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 .
PATHWAY: Porphyrin biosynthesis; chlorophyll biosynthesis .
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

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

CP000828; ABW30704.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_001520023.1; -.

3D structure databases

ModBase

B0BZF9.

Ontologies

GO:0008883;	Molecular function: glutamyl-tRNA reductase activity (inferred from electronic annotation from HAMAP).
GO:0015995;	Biological process: chlorophyll biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

HAMAP

MF_00087; -; 1.
PBIL [Tree]

InterPro

IPR000343; 4pyrrol_synth_GluRdtase.
IPR016040; NAD(P)-bd.
IPR003462; ODC_Mu_crystall.
Graphical view of domain structure.

Gene3D

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

PANTHER

PTHR13812; ODC_Mu_crystall; 1.

PIRSF

PIRSF000445; 4pyrrol_synth_GluRdtase; 1.

TIGR01035; hemA; 1.

PS00747; GLUTR; 1.

Genome annotation databases

GeneID

5684546; -.

GenomeReviews

CP000828_GR; AM1_5760.

KEGG

amr:AM1_5760; -.

CMR

B0BZF9; AM1_5760.

Other

UniRef

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

Keywords

Chlorophyll biosynthesis; Complete proteome; NADP; Oxidoreductase; Porphyrin biosynthesis.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 433`	`433`	`Glutamyl-tRNA reductase.`	`PRO_1000075400`
`NP_BIND`	`189 194`	`6`	`NADP (By similarity).`
`REGION`	`49 52`	`4`	`Substrate binding (By similarity).`
`REGION`	`114 116`	`3`	`Substrate binding (By similarity).`
`ACT_SITE`	`50 50`		`Nucleophile (By similarity).`
`BINDING`	`109 109`		`Substrate (By similarity).`
`BINDING`	`120 120`		`Substrate (By similarity).`
`SITE`	`99 99`	`1`	`Important for activity (By similarity).`

Sequence information

Length: 433 AA [This is the length of the unprocessed precursor]

Molecular weight: 48281 Da [This is the MW of the unprocessed precursor]

CRC64: A7BF0E37642CCEC7 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MNIAVVGLSH KTAPVDVREK LSIPDDVKEK ATSQLRSYPH LEEVAILSTC NRMEVYVVAQ 

        70         80         90        100        110        120 
ETDDGIRELT QFLSEWSQIP LLELRQHLFI LLHQDAVMHL MRVSAGLDSL VLGEGQILAQ 

       130        140        150        160        170        180 
VKQTHKLSQK YSGAGPILNR LFKQAISAGK RVRTETSIGT GAVSISSAAV ELAQIKTEDL 

       190        200        210        220        230        240 
SAHRVAIIGA GKMSRLLVKH LLSKGANQIA ILNRSLKRAE QLADQFQGAD LKLHTLADMQ 

       250        260        270        280        290        300 
AVLTESDLIF TSTASTEPLL DRDILEPIVC DRQSCMIFDI SVPRNVHSNV NELSQVHAFN 

       310        320        330        340        350        360 
VDDLKAVVAQ NQESRRQMAL EAESLLEEEV ASFDVWWRSL ETVPTISSLR TKVESIREQE 

       370        380        390        400        410        420 
LEKALSRLGT EFAEKHQEVI EALTRGIVNK ILHDPMVQLR AQQDIEVRRK AMQSLNMLFN 

       430 
LNSSQGVAKQ RNT

B0BZF9 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