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

Q0RS17 (HEM1_FRAAA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 67. 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:FRAAL0983
OrganismFrankia alni (strain ACN14a) [Complete proteome] [HAMAP]
Taxonomic identifier326424 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesFrankineaeFrankiaceaeFrankia

Protein attributes

Sequence length470 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 CAJ59648.1 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 – 470470Glutamyl-tRNA reductase HAMAP-Rule MF_00087
PRO_0000335038

Regions

Nucleotide binding223 – 2286NADP By similarity
Region49 – 524Substrate binding By similarity
Region114 – 1163Substrate binding By similarity

Sites

Active site501Nucleophile By similarity
Binding site1091Substrate By similarity
Binding site1201Substrate By similarity
Site991Important for activity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0RS17 [UniParc].

Last modified May 20, 2008. Version 2.
Checksum: 20F2C619487E7C0C

FASTA47048,260
        10         20         30         40         50         60 
MSLLVVGLNH RTAPTSLLEQ ASVSGDDTPK VLHDLAAAAH VNEAVVLSTC NRTEIYADVE 

        70         80         90        100        110        120 
TFHGGVADIS DQLSRISGID LGDLAGHLYV HHDARAVGHL FSVVCGLDSM LVGESQILGQ 

       130        140        150        160        170        180 
VRGAFRTGQS AGVAGSALSG LFQAALRVGK RAHSETSIDA AGASIVAVGI RLAASSLGIL 

       190        200        210        220        230        240 
SEVPAVPVAP PGGVAGELGG AAVLAAPVAE PPPLAGARVL LIGAGAVGSL AAQTARRAGA 

       250        260        270        280        290        300 
TEIVIANRTP ARAARVAEMH DGRAVGLTDL PHEILMADLV ISSTGATGLV VDHDLVAAAL 

       310        320        330        340        350        360 
PGRGGRPLVF LDLALPHDID PGVRALPGVS LIDLEALRVA LDGAQVAHDV EAVRALVSTE 

       370        380        390        400        410        420 
VAGFLDRRRA GRVAPTVVAL RAHADSVVHG ELARLHSRLP DLDDREWELV EGAVRRVVDK 

       430        440        450        460        470 
LLHAPTVRVQ QLAGAPGGDS YAEALRELFD LPREVPAVVS APDLDLVERS 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CT573213 Genomic DNA. Translation: CAJ59648.1. Different initiation.
RefSeqYP_711244.1. NC_008278.1.

3D structure databases

ProteinModelPortalQ0RS17.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING326424.FRAAL0983.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4231191.
KEGGfal:FRAAL0983.
PATRIC21911825. VBIFraAln347_0880.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0373.
HOGENOMHOG000109649.
KOK02492.
OrthoDBEOG6MWNBM.

Enzyme and pathway databases

BioCycFALN326424:GJ82-964-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.
PROSITEPS00747. GLUTR. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHEM1_FRAAA
AccessionPrimary (citable) accession number: Q0RS17
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: May 20, 2008
Last modified: May 14, 2014
This is version 67 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