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Q5WUB2 (HEM1_LEGPL) 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:lpl2256
OrganismLegionella pneumophila (strain Lens) [Complete proteome] [HAMAP]
Taxonomic identifier297245 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaLegionellalesLegionellaceaeLegionella

Protein attributes

Sequence length424 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 – 424424Glutamyl-tRNA reductase HAMAP-Rule MF_00087
PRO_1000004631

Regions

Nucleotide binding185 – 1906NADP By similarity
Region49 – 524Substrate binding By similarity
Region110 – 1123Substrate binding By similarity

Sites

Active site501Nucleophile By similarity
Binding site1051Substrate By similarity
Binding site1161Substrate By similarity
Site951Important for activity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5WUB2 [UniParc].

Last modified November 23, 2004. Version 1.
Checksum: A72A07565967B5F3

FASTA42447,960
        10         20         30         40         50         60 
MVFVACGLNH KTAPIHVREK VALQPAMQDS LLSSLLDLPE VNEAAILSTC NRTEIYCDTN 

        70         80         90        100        110        120 
TPEVLGNWLA HEHQLSEELL SQFLYIHQGK EGIKHTLRVA SGLDSMMIGE PQILGQMKQA 

       130        140        150        160        170        180 
YQHACRLGTV KTQLRPVFEY IFRASKRIRT RSGIGANPVS IAYAAVQLIG QLFKNYHSLS 

       190        200        210        220        230        240 
VFLIGSGETA SLVAKYLHQH GVHRFLIASR TLENAQKLAE TFDGKTLSIG DIPQYLPLAD 

       250        260        270        280        290        300 
VVISATACPL PFINKSLVEH ALEQRNHAPM FLLDLAVPRD IEGNVNELEQ VHLYNVDDLQ 

       310        320        330        340        350        360 
SMIEKGMDER RNAALQAEQL IESELDNYIR WHRSLRAKDV ICDYRNQMHT LAQQELQRAL 

       370        380        390        400        410        420 
KKISAGQNQQ DVLNEFSMRL VNKLTHNPTI GLRQMAWDNR EDLLDLARYL FDTTANQSLY 


EEIS 

« Hide

References

[1]"Evidence in the Legionella pneumophila genome for exploitation of host cell functions and high genome plasticity."
Cazalet C., Rusniok C., Brueggemann H., Zidane N., Magnier A., Ma L., Tichit M., Jarraud S., Bouchier C., Vandenesch F., Kunst F., Etienne J., Glaser P., Buchrieser C.
Nat. Genet. 36:1165-1173(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Lens.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR628337 Genomic DNA. Translation: CAH16496.1.
RefSeqYP_127591.1. NC_006369.1.

3D structure databases

ProteinModelPortalQ5WUB2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING297245.lpl2256.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAH16496; CAH16496; lpl2256.
GeneID3114156.
KEGGlpf:lpl2256.
PATRIC22318329. VBILegPne33733_2475.

Organism-specific databases

LegioListlpl2256.
CMRSearch...

Phylogenomic databases

eggNOGCOG0373.
HOGENOMHOG000109650.
KOK02492.
OMARTEIYCA.
OrthoDBEOG6MWNBM.
ProtClustDBPRK00045.

Enzyme and pathway databases

BioCycLPNE297245:GJD4-2446-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_LEGPL
AccessionPrimary (citable) accession number: Q5WUB2
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: November 23, 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