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A0PXA4 (PROA_CLONN) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 44. 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:NT01CX_0901
OrganismClostridium novyi (strain NT) [Complete proteome] [HAMAP]
Taxonomic identifier386415 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length417 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.

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 – 417417Gamma-glutamyl phosphate reductase HAMAP MF_00412
PRO_1000049944

Sequences

Sequence LengthMass (Da)Tools
A0PXA4 [UniParc].

Last modified January 9, 2007. Version 1.
Checksum: 2E0C10009845E73D

FASTA41745,237
        10         20         30         40         50         60 
MNIENYVIET ASLAKSAARK MSIVSTVTKN NALNAMADAL IENTNAIIEA NKKDMENGRE 

        70         80         90        100        110        120 
KGLTESLLDR LLLDEARIKS MAQGLRDVAS LEDPIGEVIR MWRRPNNLKI GQIRVPLGVI 

       130        140        150        160        170        180 
GIIYEARPNV TVDAAALCVK SGNAVILRGG SEAINSNTTV ARIISEAATK AGLPEGAINL 

       190        200        210        220        230        240 
IENPSRDAVN VMMKLNDYID VLIPRGGAGL INAVVKNATV PVIQTGVGNC HVFVDASADL 

       250        260        270        280        290        300 
EMAANIVINA KTQRPAVCNA MESLLVHKDI ADKFLPYLAE KLKPLNVEIK GCIRTQSLVE 

       310        320        330        340        350        360 
GATEATEEDW AKEYLDFKFA SKVVDSLDEA LDHIYKYSTK HSEVIVTNNY ENSQRFLAEV 

       370        380        390        400        410 
DAAAVYVNAS SRFTDGSEFG FGAEIGISTQ KLHARGPMGL KELTSSKYII YGEGQIR 

« Hide

References

[1]"The genome and transcriptomes of the anti-tumor agent Clostridium novyi-NT."
Bettegowda C., Huang X., Lin J., Cheong I., Kohli M., Szabo S.A., Zhang X., Diaz L.A. Jr., Velculescu V.E., Parmigiani G., Kinzler K.W., Vogelstein B., Zhou S.
Nat. Biotechnol. 24:1573-1580(2006) [PubMed: 17115055] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000382 Genomic DNA. Translation: ABK60892.1.
RefSeqYP_877006.1. NC_008593.1.

3D structure databases

ProteinModelPortalA0PXA4.
SMRA0PXA4. Positions 7-417.
ModBaseSearch...

Protein-protein interaction databases

STRINGA0PXA4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4541291.
GenomeReviewsGene locus NT01CX_0901 in contig CP000382_GR.
KEGGcno:NT01CX_0901.
PATRIC19477464. VBICloNov112828_0033.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0014.
HOGENOMHBG318080.
OMAQYPAACN.
ProtClustDBPRK00197.

Enzyme and pathway databases

BioCycCNOV386415:NT01CX_0901-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. 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 namePROA_CLONN
AccessionPrimary (citable) accession number: A0PXA4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 9, 2007
Last modified: December 14, 2011
This is version 44 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