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

CP000679; ABP67239.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_001180430.1; -.

3D structure databases

ModBase

A4XK04.

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

IPR000343; 4pyrrol_synth_GluRdtase.
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.

PIRSF

PIRSF000445; 4pyrrol_synth_GluRdtase; 1.

TIGR01035; hemA; 1.

PS00747; GLUTR; 1.

Genome annotation databases

GeneID

5088968; -.

GenomeReviews

CP000679_GR; Csac_1649.

KEGG

csc:Csac_1649; -.

CMR

A4XK04; Csac_1649.

Other

ProtoNet

A4XK04.

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`	`1 394`	`394`	`Glutamyl-tRNA reductase.`	`PRO_1000004603`
`NP_BIND`	`175 180`	`6`	`NADP (By similarity).`
`REGION`	`45 48`	`4`	`Substrate binding (By similarity).`
`REGION`	`104 106`	`3`	`Substrate binding (By similarity).`
`ACT_SITE`	`46 46`		`Nucleophile (By similarity).`
`BINDING`	`99 99`		`Substrate (By similarity).`
`BINDING`	`110 110`		`Substrate (By similarity).`
`SITE`	`89 89`	`1`	`Important for activity (By similarity).`

Sequence information

Length: 394 AA [This is the length of the unprocessed precursor]

Molecular weight: 46005 Da [This is the MW of the unprocessed precursor]

CRC64: 375F79C2B3BD64E1 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MLWVIGINHK VEVDIRQKFS LTKTKLQEKL ISLKKLADEV IILSTCNRTE IYFFSEEYVD 

        70         80         90        100        110        120 
IEKIFTELDW DRRYMPLFYI YKDKDCIKHL FEVVCGFDSL LIGEEQIVAQ VKEAKDIAKQ 

       130        140        150        160        170        180 
VGGKNPVLER LFEVALKCSK EFRTKARLNE HPITIASVVG KVLKESNIRK IAIIGLGNIG 

       190        200        210        220        230        240 
FLFCNYFKNS DVDKVFLIGR KNERIDQFVK LYPGKFEYSD KKDAISEAQC LICSTSAPHA 

       250        260        270        280        290        300 
VVHKDDIPDG KNLLIFDLAV PRDVDVEVYK LPNVKVIDID QVHKMDATSR EIRISKMQEN 

       310        320        330        340        350        360 
YNIIEKYIDE FIEWLGFRQY RNLIIEVKRH AEQLCKAQVK YLKNVDSRER EEVERLLIRM 

       370        380        390 
ANLYIDRAIE VLREAHKEGS GEICSNLIKR IFLK

A4XK04 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