[1]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=cv. Klages; 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).
[2]	PROTEIN SEQUENCE OF 44-65, AND CHARACTERIZATION. PubMed=7957167 [NCBI, ExPASy, EBI, Israel, Japan] Pontoppidan B., Kannangara C.G.; "Purification and partial characterisation of barley glutamyl-tRNA(Glu) reductase, the enzyme that directs glutamate to chlorophyll biosynthesis."; Eur. J. Biochem. 225:529-537(1994).
[3]	FUNCTION, CHARACTERIZATION, HEME BINDING, AND SUBUNIT. DOI=10.1073/pnas.93.17.9287; PubMed=8799193 [NCBI, ExPASy, EBI, Israel, Japan] Vothknecht U.C., Kannangara C.G., von Wettstein D.; "Expression of catalytically active barley glutamyl tRNAGlu reductase in Escherichia coli as a fusion protein with glutathione S-transferase."; Proc. Natl. Acad. Sci. U.S.A. 93:9287-9291(1996).
[4]	3D-STRUCTURE MODELING OF 76-460. DOI=10.1002/(SICI)1097-0134(19991115)37:3<485::AID-PROT15>3.0.CO;2-G; PubMed=10591107 [NCBI, ExPASy, EBI, Israel, Japan] Brody S.S., Gough S.P., Kannangara C.G.; "Predicted structure and fold recognition for the glutamyl tRNA reductase family of proteins."; Proteins 37:485-493(1999).

Comments

FUNCTION: Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).
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.
SUBCELLULAR LOCATION: Plastid, chloroplast.
MISCELLANEOUS: Was shown to bind heme, but the precise role of heme is unclear.
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

X92403; CAA63140.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X86101; CAA60054.1; ALT_INIT; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

T05732; T05732.

3D structure databases

PDB

1B29; Model; -; A=76-460.	[ExPASy / RCSB / EBI]
1B61; Model; -; A=76-460.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1B29; -.
1B61; -.

ModBase

Q42843.

Organism-specific databases

Gramene

Q42843; -.

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

Q42843; -.

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

Keywords

3D-structure; Chlorophyll biosynthesis; Chloroplast; Direct protein sequencing; NADP; Oxidoreductase; Plastid; Porphyrin biosynthesis; Transit peptide.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 43`	`43`	`Chloroplast.`
`CHAIN`	`44 527`	`484`	`Glutamyl-tRNA reductase 1, chloroplastic.`	`PRO_0000013311`
`NP_BIND`	`266 271`	`6`	`NADP (By similarity).`
`REGION`	`124 127`	`4`	`Substrate binding (By similarity).`
`REGION`	`189 191`	`3`	`Substrate binding (By similarity).`
`COMPBIAS`	`286 289`	`4`	`Poly-Val.`
`ACT_SITE`	`125 125`		`Nucleophile (By similarity).`
`BINDING`	`184 184`		`Substrate (By similarity).`
`BINDING`	`195 195`		`Substrate (By similarity).`
`SITE`	`174 174`	`1`	`Important for activity (By similarity).`
`STRAND`	`79 81`	`3`
`STRAND`	`96 99`	`4`
`HELIX`	`104 125`	`22`
`STRAND`	`133 137`	`5`
`TURN`	`150 152`	`3`
`HELIX`	`155 159`	`5`
`HELIX`	`170 182`	`13`
`HELIX`	`193 197`	`5`
`HELIX`	`209 213`	`5`
`STRAND`	`215 222`	`8`
`HELIX`	`225 230`	`6`
`HELIX`	`233 251`	`19`
`STRAND`	`262 265`	`4`
`HELIX`	`269 281`	`13`
`STRAND`	`285 288`	`4`
`HELIX`	`293 302`	`10`
`HELIX`	`313 315`	`3`
`TURN`	`316 318`	`3`
`HELIX`	`319 321`	`3`
`STRAND`	`324 327`	`4`
`STRAND`	`334 336`	`3`
`HELIX`	`347 350`	`4`
`STRAND`	`356 358`	`3`
`STRAND`	`361 363`	`3`
`STRAND`	`365 367`	`3`
`HELIX`	`368 376`	`9`
`STRAND`	`380 383`	`4`
`HELIX`	`386 389`	`4`
`STRAND`	`392 397`	`6`
`HELIX`	`398 404`	`7`
`STRAND`	`406 410`	`5`
`HELIX`	`413 421`	`9`
`HELIX`	`423 436`	`14`
`HELIX`	`443 457`	`15`

Sequence information

Length: 527 AA [This is the length of the unprocessed precursor]

Molecular weight: 57653 Da [This is the MW of the unprocessed precursor]

CRC64: D329E56458BE1165 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAGATSATAA AGAFAAAKAR GPAAACPWLV AAGGRRRSGV VRCDAGGDAQ AASKAASITA 

        70         80         90        100        110        120 
LEQFKISADR YMKEKSSIAV IGLSVHTAPV EMREKLAVAE ELWPRAISEL TSLNHIEEAA 

       130        140        150        160        170        180 
VLSTCNRMEI YVVALSWNRG IREVVDWMSK KSGIPASELR EHLFMLRDSD ATRHLFEVSA 

       190        200        210        220        230        240 
GLDSLVLGEG QILAQVKQVV RNGQNSGGLG KNIDRMFKDA ITAGKRVRCE TNISAGAVSV 

       250        260        270        280        290        300 
SSAAVELAMM KLPKSECLSA RMLLIGAGKM GKLVVKHLIA KGCKKVVVVN RSVERVDAIR 

       310        320        330        340        350        360 
EEMKDIEIVY RPLTEMYEAA ADADVVFTST ASESLLFTKE HAEVLPPISL AMGGVRLFVD 

       370        380        390        400        410        420 
ISVPRNVGAC LSEVEHARVY NVDDLKEVVE ANKEDRVRKA MEAQTIITQE LKRFEAWRDS 

       430        440        450        460        470        480 
LETVPTIKKL RSYADRIRAS ELEKCLQKIG EDNLNKKMRR SIEELSTGIV NKLLHGPLQH 

       490        500        510        520 
LRCDGSDSRT LDETLENMHA LNRMFSLDTE KAVLEQKIKA KVEKTQS

Q42843 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