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Q1MRJ8 (HEM1_LAWIP) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 69. 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:LI0322
OrganismLawsonia intracellularis (strain PHE/MN1-00) [Complete proteome] [HAMAP]
Taxonomic identifier363253 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaDesulfovibrionalesDesulfovibrionaceaeLawsonia

Protein attributes

Sequence length430 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.

Sequence caution

The sequence CAJ54378.1 differs from that shown. Reason: Erroneous initiation.

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 – 430430Glutamyl-tRNA reductase HAMAP-Rule MF_00087
PRO_0000335048

Regions

Nucleotide binding188 – 1936NADP By similarity
Region50 – 534Substrate binding By similarity
Region113 – 1153Substrate binding By similarity

Sites

Active site511Nucleophile By similarity
Binding site1081Substrate By similarity
Binding site1191Substrate By similarity
Site981Important for activity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1MRJ8 [UniParc].

Last modified May 20, 2008. Version 2.
Checksum: E184D47B6713B983

FASTA43048,524
        10         20         30         40         50         60 
MEQHIYLIGM NHRTASIDVR ECFALTEHCS KDDWAIPLIK GIQESLILST CNRVEILAVG 

        70         80         90        100        110        120 
DSNTPEIILS AWAKVKTRSI EELVPHTYTY QGRSAISHLF CVASSLDSMV LGEPQILGQL 

       130        140        150        160        170        180 
KDAYKLATIA GASKTILNRL LHKAFSVAKR VRTETSIASN AVSISYAAVK LAKKIFGTMN 

       190        200        210        220        230        240 
QYKAMLIGAG EMAELAAMHL MQAGIQQLKI VNRTYSQAQE LASQFRGEAI PFEKLVTYLA 

       250        260        270        280        290        300 
EVDIVISSTG APQTIIHFND IKNILSKRKH YPMLFIDIAV PRDIDPNVHQ LDNIYLYDID 

       310        320        330        340        350        360 
DLKEIVEDNI VQRQDEAIKA KHIIQDEIDS FCAWLQALIL QPTIVDLRKR FSTYAEEELE 

       370        380        390        400        410        420 
RTLKKIGPVD RKTREALETM IDALIRKLTH DPISYLKCAH RTIDTNHITL ARQMFNLDKI 

       430 
PQTNKAVNED 

« Hide

References

[1]"The complete genome sequence of Lawsonia intracellularis: the causative agent of proliferative enteropathy."
Kaur K., Zhang Q., Beckler D., Munir S., Li L., Kinsley K., Herron L., Peterson A., May B., Singh S., Gebhart C., Kapur V.
Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PHE/MN1-00.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM180252 Genomic DNA. Translation: CAJ54378.1. Different initiation.
RefSeqYP_594699.1. NC_008011.1.

3D structure databases

ProteinModelPortalQ1MRJ8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING363253.LI0322.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4060260.
KEGGlip:LI0322.
PATRIC22304027. VBILawInt40445_0358.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0373.
HOGENOMHOG000109651.
KOK02492.
OrthoDBEOG6MWNBM.

Enzyme and pathway databases

BioCycLINT363253:GH6E-332-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_LAWIP
AccessionPrimary (citable) accession number: Q1MRJ8
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: May 20, 2008
Last modified: May 14, 2014
This is version 69 of the entry and version 2 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