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Q252N9 (HEM1_CHLFF) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 57. 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:CF0977
OrganismChlamydophila felis (strain Fe/C-56) [Complete proteome] [HAMAP]
Taxonomic identifier264202 [NCBI]
Taxonomic lineageBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydia/Chlamydophila groupChlamydophila

Protein attributes

Sequence length338 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 – 338338Glutamyl-tRNA reductase HAMAP-Rule MF_00087
PRO_0000335021

Regions

Nucleotide binding181 – 1866NADP By similarity
Region50 – 534Substrate binding By similarity
Region107 – 1093Substrate binding By similarity

Sites

Active site511Nucleophile By similarity
Binding site1021Substrate By similarity
Binding site1131Substrate By similarity
Site921Important for activity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q252N9 [UniParc].

Last modified April 18, 2006. Version 1.
Checksum: 514B1BAA1E41A3B2

FASTA33838,262
        10         20         30         40         50         60 
MVLGVVGISY REAALKEREA VINILKTFEA DTLLAQRFFG GDGSFVLLLT CHRAEIYYFS 

        70         80         90        100        110        120 
KSNANVQSKL LSWISSLGTR PYCYQGLACF THLFTVTSGM DSLIFGETEI QGQVKRAYIK 

       130        140        150        160        170        180 
AKTDRELPFA LHFLFQKALK EGKDFRSQVS LSYPVVTMES IVEETLDLHG KSTKDKLLFI 

       190        200        210        220        230        240 
GYSDVNRKIA KGLSAKGYRN LIFCSRKNIP IPYDTVARSQ LSFGKPYDVI FFGSSESARD 

       250        260        270        280        290        300 
FPGLSLESLA GIPNRVVFDF NVPRTFTLVE RPEGISYLDM DFISERVQKK LQISKQCTNK 

       310        320        330 
EKPFLALAAR KQWEVYEKKS SNISLSQIRT SRPKLLIL 

« Hide

References

[1]"Genome sequence of the cat pathogen, Chlamydophila felis."
Azuma Y., Hirakawa H., Yamashita A., Cai Y., Rahman M.A., Suzuki H., Mitaku S., Toh H., Goto S., Murakami T., Sugi K., Hayashi H., Fukushi H., Hattori M., Kuhara S., Shirai M.
DNA Res. 13:15-23(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Fe/C-56.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP006861 Genomic DNA. Translation: BAE81749.1.
RefSeqYP_515894.1. NC_007899.1.

3D structure databases

ProteinModelPortalQ252N9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING264202.CF0977.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3958483.
KEGGcfe:CF0977.
PATRIC20205669. VBIChlFel51660_1026.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0373.
HOGENOMHOG000110628.
KOK02492.
OMACHRAELY.
OrthoDBEOG6MWNBM.
ProtClustDBPRK00676.

Enzyme and pathway databases

BioCycCFEL264202:GJCG-1016-MONOMER.
UniPathwayUPA00251; UER00316.

Family and domain databases

HAMAPMF_00087. Glu_tRNA_reductase.
InterProIPR000343. 4pyrrol_synth_GluRdtase.
IPR015895. 4pyrrol_synth_GluRdtase_N.
IPR018214. Pyrrol_synth_GluRdtase_CS.
[Graphical view]
PfamPF05201. GlutR_N. 1 hit.
[Graphical view]
SUPFAMSSF69742. SSF69742. 1 hit.
PROSITEPS00747. GLUTR. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHEM1_CHLFF
AccessionPrimary (citable) accession number: Q252N9
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: April 18, 2006
Last modified: February 19, 2014
This is version 57 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