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Q6AHF6 (HEM1_LEIXX) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 75. 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:Lxx01050
OrganismLeifsonia xyli subsp. xyli (strain CTCB07) [Complete proteome] [HAMAP]
Taxonomic identifier281090 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaeMicrobacteriaceaeLeifsonia

Protein attributes

Sequence length432 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 – 432432Glutamyl-tRNA reductase HAMAP-Rule MF_00087
PRO_0000114034

Regions

Nucleotide binding191 – 1966NADP By similarity
Region46 – 494Substrate binding By similarity
Region116 – 1183Substrate binding By similarity

Sites

Active site471Nucleophile By similarity
Binding site1111Substrate By similarity
Binding site1221Substrate By similarity
Site1011Important for activity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6AHF6 [UniParc].

Last modified September 13, 2004. Version 1.
Checksum: EE221EFFFBE4DED5

FASTA43245,469
        10         20         30         40         50         60 
MLICFSSSHR TAAFDLLDQL ERHAPAVATA LAEHSELVTG SVVLATCNRF EAYLDIDEPL 

        70         80         90        100        110        120 
PAARAVSAET VIAAVGNAAG IDADLLRSSS RVYCDDAAAE HLLSVSSGLD SVVVGEGEIA 

       130        140        150        160        170        180 
GQVRRALTTA RQAGTVSQDL ERLFQVASRT SRGVKNRTGI ATAGRSIVRL ALDLAESRVS 

       190        200        210        220        230        240 
DWSRMRVLLI GTGKYAGASL AALRDRGVAD VQVHSPSGRA EKFALSHGVT AVPAGGLGAA 

       250        260        270        280        290        300 
LAHAHLIVTC TTVRDYTLTP GNFGQAQQQD GIERRLVIDL GLPRNVDSAV AELPGVELLD 

       310        320        330        340        350        360 
LETISLHAPV AELNAADDAR EIVGAAAAEF AAQTAEQAVK PALIALRKHV FDILDAEIAR 

       370        380        390        400        410        420 
ARTRGDSSEQ TEAALRHLAG VLLHTPSVRA RELARAGDAQ RFADAAETLF GLRIEEAPVH 

       430 
PRLIAVDRVT AS 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016822 Genomic DNA. Translation: AAT88189.1.
RefSeqYP_061294.1. NC_006087.1.

3D structure databases

ProteinModelPortalQ6AHF6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING281090.Lxx01050.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAT88189; AAT88189; Lxx01050.
GeneID2938311.
KEGGlxx:Lxx01050.
PATRIC22333648. VBILeiXyl11655_0102.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0373.
HOGENOMHOG000109649.
KOK02492.
OMAIGCSGSD.
OrthoDBEOG6MWNBM.
ProtClustDBPRK00045.

Enzyme and pathway databases

BioCycLXYL281090:GH0X-94-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_LEIXX
AccessionPrimary (citable) accession number: Q6AHF6
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: September 13, 2004
Last modified: February 19, 2014
This is version 75 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