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A0B577 (HEM1_METTP) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 59. 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:Mthe_0049
OrganismMethanosaeta thermophila (strain DSM 6194 / PT) (Methanothrix thermophila (strain DSM 6194 / PT)) [Complete proteome] [HAMAP]
Taxonomic identifier349307 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanomicrobiaMethanosarcinalesMethanosaetaceaeMethanosaeta

Protein attributes

Sequence length417 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.

Sequence caution

The sequence ABK13851.1 differs from that shown. Reason: Erroneous initiation.

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 – 417417Glutamyl-tRNA reductase HAMAP-Rule MF_00087
PRO_0000335094

Regions

Nucleotide binding180 – 1856NADP By similarity
Region48 – 514Substrate binding By similarity
Region105 – 1073Substrate binding By similarity

Sites

Active site491Nucleophile By similarity
Binding site1001Substrate By similarity
Binding site1111Substrate By similarity
Site901Important for activity By similarity

Sequences

Sequence LengthMass (Da)Tools
A0B577 [UniParc].

Last modified May 20, 2008. Version 2.
Checksum: EFBFE3904762CEEB

FASTA41746,840
        10         20         30         40         50         60 
MSRITSMLVT HKKASISEIE NAWHGDVEAL LKWVSSHDTV EECAVLKTCN RVEIYVVSPR 

        70         80         90        100        110        120 
GEKVLFEIAK KARVSSRIID IHDHDESLLH LLRLASGLES MIIGEDQILG QMKELYRTAK 

       130        140        150        160        170        180 
SLGYTGWVLD TAFKKAIQVG KRVRKETAIN ERSVSVGSAA VDLAEQILGG LEGKSVLVIG 

       190        200        210        220        230        240 
AGETGELISK ALVSKNIGSL YVTNRTFGTA LSLAASLGGT AVPYEEMKRK IREADVVISA 

       250        260        270        280        290        300 
TSAPHYILLK DDIERAMEGR KNKLLIIDIA NPRDVDEAVR EIEGVELHNI DSLKQISDEN 

       310        320        330        340        350        360 
MRLRMREIER VEAIIEEELE LLRAKYKRRE AEELLARIYS EAEKIKEQEV RRAMNKLSAY 

       370        380        390        400        410 
HTLGEIEQKV LMDMSHSIVN KIFAEPTKAL KSAAERGNTE MLRYAMELFR LNQEESD 

« Hide

References

[1]"Complete sequence of Methanosaeta thermophila PT."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N. expand/collapse author list , Kim E., Smith K.S., Ingram-Smith C., Richardson P.
Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 6194 / PT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000477 Genomic DNA. Translation: ABK13851.1. Different initiation.
RefSeqYP_842491.1. NC_008553.1.

3D structure databases

ProteinModelPortalA0B577.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING349307.Mthe_0049.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABK13851; ABK13851; Mthe_0049.
GeneID4462740.
KEGGmtp:Mthe_0049.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0373.
HOGENOMHOG000109651.
KOK02492.
ProtClustDBPRK00045.

Enzyme and pathway databases

BioCycMMET349307:GHKI-52-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_METTP
AccessionPrimary (citable) accession number: A0B577
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: May 20, 2008
Last modified: February 19, 2014
This is version 59 of the entry and version 2 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