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Q6AIM2 (HEM1_DESPS) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 76. 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:DP3079
OrganismDesulfotalea psychrophila (strain LSv54 / DSM 12343) [Complete proteome] [HAMAP]
Taxonomic identifier177439 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaDesulfobacteralesDesulfobulbaceaeDesulfotalea

Protein attributes

Sequence length426 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
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 – 426426Glutamyl-tRNA reductase HAMAP-Rule MF_00087
PRO_0000114020

Regions

Nucleotide binding190 – 1956NADP By similarity
Region51 – 544Substrate binding By similarity
Region115 – 1173Substrate binding By similarity

Sites

Active site521Nucleophile By similarity
Binding site1101Substrate By similarity
Binding site1211Substrate By similarity
Site1001Important for activity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6AIM2 [UniParc].

Last modified September 13, 2004. Version 1.
Checksum: 562DC4F013652C3F

FASTA42647,343
        10         20         30         40         50         60 
MFEKQVFLFG VNHKTTPVAV REKIAFTDGY ETALTRLQEE VGCDESYLLS TCNRVEILVY 

        70         80         90        100        110        120 
ADSTRDIEAE VSRFLFAGKV PEEDCRDYLY ALKGLPAVQH LFTVAASLDS MVVGEAQILG 

       130        140        150        160        170        180 
QLKTAYRHAS ALGCTGPLLN RLLHKSFSVA KRVRTETAIG ASAVSISYAA VQLARKIFGN 

       190        200        210        220        230        240 
LDTKKVMLVG AGEMAELAAE HLVGQGVSSV VVANRTLTRA VELADKFGGT AICMEELYAQ 

       250        260        270        280        290        300 
LEDVDIIISS TGAQHIIIES AEVRPIMRVR RNRPLFFIDI AVPRDLDPEL NELENVYLYD 

       310        320        330        340        350        360 
IDDLSNVVEV NKSGRDHEAI KAGCIVEEET RKFDEWYQGL AVKPTVLALR EKMSGIIEQE 

       370        380        390        400        410        420 
LRKTLPRLHD LGEHDQRSIE KMVASISSKF LHDPLHYLKS DSCHGRDKSQ AKVDTLRSVF 


SLKGDI 

« Hide

References

[1]"The genome of Desulfotalea psychrophila, a sulfate-reducing bacterium from permanently cold Arctic sediments."
Rabus R., Ruepp A., Frickey T., Rattei T., Fartmann B., Stark M., Bauer M., Zibat A., Lombardot T., Becker I., Amann J., Gellner K., Teeling H., Leuschner W.D., Gloeckner F.-O., Lupas A.N., Amann R., Klenk H.-P.
Environ. Microbiol. 6:887-902(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: LSv54 / DSM 12343.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR522870 Genomic DNA. Translation: CAG37808.1.
RefSeqYP_066815.1. NC_006138.1.

3D structure databases

ProteinModelPortalQ6AIM2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING177439.DP3079.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAG37808; CAG37808; DP3079.
GeneID2946048.
KEGGdps:DP3079.
PATRIC21716340. VBIDesPsy67261_3340.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0373.
HOGENOMHOG000109651.
KOK02492.
OMAHRTEESS.
OrthoDBEOG6MWNBM.

Enzyme and pathway databases

BioCycDPSY177439:GJW5-3166-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_DESPS
AccessionPrimary (citable) accession number: Q6AIM2
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: September 13, 2004
Last modified: May 14, 2014
This is version 76 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