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A4WJE1 (HEM11_PYRAR) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 57. 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:
Glutamyl-tRNA reductase 1

Short name=GluTR 1
EC=1.2.1.70
Gene names
Name:hemA1
Ordered Locus Names:Pars_0928
OrganismPyrobaculum arsenaticum (strain DSM 13514 / JCM 11321) [Complete proteome] [HAMAP]
Taxonomic identifier340102 [NCBI]
Taxonomic lineageArchaeaCrenarchaeotaThermoproteiThermoprotealesThermoproteaceaePyrobaculum

Protein attributes

Sequence length387 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA) By similarity. HAMAP-Rule MF_00087

Catalytic activity

L-glutamate 1-semialdehyde + NADP+ + tRNA(Glu) = L-glutamyl-tRNA(Glu) + NADPH. HAMAP-Rule MF_00087

Pathway

Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2. HAMAP-Rule MF_00087

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_00087

Domain

Possesses an unusual extended V-shaped dimeric structure with each monomer consisting of three distinct domains arranged along a curved 'spinal' alpha-helix. The N-terminal catalytic domain specifically recognizes the glutamate moiety of the substrate. The second domain is the NADPH-binding domain, and the third C-terminal domain is responsible for dimerization By similarity. HAMAP-Rule MF_00087

Miscellaneous

During catalysis, the active site Cys acts as a nucleophile attacking the alpha-carbonyl group of tRNA-bound glutamate with the formation of a thioester intermediate between enzyme and glutamate, and the concomitant release of tRNA(Glu). The thioester intermediate is finally reduced by direct hydride transfer from NADPH, to form the product GSA By similarity.

Sequence similarities

Belongs to the glutamyl-tRNA reductase family.

Ontologies

Keywords
   Biological processPorphyrin biosynthesis
   LigandNADP
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processprotoporphyrinogen IX biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functionNADP binding

Inferred from electronic annotation. Source: InterPro

glutamyl-tRNA reductase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 387387Glutamyl-tRNA reductase 1 HAMAP-Rule MF_00087
PRO_0000335096

Regions

Nucleotide binding175 – 1806NADP By similarity
Region45 – 484Substrate binding By similarity
Region101 – 1033Substrate binding By similarity

Sites

Active site461Nucleophile By similarity
Binding site961Substrate By similarity
Binding site1071Substrate By similarity
Site861Important for activity By similarity

Sequences

Sequence LengthMass (Da)Tools
A4WJE1 [UniParc].

Last modified May 29, 2007. Version 1.
Checksum: D8AFB667A047C5FA

FASTA38743,082
        10         20         30         40         50         60 
MDLVNGLVAL SLTHKELGVD ELSKVANGVH RVCVSLRQPL FVLHTCNRVE AYLYNPPDEV 

        70         80         90        100        110        120 
VEIVKSGYAP YVEKVVERRG VDAARHLFRV AAGLESMLIG ETDVLGQLEE AFDRQVRAGY 

       130        140        150        160        170        180 
TRELLKTVVE RAIRVGKRVR TETGISRGPR GLGSLSILYV KEKIDLTNAR VCVIGAGSVG 

       190        200        210        220        230        240 
RGLVKELIDA GARRLVVVNR SVEKAADLGV EVWPLSERSV ERCLEDFDVV FTAVATFEPI 

       250        260        270        280        290        300 
IKSVPRDARV RIIVDMGMPR NTAAGLPVEV VTIDSLRDLA DRFNAMRDAE IKKAEEIVEE 

       310        320        330        340        350        360 
ELVALERLLR IRWVEEVSAK LLEYWFKIAE EEGERAGGLE AKIAARTTVK RTLLPVVNYL 

       370        380 
KKVAVSDIDE AYRIISVLRL SYGLKDL 

« Hide

References

[1]"Complete sequence of Pyrobaculum arsenaticum DSM 13514."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N. expand/collapse author list , Cozen A.E., Fitz-Gibbon S.T., House C.H., Saltikov C., Lowe T.M., Richardson P.
Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 13514 / JCM 11321.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000660 Genomic DNA. Translation: ABP50508.1.
RefSeqYP_001153160.1. NC_009376.1.

3D structure databases

ProteinModelPortalA4WJE1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING340102.Pars_0928.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABP50508; ABP50508; Pars_0928.
GeneID5054302.
KEGGpas:Pars_0928.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0373.
HOGENOMHOG000112880.
KOK02492.
OMAVANGVHR.

Enzyme and pathway databases

BioCycPARS340102:GHGQ-939-MONOMER.
UniPathwayUPA00251; UER00316.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
HAMAPMF_00087. Glu_tRNA_reductase.
InterProIPR000343. 4pyrrol_synth_GluRdtase.
IPR015895. 4pyrrol_synth_GluRdtase_N.
IPR016040. NAD(P)-bd_dom.
IPR018214. Pyrrol_synth_GluRdtase_CS.
IPR006151. Shikm_DH/Glu-tRNA_Rdtase.
[Graphical view]
PfamPF05201. GlutR_N. 1 hit.
PF01488. Shikimate_DH. 1 hit.
[Graphical view]
SUPFAMSSF69742. SSF69742. 1 hit.
PROSITEPS00747. GLUTR. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHEM11_PYRAR
AccessionPrimary (citable) accession number: A4WJE1
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: May 29, 2007
Last modified: May 14, 2014
This is version 57 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