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O28304 (HEM1_ARCFU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 102. 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:AF_1975
OrganismArchaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126) [Reference proteome] [HAMAP]
Taxonomic identifier224325 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaArchaeoglobiArchaeoglobalesArchaeoglobaceaeArchaeoglobus

Protein attributes

Sequence length437 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
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 – 437437Glutamyl-tRNA reductase HAMAP-Rule MF_00087
PRO_0000114098

Regions

Nucleotide binding177 – 1826NADP By similarity
Region46 – 494Substrate binding By similarity
Region102 – 1043Substrate binding By similarity

Sites

Active site471Nucleophile By similarity
Binding site971Substrate By similarity
Binding site1081Substrate By similarity
Site871Important for activity By similarity

Sequences

Sequence LengthMass (Da)Tools
O28304 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: DD0A999D55790CD6

FASTA43748,442
        10         20         30         40         50         60 
MEIGCITISH KNAKVEEIEK IWLTVKPRLE DVISKCSFSE YAYIFTCNRF EIYLVGENLK 

        70         80         90        100        110        120 
SCLQDIAEEL GITGKAEIFV GESCLRHLLR VASGIESMIV GEEQILGQVR QCFNLCREGG 

       130        140        150        160        170        180 
QAGEVLERVF GKAVQVGRRV RRETAISKGS VSIGSAAVEV AERVLGTLKG KKALLVGAGE 

       190        200        210        220        230        240 
MGTLVAKAIA GKEVEAVLIA NRTYEKAEEL AKRIGGVAVK FDKLVDYLKV CDVVISATSA 

       250        260        270        280        290        300 
PHAVITRGDV ERAMRERSQK LLIIDIALPR DVDESVAQLD GVELLTIDDL RRISEENLAR 

       310        320        330        340        350        360 
RREEIAKVEG IIEEELEQLK LLLKDISARD AIAAMYSLAE RFVGEEVEEL YAKLNARYGV 

       370        380        390        400        410        420 
SEDVKEILND FANSLIKKFL REPTVRLREA ARKDEFHVIE SIKYVFGDGN GRVSEGKDAK 

       430 
VEEGKPEVDV QRSKAES 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE000782 Genomic DNA. Translation: AAB89281.1.
PIRF69496.
RefSeqNP_070799.1. NC_000917.1.

3D structure databases

ProteinModelPortalO28304.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224325.AF1975.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAB89281; AAB89281; AF_1975.
GeneID1485197.
KEGGafu:AF1975.

Phylogenomic databases

eggNOGCOG0373.
KOK02492.
OMAKMLHGTM.

Enzyme and pathway databases

BioCycAFUL224325:GJBC-2012-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_ARCFU
AccessionPrimary (citable) accession number: O28304
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 1, 1998
Last modified: May 14, 2014
This is version 102 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