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Q6MEC8 (HEM1_PARUW) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 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:pc0347
OrganismProtochlamydia amoebophila (strain UWE25) [Complete proteome] [HAMAP]
Taxonomic identifier264201 [NCBI]
Taxonomic lineageBacteriaChlamydiaeChlamydialesParachlamydiaceaeCandidatus Protochlamydia

Protein attributes

Sequence length340 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 – 340340Glutamyl-tRNA reductase HAMAP-Rule MF_00087
PRO_0000114051

Regions

Nucleotide binding183 – 1886NADP By similarity
Region46 – 494Substrate binding By similarity
Region108 – 1103Substrate binding By similarity

Sites

Active site471Nucleophile By similarity
Binding site1031Substrate By similarity
Binding site1141Substrate By similarity
Site931Important for activity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6MEC8 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 93824A5CBA5E3D40

FASTA34039,232
        10         20         30         40         50         60 
MRIGVIGINH KLADLKLRDA LAKACQKRFG ANQSVHDQHH FILLSTCNRT EVYFSSHDLT 

        70         80         90        100        110        120 
ATHSYLLSIL RQDVKEDFDH KLYSFFGMDC FSHLTRVTSG LDSAIVAETE IQGQVKNAYN 

       130        140        150        160        170        180 
LATTFLCLPK ELHFLFQKSM GIAKRIRSEL HLGRGLPNLE HAILQTGKYF FRNTQQPKIL 

       190        200        210        220        230        240 
FVGASEINRK ILHFLKSKQY SDMTICNRSE IRSKELAILY GLHLLPWCQL DSWHQYDWII 

       250        260        270        280        290        300 
FGTKSSEYLI KPEKNFIPAD NDKLIMDLCV PRNVEPKLGQ NAKITLLNID QINRLLKIRH 

       310        320        330        340 
RGMTQALIEA ENRVNLATYE HTNRYRQKED SKITIFAASA 

« Hide

References

[1]"Illuminating the evolutionary history of chlamydiae."
Horn M., Collingro A., Schmitz-Esser S., Beier C.L., Purkhold U., Fartmann B., Brandt P., Nyakatura G.J., Droege M., Frishman D., Rattei T., Mewes H.-W., Wagner M.
Science 304:728-730(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: UWE25.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX908798 Genomic DNA. Translation: CAF23071.1.
RefSeqYP_007346.1. NC_005861.1.

3D structure databases

ProteinModelPortalQ6MEC8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING264201.pc0347.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAF23071; CAF23071; pc0347.
GeneID2779718.
KEGGpcu:pc0347.
PATRIC31995996. VBICanPro72727_0353.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0373.
HOGENOMHOG000112883.
KOK02492.
OMAIKGEDQI.
OrthoDBEOG6MWNBM.
ProtClustDBCLSK2762142.

Enzyme and pathway databases

BioCycPAMO264201:GH0M-356-MONOMER.
UniPathwayUPA00251; UER00316.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
HAMAPMF_00087. Glu_tRNA_reductase.
InterProIPR000343. 4pyrrol_synth_GluRdtase.
IPR015895. 4pyrrol_synth_GluRdtase_N.
IPR016040. NAD(P)-bd_dom.
IPR018214. Pyrrol_synth_GluRdtase_CS.
IPR006151. Shikm_DH/Glu-tRNA_Rdtase.
[Graphical view]
PfamPF05201. GlutR_N. 1 hit.
PF01488. Shikimate_DH. 1 hit.
[Graphical view]
SUPFAMSSF69742. SSF69742. 1 hit.
PROSITEPS00747. GLUTR. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHEM1_PARUW
AccessionPrimary (citable) accession number: Q6MEC8
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: July 5, 2004
Last modified: February 19, 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