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Q2S2A5 (HEM1_SALRD) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 73. 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:SRU_1555
OrganismSalinibacter ruber (strain DSM 13855 / M31) [Reference proteome] [HAMAP]
Taxonomic identifier309807 [NCBI]
Taxonomic lineageBacteriaBacteroidetesBacteroidetes Order II. Incertae sedisRhodothermaceaeSalinibacter

Protein attributes

Sequence length479 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.

Sequence caution

The sequence ABC43868.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processPorphyrin biosynthesis
   LigandNADP
   Molecular functionOxidoreductase
   Technical termComplete proteome
Reference 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 – 479479Glutamyl-tRNA reductase HAMAP-Rule MF_00087
PRO_0000335070

Regions

Nucleotide binding189 – 1946NADP By similarity
Region48 – 514Substrate binding By similarity
Region109 – 1113Substrate binding By similarity

Sites

Active site491Nucleophile By similarity
Binding site1041Substrate By similarity
Binding site1151Substrate By similarity
Site941Important for activity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2S2A5 [UniParc].

Last modified May 20, 2008. Version 2.
Checksum: CCBDCF4F287BBB5D

FASTA47951,933
        10         20         30         40         50         60 
MRFYAVGLNH ECTSLEQTET FALSAEEQEA LYANLSLSAD AEVVVLSTCN RTEAYLYGTE 

        70         80         90        100        110        120 
ADLRQVKALI GQGGGTRWPE ETAFQERDEA AVRHLLQVTS GLRSVVLGER QIFAQVKAAY 

       130        140        150        160        170        180 
ERAVDAGGIH SVMHRLFHTA FRAAKRVSSE TGLGRGAASV STAAVEMARQ DLSEAGGEGL 

       190        200        210        220        230        240 
RNTEIVLVGA GKMGRLALEA LADESLASLT VVNRSPDRAR EVASPFGGDT EPWADRHRAV 

       250        260        270        280        290        300 
ATADLALVAT GASDPVLHAP ALPAPDEATL VVDVAMPRNV DPAVDERPGY RLYDLDDLEA 

       310        320        330        340        350        360 
WTAEVRERRA DAVPEAESIC EELLEDFVTW VFHQQALQPA IQAIRSTFDT IREQEVDRHA 

       370        380        390        400        410        420 
HRTGMDREEV DRLTESIMQK LLAVPIVRLK NVDPESIDFV QGIELLHALF APSDESDAGR 

       430        440        450        460        470 
SLAEAPDADT PDLGEAPSRC PYMTHDPGGD GTETEEVQKA LRLSAAHQAA SHSEEVRGG 

« Hide

References

[1]"The genome of Salinibacter ruber: convergence and gene exchange among hyperhalophilic bacteria and archaea."
Mongodin E.F., Nelson K.E., Daugherty S., DeBoy R.T., Wister J., Khouri H., Weidman J., Walsh D.A., Papke R.T., Sanchez Perez G., Sharma A.K., Nesbo C.L., MacLeod D., Bapteste E., Doolittle W.F., Charlebois R.L., Legault B., Rodriguez-Valera F.
Proc. Natl. Acad. Sci. U.S.A. 102:18147-18152(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 13855 / M31.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000159 Genomic DNA. Translation: ABC43868.1. Different initiation.
RefSeqYP_445676.1. NC_007677.1.

3D structure databases

ProteinModelPortalQ2S2A5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING309807.SRU_1555.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABC43868; ABC43868; SRU_1555.
GeneID3851349.
KEGGsru:SRU_1555.
PATRIC23425545. VBISalRub86502_1609.

Phylogenomic databases

eggNOGCOG0373.
HOGENOMHOG000106238.
KOK02492.
OrthoDBEOG6MWNBM.

Enzyme and pathway databases

BioCycSRUB309807:GJJD-1552-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.
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_SALRD
AccessionPrimary (citable) accession number: Q2S2A5
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: May 20, 2008
Last modified: May 14, 2014
This is version 73 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