NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Aonagajibai;
TISSUE=Cotyledon;
DOI=10.1104/pp.110.4.1223; PubMed=8934625 [NCBI, ExPASy, EBI, Israel, Japan]
Tanaka R., Yoshida K., Nakayashiki T., Masuda T., Tsuji H., Inokuchi H., Tanaka A.;
"Differential expression of two hemA mRNAs encoding glutamyl-tRNA reductase proteins in greening cucumber seedlings.";
Plant Physiol. 110:1223-1230(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 (By similarity).
TISSUE SPECIFICITY: Found in all tissues examined.
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

D67088; BAA11091.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

T10245; T10245.

3D structure databases

HSSP

Q9UXR8; 1GPJ. [HSSP ENTRY / PDB]

ModBase

P49295.

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.

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; Transit peptide.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 ?`		`Chloroplast (Potential).`
`CHAIN`	`? 542`		`Glutamyl-tRNA reductase 2, chloroplastic.`	`PRO_0000013310`
`NP_BIND`	`284 289`	`6`	`NADP (By similarity).`
`REGION`	`142 145`	`4`	`Substrate binding (By similarity).`
`REGION`	`207 209`	`3`	`Substrate binding (By similarity).`
`ACT_SITE`	`143 143`		`Nucleophile (By similarity).`
`BINDING`	`202 202`		`Substrate (By similarity).`
`BINDING`	`213 213`		`Substrate (By similarity).`
`SITE`	`192 192`	`1`	`Important for activity (By similarity).`

Sequence information

Length: 542 AA [This is the length of the unprocessed precursor]

Molecular weight: 59707 Da [This is the MW of the unprocessed precursor]

CRC64: A576B3B96A0B6EEF [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAAAVGGLTT CFARPTPEFI APSTSYSAPV RVFFKPFKVR DLCCAGEVVG VLSARSIPIS 

        70         80         90        100        110        120 
PRFELIRLVR MQPGLSALEL LKTSSVNRYT KERISIVVIG LNVHTAPVEL REKLAIPEAQ 

       130        140        150        160        170        180 
WPPGIGELCA LNHIEEAAVL STCNRIEIYV VALSQHRGVK EVTEWMSKRS GIPISELCKH 

       190        200        210        220        230        240 
RVLLYNTDAT QHLFEVSAGL DSLVLGEGQI LAQVKHVVKT GQGVAGFDRK ISGLFKHAIT 

       250        260        270        280        290        300 
VGKRVRTETN ISSGSFSVSS AAVELAQKKL PESSYATAKV MVVGAGKMGK LVIKHLVAKG 

       310        320        330        340        350        360 
CRKMVVVNRT QDSVDAVEEL KDVEIIYKPL SKILACASEA DVIFTCTASK TPLFTKEHVA 

       370        380        390        400        410        420 
MLPPAGTETG RRLFVDISVP RNVEQRVSDL ETVSVFNVDD LKEVVAANKE DRLKKVQEAQ 

       430        440        450        460        470        480 
SIIGEEINKF EAWRDSLETV PTIKKFRAYV ERIRAAELDK CLSKMGEDIP KKKKVAINDL 

       490        500        510        520        530        540 
SLGIANKLLH GPIQHLRCDG NDSRTLDEIL QNMHAINRMF DLETDLSVLE EKIRAKVERG 


QK

P49295 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