Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

C6BV55 (HEM1_DESAD) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 39. 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:Desal_1970
OrganismDesulfovibrio salexigens (strain ATCC 14822 / DSM 2638 / NCIB 8403 / VKM B-1763) [Complete proteome] [HAMAP]
Taxonomic identifier526222 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaDesulfovibrionalesDesulfovibrionaceaeDesulfovibrio

Protein attributes

Sequence length439 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 – 439439Glutamyl-tRNA reductase HAMAP-Rule MF_00087
PRO_1000202631

Regions

Nucleotide binding187 – 1926NADP By similarity
Region48 – 514Substrate binding By similarity
Region112 – 1143Substrate binding By similarity

Sites

Active site491Nucleophile By similarity
Binding site1071Substrate By similarity
Binding site1181Substrate By similarity
Site971Important for activity By similarity

Sequences

Sequence LengthMass (Da)Tools
C6BV55 [UniParc].

Last modified September 1, 2009. Version 1.
Checksum: D137EF8C0C0966D1

FASTA43949,019
        10         20         30         40         50         60 
MDHNIYLIGL NHRSAGVDVR ERYALTNVEE FESGLLELGV REVMALSTCN RVEILVVCAP 

        70         80         90        100        110        120 
EITQPNILEY WAKRCCGSVS ELEPNTYCHD GLNAVKHLFR VACSLDSMIV GEPQILGQLK 

       130        140        150        160        170        180 
DSYRKAVEAG AARVIINRML HKSFFVAKRV RTETSIASSA VSISYAAVEL AKKIFGELEG 

       190        200        210        220        230        240 
QRAMLIGAGE MAELAATHLL NSGVEQISIA NRTYSRAEDL AKCMGGSAVS FDNLYDHLVE 

       250        260        270        280        290        300 
TDIIISSTGA PHAVISAKEM KKVIKKRKYR PMFFIDIAVP RDIDPDVNGL DNVYLYDIDD 

       310        320        330        340        350        360 
LKDVVEENKS QREDEAIKAN SIVEFETLSF GNWINSLDLQ PTIVDLFNRS ENVAQQELAK 

       370        380        390        400        410        420 
TLKRLGDVDA KTHKALETMA MSIGKKLLHE PVAFLKRRTE EEGKADEFVD LARRMFNLDN 

       430 
ETIPADAHCG RKKNRNPEN 

« Hide

References

[1]"Complete sequence of Desulfovibrio salexigens DSM 2638."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D., Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C., Han C., Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Anderson I. expand/collapse author list , Wall J.D., Arkin A.P., Dehal P., Chivian D., Giles B., Hazen T.C.
Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 14822 / DSM 2638 / NCIB 8403 / VKM B-1763.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001649 Genomic DNA. Translation: ACS80030.1.
RefSeqYP_002991569.1. NC_012881.1.

3D structure databases

ProteinModelPortalC6BV55.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING526222.Desal_1970.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACS80030; ACS80030; Desal_1970.
GeneID8092998.
KEGGdsa:Desal_1970.
PATRIC21759443. VBIDesSal121003_1975.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0373.
HOGENOMHOG000109651.
KOK02492.
OMARTEIYCA.
OrthoDBEOG6MWNBM.
ProtClustDBPRK00045.

Enzyme and pathway databases

BioCycDSAL526222:GHES-2005-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.
IPR018214. Pyrrol_synth_GluRdtase_CS.
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.
PROSITEPS00747. GLUTR. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHEM1_DESAD
AccessionPrimary (citable) accession number: C6BV55
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: September 1, 2009
Last modified: February 19, 2014
This is version 39 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