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P04907

- GSTF3_MAIZE

UniProt

P04907 - GSTF3_MAIZE

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Protein

Glutathione S-transferase 3

Gene

GST3

Organism
Zea mays (Maize)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Involved in the detoxification of certain herbicides.

Catalytic activityi

RX + glutathione = HX + R-S-glutathione.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei12 – 121GlutathioneBy similarity

GO - Molecular functioni

  1. glutathione transferase activity Source: UniProtKB-EC

GO - Biological processi

  1. response to toxic substance Source: EnsemblPlants/Gramene
  2. toxin catabolic process Source: EnsemblPlants/Gramene
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Enzyme and pathway databases

BioCyciRETL1328306-WGS:GSTH-1279-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione S-transferase 3 (EC:2.5.1.18)
Alternative name(s):
GST class-phi member 3
GST-III
Gene namesi
Name:GST3
OrganismiZea mays (Maize)
Taxonomic identifieri4577 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaePACMAD cladePanicoideaeAndropogoneaeZea

Organism-specific databases

GrameneiP04907.
MaizeGDBi65344.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: EnsemblPlants/Gramene
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed
Chaini2 – 222221Glutathione S-transferase 3PRO_0000185842Add
BLAST

Proteomic databases

PRIDEiP04907.

Interactioni

Subunit structurei

Homodimer.

Structurei

3D structure databases

ProteinModelPortaliP04907.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 8382GST N-terminalAdd
BLAST
Domaini89 – 219131GST C-terminalAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni41 – 422Glutathione bindingBy similarity
Regioni54 – 552Glutathione bindingBy similarity
Regioni67 – 682Glutathione bindingBy similarity

Sequence similaritiesi

Belongs to the GST superfamily. Phi family.Curated
Contains 1 GST C-terminal domain.Curated
Contains 1 GST N-terminal domain.Curated

Phylogenomic databases

HOGENOMiHOG000125746.
KOiK00799.

Family and domain databases

Gene3Di1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProiIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR004046. GST_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
SUPFAMiSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEiPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P04907-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAPLKLYGMP LSPNVVRVAT VLNEKGLDFE IVPVDLTTGA HKQPDFLALN
60 70 80 90 100
PFGQIPALVD GDEVLFESRA INRYIASKYA SEGTDLLPAT ASAAKLEVWL
110 120 130 140 150
EVESHHFHPN ASPLVFQLLV RPLLGGAPDA AVVEKHAEQL AKVLDVYEAH
160 170 180 190 200
LARNKYLAGD EFTLADANHA LLPALTSARP PRPGCVAARP HVKAWWEAIA
210 220
ARPAFQKTVA AIPLPPPPSS SA
Length:222
Mass (Da):23,849
Last modified:January 23, 2007 - v4
Checksum:i4CB77A3B1B6E3C46
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti108 – 1081H → Y(PubMed:3532034)Curated
Sequence conflicti111 – 12717ASPLV…LLGGA → RVAAGVPAAREAAPGRR in CAA27957. (PubMed:3532034)CuratedAdd
BLAST
Sequence conflicti111 – 12717ASPLV…LLGGA → RVAAGVPAAREAAPGRR in CAA28053. (PubMed:3532034)CuratedAdd
BLAST
Sequence conflicti134 – 1341E → D in CAA27957. (PubMed:3532034)Curated
Sequence conflicti134 – 1341E → D in CAA28053. (PubMed:3532034)Curated
Sequence conflicti149 – 18032AHLAR…TSARP → RTSPATSTSPGTSSRSPTPT TRSYLLYLSKT in CAA27957. (PubMed:3532034)CuratedAdd
BLAST
Sequence conflicti184 – 1896GCVAAR → ARRRP in CAA27957. (PubMed:3532034)Curated
Sequence conflicti200 – 2001A → V in CAA27957. (PubMed:3532034)Curated
Sequence conflicti200 – 2001A → V in CAA28053. (PubMed:3532034)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X06755 mRNA. Translation: CAA29929.1.
X04375 mRNA. Translation: CAA27957.1.
X04455 mRNA. Translation: CAA28053.1.
PIRiA24703. XUZM31.
S00717. XUZM32.
RefSeqiNP_001106075.1. NM_001112605.1.
UniGeneiZm.103382.

Genome annotation databases

GeneIDi100127012.
KEGGizma:100127012.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X06755 mRNA. Translation: CAA29929.1 .
X04375 mRNA. Translation: CAA27957.1 .
X04455 mRNA. Translation: CAA28053.1 .
PIRi A24703. XUZM31.
S00717. XUZM32.
RefSeqi NP_001106075.1. NM_001112605.1.
UniGenei Zm.103382.

3D structure databases

ProteinModelPortali P04907.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi P04907.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 100127012.
KEGGi zma:100127012.

Organism-specific databases

Gramenei P04907.
MaizeGDBi 65344.

Phylogenomic databases

HOGENOMi HOG000125746.
KOi K00799.

Enzyme and pathway databases

BioCyci RETL1328306-WGS:GSTH-1279-MONOMER.

Family and domain databases

Gene3Di 1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProi IPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR004046. GST_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view ]
Pfami PF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view ]
SUPFAMi SSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEi PS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Characterization and heterospecific expression of cDNA clones of genes in the maize GSH S-transferase multigene family."
    Grove G., Zarlengo R.P., Timmerman K.P., Li N.-Q., Tam M.F., Tu C.-P.D.
    Nucleic Acids Res. 16:425-438(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Cloning and expression of a cDNA encoding a maize glutathione-S-transferase in E. coli."
    Moore R.E., Davies M.S., O'Connell K.M., Harding E.I., Wiegand R.C., Tiemeier D.C.
    Nucleic Acids Res. 14:7227-7235(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "The maize two dimensional gel protein database: towards an integrated genome analysis program."
    Touzet P., Riccardi F., Morin C., Damerval C., Huet J.-C., Pernollet J.-C., Zivy M., de Vienne D.
    Theor. Appl. Genet. 93:997-1005(1996)
    [AGRICOLA] [Europe PMC]
    Cited for: PROTEIN SEQUENCE OF 143-153.
    Tissue: Coleoptile.

Entry informationi

Entry nameiGSTF3_MAIZE
AccessioniPrimary (citable) accession number: P04907
Secondary accession number(s): P15542
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 94 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3