NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Bonus;
TISSUE=Root;
Tanaka R., Yoshida K., Nakayashiki T., Tsuji H., Inokuchi H., Okada K., Tanaka A.;
"The third member of the hemA gene family encoding glutamyl-tRNA reductase is primarily expressed in roots in Hordeum vulgare.";
Photosyn. Res. 53:161-171(1997).

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.
TISSUE SPECIFICITY: Primarily expressed in roots.
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

D88383; BAA25168.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

T04402; T04402.

3D structure databases

HSSP

Q42843; 1B29. [HSSP ENTRY / PDB]

ModBase

O65796.

Organism-specific databases

Gramene

O65796; -.

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.

PIRSF

PIRSF000445; 4pyrrol_synth_GluRdtase; 1.

TIGRFAMs

TIGR01035; hemA; 1.

PROSITE

PS00747; GLUTR; 1.

Other

ProtoNet

O65796.

UniRef

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`	`? 535`		`Glutamyl-tRNA reductase 3, chloroplastic.`	`PRO_0000013312`
`NP_BIND`	`272 277`	`6`	`NADP (By similarity).`
`REGION`	`131 133`	`3`	`Substrate binding (By similarity).`
`REGION`	`195 197`	`3`	`Substrate binding (By similarity).`
`ACT_SITE`	`131 131`		`Nucleophile (By similarity).`
`BINDING`	`190 190`		`Substrate (By similarity).`
`BINDING`	`201 201`		`Substrate (By similarity).`
`SITE`	`180 180`	`1`	`Important for activity (By similarity).`

Sequence information

Length: 535 AA [This is the length of the unprocessed precursor]

Molecular weight: 58419 Da [This is the MW of the unprocessed precursor]

CRC64: B2830889AE6A3224 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MASTSTASAT AMAGAFAAAG VNKPRGSAAC PRVPAGGRQR LSCVVRCDAG PGVPAQMAAM 

        70         80         90        100        110        120 
AASVAALEQF KISADRYMKE KSSIAVIGLS IHTAPVEMRE KLAVAEELWP RAVAELTNLN 

       130        140        150        160        170        180 
HIEKAAVLSP CNRMEIYVVA LSWNRGIREI VDWMSMKSGI PAVELREHLF MFRDSDATRH 

       190        200        210        220        230        240 
LFEVSSGLDS LVLGEGQILA QVKQVVRSGQ NSGGLGKNID RMFKDAITAG KRVRSETNIS 

       250        260        270        280        290        300 
CGAVSVSSAA VELALMKLPK SECLSARMLL IGAGKMGRLV AKHLAAKGCK KVVIVNRSVE 

       310        320        330        340        350        360 
RVDAIREEMQ GIEIVYRSLT EMYEAAADAD VVFTSTSSES PLFTKEHAEA LPPVSGALGG 

       370        380        390        400        410        420 
VRLFVDISVP RNVSACVSDV GHARVYNVDD LKEVVEANKE DRLRKAMEAQ TIISEELKRF 

       430        440        450        460        470        480 
EAWRDSMETV PTIKKLRSYA DRVRASELDK CLQKIGEDAL TKKMRRSIEQ LSTGIVNRLL 

       490        500        510        520        530 
HGPLQHLRCD GTDNRTLDET LENMHALNRM FGLDTEKAVM EQKIKTKVEK QKTQN

O65796 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