SALGCTFRAD DAARAIMPGL PAASDADFDT EWLDAILSIK VVDGIDAALA 

       370        380        390        400        410        420 
HIARHGSEHT EAIITEDEAA AEYFLSHVQS AVAMWNASTQ FCDGGEFGFG AEIGIATGRI 

       430        440 
HARGPVGPEQ LTTYRYLVLG NGQIRP

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References

[1]"Genome sequence analysis of the emerging human pathogenic acetic acid bacterium Granulibacter bethesdensis."
Greenberg D.E., Porcella S.F., Zelazny A.M., Virtaneva K., Sturdevant D.E., Kupko J.J. III, Barbian K.D., Babar A., Dorward D.W., Holland S.M.
J. Bacteriol. 189:8727-8736(2007) [PubMed: 17827295] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000394 Genomic DNA. Translation: ABI62606.1.
RefSeqYP_745529.1. NC_008343.1.

3D structure databases

ProteinModelPortalQ0BRE6.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ0BRE6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4276632.
GenomeReviewsGene locus GbCGDNIH1_1708 in contig CP000394_GR.
KEGGgbe:GbCGDNIH1_1708.
NMPDRfig|391165.8.peg.1657.
PATRIC22079611. VBIGraBet83793_1763.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0014.
HOGENOMHBG318080.
OMAYGICGAM.
PhylomeDBQ0BRE6.
ProtClustDBPRK00197.

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 nameQ0BRE6_GRABC
AccessionPrimary (citable) accession number: Q0BRE6
Entry history
Integrated into UniProtKB/TrEMBL: October 17, 2006
Last sequence update: October 17, 2006
Last modified: December 14, 2011
This is version 48 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequences·References·Cross-refs·Entry info