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

A5ULU4 (HEM1_METS3) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 54. 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:Msm_0967
OrganismMethanobrevibacter smithii (strain PS / ATCC 35061 / DSM 861) [Complete proteome] [HAMAP]
Taxonomic identifier420247 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanobacteriaMethanobacterialesMethanobacteriaceaeMethanobrevibacter

Protein attributes

Sequence length399 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 – 399399Glutamyl-tRNA reductase HAMAP-Rule MF_00087
PRO_1000004642

Regions

Nucleotide binding173 – 1786NADP By similarity
Region45 – 484Substrate binding By similarity
Region98 – 1003Substrate binding By similarity

Sites

Active site461Nucleophile By similarity
Binding site931Substrate By similarity
Binding site1041Substrate By similarity
Site831Important for activity By similarity

Sequences

Sequence LengthMass (Da)Tools
A5ULU4 [UniParc].

Last modified July 10, 2007. Version 1.
Checksum: F2BB1E52489E6504

FASTA39944,990
        10         20         30         40         50         60 
MILNLRVDHK IANIDAMENI AKEMDQLFLE LQEKYSIVEY VEISTCNRKE YYIHNDNIDA 

        70         80         90        100        110        120 
SDSLLSHENK SIIIDYGDSV IKHLFRMTSG LESMIVGEDQ ILGQVSDAKQ KAFKERHCGK 

       130        140        150        160        170        180 
ILDSIFTKAI HVGRVVRNKT NINKGSISIG SAAVDLAEKH LGNLENKSVL VIGAGKMGKL 

       190        200        210        220        230        240 
VAKALAEKNL NAIFVANRTY YVAVELANDL NGHAVLFNEL GKYVQTADLI ISATGAPHYI 

       250        260        270        280        290        300 
LNKERLEKTD GDFKDLLMID IANPRDICED VCELGVKLFN IDDLREIADE NTKLRKKEFA 

       310        320        330        340        350        360 
EAENIIDEEF SLLKESFKLI GVEDIIANLR VSMENIRERE TEKAIAKLSD VDANAKIIDN 

       370        380        390 
LTNSIVNKIF FDISKKIKQA AHENDEELIR AIEFMFEEK 

« Hide

References

[1]"Genomic and metabolic adaptations of Methanobrevibacter smithii to the human gut."
Samuel B.S., Hansen E.E., Manchester J.K., Coutinho P.M., Henrissat B., Fulton R., Latreille P., Kim K., Wilson R.K., Gordon J.I.
Proc. Natl. Acad. Sci. U.S.A. 104:10643-10648(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PS / ATCC 35061 / DSM 861.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000678 Genomic DNA. Translation: ABQ87172.1.
RefSeqYP_001273540.1. NC_009515.1.

3D structure databases

ProteinModelPortalA5ULU4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING420247.Msm_0967.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABQ87172; ABQ87172; Msm_0967.
GeneID5217012.
KEGGmsi:Msm_0967.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0373.
HOGENOMHOG000109651.
KOK02492.
OMAKMLHGTM.

Enzyme and pathway databases

BioCycMSMI420247:GHWZ-992-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.
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.
ProtoNetSearch...

Entry information

Entry nameHEM1_METS3
AccessionPrimary (citable) accession number: A5ULU4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: July 10, 2007
Last modified: May 14, 2014
This is version 54 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