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Q8R687 (HEM1_FUSNN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 84. 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:FN0646
OrganismFusobacterium nucleatum subsp. nucleatum (strain ATCC 25586 / CIP 101130 / JCM 8532 / LMG 13131) [Reference proteome] [HAMAP]
Taxonomic identifier190304 [NCBI]
Taxonomic lineageBacteriaFusobacteriaFusobacterialesFusobacteriaceaeFusobacterium

Protein attributes

Sequence length329 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.

Caution

Lacks the conserved histidine residue in position 89 which is potentially part of the active site; it is replaced by a tyrosine residue.

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 – 329329Glutamyl-tRNA reductase HAMAP-Rule MF_00087
PRO_0000114027

Regions

Nucleotide binding179 – 1846NADP By similarity
Region51 – 544Substrate binding By similarity
Region104 – 1063Substrate binding By similarity

Sites

Active site521Nucleophile By similarity
Binding site991Substrate By similarity
Binding site1101Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8R687 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: 675E1B115629E9E2

FASTA32938,592
        10         20         30         40         50         60 
MLDLENIIVI GVSHENLSLL ERENFMRTRP KYIIERLYTE KKINAYINLS TCLRTEFYIE 

        70         80         90        100        110        120 
LNSNIKAKEI KNLFSVDMIV KSRVEAIEYL FKVGCGFYSV IKGEDQILAQ VKGAYAEALE 

       130        140        150        160        170        180 
NEHSSKFLNI IFNKSIELGK KFRTKSMIAH NALSLEAISL KFIKSKFPNI EDKNIFILGI 

       190        200        210        220        230        240 
GELAQDILTL LTKEQLKNIY IANRTYHKAE QIKKEFDIVN IVDYREKYPK MIEADVIISA 

       250        260        270        280        290        300 
TSAPHIVVEY DKFVAQMKEN KDYLFIDLAV PRDVDERLAN FKNIEIYNLD DIWEVYHLNS 

       310        320 
MNRDKLLEDY SYLIDEQMEK LIKTLNYYK 

« Hide

References

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE009951 Genomic DNA. Translation: AAL94842.1.
RefSeqNP_603543.1. NC_003454.1.

3D structure databases

ProteinModelPortalQ8R687.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING190304.FN0646.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAL94842; AAL94842; FN0646.
GeneID993220.
KEGGfnu:FN0646.
PATRIC21951055. VBIFusNuc122357_1210.

Phylogenomic databases

eggNOGCOG0373.
HOGENOMHOG000109108.
KOK02492.
OMAAETEIQG.
OrthoDBEOG6MWNBM.

Enzyme and pathway databases

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.
IPR018214. Pyrrol_synth_GluRdtase_CS.
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.
PROSITEPS00747. GLUTR. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHEM1_FUSNN
AccessionPrimary (citable) accession number: Q8R687
Entry history
Integrated into UniProtKB/Swiss-Prot: April 30, 2003
Last sequence update: June 1, 2002
Last modified: May 14, 2014
This is version 84 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