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Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Methanosphaera stadtmanae (strain ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3)
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

Catalytic activityi

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

Pathway: 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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei46 – 461NucleophileUniRule annotation
Sitei77 – 771Important for activityUniRule annotation
Binding sitei87 – 871SubstrateUniRule annotation
Binding sitei98 – 981SubstrateUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi167 – 1726NADPUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Porphyrin biosynthesis

Keywords - Ligandi

NADP

Enzyme and pathway databases

BioCyciMSTA339860:GJEZ-1410-MONOMER.
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:Msp_1408
OrganismiMethanosphaera stadtmanae (strain ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3)
Taxonomic identifieri339860 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanobacteriaMethanobacterialesMethanobacteriaceaeMethanosphaera
ProteomesiUP000001931 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 395395Glutamyl-tRNA reductasePRO_1000004643Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi339860.Msp_1408.

Structurei

3D structure databases

ProteinModelPortaliQ2NEH4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni45 – 484Substrate bindingUniRule annotation
Regioni92 – 943Substrate bindingUniRule annotation

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

eggNOGiCOG0373.
HOGENOMiHOG000109651.
KOiK02492.
OMAiEIIFDAD.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_00087. Glu_tRNA_reductase.
InterProiIPR000343. 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.
[Graphical view]
PfamiPF00745. GlutR_dimer. 1 hit.
PF05201. GlutR_N. 1 hit.
PF01488. Shikimate_DH. 1 hit.
[Graphical view]
PIRSFiPIRSF000445. 4pyrrol_synth_GluRdtase. 1 hit.
SUPFAMiSSF69075. SSF69075. 1 hit.
SSF69742. SSF69742. 1 hit.
TIGRFAMsiTIGR01035. hemA. 1 hit.
PROSITEiPS00747. GLUTR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q2NEH4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLVNIRIDFK IADIETMEKS YAKLDMINAE LHEKLDILEE VTLKTCNRYE
60 70 80 90 100
IYLLIDEEVN IPTTTFIVEK NDMAINHLLR LASGLESMIM GEDQILGQIK
110 120 130 140 150
TARKNAIKNK TIGPKLEKVF TKAIHVGQTI RKNTHINEGG VSVGSGAVEL
160 170 180 190 200
IEEKYGSLKG KNVLIIGAGE MGTVVSKALL EKETNTIVVA NRTYDKARQL
210 220 230 240 250
AQELDGEAIK FDEMNNELVN IDIVISSTGA PHSIISKERI AFLPEEHLHD
260 270 280 290 300
MIMLDLANPH DIENDVQELG VKLYNLDDLR YVTDKNKERR NKEAIKAEAI
310 320 330 340 350
IEDETLLLKE SLKQMEITPI LSSLNIEAEK IRKQELDKTL HMLDLDKKSS
360 370 380 390
KKVDYLTRSI TDKLLYNIIN NLKEAAANND KDTIRNAKKI LLEYN
Length:395
Mass (Da):44,733
Last modified:February 7, 2006 - v1
Checksum:iA78341A99DDE5269
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000102 Genomic DNA. Translation: ABC57779.1.
RefSeqiWP_011406978.1. NC_007681.1.
YP_448422.1. NC_007681.1.

Genome annotation databases

EnsemblBacteriaiABC57779; ABC57779; Msp_1408.
GeneIDi3854884.
KEGGimst:Msp_1408.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000102 Genomic DNA. Translation: ABC57779.1.
RefSeqiWP_011406978.1. NC_007681.1.
YP_448422.1. NC_007681.1.

3D structure databases

ProteinModelPortaliQ2NEH4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi339860.Msp_1408.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABC57779; ABC57779; Msp_1408.
GeneIDi3854884.
KEGGimst:Msp_1408.

Phylogenomic databases

eggNOGiCOG0373.
HOGENOMiHOG000109651.
KOiK02492.
OMAiEIIFDAD.

Enzyme and pathway databases

UniPathwayiUPA00251; UER00316.
BioCyciMSTA339860:GJEZ-1410-MONOMER.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_00087. Glu_tRNA_reductase.
InterProiIPR000343. 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.
[Graphical view]
PfamiPF00745. GlutR_dimer. 1 hit.
PF05201. GlutR_N. 1 hit.
PF01488. Shikimate_DH. 1 hit.
[Graphical view]
PIRSFiPIRSF000445. 4pyrrol_synth_GluRdtase. 1 hit.
SUPFAMiSSF69075. SSF69075. 1 hit.
SSF69742. SSF69742. 1 hit.
TIGRFAMsiTIGR01035. hemA. 1 hit.
PROSITEiPS00747. GLUTR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The genome sequence of Methanosphaera stadtmanae reveals why this human intestinal archaeon is restricted to methanol and H2 for methane formation and ATP synthesis."
    Fricke W.F., Seedorf H., Henne A., Kruer M., Liesegang H., Hedderich R., Gottschalk G., Thauer R.K.
    J. Bacteriol. 188:642-658(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3.

Entry informationi

Entry nameiHEM1_METST
AccessioniPrimary (citable) accession number: Q2NEH4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: February 7, 2006
Last modified: April 1, 2015
This is version 71 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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

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

External Data

Dasty 3

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 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.