A0A101XM98 · A0A101XM98_9CREN

Function

function

Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).

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.

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

Pathway

Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2.

Features

Showing features for binding site, active site, site.

TypeIDPosition(s)Description
Binding site44-47substrate
Active site45Nucleophile
Site84Important for activity
Binding site94substrate
Binding site99-101substrate
Binding site105substrate
Binding site166-171NADP+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Molecular Functionglutamyl-tRNA reductase activity
Molecular FunctionNADP binding
Biological Processprotoporphyrinogen IX biosynthetic process from glutamate

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Glutamyl-tRNA reductase
  • EC number
  • Short names
    GluTR

Gene names

    • Name
      hemA
    • ORF names
      AT717_03095

Organism names

  • Taxonomic identifier
  • Organism
  • Taxonomic lineage
    Archaea > Thermoproteota > Thermoprotei > Thermoproteales > Thermoproteaceae > Vulcanisaeta

Accessions

  • Primary accession
    A0A101XM98

Proteomes

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain9-135Glutamyl-tRNA reductase N-terminal
Domain158-272Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA reductase
Domain292-382Tetrapyrrole biosynthesis glutamyl-tRNA reductase dimerisation

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.

Sequence similarities

Belongs to the glutamyl-tRNA reductase family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    389
  • Mass (Da)
    44,667
  • Last updated
    2016-04-13 v1
  • Checksum
    41D08F0E253F763B
MVRIKALVLTYRDYDLDTLAKAYLLDNELKDLYGHYDSLIALQTCNRIEFYLDGGENEDHLISMLKNRAGVEPRVLFDLDAVKHLLLVTTGLDSMFFGEREILSQVKKAYATGKRSERLRILFESAIRFGENFRRKYNLSEISFIKFLSNFIMNNVDSEDKLLVIGGGEVARGVVRELLRNGYSNIVVANRTLDRLKYEFGNSVKVVNLESLKNEVATNKYDVWLAAISVKQPIISVKDSREIPDLIIDVSTPSAVDVDGTPVRIIRLEDLREPYLKYVNGKSSILKEFGEVDKEAERIMRLIIRRDADDVIRDITRFTENIREEEVREAINALNNGADPKVVVEAMSRSLVKKIMHNYLENIRALTEKGDLDEIRRLRDLFIMAHDNS

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
LOCG01000072
EMBL· GenBank· DDBJ
KUO93941.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
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