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: Primarily in cotyledons and hypocotyls of greening cucumber seedlings.
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

D50407; BAA08910.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

T10186; T10186.

3D structure databases

HSSP

Q9UXR8; 1GPJ. [HSSP ENTRY / PDB]

ModBase

P93111.

Ontologies

GO:0009507;	Cellular component: chloroplast (inferred from electronic annotation from UniProtKB-KW).
GO:0008883;	Molecular function: glutamyl-tRNA reductase activity (inferred from electronic annotation from InterPro).
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:0015995;	Biological process: chlorophyll biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

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`	`? 552`		`Glutamyl-tRNA reductase 1, chloroplastic.`	`PRO_0000013309`
`NP_BIND`	`292 297`	`6`	`NADP (By similarity).`
`REGION`	`150 153`	`4`	`Substrate binding (By similarity).`
`REGION`	`215 217`	`3`	`Substrate binding (By similarity).`
`ACT_SITE`	`151 151`		`Nucleophile (By similarity).`
`BINDING`	`210 210`		`Substrate (By similarity).`
`BINDING`	`221 221`		`Substrate (By similarity).`
`SITE`	`200 200`	`1`	`Important for activity (By similarity).`

Sequence information

Length: 552 AA [This is the length of the unprocessed precursor]

Molecular weight: 60895 Da [This is the MW of the unprocessed precursor]

CRC64: 9C7A72AF24FF00F5 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAVSTSFSGA KLEALLFKSA SNSSSTRNLS SSHLPGFCKS IRTRRILFQR TGVSSFTPFK 

        70         80         90        100        110        120 
CELASSDVLV QNDEIDPPKS SNLSALEQLK TSAVDRYTKE RSSIVVIGLS IHTTPVEMRE 

       130        140        150        160        170        180 
KLAIPEAEWP RAIGELCGLN HIEEAAVLST CNRMEIYVVA LSQHRGVKEV TEWMSKTSGI 

       190        200        210        220        230        240 
PVSEICQHRF LLYNNDATQH IFEVSAGLDS LVLGEGQILA QVKQVVKVGQ GVAGFGRNIS 

       250        260        270        280        290        300 
GLFKHAITVG KRVRTETNIA AGAVSVSSAA VELALMKLPE PSHATARMLV IGAGKMGKLV 

       310        320        330        340        350        360 
IKHLVAKGCT KMVVVNRSEE RVTAIREEMK DVEIIYKPLT EMLSCTAEAD VIFTSTASES 

       370        380        390        400        410        420 
LLFTKEQVKD LPPVGHDVGG LRLFIDISVP RNVGACINNL EDVRVYNVDD LKEVVAANKE 

       430        440        450        460        470        480 
DRLRKAMEAQ SIITEESKQF EAWRDSLETV PTIKKLRAYA ERIRTAELEK CLSKMGDDIP 

       490        500        510        520        530        540 
KKTRRAVDDL SRGIVNKLLH GPMQHLRCDG SDSRTLSETL ENMHALNRMF SLETEIAVLE 

       550 
QKIRAKVEQN QK

P93111 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