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A3DIE8 (HEM1_CLOTH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 61. 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:Cthe_2525
OrganismClostridium thermocellum (strain ATCC 27405 / DSM 1237) [Complete proteome] [HAMAP]
Taxonomic identifier203119 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length331 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 – 331331Glutamyl-tRNA reductase HAMAP-Rule MF_00087
PRO_1000004614

Regions

Nucleotide binding184 – 1896NADP By similarity
Region49 – 524Substrate binding By similarity
Region112 – 1143Substrate binding By similarity

Sites

Active site501Nucleophile By similarity
Binding site1071Substrate By similarity
Binding site1181Substrate By similarity
Site971Important for activity By similarity

Sequences

Sequence LengthMass (Da)Tools
A3DIE8 [UniParc].

Last modified March 20, 2007. Version 1.
Checksum: 180492694F8EB897

FASTA33138,025
        10         20         30         40         50         60 
MNVIMAGIDY TLAPIDIREK FSFTKSTLQA VYNDLLKNEN IFGAVIVSTC NRTELYLSCE 

        70         80         90        100        110        120 
EGLYINPFEL LCDAANFDYE EYSNMHVLRT GVDVIRHLCE LACGVKSQIW GEDQIITQVR 

       130        140        150        160        170        180 
NAIELAREMN ASDSTLEVMF RIAVTSAKKV KTTLKLSSTE RSIAYSALKI IKSKENISKA 

       190        200        210        220        230        240 
LVIGNGEIGR LMASILIENG YDTTITLRRY RHGDNIIPLG AKTIEYVARY EKLKDCDVVI 

       250        260        270        280        290        300 
SATLSPHYTL EIDKIDRIKY PRLFIDLAVP RDIDPKIKSL DNVELYDLDS IYAGEVDKNR 

       310        320        330 
TEQMIQVKKI IDKYIFDYYR WYEYRKRLVL T 

« Hide

References

[1]"Complete sequence of Clostridium thermocellum ATCC 27405."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Wu J.H.D., Newcomb M., Richardson P.
Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 27405 / DSM 1237.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000568 Genomic DNA. Translation: ABN53727.1.
RefSeqYP_001038920.1. NC_009012.1.

3D structure databases

ProteinModelPortalA3DIE8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING203119.Cthe_2525.

Protocols and materials databases

DNASU4809281.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABN53727; ABN53727; Cthe_2525.
GeneID4809281.
KEGGcth:Cthe_2525.
PATRIC19519058. VBICloThe47081_2688.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0373.
HOGENOMHOG000069583.
KOK02492.
OMANISRGPR.
OrthoDBEOG6MWNBM.

Enzyme and pathway databases

BioCycCTHE203119:GIW8-2613-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.
IPR006151. Shikm_DH/Glu-tRNA_Rdtase.
[Graphical view]
PfamPF05201. GlutR_N. 1 hit.
PF01488. Shikimate_DH. 1 hit.
[Graphical view]
SUPFAMSSF69742. SSF69742. 1 hit.
TIGRFAMsTIGR01035. hemA. 1 hit.
ProtoNetSearch...

Entry information

Entry nameHEM1_CLOTH
AccessionPrimary (citable) accession number: A3DIE8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: March 20, 2007
Last modified: May 14, 2014
This is version 61 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