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P56125 (HEM1_HELPY) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 99. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:HP_0239
OrganismHelicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori) [Reference proteome] [HAMAP]
Taxonomic identifier85962 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesHelicobacteraceaeHelicobacter

Protein attributes

Sequence length449 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 – 449449Glutamyl-tRNA reductase HAMAP-Rule MF_00087
PRO_0000114032

Regions

Nucleotide binding203 – 2086NADP By similarity
Region58 – 614Substrate binding By similarity
Region126 – 1283Substrate binding By similarity

Sites

Active site591Nucleophile By similarity
Binding site1211Substrate By similarity
Binding site1321Substrate By similarity
Site1111Important for activity By similarity

Sequences

Sequence LengthMass (Da)Tools
P56125 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: C4B12225DE4D83CB

FASTA44951,902
        10         20         30         40         50         60 
MELETHLSKY FTLAFTHKSM SLEMREKLAI NSNATLKEFL QTIKNHCPNI KECMVLSTCN 

        70         80         90        100        110        120 
RFEIYASLKH GANTNEQKNA LLKILAQNKK MSVSDLEKCV LMNTDESAVH HVFSVCSSLD 

       130        140        150        160        170        180 
SLVVGETQIT GQMKNAYKFA FEEKFCSKDL TRLLHFAFKC AAKVRNLTGI SKQGVSISSV 

       190        200        210        220        230        240 
AVKEALNIFE KERIKDKKAL VIGLGEMAQL VIKHLLNKQF EALILGRNAA KFEDFIKELE 

       250        260        270        280        290        300 
EPKKVSFQNI ENLNAYINEY ELLFCATSSP HFIVQNRMLK ETIFRRFWFD LAVPRNIEKP 

       310        320        330        340        350        360 
VLDNIFLYSV DDLEPMVREN VENRQESRMR AYEIVGLATM EFYQWIQSLE VEPVIKDLRE 

       370        380        390        400        410        420 
LARISAQKEL QKALKKRYVP KEYENNIEKI LHNAFNTFLH NPTIALKKNA QKEESDVLVG 

       430        440 
AIKNLFNLDK SNANHAQNLN LYKCEYYEE 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE000511 Genomic DNA. Translation: AAD07306.1.
PIRG64549.
RefSeqNP_207037.1. NC_000915.1.
YP_006934166.1. NC_018939.1.

3D structure databases

ProteinModelPortalP56125.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING85962.HP0239.

Proteomic databases

PRIDEP56125.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAD07306; AAD07306; HP_0239.
GeneID13869423.
898973.
KEGGheo:C694_01210.
hpy:HP0239.
PATRIC20591703. VBIHelPyl33062_0250.

Phylogenomic databases

eggNOGCOG0373.
KOK02492.
OMAKCVLINT.
OrthoDBEOG6MWNBM.
ProtClustDBPRK00045.

Enzyme and pathway databases

BioCycHPY:HP0239-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_HELPY
AccessionPrimary (citable) accession number: P56125
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: February 19, 2014
This is version 99 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

Helicobacter pylori

Helicobacter pylori (strain 26695): entries and gene names