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 .
SUBUNIT: Homodimer (By similarity).
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.

Copyright

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Cross-references

Sequence databases

EMBL

CP000853; ABW18869.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_001512865.1; -.

3D structure databases

ModBase

A8MGE1.

Ontologies

GO:0008883;	Molecular function: glutamyl-tRNA reductase activity (inferred from electronic annotation from HAMAP).
GO:0006779;	Biological process: porphyrin biosynthetic process (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_00087; -; 1.
PBIL [Tree]

InterPro

IPR015895; 4pyrrol_synth_GluRdtase_N.
IPR016040; NAD(P)-bd.
IPR006151; Shikm_DHase/Glu-tRNA_Rdtase.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.50.720; NAD(P)-bd; 1.

Pfam

PF05201; GlutR_N; 1.
PF01488; Shikimate_DH; 1.
Pfam graphical view of domain structure.

PROSITE

PS00747; GLUTR; FALSE_NEG.

BLOCKS

A8MGE1.

Genome annotation databases

GeneID

5677168; -.

GenomeReviews

CP000853_GR; Clos_1324.

CMR

A8MGE1; Clos_1324.

Other

ProtoNet

A8MGE1.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; NADP; Oxidoreductase; Porphyrin biosynthesis.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 334`	`334`	`Glutamyl-tRNA reductase.`	`PRO_1000057568`
`NP_BIND`	`186 191`	`6`	`NADP (By similarity).`
`REGION`	`49 52`	`4`	`Substrate binding (By similarity).`
`REGION`	`112 114`	`3`	`Substrate binding (By similarity).`
`ACT_SITE`	`50 50`		`Nucleophile (By similarity).`
`BINDING`	`107 107`		`Substrate (By similarity).`
`BINDING`	`118 118`		`Substrate (By similarity).`
`SITE`	`97 97`	`1`	`Important for activity (By similarity).`

Sequence information

Length: 334 AA [This is the length of the unprocessed precursor]

Molecular weight: 38048 Da [This is the MW of the unprocessed precursor]

CRC64: 8F26F7A9D7D44A9F [This is a checksum on the sequence]

        10         20         30         40         50         60 
MNIIMAGIDY KLAPIDVREG FSFTKAMMKQ VYSNILKDTM IYGTVIISTC NRTEIYISCE 

        70         80         90        100        110        120 
EDFCVNPFEV LCNAAGIDFT PYEKVHRVKE GDEVIKHLCQ LACGVKSQIW GEDQIITQVK 

       130        140        150        160        170        180 
NAIAVSREMR AADSYLEVMF RNAIAAAKKV KSTLILNSRE NSIVHKALKI IKDQETMNIR 

       190        200        210        220        230        240 
EILVIGNGEM GRLMTNVLIE NGYRATMTLR QYRYHANVIP LNANTVDYSN RYEKMKDCDV 

       250        260        270        280        290        300 
VISATLSPHY TVEMENLKKI DKIPKLFIDL AVPRDIDPSI KNLPNIELYD VDGIGADEIS 

       310        320        330 
KNHAQQLKGI ERIIEKYICD YHKWCLFKEG LGCI

A8MGE1 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools