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B0R6C0 (HEM1_HALS3) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 52. 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:OE_3496R
OrganismHalobacterium salinarum (strain ATCC 29341 / DSM 671 / R1) [Complete proteome] [HAMAP]
Taxonomic identifier478009 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaHalobacteriaHalobacterialesHalobacteriaceaeHalobacterium

Protein attributes

Sequence length436 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 – 436436Glutamyl-tRNA reductase HAMAP-Rule MF_00087
PRO_1000093142

Regions

Nucleotide binding184 – 1896NADP By similarity
Region52 – 554Substrate binding By similarity
Region110 – 1123Substrate binding By similarity

Sites

Active site531Nucleophile By similarity
Binding site1051Substrate By similarity
Binding site1161Substrate By similarity
Site951Important for activity By similarity

Sequences

Sequence LengthMass (Da)Tools
B0R6C0 [UniParc].

Last modified April 8, 2008. Version 1.
Checksum: 3016F114705F6987

FASTA43645,450
        10         20         30         40         50         60 
MNGNTGVVSG VRVSHETASL DELAAASAAS TEAALDALLE QPPVEEAFVL QTCHRVEAYV 

        70         80         90        100        110        120 
VTADQASGRR ALGGAGFNPA GGGAISMGHE DSLRHLLRVA AGLESLVVGE DQILGQLRDA 

       130        140        150        160        170        180 
YDAAKDAGGI DHVLREAVTK AMHVGERART ETAINEGATS LGTAAVRLAE RKTQLADARA 

       190        200        210        220        230        240 
VVVGAGEMGA LAAKAFASAT VAEIVIANRT PARAVRVADM VSVPAEATTL ADARGRLDAA 

       250        260        270        280        290        300 
DVVVTATGSP EHVLPASAFA DAGDTVVVDL AQPRDVAPGA GGHDGVAVHD LDDLEAVTAA 

       310        320        330        340        350        360 
TRERREDAAR EVEAMIETEF ERLLTQYKRK RADEVIARMY ESADRLKSRE VQTAVHRLEA 

       370        380        390        400        410        420 
ESGSLSADER EVVESMADAL VSQLLAAPTK SLRDAAAEDD WSTIATALEL FNPEFEDGMP 

       430 
FDASRGGDAA SAESED 

« Hide

References

[1]"Evolution in the laboratory: the genome of Halobacterium salinarum strain R1 compared to that of strain NRC-1."
Pfeiffer F., Schuster S.C., Broicher A., Falb M., Palm P., Rodewald K., Ruepp A., Soppa J., Tittor J., Oesterhelt D.
Genomics 91:335-346(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 29341 / DSM 671 / R1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM774415 Genomic DNA. Translation: CAP14289.1.
RefSeqYP_001689635.1. NC_010364.1.

3D structure databases

ProteinModelPortalB0R6C0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING478009.OE3496R.

Proteomic databases

PRIDEB0R6C0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAP14289; CAP14289; OE_3496R.
GeneID5953600.
KEGGhsl:OE3496R.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0373.
HOGENOMHOG000109651.
KOK02492.
OMAYREADAN.

Enzyme and pathway databases

BioCycHSAL478009:GJVF-1440-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]
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.
PROSITEPS00747. GLUTR. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHEM1_HALS3
AccessionPrimary (citable) accession number: B0R6C0
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: April 8, 2008
Last modified: May 14, 2014
This is version 52 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