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Reviewed, UniProtKB/Swiss-Prot A1SE01 (HEM11_NOCSJ)

Last modified November 4, 2008. Version 22. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Glutamyl-tRNA reductase 1
      Short name=GluTR 1
    EC=1.2.1.70
Gene names
Name: hemA1
Ordered Locus Names: Noca_0494
OrganismNocardioides sp. (strain BAA-499 / JS614) [Complete proteome] [HAMAP]
Taxonomic identifier196162 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesPropionibacterineaeNocardioidaceaeNocardioides

Protein attributes

Sequence length430 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA) By similarity.

Catalytic activity

L-glutamate 1-semialdehyde + NADP(+) + tRNA(Glu) = L-glutamyl-tRNA(Glu) + NADPH.

Pathway

Porphyrin metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2.

Subunit structure

Homodimer By similarity.

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.

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 processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

porphyrin biosynthetic process

Inferred from electronic annotation. Source: HAMAP

   Molecular functionglutamyl-tRNA reductase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 430430Glutamyl-tRNA reductase 1
PRO_0000335055

Regions

Nucleotide binding189 – 1946NADP 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
A1SE01-1 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: 206566D654A5AD26

FASTA43044,973
        10         20         30         40         50         60 
MSVLVVGISH KSAPVALLEQ LALDGPGLHK LIDDVAASEH VTEATVIATC NRLEIYAEVD 

        70         80         90        100        110        120 
RFHGSVEEVS RLVVDRAGER TEAMLPHLYV HYDDGAVSHL FQVVAGLDSM AVGEGQILGQ 

       130        140        150        160        170        180 
TRAALNAGQE IGTVGPALNV LFQQALRVGK RARAETGIDR AAPSLVSAAL DRSRATVGEL 

       190        200        210        220        230        240 
SGKRVLVVGA GSMAGLATST VAARGTASVT VVNRTSGNAD RLAEEYGARS ATLAELAAEL 

       250        260        270        280        290        300 
AVADVVISCT GATGTLITRD MVAAATVDGR ELSILDLALP HDVDPTVADL PGVSLVGLTD 

       310        320        330        340        350        360 
LADELRDSDA GQEVEAVRQI VTQEVAAFLS ARRQASVTPT VVALRSMATS VVEAEMERLT 

       370        380        390        400        410        420 
SRVPGLDDDI RAEVLHTVRR VADKLLHQPT VRVRELANET GAVSYAAALA ELFALDQEAV 

       430 
DAVTRPEGLT 

« Hide

References

[1]"Complete sequence of chromosome 1 of Nocardioides sp. JS614."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Thompson L.S., Brettin T., Bruce D., Han C., Tapia R., Schmutz J., Larimer F. expand/collapse author list , Land M., Hauser L., Kyrpides N., Kim E., Mattes T., Gossett J., Richardson P.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000509 Genomic DNA. Translation: ABL80036.1.
RefSeqYP_921723.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID4597393.
GenomeReviewsGene locus Noca_0494 in contig CP000509_GR.
KEGGnca:Noca_0494.

Organism-specific databases

CMRSearch...

Family and domain databases

HAMAPMF_00087.
[Tree]
InterProIPR000343. 4pyrrol_synth_GluRdtase.
IPR015896. 4pyrrol_synth_GluRdtase_C.
IPR015895. 4pyrrol_synth_GluRdtase_N.
IPR016040. NAD(P)-bd.
IPR006151. Shikm_DHase/Glu-tRNA_Rdtase.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PfamPF00745. GlutR_dimer. 1 hit.
PF05201. GlutR_N. 1 hit.
PF01488. Shikimate_DH. 1 hit.
[Graphical view]
PIRSFPIRSF000445. 4pyrrol_synth_GluRdtase. 1 hit.
TIGRFAMsTIGR01035. hemA. 1 hit.
PROSITEPS00747. GLUTR. False negative.
[Graphical view]
BLOCKSSearch...
ProtoNetSearch...

Entry information

Entry nameHEM11_NOCSJ
AccessionPrimary (citable) accession number: A1SE01
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: February 6, 2007
Last modified: November 4, 2008
This is version 22 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents