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Q9RRE5 (HEM1_DEIRA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 101. 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:DR_2547
OrganismDeinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422) [Reference proteome] [HAMAP]
Taxonomic identifier243230 [NCBI]
Taxonomic lineageBacteriaDeinococcus-ThermusDeinococciDeinococcalesDeinococcaceaeDeinococcus

Protein attributes

Sequence length350 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 – 350350Glutamyl-tRNA reductase HAMAP-Rule MF_00087
PRO_0000114019

Regions

Nucleotide binding185 – 1906NADP By similarity
Region53 – 564Substrate binding By similarity
Region110 – 1123Substrate binding By similarity

Sites

Active site541Nucleophile By similarity
Binding site1051Substrate By similarity
Binding site1161Substrate By similarity
Site951Important for activity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9RRE5 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 72B9BC71CA368507

FASTA35037,529
        10         20         30         40         50         60 
MPQPAPLDFV VVGLNHQTAP VEVRERVAVR PEEEGALLGH LARHADEVLL LATCNRTEVY 

        70         80         90        100        110        120 
LAGVHGDPLA AFEGAWGHAL LDHLYVYRGE AAVRHLYRVT AGLDSLVIGE TQIQGQVKRA 

       130        140        150        160        170        180 
WQSARERGLS GTLMNKVVQG ALAAGKRVRS HTGLSDKVVS VSSAAVELAQ AALGELSQRR 

       190        200        210        220        230        240 
ALILGAGETA ELTLTHLRAA GVQDVLVVNR TAERARALAE KLGGRACPAE ELSAALPEVD 

       250        260        270        280        290        300 
VVIASSAAPH YVVTAQNVRE ALAGRPGRAM FLIDISVPRI LDPEIASVPG AHLYNLDDLT 

       310        320        330        340        350 
AVVQRNMQSR RAALPQAEAI IRELGSDLSR WYLTRETQLA RQAELALACD 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE000513 Genomic DNA. Translation: AAF12088.1.
PIRF75259.
RefSeqNP_296267.1. NC_001263.1.

3D structure databases

ProteinModelPortalQ9RRE5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243230.DR_2547.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAF12088; AAF12088; DR_2547.
GeneID1798429.
KEGGdra:DR_2547.
PATRIC21632833. VBIDeiRad64572_2790.

Phylogenomic databases

eggNOGCOG0373.
HOGENOMHOG000109651.
KOK02492.
OMAMIICEEL.
OrthoDBEOG6MWNBM.

Enzyme and pathway databases

BioCycDRAD243230:GH46-2600-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]
PIRSFPIRSF000445. 4pyrrol_synth_GluRdtase. 1 hit.
SUPFAMSSF69742. SSF69742. 1 hit.
TIGRFAMsTIGR01035. hemA. 1 hit.
PROSITEPS00747. GLUTR. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHEM1_DEIRA
AccessionPrimary (citable) accession number: Q9RRE5
Entry history
Integrated into UniProtKB/Swiss-Prot: April 3, 2002
Last sequence update: May 1, 2000
Last modified: May 14, 2014
This is version 101 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