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A4YD89 (HEM1_METS5) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 58. 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:Msed_0214
OrganismMetallosphaera sedula (strain ATCC 51363 / DSM 5348) [Complete proteome] [HAMAP]
Taxonomic identifier399549 [NCBI]
Taxonomic lineageArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeMetallosphaera

Protein attributes

Sequence length424 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 – 424424Glutamyl-tRNA reductase HAMAP-Rule MF_00087
PRO_1000075413

Regions

Nucleotide binding188 – 1936NADP By similarity
Region52 – 554Substrate binding By similarity
Region113 – 1153Substrate binding By similarity

Sites

Active site531Nucleophile By similarity
Binding site1081Substrate By similarity
Binding site1191Substrate By similarity
Site981Important for activity By similarity

Sequences

Sequence LengthMass (Da)Tools
A4YD89 [UniParc].

Last modified May 29, 2007. Version 1.
Checksum: 3E18D902434B5E92

FASTA42448,090
        10         20         30         40         50         60 
MNPVNDIIDS YSAIVYTHKT VGVDKLASHY LGWNEIKELS KYYDGEMAVL QTCNRIEIYL 

        70         80         90        100        110        120 
FSRNESSVNE ILHYLNEVHN KVISTDATIL RGEEAIKHLF EVASGIDSLS VGEYEILKQI 

       130        140        150        160        170        180 
KDAMRDSIKL GIGSRYIRAL LERSLKVGRR VRLETGISRG KVGVYSLAVE FAKSRFGDIL 

       190        200        210        220        230        240 
GKKIAILGAG EIGGKLALIL HNEGATDVTI FNRTFERGRN LAIKYGYSYF PLDFSRLHNY 

       250        260        270        280        290        300 
DIIFSAIFYP EKVKAPEGTV VIDLGSPPVF EGSNVYTLKD LEELSKATLE ERQREIERAE 

       310        320        330        340        350        360 
SIIREGLEEF RKDCLNLVYD NFVSSFMSRV EETRKEEVER ALKVLGDDGE ETREVLEAMT 

       370        380        390        400        410        420 
RSMIKKIFSP MFQNLRRAVE NNEINYINLA TSLLTHGGIS QDKTKEIKTE QEYKGRSSGD 


ETDS 

« Hide

References

[1]"The genome sequence of the metal-mobilizing, extremely thermoacidophilic archaeon Metallosphaera sedula provides insights into bioleaching-associated metabolism."
Auernik K.S., Maezato Y., Blum P.H., Kelly R.M.
Appl. Environ. Microbiol. 74:682-692(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 51363 / DSM 5348.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000682 Genomic DNA. Translation: ABP94391.1.
RefSeqYP_001190315.1. NC_009440.1.

3D structure databases

ProteinModelPortalA4YD89.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING399549.Msed_0214.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABP94391; ABP94391; Msed_0214.
GeneID5104080.
KEGGmse:Msed_0214.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0373.
HOGENOMHOG000107850.
KOK02492.
OMAKGMAVHF.
ProtClustDBPRK00045.

Enzyme and pathway databases

BioCycMSED399549:GH1O-227-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_METS5
AccessionPrimary (citable) accession number: A4YD89
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: May 29, 2007
Last modified: February 19, 2014
This is version 58 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