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Reviewed, UniProtKB/Swiss-Prot Q8YV15 (PROA_ANASP)

Last modified November 25, 2008. Version 43. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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: all2166
OrganismAnabaena sp. (strain PCC 7120) [Complete proteome] [HAMAP]
Taxonomic identifier103690 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaNostocalesNostocaceaeNostoc

Protein attributes

Sequence length434 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

Catalytic activity

L-glutamate 5-semialdehyde + phosphate + NADP(+) = L-glutamyl 5-phosphate + NADPH.

Pathway

Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-glutamate: step 2/2.

Subcellular location

CytoplasmBy similarity.

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 processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

proline biosynthetic process

Inferred from electronic annotation. Source: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: HAMAP

   Molecular functionNADP binding

Inferred from electronic annotation. Source: InterPro

glutamate-5-semialdehyde dehydrogenase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 434434Gamma-glutamyl phosphate reductase
PRO_0000189683

Sequences

Sequence LengthMass (Da)Tools
Q8YV15-1 [UniParc].

Last modified October 17, 2006. Version 2.
Checksum: 6A7DD657D45D8F08

FASTA43446,964
        10         20         30         40         50         60 
MTTLQVASSL NDIAQQTRQA ASLLAMLSTE AKNQAIAAVA QALESAKEEI LQANIDDCEA 

        70         80         90        100        110        120 
ATAEGIAKPL YKRLQLDEHK LRDAIAGVRD VGKLADPIGQ VQIQRELDTG LVLKRITCPL 

       130        140        150        160        170        180 
GVLGIIFEAR PEAAIQIISL AIKSGNGVIL KCGKEAVRSC EAIVKAVKQG LSTTDVNPEV 

       190        200        210        220        230        240 
VQLLTTREET LELLRLDKYV DLIIPRGSNS FVRFVQENTR IPVLGHADGI CHVYIDKSAD 

       250        260        270        280        290        300 
IEKAIAVSVD AKVQYPAACN AIETLLVHQS IAAEFLPKVA QALAEREVEL KGDERTLQIL 

       310        320        330        340        350        360 
PEIAAATAID WETEYSDFIL SIKIVDSLTE AIAHINQYGS RHTDAIITED VAAVKTFFGL 

       370        380        390        400        410        420 
VNSAGVFHNC STRFADGFRY GFGAEVGIST QQMPPRGPVG LEGLVTYKYQ MTGAGHIVAT 

       430 
YTGENAKPFT HKDF 

« Hide

References

[1]"Complete genomic sequence of the filamentous nitrogen-fixing cyanobacterium Anabaena sp. strain PCC 7120."
Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A., Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M. expand/collapse author list , Takazawa M., Yamada M., Yasuda M., Tabata S.
DNA Res. 8:205-213(2001) [PubMed: 11759840] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

BA000019 Genomic DNA. Translation: BAB73865.1. Different initiation.
PIRAH2076.
RefSeqNP_486206.1.

3D structure databases

HSSPHSSP built from PDB template 1O20 based on UniProtKB Q9WYC9.
ModBaseSearch...

Genome annotation databases

GeneID1105764.
GenomeReviewsGene locus all2166 in contig BA000019_GR.
KEGGana:all2166.
NMPDRfig|103690.1.peg.2473.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ8YV15.

Enzyme and pathway databases

BioCycNSP103690:ALL2166-MON.

Family and domain databases

HAMAPMF_00412.
[Tree]
InterProIPR016163. Ald_DHase_C.
IPR016162. Ald_DHase_N.
IPR015590. Aldehyde_DHase.
IPR000965. Gglut_pp_reduct.
IPR012134. Glu-5-SA_DHase.
[Graphical view]
Gene3DG3DSA:3.40.309.10. Aldehyde_dehydrogenase_C. 1 hit.
G3DSA:3.40.605.10. Aldehyde_dehydrogenase_N. 1 hit.
PfamPF00171. Aldedh. 1 hit.
[Graphical view]
PIRSFPIRSF000151. GPR. 1 hit.
TIGRFAMsTIGR00407. proA. 1 hit.
PROSITEPS01223. PROA. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePROA_ANASP
AccessionPrimary (citable) accession number: Q8YV15
Entry history
Integrated into UniProtKB/Swiss-Prot: June 6, 2002
Last sequence update: October 17, 2006
Last modified: November 25, 2008
This is version 43 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents