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B3DSW1 (B3DSW1_BIFLD) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 39. 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-Rule MF_00412
Short name=GPR HAMAP-Rule MF_00412
EC=1.2.1.41 HAMAP-Rule MF_00412
Alternative name(s):
Glutamate-5-semialdehyde dehydrogenase HAMAP-Rule MF_00412
Glutamyl-gamma-semialdehyde dehydrogenase HAMAP-Rule MF_00412
Gene names
Name:proA HAMAP-Rule MF_00412 EMBL ACD98230.1
Ordered Locus Names:BLD_0784 EMBL ACD98230.1
OrganismBifidobacterium longum (strain DJO10A) [Complete proteome] [HAMAP] EMBL ACD98230.1
Taxonomic identifier205913 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Bifidobacteriales › Bifidobacteriaceae › Bifidobacterium ›

Protein attributes

Sequence length423 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-Rule MF_00412 SAAS SAAS020593

Catalytic activity

L-glutamate 5-semialdehyde + phosphate + NADP+ = L-glutamyl 5-phosphate + NADPH. HAMAP-Rule MF_00412 SAAS SAAS020593

Pathway

Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-glutamate: step 2/2. HAMAP-Rule MF_00412 SAAS SAAS020593

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00412 SAAS SAAS020593.

Sequence similarities

Belongs to the gamma-glutamyl phosphate reductase family. HAMAP-Rule MF_00412

Sequences

Sequence LengthMass (Da)Tools
B3DSW1 [UniParc].

Last modified July 22, 2008. Version 1.
Checksum: 9B0E637B442D6A8F

FASTA42344,711
        10         20         30         40         50         60 
MFDAVCRQAD QAARAQERLA QANAEAKNEL LLAIADALDE HAADIEAANA LDMLESKENG 

        70         80         90        100        110        120 
MDAGKLDRLL FDVPRVAAAA QGVRHVATLP DPVGEIVRGY NLPNGLRLTQ TRVPMGVIGM 

       130        140        150        160        170        180 
IYEARPNVTV DVASLCLKSG NAALLRGGHA AERTNAATLG VIAPVLEAHG FESALVQSVD 

       190        200        210        220        230        240 
QYGRAGATAM MEARGHIDVL VPRGGAGLIQ AVVRNSKVPV IETGAGNVHI YIDKSGNLAK 

       250        260        270        280        290        300 
AIPIIINAKT QRVGVCNAAE KLLVHKDVAA EFLPRIAAAL AEANVVLQAD TTSYDIISGA 

       310        320        330        340        350        360 
AIEGLDLNHA TEEDWDTEYL ALKMGIKVVS DLGAAIDHIN THSTGHTESI IAEDYAAIEE 

       370        380        390        400        410        420 
FTKRIDSAVV MVNASTRFTD GGVFGFGAEL GISTQKMHAR GPMGLREMTT TKWIGYGTGQ 


VRA

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References

[1]"Comparative genomic analysis of the gut bacterium Bifidobacterium longum reveals loci susceptible to deletion during pure culture growth."
Lee J.H., Karamychev V.N., Kozyavkin S.A., Mills D., Pavlov A.R., Pavlova N.V., Polouchine N.N., Richardson P.M., Shakova V.V., Slesarev A.I., Weimer B., O'Sullivan D.J.
BMC Genomics 9:247-247(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DJO10A EMBL ACD98230.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000605 Genomic DNA. Translation: ACD98230.1.
RefSeqYP_001954728.1. NC_010816.1.

3D structure databases

ProteinModelPortalB3DSW1.
ModBaseSearch...

Protein-protein interaction databases

STRING205913.BLD_0784.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACD98230; ACD98230; BLD_0784.
GeneID6362931.
KEGGblj:BLD_0784.
PATRIC21114512. VBIBifLon134794_0796.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0014.
HOGENOMHOG000246356.
KOK00147.
OMAEVGISTQ.
ProtClustDBPRK00197.

Enzyme and pathway databases

BioCycBLON205913:GJB4-812-MONOMER.
UniPathwayUPA00098; UER00360.

Family and domain databases

Gene3D3.40.309.10. 1 hit.
3.40.605.10. 2 hits.
HAMAPMF_00412. ProA.
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]
PANTHERPTHR11063:SF1. PTHR11063:SF1. 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 nameB3DSW1_BIFLD
AccessionPrimary (citable) accession number: B3DSW1
Entry history
Integrated into UniProtKB/TrEMBL: July 22, 2008
Last sequence update: July 22, 2008
Last modified: May 1, 2013
This is version 39 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