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P12653

- GSTF1_MAIZE

UniProt

P12653 - GSTF1_MAIZE

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Protein

Glutathione S-transferase 1

Gene

GST1

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
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Enzyme and pathway databases

SABIO-RKP12653.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione S-transferase 1 (EC:2.5.1.18)
Alternative name(s):
GST class-phi member 1
GST-29
GST-I
Gene namesi
Name:GST1
OrganismiZea mays (Maize)
Taxonomic identifieri4577 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaePACMAD cladePanicoideaeAndropogoneaeZea

Organism-specific databases

GrameneiP12653.
MaizeGDBi65344.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 214213Glutathione S-transferase 1PRO_0000185841Add
BLAST

Proteomic databases

PRIDEiP12653.

Expressioni

Tissue specificityi

Expressed in the stem and leaves, lower levels are seen in the pollen and endosperm.

Interactioni

Subunit structurei

Homodimer or heterodimer of GST-I and GST-IV (=GST-II).2 Publications

Structurei

Secondary structure

1
214
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 85
Beta strandi10 – 145
Helixi15 – 2511
Beta strandi29 – 324
Turni36 – 394
Helixi40 – 423
Helixi44 – 474
Beta strandi57 – 604
Beta strandi63 – 675
Helixi68 – 7912
Helixi81 – 844
Turni85 – 873
Helixi89 – 10416
Helixi106 – 11712
Helixi119 – 1224
Helixi129 – 15224
Beta strandi154 – 1607
Helixi163 – 1664
Helixi169 – 1757
Helixi179 – 1868
Helixi188 – 19912
Helixi201 – 2099

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AXDX-ray2.50A/B2-210[»]
1BYEX-ray2.80A/B/C/D2-214[»]
ProteinModelPortaliP12653.
SMRiP12653. Positions 2-214.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP12653.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 8382GST N-terminalAdd
BLAST
Domaini88 – 214127GST C-terminalAdd
BLAST

Region

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

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.

P12653-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAPMKLYGAV MSWNLTRCAT ALEEAGSDYE IVPINFATAE HKSPEHLVRN
60 70 80 90 100
PFGQVPALQD GDLYLFESRA ICKYAARKNK PELLREGNLE EAAMVDVWIE
110 120 130 140 150
VEANQYTAAL NPILFQVLIS PMLGGTTDQK VVDENLEKLK KVLEVYEARL
160 170 180 190 200
TKCKYLAGDF LSLADLNHVS VTLCLFATPY ASVLDAYPHV KAWWSGLMER
210
PSVQKVAALM KPSA
Length:214
Mass (Da):23,822
Last modified:January 23, 2007 - v4
Checksum:i97DA6337ADF03CB1
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti15 – 151L → V in AAA33470. 1 PublicationCurated
Sequence conflicti15 – 151L → V in AAA33469. 1 PublicationCurated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X06754 mRNA. Translation: CAA29928.1.
M16901 mRNA. Translation: AAA33470.1.
M16902, M16900 Genomic DNA. Translation: AAA33469.1.
PIRiS03726. XUZM1.
RefSeqiNP_001105412.1. NM_001111942.1.
UniGeneiZm.9.

Genome annotation databases

GeneIDi542366.
KEGGizma:542366.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X06754 mRNA. Translation: CAA29928.1 .
M16901 mRNA. Translation: AAA33470.1 .
M16902 , M16900 Genomic DNA. Translation: AAA33469.1 .
PIRi S03726. XUZM1.
RefSeqi NP_001105412.1. NM_001111942.1.
UniGenei Zm.9.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1AXD X-ray 2.50 A/B 2-210 [» ]
1BYE X-ray 2.80 A/B/C/D 2-214 [» ]
ProteinModelPortali P12653.
SMRi P12653. Positions 2-214.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi P12653.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 542366.
KEGGi zma:542366.

Organism-specific databases

Gramenei P12653.
MaizeGDBi 65344.

Phylogenomic databases

HOGENOMi HOG000125746.
KOi K00799.

Enzyme and pathway databases

SABIO-RK P12653.

Miscellaneous databases

EvolutionaryTracei P12653.

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. "Structural analysis of a maize gene coding for glutathione-S-transferase involved in herbicide detoxification."
    Shah D.M., Hironaka C.M., Wiegand R.C., Harding E.I., Krivi G.G., Tiemeier D.C.
    Plant Mol. Biol. 6:203-211(1986)
    [AGRICOLA] [Europe PMC]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Messenger RNA encoding a glutathione-S-transferase responsible for herbicide tolerance in maize is induced in response to safener treatment."
    Wiegand R.C., Shah D.M., Mozer T.J., Harding E.I., Diaz-Collier J., Saunders C., Jaworski E.G., Tiemeier D.C.
    Plant Mol. Biol. 7:235-243(1986)
    [AGRICOLA] [Europe PMC]
    Cited for: PROTEIN SEQUENCE OF 2-16.
  4. "Crystal structure of herbicide-detoxifying maize glutathione S-transferase-I in complex with lactoylglutathione: evidence for an induced-fit mechanism."
    Neuefeind T., Huber R., Dasenbrock H., Prade L., Bieseler B.
    J. Mol. Biol. 274:446-453(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH LACTOYLGLUTATHIONE, SUBUNIT.
  5. "Structures of herbicides in complex with their detoxifying enzyme glutathione S-transferase -- explanations for the selectivity of the enzyme in plants."
    Prade L., Huber R., Bieseler B.
    Structure 6:1445-1452(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH ATRAZINE-GLUTATHIONE CONJUGATE.

Entry informationi

Entry nameiGSTF1_MAIZE
AccessioniPrimary (citable) accession number: P12653
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: January 23, 2007
Last modified: October 1, 2014
This is version 101 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

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3