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Q63QF1 (HEM1_BURPS) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 74. 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:BPSL3072
OrganismBurkholderia pseudomallei (strain K96243) [Reference proteome] [HAMAP]
Taxonomic identifier272560 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiapseudomallei group

Protein attributes

Sequence length441 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
Reference 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 – 441441Glutamyl-tRNA reductase HAMAP-Rule MF_00087
PRO_0000114001

Regions

Nucleotide binding203 – 2086NADP By similarity
Region64 – 674Substrate binding By similarity
Region128 – 1303Substrate binding By similarity

Sites

Active site651Nucleophile By similarity
Binding site1231Substrate By similarity
Binding site1341Substrate By similarity
Site1131Important for activity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q63QF1 [UniParc].

Last modified October 25, 2004. Version 1.
Checksum: 06D2A7C3C3F1D032

FASTA44148,258
        10         20         30         40         50         60 
MGLNDSLLDM QLLTIGINHH TAPVALRERV AFPLEQIKPA LSTFKSVFLG HPAPNAPEAA 

        70         80         90        100        110        120 
ILSTCNRTEL YCATNDRAAR DAAIRWMSDY HRIPADELAP HVYALPQSEA VRHAFRVASG 

       130        140        150        160        170        180 
LDSMVLGETQ ILGQMKNAVR TASEAGSLGT YLNQLFQRTF AVAKEVRGTT EIGAQSVSMA 

       190        200        210        220        230        240 
AAAVRLAQRI FEQVAQQRVL FIGAGEMIEL CATHFAAQGP RELVVANRTA ERGAKLAERF 

       250        260        270        280        290        300 
GGRAMPLADL PARMHEFDII VSCTASTLPI IGLGAVERAV KARRHRPIFM VDLAVPRDIE 

       310        320        330        340        350        360 
PEVGKLKDVF LYTVDDLGAI VREGNASRQA AVAQAEAIIE TRVQNFMQWL DARSIVPVIR 

       370        380        390        400        410        420 
HMHTQADALR RAEVERARKM LARGDDPDAV LDALSQALTN KLIHGPTSAL NRANGADRDS 

       430        440 
LIDLMRGFYQ HAPRSSDTSD R 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX571965 Genomic DNA. Translation: CAH37083.1.
RefSeqYP_109667.2. NC_006350.1.

3D structure databases

ProteinModelPortalQ63QF1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272560.BPSL3072.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAH37083; CAH37083; BPSL3072.
GeneID3094369.
KEGGbps:BPSL3072.
PATRIC19266651. VBIBurPse99623_3515.

Phylogenomic databases

eggNOGCOG0373.
HOGENOMHOG000109650.
KOK02492.
OMARTEIYCA.
OrthoDBEOG6C2WN5.
ProtClustDBPRK00045.

Enzyme and pathway databases

BioCycBPSE272560:GJNI-3156-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_BURPS
AccessionPrimary (citable) accession number: Q63QF1
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: October 25, 2004
Last modified: February 19, 2014
This is version 74 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