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Reviewed, UniProtKB/Swiss-Prot A3NZS3 (HEM1_BURP0)

Last modified November 25, 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
      Short name=GluTR
    EC=1.2.1.70
Gene names
Name: hemA
Ordered Locus Names: BURPS1106A_3613
OrganismBurkholderia pseudomallei (strain 1106a) [Complete proteome] [HAMAP]
Taxonomic identifier357348 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiapseudomallei group

Protein attributes

Sequence length434 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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 434434Glutamyl-tRNA reductase
PRO_0000335016

Regions

Nucleotide binding196 – 2016NADP By similarity
Region57 – 604Substrate binding By similarity
Region121 – 1233Substrate binding By similarity

Sites

Active site581Nucleophile By similarity
Binding site1161Substrate By similarity
Binding site1271Substrate By similarity
Site1061Important for activity By similarity

Sequences

Sequence LengthMass (Da)Tools
A3NZS3-1 [UniParc].

Last modified April 3, 2007. Version 1.
Checksum: D9DC915D8233453A

FASTA43447,546
        10         20         30         40         50         60 
MDMQLLTIGI NHHTAPVALR ERVAFPLEQI KPALSTFKSV FLGHPAPNAP EAAILSTCNR 

        70         80         90        100        110        120 
TELYCATNDR AARDAAIRWM SDYHRIPADE LAPHVYALPQ SEAVRHAFRV ASGLDSMVLG 

       130        140        150        160        170        180 
ETQILGQMKN AVRTASEAGS LGTYLNQLFQ RTFAVAKEVR GTTEIGAQSV SMAAAAVRLA 

       190        200        210        220        230        240 
QRIFEQVAQQ RVLFIGAGEM IELCATHFAA QGPRELVVAN RTAERGAKLA ERFGGRAMPL 

       250        260        270        280        290        300 
ADLPARMHEF DIIVSCTAST LPIIGLGAVE RAVKARRHRP IFMVDLAVPR DIEPEVGKLK 

       310        320        330        340        350        360 
DVFLYTVDDL GAIVREGNAS RQAAVAQAEA IIETRVQNFM QWLDARSIVP VIRHMHTQAD 

       370        380        390        400        410        420 
ALRRAEVERA RKMLARGDDP DAVLDALSQA LTNKLIHGPT SALNRANGAD RDSLIDLMRG 

       430 
FYQHAPRSSD TSDR 

« Hide

References

[1]DeShazer D., Woods D.E., Nierman W.C.
Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000572 Genomic DNA. Translation: ABN91520.1.
RefSeqYP_001067844.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID4902084.
GenomeReviewsGene locus BURPS1106A_3613 in contig CP000572_GR.
KEGGbpl:BURPS1106A_3613.
TIGRBURPS1106A_3613.

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. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHEM1_BURP0
AccessionPrimary (citable) accession number: A3NZS3
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: April 3, 2007
Last modified: November 25, 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