[1]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=cv. Bonus; PubMed=8696365 [NCBI, ExPASy, EBI, Israel, Japan] Bougri O., Grimm B.; "Members of a low-copy number gene family encoding glutamyl-tRNA reductase are differentially expressed in barley."; Plant J. 9:867-878(1996).

Comments

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 .
SUBCELLULAR LOCATION: Plastid, chloroplast.
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

X86102; CAA60055.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

T05734; T05734.

3D structure databases

HSSP

Q9UXR8; 1GPJ. [HSSP ENTRY / PDB]

ModBase

Q96563.

Organism-specific databases

Gramene

Q96563; -.

Family and domain databases

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.

Other

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

Keywords

Chlorophyll biosynthesis; Chloroplast; NADP; Oxidoreductase; Plastid; Porphyrin biosynthesis.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`<1 465`	`>465`	`Glutamyl-tRNA reductase 2.`	`PRO_0000114114`
`NP_BIND`	`204 209`	`6`	`NADP (By similarity).`
`REGION`	`62 65`	`4`	`Substrate binding (By similarity).`
`REGION`	`127 129`	`3`	`Substrate binding (By similarity).`
`COMPBIAS`	`224 227`	`4`	`Poly-Val.`
`ACT_SITE`	`63 63`		`Nucleophile (By similarity).`
`BINDING`	`122 122`		`Substrate (By similarity).`
`BINDING`	`133 133`		`Substrate (By similarity).`
`SITE`	`112 112`	`1`	`Important for activity (By similarity).`
`NON_TER`	`1 1`

Sequence information

Length: 465 AA [This is the length of the partial sequence of the unprocessed precursor]

Molecular weight: 51675 Da [This is the MW of the partial sequence of the unprocessed precursor]

CRC64: E42A50A3E749CE6D [This is a checksum on the sequence]

        10         20         30         40         50         60 
QFKISADRYI KEKSSIAVIG LSVHTAPVDM REKLAVAEEL WPRAISELTS LNHIEEAAVL 

        70         80         90        100        110        120 
STCNRMEIYV VALSWNRGIR EVVDWMSKKS GIPASELREH LFMLRDSGAT RHLFEVSAGL 

       130        140        150        160        170        180 
DSLVLGEGQI LAQVKQVVRN GQNSGGLGKN IDRMFKDAIT AGKRARCETN ISAGAVSVSS 

       190        200        210        220        230        240 
AAVELAMMKL PKSECLSARM LLIGAGKMGK LVVKHLIAKG CKKVVVVNRS VERVDAIREE 

       250        260        270        280        290        300 
MKDIEIVYRP LTEMYEAAAD ADVVFTSTAS ESLLFTKEHA EALPPISLAM GGVRLFVDIS 

       310        320        330        340        350        360 
VPRNVGACLS QVEHARVYNV DDLKEVVEAN KEDRVRKAME AQAIITQELK RFEAWRDSLE 

       370        380        390        400        410        420 
TVPTIKKLRS YADRIRASEL DKCLQKIGED NLNKKTRRSI EELSTGIVNK LLHGPLQHLR 

       430        440        450        460 
CDGSDSRTLD ETLDNMHALN RMFNLDTEKA VLEQKIKAKV EKTQS

Q96563 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