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B9LE47 (PROA_CHLSY) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 37. 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:Chy400_1753
OrganismChloroflexus aurantiacus (strain ATCC 29364 / DSM 637 / Y-400-fl) [Complete proteome] [HAMAP]
Taxonomic identifier480224 [NCBI]
Taxonomic lineageBacteriaChloroflexiChloroflexalesChloroflexaceaeChloroflexus

Protein attributes

Sequence length422 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-Rule MF_00412

Catalytic activity

L-glutamate 5-semialdehyde + phosphate + NADP+ = L-glutamyl 5-phosphate + NADPH. HAMAP-Rule MF_00412

Pathway

Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-glutamate: step 2/2. HAMAP-Rule MF_00412

Subcellular location

Cytoplasm By similarity HAMAP-Rule 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_processL-proline biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   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: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 422422Gamma-glutamyl phosphate reductase HAMAP-Rule MF_00412
PRO_1000193586

Sequences

Sequence LengthMass (Da)Tools
B9LE47 [UniParc].

Last modified March 24, 2009. Version 1.
Checksum: 68BC84715CCE3378

FASTA42244,515
        10         20         30         40         50         60 
MVDLEAIGRR AKTAARALAK LSTEQKNAAL CAIADGLLAR QDKILAANAA DVADAEKGGT 

        70         80         90        100        110        120 
PPAIVDRMLL TPARLAAIAG DCRQVASLPD PVGEIFDRRE LPSGLRLYKR RVPIGVIGAI 

       130        140        150        160        170        180 
YEARPNVTVD IASLCLKAGN AVILRGGSDI ARSVAATTEV IALALEQAGL PAFAVQSIID 

       190        200        210        220        230        240 
PDRELVRQLL RLDRYVDMII PRGGAGLHRF CVENATVPVI VGGMGVSHIY VEPSADFARA 

       250        260        270        280        290        300 
VPVIVNAKVQ RPGACNALDT LLVHRAAAST FLPLVAAALA QHGVELRCDL EALAILADAP 

       310        320        330        340        350        360 
GHEAWNLKPA SPTDFGCEFL ALIVAIKIVG SIDEALDHIA LYGGHSEAIL TGDPISAERF 

       370        380        390        400        410        420 
TREVDATAVF VNASTRFNDG GQFGLGAEVA ISTNRLHARG PMGLQELTTY TWIGEGDYLV 


RA 

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References

[1]"Complete sequence of Chloroflexus sp. Y-400-fl."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Kiss H., Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N. expand/collapse author list , Ovchinnikova G., Bryant D.A., Richardson P.
Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 29364 / DSM 637 / Y-400-fl.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001364 Genomic DNA. Translation: ACM53163.1.
RefSeqYP_002569489.1. NC_012032.1.

3D structure databases

ProteinModelPortalB9LE47.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING480224.Chy400_1753.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACM53163; ACM53163; Chy400_1753.
GeneID7405142.
KEGGchl:Chy400_1753.
PATRIC21423067. VBIChlSp61043_1833.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0014.
HOGENOMHOG000246356.
KOK00147.
OMACNAIETL.
OrthoDBEOG6FFSCX.
ProtClustDBPRK00197.

Enzyme and pathway databases

BioCycCSP480224:GHIY-1773-MONOMER.
UniPathwayUPA00098; UER00360.

Family and domain databases

Gene3D3.40.309.10. 1 hit.
3.40.605.10. 2 hits.
HAMAPMF_00412. ProA.
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]
PANTHERPTHR11063:SF1. PTHR11063:SF1. 1 hit.
PfamPF00171. Aldedh. 1 hit.
[Graphical view]
PIRSFPIRSF000151. GPR. 1 hit.
SUPFAMSSF53720. SSF53720. 1 hit.
TIGRFAMsTIGR00407. proA. 1 hit.
PROSITEPS01223. PROA. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePROA_CHLSY
AccessionPrimary (citable) accession number: B9LE47
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 24, 2009
Last modified: February 19, 2014
This is version 37 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways