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

B8IZD9 (HEM1_DESDA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 41. 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:Ddes_0959
OrganismDesulfovibrio desulfuricans (strain ATCC 27774 / DSM 6949) [Complete proteome] [HAMAP]
Taxonomic identifier525146 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaDesulfovibrionalesDesulfovibrionaceaeDesulfovibrio

Protein attributes

Sequence length430 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 – 430430Glutamyl-tRNA reductase HAMAP-Rule MF_00087
PRO_1000190520

Regions

Nucleotide binding188 – 1936NADP By similarity
Region50 – 534Substrate binding By similarity
Region113 – 1153Substrate binding By similarity

Sites

Active site511Nucleophile By similarity
Binding site1081Substrate By similarity
Binding site1191Substrate By similarity
Site981Important for activity By similarity

Sequences

Sequence LengthMass (Da)Tools
B8IZD9 [UniParc].

Last modified March 3, 2009. Version 1.
Checksum: F6C0AFD678B6B81C

FASTA43047,662
        10         20         30         40         50         60 
MDCDIFLVGL NHRTAGVDVR ERFALANHCD EEHWALPCTG AVSESIILST CNRVEILAAG 

        70         80         90        100        110        120 
TGEVAEQVLR NWAGARKSDV EDLRPYVYVH KNLEAVRHLF SVASSLDSMV LGEPQILGQL 

       130        140        150        160        170        180 
KTAYRKAVKS RATGVILNRL LHKAFSVAKR VRTETAVASS AVSISYAAVE LAKRIFGDMR 

       190        200        210        220        230        240 
AHKAMLVGAG EMAELAAMHL LQAGIADILV ANRTLVRGQE LAKQFNGHAI PFEDMPRHLL 

       250        260        270        280        290        300 
DVDIIITSTG SQEPIIRARD IRAALKIRKN RPMFFIDIAV PRDIDPDVNG LDNVYLYDID 

       310        320        330        340        350        360 
DLKEVVEENL ATRRDEAAKA AEIVNEEVVQ FSRWLASLDM QPTIVDLIKK GQRAAEEELA 

       370        380        390        400        410        420 
KTLKRLGPVD DNTREALEAM AGALVRKLNH DPIMFLKHGG MSQEGNGPRI SIMRRIFNLD 

       430 
KTGCIYSEEN 

« Hide

References

[1]"Complete sequence of Desulfovibrio desulfuricans subsp. desulfuricans str. ATCC 27774."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Lu M., Kiss H., Meineke L., Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L. expand/collapse author list , Kyrpides N., Ovchinnikova G., Hazen T.C.
Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 27774 / DSM 6949.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001358 Genomic DNA. Translation: ACL48866.1.
RefSeqYP_002479544.1. NC_011883.1.

3D structure databases

ProteinModelPortalB8IZD9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING525146.Ddes_0959.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACL48866; ACL48866; Ddes_0959.
GeneID7284639.
KEGGdds:Ddes_0959.
PATRIC21735548. VBIDesDes50650_1137.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0373.
HOGENOMHOG000109651.
KOK02492.
OrthoDBEOG6MWNBM.

Enzyme and pathway databases

BioCycDDES525146:GIWF-988-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_DESDA
AccessionPrimary (citable) accession number: B8IZD9
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 3, 2009
Last modified: May 14, 2014
This is version 41 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