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Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Methanosaeta thermophila (strain DSM 6194 / JCM 14653 / NBRC 101360 / PT) (Methanothrix thermophila)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-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 sitei49NucleophileUniRule annotation1
Sitei90Important for activityUniRule annotation1
Binding sitei100SubstrateUniRule annotation1
Binding sitei111SubstrateUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi180 – 185NADPUniRule 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:Mthe_0049
OrganismiMethanosaeta thermophila (strain DSM 6194 / JCM 14653 / NBRC 101360 / PT) (Methanothrix thermophila)
Taxonomic identifieri349307 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanomicrobiaMethanosarcinalesMethanosaetaceaeMethanosaeta
Proteomesi
  • UP000000674 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003350941 – 417Glutamyl-tRNA reductaseAdd BLAST417

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi349307.Mthe_0049.

Structurei

3D structure databases

ProteinModelPortaliA0B577.
SMRiA0B577.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni48 – 51Substrate bindingUniRule annotation4
Regioni105 – 107Substrate 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

eggNOGiarCOG01036. Archaea.
COG0373. LUCA.
HOGENOMiHOG000109651.
KOiK02492.
OrthoDBiPOG093Z06M3.

Family and domain databases

HAMAPiMF_00087. Glu_tRNA_reductase. 1 hit.
InterProiView protein in InterPro
IPR000343. 4pyrrol_synth_GluRdtase.
IPR015896. 4pyrrol_synth_GluRdtase_dimer.
IPR015895. 4pyrrol_synth_GluRdtase_N.
IPR018214. GluRdtase_CS.
IPR016040. NAD(P)-bd_dom.
IPR006151. Shikm_DH/Glu-tRNA_Rdtase.
PfamiView protein in Pfam
PF00745. GlutR_dimer. 1 hit.
PF05201. GlutR_N. 1 hit.
PF01488. Shikimate_DH. 1 hit.
PIRSFiPIRSF000445. 4pyrrol_synth_GluRdtase. 1 hit.
SUPFAMiSSF51735. SSF51735. 1 hit.
SSF69075. SSF69075. 1 hit.
SSF69742. SSF69742. 1 hit.
TIGRFAMsiTIGR01035. hemA. 1 hit.
PROSITEiView protein in PROSITE
PS00747. GLUTR. 1 hit.

Sequencei

Sequence statusi: Complete.

A0B577-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSRITSMLVT HKKASISEIE NAWHGDVEAL LKWVSSHDTV EECAVLKTCN
60 70 80 90 100
RVEIYVVSPR GEKVLFEIAK KARVSSRIID IHDHDESLLH LLRLASGLES
110 120 130 140 150
MIIGEDQILG QMKELYRTAK SLGYTGWVLD TAFKKAIQVG KRVRKETAIN
160 170 180 190 200
ERSVSVGSAA VDLAEQILGG LEGKSVLVIG AGETGELISK ALVSKNIGSL
210 220 230 240 250
YVTNRTFGTA LSLAASLGGT AVPYEEMKRK IREADVVISA TSAPHYILLK
260 270 280 290 300
DDIERAMEGR KNKLLIIDIA NPRDVDEAVR EIEGVELHNI DSLKQISDEN
310 320 330 340 350
MRLRMREIER VEAIIEEELE LLRAKYKRRE AEELLARIYS EAEKIKEQEV
360 370 380 390 400
RRAMNKLSAY HTLGEIEQKV LMDMSHSIVN KIFAEPTKAL KSAAERGNTE
410
MLRYAMELFR LNQEESD
Length:417
Mass (Da):46,840
Last modified:May 20, 2008 - v2
Checksum:iEFBFE3904762CEEB
GO

Sequence cautioni

The sequence ABK13851 differs from that shown. Reason: Erroneous initiation.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000477 Genomic DNA. Translation: ABK13851.1. Different initiation.

Genome annotation databases

EnsemblBacteriaiABK13851; ABK13851; Mthe_0049.
KEGGimtp:Mthe_0049.

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.

Entry informationi

Entry nameiHEM1_METTP
AccessioniPrimary (citable) accession number: A0B577
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: May 20, 2008
Last modified: May 10, 2017
This is version 75 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

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families