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

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

Cross-references

Sequence databases

EMBL

CP000570; ABN81561.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_001060594.1; -.

3D structure databases

ModBase

A3NE23.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from InterPro).
GO:0008883;	Molecular function: glutamyl-tRNA reductase activity (inferred from electronic annotation from HAMAP).
GO:0050661;	Molecular function: NADP binding (inferred from electronic annotation from InterPro).
GO:0004764;	Molecular function: shikimate 5-dehydrogenase activity (inferred from electronic annotation from InterPro).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
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

IPR000343; 4pyrrol_synth_GluRdtase.
IPR015896; 4pyrrol_synth_GluRdtase_C.
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

PF00745; GlutR_dimer; 1.
PF05201; GlutR_N; 1.
PF01488; Shikimate_DH; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF000445; 4pyrrol_synth_GluRdtase; 1.

TIGR01035; hemA; 1.

PS00747; GLUTR; 1.

Genome annotation databases

GeneID

4882765; -.

GenomeReviews

CP000570_GR; BURPS668_3589.

KEGG

bpd:BURPS668_3589; -.

NMPDR

fig|320373.3.peg.2520; -.

TIGR

BURPS668_3589; -.

Other

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`	`1 434`	`434`	`Glutamyl-tRNA reductase.`	`PRO_0000335018`
`NP_BIND`	`196 201`	`6`	`NADP (By similarity).`
`REGION`	`57 60`	`4`	`Substrate binding (By similarity).`
`REGION`	`121 123`	`3`	`Substrate binding (By similarity).`
`ACT_SITE`	`58 58`		`Nucleophile (By similarity).`
`BINDING`	`116 116`		`Substrate (By similarity).`
`BINDING`	`127 127`		`Substrate (By similarity).`
`SITE`	`106 106`	`1`	`Important for activity (By similarity).`

Sequence information

Length: 434 AA [This is the length of the unprocessed precursor]

Molecular weight: 47560 Da [This is the MW of the unprocessed precursor]

CRC64: 82F9FDE5A752B98F [This is a checksum on the sequence]

        10         20         30         40         50         60 
MDMQLLTIGI NHHTAPVALR ERVAFPLEQI KPALSTFKSV FLGHPAPNAP EAAILSTCNR 

        70         80         90        100        110        120 
TELYCATNDR AARDAAIRWM SDYHRIPADE LAPHVYALPQ SEAVRHAFRV ASGLDSMVLG 

       130        140        150        160        170        180 
ETQILGQMKN AVRTASEAGS LGTYLNQLFQ RTFAVAKEVR GTTEIGAQSV SMAAAAVRLA 

       190        200        210        220        230        240 
QRIFEQVAQQ RVLFIGAGEM IELCATHFAA QGPRELIVAN RTAERGAKLA ERFGGRAMPL 

       250        260        270        280        290        300 
ADLPARMHEF DIIVSCTAST LPIIGLGAVE RAVKARRHRP IFMVDLAVPR DIEPEVGKLK 

       310        320        330        340        350        360 
DVFLYTVDDL GAIVREGNAS RQAAVAQAEA IIETRVQNFM QWLDARSIVP VIRHMHTQAD 

       370        380        390        400        410        420 
ALRRAEVERA RKMLARGDDP DAVLDALSQA LTNKLIHGPT SALNRANGAD RDSLIDLMRG 

       430 
FYQHAPRSSD TSDR

A3NE23 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	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