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A2BJB7 (HEM1_HYPBU) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 63. 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:Hbut_0206
OrganismHyperthermus butylicus (strain DSM 5456 / JCM 9403) [Reference proteome] [HAMAP]
Taxonomic identifier415426 [NCBI]
Taxonomic lineageArchaeaCrenarchaeotaThermoproteiDesulfurococcalesPyrodictiaceaeHyperthermus

Protein attributes

Sequence length411 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
Reference 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 – 411411Glutamyl-tRNA reductase HAMAP-Rule MF_00087
PRO_0000335089

Regions

Nucleotide binding179 – 1846NADP By similarity
Region49 – 524Substrate binding By similarity
Region104 – 1063Substrate binding By similarity

Sites

Active site501Nucleophile By similarity
Binding site991Substrate By similarity
Binding site1101Substrate By similarity
Site891Important for activity By similarity

Sequences

Sequence LengthMass (Da)Tools
A2BJB7 [UniParc].

Last modified February 20, 2007. Version 1.
Checksum: C744C393B3D4C4FE

FASTA41145,007
        10         20         30         40         50         60 
MPRLLEELTA VILTHRDAPL DVVGSFESRV GEAYQILRGV VDEAVVLATC NRFEVYALPR 

        70         80         90        100        110        120 
RGFVETVIGF LGEASRYARI LHGMDVVRHL FRVAAGLESA IIGENEILGQ VARAYEEARR 

       130        140        150        160        170        180 
RGVAGKYLGL LFSQAVRTGK LVRSRTRISY GNVGAPGAAV KLAREAAGGF DGKHVVVVGA 

       190        200        210        220        230        240 
GEAGSIMASL VREEAPTARI SIVNRSVDRA RELAGKVRGE AYGLDMLPKL LAAADVVLVA 

       250        260        270        280        290        300 
VTVNEPVIKR SMLEDVGRHL VVVDISNPPA VEQPIPSNVY YAGLRDVEKV IKEVLAVRIR 

       310        320        330        340        350        360 
EVPKAEAIVE EQVALLRKLW LKRGADEAIA EIMRYANRVM EEEVEELVSR LRGLGVDGAA 

       370        380        390        400        410 
LLVARSFAYS LTKKLLRPLI LYAHEAALEG SLSKLEEIAQ KYRDELARRQ H 

« Hide

References

[1]"The genome of Hyperthermus butylicus: a sulfur-reducing, peptide fermenting, neutrophilic Crenarchaeote growing up to 108 degrees C."
Bruegger K., Chen L., Stark M., Zibat A., Redder P., Ruepp A., Awayez M., She Q., Garrett R.A., Klenk H.-P.
Archaea 2:127-135(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 5456 / JCM 9403.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000493 Genomic DNA. Translation: ABM80078.1.
RefSeqYP_001012423.1. NC_008818.1.

3D structure databases

ProteinModelPortalA2BJB7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING415426.Hbut_0206.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABM80078; ABM80078; Hbut_0206.
GeneID4782332.
KEGGhbu:Hbut_0206.

Phylogenomic databases

eggNOGCOG0373.
KOK02492.
OMAEHMIEDE.

Enzyme and pathway databases

BioCycHBUT415426:GC56-206-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.
IPR006151. Shikm_DH/Glu-tRNA_Rdtase.
[Graphical view]
PfamPF00745. GlutR_dimer. 1 hit.
PF05201. GlutR_N. 1 hit.
PF01488. Shikimate_DH. 1 hit.
[Graphical view]
PIRSFPIRSF000445. 4pyrrol_synth_GluRdtase. 1 hit.
SUPFAMSSF69075. SSF69075. 1 hit.
SSF69742. SSF69742. 1 hit.
TIGRFAMsTIGR01035. hemA. 1 hit.
ProtoNetSearch...

Entry information

Entry nameHEM1_HYPBU
AccessionPrimary (citable) accession number: A2BJB7
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: February 20, 2007
Last modified: July 9, 2014
This is version 63 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