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Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Deinococcus geothermalis (strain DSM 11300)
Status
Reviewed-Annotation score: -Protein inferred from homologyi

Functioni

Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).UniRule annotation

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.UniRule annotation

Catalytic activityi

L-glutamate 1-semialdehyde + NADP+ + tRNA(Glu) = L-glutamyl-tRNA(Glu) + NADPH.UniRule annotation

Pathwayi: protoporphyrin-IX biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes 5-aminolevulinate from L-glutamyl-tRNA(Glu).UniRule annotation
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Glutamyl-tRNA reductase (hemA)
  2. Glutamate-1-semialdehyde 2,1-aminomutase (hemL)
This subpathway is part of the pathway protoporphyrin-IX biosynthesis, which is itself part of Porphyrin-containing compound metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 5-aminolevulinate from L-glutamyl-tRNA(Glu), the pathway protoporphyrin-IX biosynthesis and in Porphyrin-containing compound metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei54NucleophileUniRule annotation1
Sitei95Important for activityUniRule annotation1
Binding sitei105SubstrateUniRule annotation1
Binding sitei116SubstrateUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi185 – 190NADPUniRule annotation6

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionOxidoreductase
Biological processPorphyrin biosynthesis
LigandNADP

Enzyme and pathway databases

UniPathwayiUPA00251; UER00316

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamyl-tRNA reductaseUniRule annotation (EC:1.2.1.70UniRule annotation)
Short name:
GluTRUniRule annotation
Gene namesi
Name:hemAUniRule annotation
Ordered Locus Names:Dgeo_2128
OrganismiDeinococcus geothermalis (strain DSM 11300)
Taxonomic identifieri319795 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciDeinococcalesDeinococcaceaeDeinococcus
Proteomesi
  • UP000002431 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003350271 – 349Glutamyl-tRNA reductaseAdd BLAST349

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi319795.Dgeo_2128

Structurei

3D structure databases

ProteinModelPortaliQ1IWG2
SMRiQ1IWG2
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni53 – 56Substrate bindingUniRule annotation4
Regioni110 – 112Substrate bindingUniRule annotation3

Domaini

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.UniRule annotation

Sequence similaritiesi

Belongs to the glutamyl-tRNA reductase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105C7E Bacteria
COG0373 LUCA
HOGENOMiHOG000109651
KOiK02492
OrthoDBiPOG091H05DA

Family and domain databases

Gene3Di3.30.460.301 hit
HAMAPiMF_00087 Glu_tRNA_reductase, 1 hit
InterProiView protein in InterPro
IPR000343 4pyrrol_synth_GluRdtase
IPR015895 4pyrrol_synth_GluRdtase_N
IPR018214 GluRdtase_CS
IPR036343 GluRdtase_N_sf
IPR036291 NAD(P)-bd_dom_sf
IPR006151 Shikm_DH/Glu-tRNA_Rdtase
PfamiView protein in Pfam
PF05201 GlutR_N, 1 hit
PF01488 Shikimate_DH, 1 hit
PIRSFiPIRSF000445 4pyrrol_synth_GluRdtase, 1 hit
SUPFAMiSSF51735 SSF51735, 1 hit
SSF69742 SSF69742, 1 hit
TIGRFAMsiTIGR01035 hemA, 1 hit
PROSITEiView protein in PROSITE
PS00747 GLUTR, 1 hit

Sequencei

Sequence statusi: Complete.

Q1IWG2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPPLAPLDFA VIGLNHQTAP VEVREQAAVR AGDEGKVLQH LSRYAREVML
60 70 80 90 100
LNTCNRTEVY LAGLQGDPLR AFESGWGRAL DGHLYVHRGE AAATHLYRVA
110 120 130 140 150
AGLDSLVIGE TQIQGQVKRA WQEAHARGLS GTLLNKVAQG ALAAGKRVRS
160 170 180 190 200
ETGLSDKVVS VSSAAVELAE AALGELRHRT ALILGAGETA ELTLTHLRAA
210 220 230 240 250
GVQDVIVVNR TEARARQLAD KLGGRACAAE YLHEVLPEAD VVIASSAAPH
260 270 280 290 300
YVLHGEGVRA ALAKRPERPI FLIDISVPRI LDPDIRAVSG AHLYNLDDLT
310 320 330 340
AIVSRNLQSR RAALPYAEAI IREAVADLLR WHLTREAQLG RRAVALASD
Length:349
Mass (Da):37,531
Last modified:May 20, 2008 - v2
Checksum:i9B1FA1D2703A99E9
GO

Sequence cautioni

The sequence ABF46422 differs from that shown. Reason: Erroneous initiation.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000359 Genomic DNA Translation: ABF46422.1 Different initiation.

Genome annotation databases

EnsemblBacteriaiABF46422; ABF46422; Dgeo_2128
KEGGidge:Dgeo_2128

Similar proteinsi

Entry informationi

Entry nameiHEM1_DEIGD
AccessioniPrimary (citable) accession number: Q1IWG2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: May 20, 2008
Last modified: March 28, 2018
This is version 92 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome