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| HAMAP annotation rule MF_00087 |
| Accession | MF_00087 |
| Dates | 1-JUN-2001 (Created) 6-OCT-2011 (Last updated, Version 39) |
| Name | Glu-tRNA_reductase |
| Scope | Bacteria Archaea Plastid |
| Triggered by |
| Identifier |
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| Protein name |
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| Gene name |
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| FUNCTION | Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA) (By similarity). |
| CATALYTIC ACTIVITY | L-glutamate 1-semialdehyde + NADP(+) + tRNA(Glu) = L-glutamyl-tRNA(Glu) + NADPH. |
| PATHWAY | Porphyrin metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu); step 1/2. |
case <Property:PHOTOSYN>
end case
| SUBUNIT | Homodimer (By similarity). |
case <OG:Chloroplast>
| SUBCELLULAR LOCATION | Plastid, chloroplast. |
end case
| 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). |
| 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). |
| SIMILARITY | Belongs to the glutamyl-tRNA reductase family. |
case <Property:PHOTOSYN>
end case
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
| From: HEM1_METKA (Q9UXR8) | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| NP_BIND | 174 | 179 | NADP (By similarity) | |||||||||
| REGION | 47 | 50 | Substrate binding (By similarity) | T-C-x-R | ||||||||
| REGION | 99 | 101 | Substrate binding (By similarity) | [ED]-x-[EDQ] | ||||||||
| ACT_SITE | 48 | 48 | Nucleophile (By similarity) | C | ||||||||
| BINDING | 94 | 94 | Substrate (By similarity) | S | ||||||||
| BINDING | 105 | 105 | Substrate (By similarity) | Q | ||||||||
| SITE (Optional) | 84 | 84 | Important for activity (By similarity) | H | ||||||||
| Size range: | 329-497 amino acids |
| Related Rules: | None |
| Templates: | P0A6X1 (HEM1_ECOLI); Q9UXR8 (HEM1_METKA); P28462 (HEM1_CHLP8); P42809 (HEM1_METTM); P28463 (HEM1_SYNY3); Q59292 (HEM1_CLOJO); P42808 (HEM1_XANCH): [Recover all] |
| Fusion: | None |
| Comments: | STRAW and STRCO have an internal inserted domains of about 120 residues; sequence not included in alignment. Highly divergent CLOJO; sequence not included in alignment SORC5 has a long C-terminus; not included in alignment |