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A9A8K3 (HEM1_METM6) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 51. 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:MmarC6_0859
OrganismMethanococcus maripaludis (strain C6 / ATCC BAA-1332) [Complete proteome] [HAMAP]
Taxonomic identifier444158 [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_1000093150

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
A9A8K3 [UniParc].

Last modified January 15, 2008. Version 1.
Checksum: F42CF2F9564B848E

FASTA38243,638
        10         20         30         40         50         60 
MLVVKADYKK YPIPVLEKMR IDEDEFYKKY EACVVVQTCN RIEAYFDTEV NSDIDCILND 

        70         80         90        100        110        120 
FSGFDVLKGK TATFHFLRVS CGMESMILGE NQILGQIKTS FQKARELKKT SRYLDGLFLK 

       130        140        150        160        170        180 
AIHVGQRART ETKINEGGVS IGSAAVELAE KNFGLTNRNV LLIGAGEMGT LVAKALLEKH 

       190        200        210        220        230        240 
IKAVIVSNRT YERAETLAEE LKGIAVHFDK LKEAINFSDV IICATSSPHY ILKKEDLNDV 

       250        260        270        280        290        300 
GNKIIIDIAN PRDVDDAVRE FENIKLYTID DLRNISDKNI QKRVEEVPAV EKIINEEYEV 

       310        320        330        340        350        360 
LMKQIEKINI EEVLKDFNSY VEEIRVKELE KAIKLSKTKN PEEIMENFSK AFVKRITHDF 

       370        380 
VSYSINTSKE DLMNSAWWKN GK 

« Hide

References

[1]"Complete sequence of Methanococcus maripaludis C6."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Clum A., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Sieprawska-Lupa M., Whitman W.B., Richardson P.
Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C6 / ATCC BAA-1332.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000867 Genomic DNA. Translation: ABX01676.1.
RefSeqYP_001548908.1. NC_009975.1.

3D structure databases

ProteinModelPortalA9A8K3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING444158.MmarC6_0859.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABX01676; ABX01676; MmarC6_0859.
GeneID5738024.
KEGGmmx:MmarC6_0859.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0373.
HOGENOMHOG000109651.
KOK02492.
OMAMIICEEL.

Enzyme and pathway databases

BioCycMMAR444158:GHN2-876-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_METM6
AccessionPrimary (citable) accession number: A9A8K3
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: January 15, 2008
Last modified: May 14, 2014
This is version 51 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