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Q0W5T5 (HEM1_UNCMA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 66. 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:UNCMA_19350
ORF Names:RCIX911
OrganismUncultured methanogenic archaeon RC-I [Complete proteome] [HAMAP]
Taxonomic identifier351160 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanomicrobiaMethanocellalesMethanocellaceaeMethanocella

Protein attributes

Sequence length427 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 – 427427Glutamyl-tRNA reductase HAMAP-Rule MF_00087
PRO_1000004720

Regions

Nucleotide binding179 – 1846NADP By similarity
Region48 – 514Substrate binding By similarity
Region104 – 1063Substrate binding By similarity

Sites

Active site491Nucleophile By similarity
Binding site991Substrate By similarity
Binding site1101Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0W5T5 [UniParc].

Last modified September 5, 2006. Version 1.
Checksum: 4A31968C7217BAC7

FASTA42746,694
        10         20         30         40         50         60 
MAQVCSISVN HRHAGIEGIE RARFRDPDVA MLRLLSLPGV SEAVVLQTCN RVEIYAVAES 

        70         80         90        100        110        120 
VEDIVGFARA EGMPLEIAEV RAGDDCLKGL LRLACGLESM IVGEDQILGQ LKTALLQARR 

       130        140        150        160        170        180 
LGTIGPVLST AIQKSIHVGA RARIETEINK GSVSIGSAAV ELAESLLGDL RGRTILVVGA 

       190        200        210        220        230        240 
GEMGTLVANA MAEKSLRAIY VANRTFEQAE KLASSLQGVA IRLERLCDYM GSADVVICAT 

       250        260        270        280        290        300 
GAPHLIITKK MVEQCKGEKP LIFIDITNPR NIEETVGEVP GVTLHNIDSL RQINEASMRR 

       310        320        330        340        350        360 
RQGEARKVEA IIEEELVLLQ RDIRRLHADR VIGDLYQRTD HIRATELRRA VARLSTAGSL 

       370        380        390        400        410        420 
TEQQISILHD FSMALTNKIL AAPTRQLRRA AERCDEDCLR TAEELFDLWV EESNGIPGNK 


TKASKTD 

« Hide

References

[1]"Genome of rice cluster I archaea -- the key methane producers in the rice rhizosphere."
Erkel C., Kube M., Reinhardt R., Liesack W.
Science 313:370-372(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM114193 Genomic DNA. Translation: CAJ36258.1.
RefSeqYP_685584.1. NC_009464.1.

3D structure databases

ProteinModelPortalQ0W5T5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING351160.RCIX911.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAJ36258; CAJ36258; RCIX911.
GeneID5145812.
KEGGrci:RCIX911.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0373.
HOGENOMHOG000109651.
KOK02492.
OMAHEVTGEY.

Enzyme and pathway databases

BioCycUMET351160:GJT4-1985-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_UNCMA
AccessionPrimary (citable) accession number: Q0W5T5
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: September 5, 2006
Last modified: May 14, 2014
This is version 66 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