Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q8PW60 (HEM1_METMA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 90. 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:MM_1741
OrganismMethanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88) (Methanosarcina frisia) [Complete proteome] [HAMAP]
Taxonomic identifier192952 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanomicrobiaMethanosarcinalesMethanosarcinaceaeMethanosarcina

Protein attributes

Sequence length448 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 – 448448Glutamyl-tRNA reductase HAMAP-Rule MF_00087
PRO_0000114103

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
Q8PW60 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: 0733780153168AD9

FASTA44850,562
        10         20         30         40         50         60 
MTEISSMVIS HKKAKVEEME SAWHGDLDGL LRNLYKHEYV YECVVLKTCN RVEIYVVSPK 

        70         80         90        100        110        120 
SSSVLFSFAK EMGASTHIID FYGHDESLEH LLRLAGGLES MIVGEDQILG QIKDLYAYSK 

       130        140        150        160        170        180 
KAGTTGKILE TAFEKAIQVG KRIRNETRIN KGSVSIGSAA VDLAEDIFGG LTGKNVLVIG 

       190        200        210        220        230        240 
AGEIGVLVAK ALAEKDIEAI YIANRTYKKA EEIAYELGGH AVRLDDIRDY LPGADVVISG 

       250        260        270        280        290        300 
TGAPHYILTR EIVEEAIKCR ERKLLLIDIA NPRDIEESVV ELENVELCNI DNLRVISERT 

       310        320        330        340        350        360 
LRMRKEEAKK AEAIIQEEIR LLNLQYKRQK ADRLISELYK QVYDVRLRER QKAVNRLSSY 

       370        380        390        400        410        420 
HTIGDIETEV LDDLTRSIVN KILGEPTKVL RQAAELGNEE FLDVVSRVFC LDKEKVRFEK 

       430        440 
IKQAKFDQIK PGCTKEQAEV KEEYAVKD 

« Hide

References

[1]"The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea."
Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A., Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C., Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S., Bhattacharyya A., Lykidis A., Overbeek R. expand/collapse author list , Klenk H.-P., Gunsalus R.P., Fritz H.-J., Gottschalk G.
J. Mol. Microbiol. Biotechnol. 4:453-461(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE008384 Genomic DNA. Translation: AAM31437.1.
RefSeqNP_633765.1. NC_003901.1.

3D structure databases

ProteinModelPortalQ8PW60.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING192952.MM_1741.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAM31437; AAM31437; MM_1741.
GeneID1480083.
KEGGmma:MM_1741.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0373.
HOGENOMHOG000109651.
KOK02492.
OMALAHKLTN.

Enzyme and pathway databases

BioCycMMAZ192952:GCK2-1784-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_METMA
AccessionPrimary (citable) accession number: Q8PW60
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 2003
Last sequence update: October 1, 2002
Last modified: May 14, 2014
This is version 90 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