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C1CXJ0 (C1CXJ0_DEIDV) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 25. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Glutamyl-tRNA reductase HAMAP MF_00087
Short name=GluTR HAMAP MF_00087
EC=1.2.1.70 HAMAP MF_00087
Gene names
Name:hemA HAMAP MF_00087 EMBL ACO46907.1
Ordered Locus Names:Deide_19150
OrganismDeinococcus deserti (strain VCD115 / DSM 17065 / LMG 22923) [Complete proteome] [HAMAP]
Taxonomic identifier546414 [NCBI]
Taxonomic lineageBacteria › Deinococcus-Thermus › Deinococci › Deinococcales › Deinococcaceae › Deinococcus

Protein attributes

Sequence length365 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 MF_00087

Catalytic activity

L-glutamate 1-semialdehyde + NADP+ + tRNA(Glu) = L-glutamyl-tRNA(Glu) + NADPH. HAMAP MF_00087 RuleBase RU000584 SAAS SAAS018214

Pathway

Porphyrin metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2. HAMAP MF_00087 RuleBase RU000584 SAAS SAAS018214

Subunit structure

Homodimer By similarity. HAMAP 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 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. HAMAP MF_00087

Sequence similarities

Belongs to the glutamyl-tRNA reductase family. HAMAP MF_00087 RuleBase RU000584

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Nucleotide binding201 – 2066NADP By similarity HAMAP MF_00087
Region69 – 724Substrate binding By similarity HAMAP MF_00087
Region126 – 1283Substrate binding By similarity HAMAP MF_00087

Sites

Active site701Nucleophile By similarity HAMAP MF_00087
Binding site1211Substrate By similarity HAMAP MF_00087
Binding site1321Substrate By similarity HAMAP MF_00087
Site1111Important for activity By similarity HAMAP MF_00087

Sequences

Sequence LengthMass (Da)Tools
C1CXJ0 [UniParc].

Last modified May 26, 2009. Version 1.
Checksum: E51B58220BA7CBEA

FASTA36539,128
        10         20         30         40         50         60 
MTLSCPTAKQ FLDLSGTLPP APLDFIVVGL NHHTAPVEVR ERAAVRGGEE EALYSHLSRH 

        70         80         90        100        110        120 
AQEVMLLATC NRTEVYLAGL EGDPVAAFEG AWGHALADHL YVYRGEAAVA HLYRVAAGLD 

       130        140        150        160        170        180 
SLVIGETQIQ GQVKRAWQSA HSRGLSSKVL NKVAQGALAA GKRVRFETGM SDKVVSVSSA 

       190        200        210        220        230        240 
AVELAQAALG TLEGRTALIL GAGETAELTL THLRAAGVED VIVVNRTVER ARQLAEKLGG 

       250        260        270        280        290        300 
QACAHEYLHE VLPQADVVIA SSAAPHYVLH GEGVQAALAG RPEREMFLID ISVPRILDPD 

       310        320        330        340        350        360 
IAQVTGAHLL NLDDLTDIVT RNLQSRRDAL PHAQAIIRES AADLQRWHLT REAQLGRRAL 


ATACD

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References

[1]"Alliance of proteomics and genomics to unravel the specificities of Sahara bacterium Deinococcus deserti."
de Groot A., Dulermo R., Ortet P., Blanchard L., Guerin P., Fernandez B., Vacherie B., Dossat C., Jolivet E., Siguier P., Chandler M., Barakat M., Dedieu A., Barbe V., Heulin T., Sommer S., Achouak W., Armengaud J.
PLoS Genet. 5:E1000434-E1000434(2009) [PubMed: 19370165] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: VCD115 / DSM 17065 / LMG 22923.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001114 Genomic DNA. Translation: ACO46907.1.
RefSeqYP_002786661.1. NC_012526.1.

3D structure databases

ProteinModelPortalC1CXJ0.
ModBaseSearch...

Protein-protein interaction databases

STRINGC1CXJ0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID7737618.
GenomeReviewsGene locus Deide_19150 in contig CP001114_GR.
KEGGddr:Deide_19150.
PATRIC21617840. VBIDeiDes121019_2194.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAKETIFRR.
ProtClustDBCLSK445651.

Family and domain databases

HAMAPMF_00087. Glu_tRNA_reductase.
[Tree]
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]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
KOK02492.
PfamPF05201. GlutR_N. 1 hit.
PF01488. Shikimate_DH. 1 hit.
[Graphical view]
PIRSFPIRSF000445. 4pyrrol_synth_GluRdtase. 1 hit.
SUPFAMSSF69742. GlutR. 1 hit.
TIGRFAMsTIGR01035. HemA. 1 hit.
PROSITEPS00747. GLUTR. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameC1CXJ0_DEIDV
AccessionPrimary (citable) accession number: C1CXJ0
Entry history
Integrated into UniProtKB/TrEMBL: May 26, 2009
Last sequence update: May 26, 2009
Last modified: December 14, 2011
This is version 25 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info