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

CP000685; ABQ03976.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_001193295.1; -.

3D structure databases

ModBase

A5FLE3.

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

5091356; -.

GenomeReviews

CP000685_GR; Fjoh_0942.

KEGG

fjo:Fjoh_0942; -.

CMR

A5FLE3; Fjoh_0942.

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`	`1 416`	`416`	`Glutamyl-tRNA reductase 1.`	`PRO_0000335032`
`NP_BIND`	`193 198`	`6`	`NADP (By similarity).`
`REGION`	`57 60`	`4`	`Substrate binding (By similarity).`
`REGION`	`118 120`	`3`	`Substrate binding (By similarity).`
`ACT_SITE`	`58 58`		`Nucleophile (By similarity).`
`BINDING`	`113 113`		`Substrate (By similarity).`
`BINDING`	`124 124`		`Substrate (By similarity).`
`SITE`	`103 103`	`1`	`Important for activity (By similarity).`

Sequence information

Length: 416 AA [This is the length of the unprocessed precursor]

Molecular weight: 46757 Da [This is the MW of the unprocessed precursor]

CRC64: 3C213457520C9667 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MENNNVPKHL YFYSVGLSYK KADAEVRGQF SLDAVAKTRL LEQAKNDGIE SLLVTSTCNR 

        70         80         90        100        110        120 
TEIYGFAEHP FQLIKLICDN SNGSVDAFQK VGFVYKNQEA INHMFRVGTG LDSQILGDFE 

       130        140        150        160        170        180 
IISQIKTSFT HSKSMGLANA FMERLVNAVI QASKRIKTET EISSGATSVS FASVQYILKN 

       190        200        210        220        230        240 
VEDISNKNIL LFGTGKIGRN TCENLVKHTK NEHITLINRT KDKAEKLAGK LNLIVKDYSE 

       250        260        270        280        290        300 
LHLELQKADV VVVATGAQNP TVDKAILNLK KPLLILDLSI PKNVNENVEE LEGVTLIHMD 

       310        320        330        340        350        360 
YLSQLTDETL ENRKLHIPAA EAIIEEIKEE FVTWMKGRKF APTINALKEK LNAIKASELD 

       370        380        390        400        410 
FQSKKIADFN EEQAEIISNR IIQKITTHFA NHLKDDDTMV DESIEWIEKV FKIKAS

A5FLE3 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