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A4G0A1 (HEM1_METM5) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 57. 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:MmarC5_1588
OrganismMethanococcus maripaludis (strain C5 / ATCC BAA-1333) [Complete proteome] [HAMAP]
Taxonomic identifier402880 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanococciMethanococcalesMethanococcaceaeMethanococcus

Protein attributes

Sequence length382 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
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 – 382382Glutamyl-tRNA reductase HAMAP-Rule MF_00087
PRO_1000004639

Regions

Nucleotide binding164 – 1696NADP By similarity
Region38 – 414Substrate binding By similarity
Region90 – 923Substrate binding By similarity

Sites

Active site391Nucleophile By similarity
Binding site851Substrate By similarity
Binding site961Substrate By similarity
Site751Important for activity By similarity

Sequences

Sequence LengthMass (Da)Tools
A4G0A1 [UniParc].

Last modified April 17, 2007. Version 1.
Checksum: 1224E8DC82499F32

FASTA38243,554
        10         20         30         40         50         60 
MLVVRADYKK YPVPVLEKMR IDEDEFYNKY DACVVVQTCN RIEAYFDTEI NSNVDGILKD 

        70         80         90        100        110        120 
FQGFDVLKGK NATFHFLKVS CGMDSMILGE NQILGQIKTS FQKARELKKT SRYLDSLFLK 

       130        140        150        160        170        180 
AIHVGQRART ETKINEGGVS IGSAAVELAE KNFGLANRNV LLIGAGEMGT LVAKALIEKH 

       190        200        210        220        230        240 
IKAVIVANRT YERAETLAKE LKGMAVHFDK LKEAINFSDV IICATSSPHH ILEKKDLIDV 

       250        260        270        280        290        300 
GNKIIIDIAN PRDVDDSVRE LENIELYAID DLRHISDKNL QSRIEEIPAV EKIIDEEYEV 

       310        320        330        340        350        360 
LMKQIEKINV EEVLKEFNNY IEEIRVKELE KAIKLSKTKN PEEIMENFSK AFAKRITHDF 

       370        380 
VSYSINTSKE DLMNSAWWKN GK 

« Hide

References

[1]"Complete sequence of chromosome of Methanococcus maripaludis C5."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Han C., Detter J.C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N. expand/collapse author list , Mikhailova N., Sieprawska-Lupa M., Whitman W.B., Richardson P.
Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C5 / ATCC BAA-1333.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000609 Genomic DNA. Translation: ABO35885.1.
RefSeqYP_001098099.1. NC_009135.1.

3D structure databases

ProteinModelPortalA4G0A1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING402880.MmarC5_1588.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABO35885; ABO35885; MmarC5_1588.
GeneID4929215.
KEGGmmq:MmarC5_1588.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0373.
HOGENOMHOG000109651.
KOK02492.
OMAYREADAN.

Enzyme and pathway databases

BioCycMMAR402880:GJ2R-1617-MONOMER.
UniPathwayUPA00251; UER00316.

Family and domain databases

Gene3D1.10.1200.70. 1 hit.
3.40.50.720. 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_METM5
AccessionPrimary (citable) accession number: A4G0A1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: April 17, 2007
Last modified: May 14, 2014
This is version 57 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