AC   MF_00087;
DC   Protein; auto
TR   HAMAP; MF_00087; -; 1; level=0
XX
Names: Glu_tRNA_reductase
XX
ID   HEM1
DE   RecName: Full=Glutamyl-tRNA reductase;
DE            Short=GluTR;
DE            EC=1.2.1.70;
GN   Name=hemA;
XX
CC   -!- FUNCTION: Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu)
CC       to glutamate 1-semialdehyde (GSA).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-4-amino-5-oxopentanoate + NADP(+) + tRNA(Glu) = H(+) + L-
CC         glutamyl-tRNA(Glu) + NADPH; Xref=Rhea:RHEA:12344, Rhea:RHEA-
CC         COMP:9663, Rhea:RHEA-COMP:9680, ChEBI:CHEBI:15378, ChEBI:CHEBI:57501,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78442,
CC         ChEBI:CHEBI:78520; EC=1.2.1.70;
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC       biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2.
case <Property:PHOTOSYN>
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; chlorophyll
CC       biosynthesis.
end case
CC   -!- SUBUNIT: Homodimer.
case <OG:Chloroplast>
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
end case
CC   -!- DOMAIN: Possesses an unusual extended V-shaped dimeric structure with
CC       each monomer consisting of three distinct domains arranged along a
CC       curved 'spinal' alpha-helix. The N-terminal catalytic domain
CC       specifically recognizes the glutamate moiety of the substrate. The
CC       second domain is the NADPH-binding domain, and the third C-terminal
CC       domain is responsible for dimerization.
CC   -!- MISCELLANEOUS: During catalysis, the active site Cys acts as a
CC       nucleophile attacking the alpha-carbonyl group of tRNA-bound glutamate
CC       with the formation of a thioester intermediate between enzyme and
CC       glutamate, and the concomitant release of tRNA(Glu). The thioester
CC       intermediate is finally reduced by direct hydride transfer from NADPH,
CC       to form the product GSA.
CC   -!- SIMILARITY: Belongs to the glutamyl-tRNA reductase family.
XX
DR   PROSITE; PS00747; GLUTR; 1; trigger=no
DR   Pfam; PF01488; Shikimate_DH; 1; trigger=no
DR   NCBIfam; TIGR01035; HemA; 1; trigger=no
XX
KW   Porphyrin biosynthesis
case <Property:PHOTOSYN>
KW   Chlorophyll biosynthesis
end case
KW   Oxidoreductase
KW   NADP
XX
GO   GO:0008883; F:glutamyl-tRNA reductase activity
case <Property:PHOTOSYN>
GO   GO:0015995; P:chlorophyll biosynthetic process
end case
GO   GO:0006779; P:porphyrin-containing compound biosynthetic process
case <OG:Chloroplast>
GO   GO:0009507; C:chloroplast
end case
XX
FT   From: HEM1_METKA (Q9UXR8)
FT   BINDING         174..179
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT   BINDING         47..50
FT                   /ligand="substrate"
FT   Condition: T-C-x-R
FT   BINDING         99..101
FT                   /ligand="substrate"
FT   Condition: [ED]-x-[EDQ]
FT   ACT_SITE        48
FT                   /note="Nucleophile"
FT   Condition: C
FT   BINDING         94
FT                   /ligand="substrate"
FT   Condition: S
FT   BINDING         105
FT                   /ligand="substrate"
FT   Condition: Q
FT   SITE            84
FT                   /note="Important for activity"
FT   Optional; Condition: H
XX
Size: 329-497;
Related: None;
Template: P0A6X1; Q9UXR8; P28462; P42809; P28463; Q59292; P42808;
Scope:
 Bacteria
 Archaea
 Plastid
Fusion:
 Nter: None
 Cter: None
Duplicate: in KORVE, ANADE, ANADF, LACP7, FLAJ1, NOCSJ, PYRAR, PYRCJ
Plasmid: 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
XX
# Revision 1.50 2023/06/01
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