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Q2RWE2 (HEM1_RHORT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 71. 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:Rru_A0749
OrganismRhodospirillum rubrum (strain ATCC 11170 / NCIB 8255) [Reference proteome] [HAMAP]
Taxonomic identifier269796 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesRhodospirillaceaeRhodospirillum

Protein attributes

Sequence length431 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

Porphyrin-containing compound metabolism; chlorophyll biosynthesis. 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.

Sequence caution

The sequence ABC21553.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 431431Glutamyl-tRNA reductase HAMAP-Rule MF_00087
PRO_0000335067

Regions

Nucleotide binding189 – 1946NADP By similarity
Region49 – 524Substrate binding By similarity
Region114 – 1163Substrate binding Potential

Sites

Active site501Nucleophile By similarity
Binding site1091Substrate By similarity
Binding site1201Substrate By similarity
Site991Important for activity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2RWE2 [UniParc].

Last modified May 20, 2008. Version 2.
Checksum: A9E8C28641E98D68

FASTA43145,596
        10         20         30         40         50         60 
MDGYVMVGVN HQTTPMALRD RLVLDDPALA ALLVRLRARG VTEALALSTC DRVEIFGHGG 

        70         80         90        100        110        120 
DPRALRALLL AELCAVGPIE PAALAGQMVD LRGLAVVAHM FRITSALESQ VLGEPHILGQ 

       130        140        150        160        170        180 
VKAAHRIARD AGTVGSATEA LMQAAYAIAK RVRSETRISE GPVSLAAVAA QIARDLHGDL 

       190        200        210        220        230        240 
GETCLLLLGT QEMGELIAEQ LQMAGVGRLV VCAPRRPRAE AVAARLGASV GDHGALLDLL 

       250        260        270        280        290        300 
PNADIVVVGV GGGLLALGEE AMRRTLKRRR NRPVFIVDAG VPGNVEPSVQ RLEAAFLYDL 

       310        320        330        340        350        360 
ADLEAVAEEG RAARDQASRE AHALVADAVA AFERHRAERA AVPAIAALRA HFEGERLRAL 

       370        380        390        400        410        420 
AEAPDDAEKA TRLLVGRLLH GPSEALRDLA AGSADKEFMT VRAEMLLRRL FDLPTSIAET 

       430 
GATDREDGSK G 

« Hide

References

[1]"Complete sequence of the chromosome of Rhodospirillum rubrum ATCC 11170."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M. expand/collapse author list , Kyrpides N., Mavrommatis K., Richardson P., Zhang Y., Roberts G., Reslewic S., Zhou S., Schwartz D.C.
Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIB 8255 / S.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000230 Genomic DNA. Translation: ABC21553.1. Different initiation.
RefSeqYP_425840.1. NC_007643.1.

3D structure databases

ProteinModelPortalQ2RWE2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING269796.Rru_A0749.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABC21553; ABC21553; Rru_A0749.
GeneID3834158.
KEGGrru:Rru_A0749.
PATRIC23325073. VBIRhoRub82919_0802.

Phylogenomic databases

eggNOGCOG0373.
HOGENOMHOG000109649.
KOK02492.
OrthoDBEOG6MWNBM.

Enzyme and pathway databases

BioCycRRUB269796:GCN1-764-MONOMER.
UniPathwayUPA00251; UER00316.
UPA00668.

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.
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.
ProtoNetSearch...

Entry information

Entry nameHEM1_RHORT
AccessionPrimary (citable) accession number: Q2RWE2
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: May 20, 2008
Last modified: May 14, 2014
This is version 71 of the entry and version 2 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