[1]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=cv. UE95; TISSUE=Seedling root; DOI=10.1007/BF00019498; PubMed=7858222 [NCBI, ExPASy, EBI, Israel, Japan] Jepson I., Lay V.J., Holt D.C., Bright S.W.J., Greenland A.J.; "Cloning and characterization of maize herbicide safener-induced cDNAs encoding subunits of glutathione S-transferase isoforms I, II and IV."; Plant Mol. Biol. 26:1855-1866(1994).
[2]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=cv. Pioneer hybrid 3906; DOI=10.1104/pp.107.1.311; PubMed=7870838 [NCBI, ExPASy, EBI, Israel, Japan] Irzyk G.P., Potter S., Ward E., Fuerst E.P.; "A cDNA clone encoding the 27-kilodalton subunits of glutathione S-transferase IV from Zea mays."; Plant Physiol. 107:311-312(1995).
[3]	PARTIAL PROTEIN SEQUENCE, AND CHARACTERIZATION. DOI=10.1104/pp.102.3.803; PubMed=8278534 [NCBI, ExPASy, EBI, Israel, Japan] Irzyk G.P., Fuerst E.P.; "Purification and characterization of a glutathione S-transferase from benoxacor-treated maize (Zea mays)."; Plant Physiol. 102:803-810(1993).

Comments

FUNCTION: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Involved in the detoxification of certain herbicides. Most active with substrates possessing a chloroacetamide structure. Trans-cinnamic acid and 1-chloro-2,4-dinitrobenzene are not effective substrates. May play an important role in the benoxacor-mediated protection of maize from metolachlor injury.
CATALYTIC ACTIVITY: RX + glutathione = HX + R-S-glutathione.
BIOPHYSICOCHEMICAL PROPERTIES:

pH dependence: Optimum pH is 7.5-8. Active from pH 6 to 9;
SUBUNIT: Homodimer or heterodimer of GST-I and GST-IV (=GST-II).
TISSUE SPECIFICITY: Seedling roots.
INDUCTION: By herbicides.
SIMILARITY: Belongs to the GST superfamily. Phi family.
SIMILARITY: Contains 1 GST C-terminal domain.
SIMILARITY: Contains 1 GST N-terminal domain.

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

X79515; CAA56047.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U12679; AAA20585.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

S52037; S52037.

NP_001105366.1; -.

3D structure databases

HSSP

P12653; 1AXD. [HSSP ENTRY / PDB]

ModBase

P46420.

Organism-specific databases

Gramene

P46420; -.

MaizeGDB

113242; -.

Ontologies

GO:0004364;	Molecular function: glutathione transferase activity (inferred from electronic annotation from EC).
QuickGo view.

Family and domain databases

InterPro

IPR010987; Glutathione-S-Trfase_C-like.
IPR004046; GST_C.
IPR004045; GST_N.
IPR012335; Thioredoxin_fold.
Graphical view of domain structure.

Gene3D

G3DSA:1.20.1050.10; GST_C_like; 1.
G3DSA:3.40.30.10; Thioredoxin_fold; 1.

Pfam

PF00043; GST_C; 1.
PF02798; GST_N; 1.
Pfam graphical view of domain structure.

PROSITE

PS50405; GST_CTER; 1.
PS50404; GST_NTER; 1.
PROSITE graphical view of domain structure (profiles).

ProtoNet

P46420.

Genome annotation databases

GeneID

542311; -.

Other

UniRef

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

Keywords

Direct protein sequencing; Transferase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 223`	`222`	`Glutathione S-transferase 4.`	`PRO_0000185843`
`DOMAIN`	`4 85`	`82`	`GST N-terminal.`
`DOMAIN`	`90 223`	`134`	`GST C-terminal.`
`MOD_RES`	`2 2`		`Blocked amino end (Ala).`

Sequence information

Length: 223 AA [This is the length of the unprocessed precursor]

Molecular weight: 24570 Da [This is the MW of the unprocessed precursor]

CRC64: 24235245AFB4A403 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MATPAVKVYG WAISPFVSRA LLALEEAGVD YELVPMSRQD GDHRRPEHLA RNPFGKVPVL 

        70         80         90        100        110        120 
EDGDLTLFES RAIARHVLRK HKPELLGGGR LEQTAMVDVW LEVEAHQLSP PAIAIVVECV 

       130        140        150        160        170        180 
FAPFLGRERN QAVVDENVEK LKKVLEVYEA RLATCTYLAG DFLSLADLSP FTIMHCLMAT 

       190        200        210        220 
EYAALVHALP HVSAWWQGLA ARPAANKVAQ FMPVGAGAPK EQE

P46420 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