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A1A1U9 (PROA_BIFAA) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 46. 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:BAD_0901
OrganismBifidobacterium adolescentis (strain ATCC 15703 / DSM 20083 / NCTC 11814 / E194a) [Complete proteome] [HAMAP]
Taxonomic identifier367928 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeBifidobacterialesBifidobacteriaceaeBifidobacterium

Protein attributes

Sequence length427 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 – 427427Gamma-glutamyl phosphate reductase HAMAP MF_00412
PRO_0000340873

Sequences

Sequence LengthMass (Da)Tools
A1A1U9 [UniParc].

Last modified January 23, 2007. Version 1.
Checksum: 3DF4BACCB17513E4

FASTA42745,480
        10         20         30         40         50         60 
MNADVFEAVC AMGDAARTAQ SQLAQANTEA KNQLLNAIAD ALDQHADDIA AANTLDMNKA 

        70         80         90        100        110        120 
ETDGMDAGKL DRLKFDQQRI TAAAQGVRHV ASLPDPIGEI VRGYHLENGL RLQQVRVPIG 

       130        140        150        160        170        180 
VLGMIYEARP NVTVDVASLC IKSGNAVLLR GGHAAEHTNA ATLAVIADVL TKHGYDHNMI 

       190        200        210        220        230        240 
ATVDQYGRDG ATAMMEARGH IDVLIPRGGA GLIQAVVRNS KVPVIETGAG NVHIYVDRTG 

       250        260        270        280        290        300 
NPDKAIPILI NAKTQRVGVC NATEKLLVHK DIAESFLPKA AAALAAAGVE MHADERAYGI 

       310        320        330        340        350        360 
IEHAGIANAQ LVHATDEDWD TEYLALKIGI KVVDSLDEAI AHINRHSTGH TESIIAEDYS 

       370        380        390        400        410        420 
AIEEFTARID SAVVMVNAST RFTDGGVFGF GAELGISTQK MHARGPMGLH EMTTTKWIGY 


GTGQVRE 

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References

[1]"Bifidobacterium adolescentis complete genome sequence."
Suzuki T., Tsuda Y., Kanou N., Inoue T., Kumazaki K., Nagano S., Hirai S., Tanaka K., Watanabe K.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 15703 / DSM 20083 / NCTC 11814 / E194a.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP009256 Genomic DNA. Translation: BAF39682.1.
RefSeqYP_909764.1. NC_008618.1.

3D structure databases

ProteinModelPortalA1A1U9.
ModBaseSearch...

Protein-protein interaction databases

STRINGA1A1U9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4556586.
GenomeReviewsGene locus BAD_0901 in contig AP009256_GR.
KEGGbad:BAD_0901.
NMPDRfig|1680.3.peg.1171.
PATRIC21101221. VBIBifAdo27973_0974.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0014.
HOGENOMHBG318080.
OMAYGICGAM.
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. 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_BIFAA
AccessionPrimary (citable) accession number: A1A1U9
Entry history
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: January 23, 2007
Last modified: December 14, 2011
This is version 46 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