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A0M6C1 (HEM1_GRAFK) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 63. 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:GFO_3223
OrganismGramella forsetii (strain KT0803) [Complete proteome] [HAMAP]
Taxonomic identifier411154 [NCBI]
Taxonomic lineageBacteriaBacteroidetesFlavobacteriiaFlavobacterialesFlavobacteriaceaeGramella

Protein attributes

Sequence length418 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 – 418418Glutamyl-tRNA reductase HAMAP-Rule MF_00087
PRO_0000335042

Regions

Nucleotide binding193 – 1986NADP By similarity
Region57 – 604Substrate binding By similarity
Region118 – 1203Substrate binding By similarity

Sites

Active site581Nucleophile By similarity
Binding site1131Substrate By similarity
Binding site1241Substrate By similarity
Site1031Important for activity By similarity

Sequences

Sequence LengthMass (Da)Tools
A0M6C1 [UniParc].

Last modified December 12, 2006. Version 1.
Checksum: 6CBDC8FB775EA398

FASTA41847,931
        10         20         30         40         50         60 
MEDYHISRGK HFYTIGLSYK KADAEIRGHF SLTEESKQRL LEQAKEEGID GILVTSTCNR 

        70         80         90        100        110        120 
TEIYGFAQHP FQLIKLLCEH THGTVEEFEK VAYVYKNKQA ITHIFKVGTG LDSQILGDFE 

       130        140        150        160        170        180 
IISQLKIAFV RSKKLGLVNA FLERLVNAVI QASKRIKNET EISTGATSVS FASVQYILKH 

       190        200        210        220        230        240 
IDKVSEKNIL LFGTGKIGRN TCENLVKHTR NNHITLINRT KDKAERIAGK FNLIVKDYAD 

       250        260        270        280        290        300 
LQAEIRNSDI LIVATGAQNP TISKELIYPK KELLILDLSI PKNVSDDVHE LENVKLIHLD 

       310        320        330        340        350        360 
HLSQMTDETL EKRKQFIPQA KEIITEVESE FNRWLETRKF APTIKALKKK LKTMKDDELD 

       370        380        390        400        410 
FQRKKISDFN DEQAEIVSNR IIQKIMKHFA NHLKGDAETT DESLELIQKV FQLEEVNK 

« Hide

References

[1]"Whole genome analysis of the marine Bacteroidetes'Gramella forsetii' reveals adaptations to degradation of polymeric organic matter."
Bauer M., Kube M., Teeling H., Richter M., Lombardot T., Allers E., Wuerdemann C.A., Quast C., Kuhl H., Knaust F., Woebken D., Bischof K., Mussmann M., Choudhuri J.V., Meyer F., Reinhardt R., Amann R.I., Gloeckner F.O.
Environ. Microbiol. 8:2201-2213(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: KT0803.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU207366 Genomic DNA. Translation: CAL68166.1.
RefSeqYP_863233.1. NC_008571.1.

3D structure databases

ProteinModelPortalA0M6C1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING411154.GFO_3223.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAL68166; CAL68166; GFO_3223.
GeneID4651311.
KEGGgfo:GFO_3223.
PATRIC22075182. VBIGraFor5527_3106.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0373.
HOGENOMHOG000251726.
KOK02492.
OMAKCVLINT.
OrthoDBEOG6MWNBM.
ProtClustDBCLSK851822.

Enzyme and pathway databases

BioCycGFOR411154:GI79-3223-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_GRAFK
AccessionPrimary (citable) accession number: A0M6C1
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: December 12, 2006
Last modified: February 19, 2014
This is version 63 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