Skip Header

Contribute Send feedback
Read comments (?) or add your own

B6YS10 (PROA_AZOPC) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 26. 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
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:CFPG_719
OrganismAzobacteroides pseudotrichonymphae genomovar. CFP2 [Complete proteome] [HAMAP]
Taxonomic identifier511995 [NCBI]
Taxonomic lineageBacteria › Bacteroidetes › Bacteroidia › Bacteroidales › Candidatus Azobacteroides

Protein attributes

Sequence length419 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 – 419419Gamma-glutamyl phosphate reductase HAMAP MF_00412
PRO_1000123775

Sequences

Sequence LengthMass (Da)Tools
B6YS10 [UniParc].

Last modified January 20, 2009. Version 1.
Checksum: 3AAA6BCB24EF588C

FASTA41946,619
        10         20         30         40         50         60 
MFMNDQVYDL LRQAVIASRT LVDMSNKTIK NILRNTADHL LENQNTILEA NAEDLSRIDP 

        70         80         90        100        110        120 
SDQKYDRLKL TKERLQTMAD DMRSVAVLSS PIGKVLHEIT RPNGMLIRKV SVPFGVIGII 

       130        140        150        160        170        180 
YEARPNVTFD VFSLCFKSGN ACVLKGGSDA SLSNHALVNI IHQVLQKYRI NINTCILLPP 

       190        200        210        220        230        240 
NREVTAALLG AVGLVDLIIP RGSSSLINFV RNNTRVPVIE TGAGICHTYF DKKGDKDKGR 

       250        260        270        280        290        300 
AIINNAKTRR VSVCNALDCL VLHRERLNDL PYICGDLQKN NVIIYADEPS YKVLVTCYPA 

       310        320        330        340        350        360 
NLIQLAVEES FGTEFLDYKM SIRTVNNIRE AIDHITRYSS KHSECIVSES PKTINFFLQK 

       370        380        390        400        410 
IDAACVYANV STAFTDGSQF GMGAEIGIST QKLHARGPMA LEELTTYKYL IEGSGQIRS

« Hide

References

[1]"Genome of an endosymbiont coupling N2 fixation to cellulolysis within RT protist cells in termite gut."
Hongoh Y., Sharma V.K., Prakash T., Noda S., Toh H., Taylor T.D., Kudo T., Sakaki Y., Toyoda A., Hattori M., Ohkuma M.
Science 322:1108-1109(2008) [PubMed: 19008447] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AP010656 Genomic DNA. Translation: BAG83982.1.
RefSeqYP_002309393.1. NC_011565.1.

3D structure databases

ProteinModelPortalB6YS10.
ModBaseSearch...

Protein-protein interaction databases

STRINGB6YS10.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID7039193.
GenomeReviewsGene locus CFPG_719 in contig AP010656_GR.
KEGGaps:CFPG_719.
PATRIC31963474. VBICanAzo57536_1090.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG318080.
OMAQYPAACN.
ProtClustDBPRK00197.

Family and domain databases

HAMAPMF_00412. ProA.
[Tree]
InterProIPR016161. Ald_DH/histidinol_DH.
IPR016163. Ald_DH_C.
IPR016162. Ald_DH_N.
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.
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_AZOPC
AccessionPrimary (citable) accession number: B6YS10
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: January 20, 2009
Last modified: January 25, 2012
This is version 26 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents