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Q8ZYV6 (HEM1_PYRAE) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 94. 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:PAE0601
OrganismPyrobaculum aerophilum (strain ATCC 51768 / IM2 / DSM 7523 / JCM 9630 / NBRC 100827) [Reference proteome] [HAMAP]
Taxonomic identifier178306 [NCBI]
Taxonomic lineageArchaeaCrenarchaeotaThermoproteiThermoprotealesThermoproteaceaePyrobaculum

Protein attributes

Sequence length397 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 – 397397Glutamyl-tRNA reductase HAMAP-Rule MF_00087
PRO_0000114108

Regions

Nucleotide binding177 – 1826NADP By similarity
Region47 – 504Substrate binding By similarity
Region103 – 1053Substrate binding By similarity

Sites

Active site481Nucleophile By similarity
Binding site981Substrate By similarity
Binding site1091Substrate By similarity
Site881Important for activity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8ZYV6 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: 8982B6BB6A6FE801

FASTA39743,630
        10         20         30         40         50         60 
MDLLAPLAAV ILTYREVDAD TLGRVGEEMK KCIEILGVKR PMFVLHTCGR VEAYLYNASE 

        70         80         90        100        110        120 
EEINSVTLRY RRYAESIRVV RGVEAARHLF RVAAGLESML IGETDILGQV EEAFDRQVKA 

       130        140        150        160        170        180 
GFTKGLLKTI VERAIRAGKR VRAETGISRG PAGLGSLSII YVSQLLDLTK SKVAVLGAGA 

       190        200        210        220        230        240 
VGAGLAKELA ERGVAKLYIL NRTLEKAVEI ANKLGAEARP LTREEVQKCL MECDVVFSSV 

       250        260        270        280        290        300 
HSLEYVIDRV PDGAVVKIIV DLGVPQTVAP GLPVRVVRLS DLKQLAEKYS EARKQEAARA 

       310        320        330        340        350        360 
EAIVEEELAK LPQILARRYI EEAVSHLLEK AMEVAEEEGK RAGCPTAVLA ARTTVKRTLF 

       370        380        390 
PIIEVLKKMA EDGRLEDAVK VVEILRSQKP LLRQSEE 

« Hide

References

[1]"Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum aerophilum."
Fitz-Gibbon S.T., Ladner H., Kim U.-J., Stetter K.O., Simon M.I., Miller J.H.
Proc. Natl. Acad. Sci. U.S.A. 99:984-989(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 51768 / IM2 / DSM 7523 / JCM 9630 / NBRC 100827.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE009441 Genomic DNA. Translation: AAL62887.1.
RefSeqNP_558705.1. NC_003364.1.

3D structure databases

ProteinModelPortalQ8ZYV6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING178306.PAE0601.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAL62887; AAL62887; PAE0601.
GeneID1465112.
KEGGpai:PAE0601.

Phylogenomic databases

eggNOGCOG0373.
HOGENOMHOG000112880.
KOK02492.
OMAKGMAVHF.
ProtClustDBPRK00045.

Enzyme and pathway databases

BioCycPAER178306:GCEO-405-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]
PfamPF05201. GlutR_N. 1 hit.
PF01488. Shikimate_DH. 1 hit.
[Graphical view]
SUPFAMSSF69075. SSF69075. 1 hit.
SSF69742. SSF69742. 1 hit.
PROSITEPS00747. GLUTR. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHEM1_PYRAE
AccessionPrimary (citable) accession number: Q8ZYV6
Entry history
Integrated into UniProtKB/Swiss-Prot: April 3, 2002
Last sequence update: March 1, 2002
Last modified: February 19, 2014
This is version 94 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