Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

B1YBN0 (HEM1_PYRNV) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 49. 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

Short name=GluTR
EC=1.2.1.70
Gene names
Name:hemA
Ordered Locus Names:Tneu_1917
OrganismPyrobaculum neutrophilum (strain DSM 2338 / JCM 9278 / V24Sta) (Thermoproteus neutrophilus) [Complete proteome] [HAMAP]
Taxonomic identifier444157 [NCBI]
Taxonomic lineageArchaeaCrenarchaeotaThermoproteiThermoprotealesThermoproteaceaePyrobaculum

Protein attributes

Sequence length393 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 – 393393Glutamyl-tRNA reductase HAMAP-Rule MF_00087
PRO_1000093175

Regions

Nucleotide binding177 – 1826NADP By similarity
Region47 – 504Substrate binding By similarity
Region103 – 1053Substrate binding By similarity

Sites

Active site481Nucleophile By similarity
Binding site981Substrate By similarity
Binding site1091Substrate By similarity
Site881Important for activity By similarity

Sequences

Sequence LengthMass (Da)Tools
B1YBN0 [UniParc].

Last modified May 20, 2008. Version 1.
Checksum: 27D03C3CC36DF232

FASTA39342,756
        10         20         30         40         50         60 
MDLLAPLSAV VLTYREVSAE ALGKVGQEMK RCIERRARAF PMYVLHTCSR VEAYLYGAPP 

        70         80         90        100        110        120 
EEVQEVAEAY RRYVDSVRVI TGAEAARHLF RVAAGLDSIL IGETDVLGQV EEAFDRQVRA 

       130        140        150        160        170        180 
GYTRGLLKTV VERAVRVGKR VRTETAISRG PRGLGSLSII YVSRLLDLRQ AKAAVLGAGA 

       190        200        210        220        230        240 
VGSGLAMELA SRGVGKLYIL NRTFEKAREV AAKTGGEARP LTREEVERCL RECDVVFSSV 

       250        260        270        280        290        300 
HSMEYVIDRV PEGASVKIVV DLGVPQTVAP GLPVKVVRIE DLRQVAEQYN AERAAEVAKA 

       310        320        330        340        350        360 
EAIVEEELAA LPRLLARRYV EETVAALLET AMTAAEEEGA RAGCDAAALA AKTTVKRVLL 

       370        380        390 
PLVEKMKKMA EDGQMEEAVR LANVLTQAVG RKT 

« Hide

References

[1]"Complete sequence of Thermoproteus neutrophilus V24Sta."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L. expand/collapse author list , Kyrpides N., Mikhailova N., Biddle J.F., Zhang Z., Fitz-Gibbon S.T., Lowe T.M., Saltikov C., House C.H., Richardson P.
Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 2338 / JCM 9278 / V24Sta.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001014 Genomic DNA. Translation: ACB40832.1.
RefSeqYP_001795278.1. NC_010525.1.

3D structure databases

ProteinModelPortalB1YBN0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING444157.Tneu_1917.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACB40832; ACB40832; Tneu_1917.
GeneID6164814.
KEGGtne:Tneu_1917.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0373.
HOGENOMHOG000112880.
KOK02492.
OMAYREADAN.

Enzyme and pathway databases

BioCycTNEU444157:GHL2-1966-MONOMER.
UniPathwayUPA00251; UER00316.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
HAMAPMF_00087. Glu_tRNA_reductase.
InterProIPR000343. 4pyrrol_synth_GluRdtase.
IPR015896. 4pyrrol_synth_GluRdtase_dimer.
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]
SUPFAMSSF69075. SSF69075. 1 hit.
SSF69742. SSF69742. 1 hit.
PROSITEPS00747. GLUTR. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHEM1_PYRNV
AccessionPrimary (citable) accession number: B1YBN0
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: May 20, 2008
Last modified: May 14, 2014
This is version 49 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