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Q8G5H9 (PROA_BIFLO) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 64. 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:BL1034
OrganismBifidobacterium longum (strain NCC 2705)
Taxonomic identifier206672 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeBifidobacterialesBifidobacteriaceaeBifidobacterium

Protein attributes

Sequence length431 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.

Sequence caution

The sequence AAN24839.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Proline biosynthesis
   Cellular componentCytoplasm
   LigandNADP
   Molecular functionOxidoreductase
   Technical termComplete proteome
Reference 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 – 431431Gamma-glutamyl phosphate reductase HAMAP MF_00412
PRO_0000189700

Sequences

Sequence LengthMass (Da)Tools
Q8G5H9 [UniParc].

Last modified December 15, 2003. Version 2.
Checksum: 66243B4679DABEB0

FASTA43145,571
        10         20         30         40         50         60 
MSDELSPEVF DAVCRQADQA ARAQERLAQA NTEAKNELLL AIADALDEHA ADIEAANALD 

        70         80         90        100        110        120 
MLESKENGMD AGKLDRLLFD VPRVAAAAQG VRHVATLPDP VGEIVRGYNL PNGLRLTQTR 

       130        140        150        160        170        180 
VPMGVIGMIY EARPNVTVDV ASLCLKSGNA ALLRGGHAAE RTNAATLGVI APVLEAHGFE 

       190        200        210        220        230        240 
SALVQSVDQY GRAGATAMME ARGHIDVLVP RGGAGLIQAV VRNSKVPVIE TGAGNVHIYI 

       250        260        270        280        290        300 
DKSGDLAKAI PIIINAKTQR VGVCNAAEKL LVHKDVAAEF LPQIAAALAE ANVVLQTDTT 

       310        320        330        340        350        360 
SYGIISGAAI EGLDLNHAAE EDWDTEYLAL KMGIKVVSDL DAAIDHINTH STGHTESIIA 

       370        380        390        400        410        420 
EDYAAIEEFT KRIDSAVVMV NASTRFTDGG VFGFGAELGI STQKMHARGP MGLREMTTTK 

       430 
WIGYGTGQVR A 

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References

[1]"The genome sequence of Bifidobacterium longum reflects its adaptation to the human gastrointestinal tract."
Schell M.A., Karmirantzou M., Snel B., Vilanova D., Berger B., Pessi G., Zwahlen M.-C., Desiere F., Bork P., Delley M., Pridmore R.D., Arigoni F.
Proc. Natl. Acad. Sci. U.S.A. 99:14422-14427(2002) [PubMed: 12381787] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NCC 2705.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE014295 Genomic DNA. Translation: AAN24839.1. Different initiation.
RefSeqNP_696203.1. NC_004307.2.

3D structure databases

ProteinModelPortalQ8G5H9.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1022561.
GenomeReviewsGene locus BL1034 in contig AE014295_GR.
KEGGblo:BL1034.
NMPDRfig|206672.1.peg.970.
PATRIC21118547. VBIBifLon107831_0738.

Phylogenomic databases

HOGENOMHBG318080.
OMAQYPAACN.
PhylomeDBQ8G5H9.
ProtClustDBPRK00197.

Enzyme and pathway databases

BioCycBLON206672:BL1034-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. 2 hits.
[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_BIFLO
AccessionPrimary (citable) accession number: Q8G5H9
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: December 15, 2003
Last modified: January 25, 2012
This is version 64 of the entry and version 2 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