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HAMAP rule MF_00087

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General rule information [?]

Accession MF_00087
Dates 1-JUN-2001 (Created)
1-JUN-2023 (Last updated, Version 50)
Name Glu_tRNA_reductase
Scope(s) Bacteria
Archaea
Plastid
Template(s) P0A6X1 (HEM1_ECOLI); Q9UXR8 (HEM1_METKA); P28462 (HEM1_CHLP8); P42809 (HEM1_METTM); P28463 (HEM1_SYNY3); Q59292 (HEMA_RUMJO); P42808 (HEM1_XANCH); [ Recover all ]
Triggered by HAMAP; MF_00087 (Get profile general information and statistics)

Propagated annotation [?]

Identifier, protein and gene names [?]

Identifier HEM1
Protein name RecName: Full=Glutamyl-tRNA reductase;
                 Short=GluTR;
                 EC=1.2.1.70;
Gene name Name=hemA;

Comments [?]

FUNCTIONCatalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).
CATALYTIC ACTIVITY Reaction=(S)-4-amino-5-oxopentanoate + NADP(+) + tRNA(Glu) = H(+) + L- glutamyl-tRNA(Glu) + NADPH; Xref=Rhea:RHEA:12344, Rhea:RHEA- COMP:9663, Rhea:RHEA-COMP:9680, ChEBI:CHEBI:15378, ChEBI:CHEBI:57501, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78442, ChEBI:CHEBI:78520; EC=1.2.1.70;
PATHWAYPorphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2.
case <Property:PHOTOSYN>
PATHWAYPorphyrin-containing compound metabolism; chlorophyll biosynthesis.
end case
SUBUNITHomodimer.
case <OG:Chloroplast>
SUBCELLULAR LOCATIONPlastid, chloroplast.
end case
DOMAINPossesses 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.
MISCELLANEOUSDuring 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.
SIMILARITYBelongs to the glutamyl-tRNA reductase family.

Keywords [?]


Gene Ontology [?]

GO:0008883; Molecular function:glutamyl-tRNA reductase activity
case <Property:PHOTOSYN>
GO:0015995; Biological process:chlorophyll biosynthetic process
end case
GO:0006779; Biological process:porphyrin-containing compound biosynthetic process
case <OG:Chloroplast>
GO:0009507; Cellular component:chloroplast
end case

Cross-references [?]

PROSITE PS00747; GLUTR; 1;
Pfam PF01488; Shikimate_DH; 1;
NCBIfam TIGR01035; HemA; 1;

Features [?]

From: HEM1_METKA (Q9UXR8)
Key From To Description Tag Condition FTGroup
BINDING 174 179 /ligand="NADP(+)"
/ligand_id="ChEBI:CHEBI:58349"
BINDING 47 50 /ligand="substrate" T-C-x-R
BINDING 99 101 /ligand="substrate" [ED]-x-[EDQ]
ACT_SITE 48 48 /note="Nucleophile" C
BINDING 94 94 /ligand="substrate" S
BINDING 105 105 /ligand="substrate" Q
SITE 84 84 /note="Important for activity" H

Additional information [?]

Size range 329-497 amino acids
Related rules None
Fusion Nter: None Cter: None
Comments STRAW and STRCO have an internal inserted domains of about 120 residues; sequence not included in alignment. Highly divergent RUMJO; sequence not included in alignment SORC5 has a long C-terminus; not included in alignment



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