Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P15214

- GST_PROMI

UniProt

P15214 - GST_PROMI

Protein

Glutathione S-transferase GST-6.0

Gene

gstB

Organism
Proteus mirabilis
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 84 (01 Oct 2014)
      Sequence version 2 (01 Apr 1993)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei10 – 101Glutathione1 Publication
    Binding sitei35 – 351Glutathione1 Publication

    GO - Molecular functioni

    1. glutathione transferase activity Source: UniProtKB-EC

    Keywords - Molecular functioni

    Transferase

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutathione S-transferase GST-6.0 (EC:2.5.1.18)
    Alternative name(s):
    GST B1-1
    Gene namesi
    Name:gstB
    OrganismiProteus mirabilis
    Taxonomic identifieri584 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeProteus

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 203203Glutathione S-transferase GST-6.0PRO_0000185974Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Structurei

    Secondary structure

    1
    203
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi2 – 54
    Helixi12 – 209
    Beta strandi26 – 316
    Turni32 – 354
    Helixi43 – 453
    Beta strandi54 – 563
    Beta strandi62 – 654
    Helixi66 – 749
    Helixi78 – 803
    Helixi89 – 10315
    Helixi106 – 1094
    Helixi110 – 1134
    Beta strandi115 – 1173
    Turni119 – 1213
    Helixi122 – 14019
    Beta strandi143 – 1453
    Beta strandi148 – 1503
    Helixi153 – 16210
    Helixi166 – 1683
    Helixi176 – 18611
    Helixi189 – 1979

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1PMTX-ray2.50A1-203[»]
    2PMTX-ray2.70A/B/C/D1-203[»]
    ProteinModelPortaliP15214.
    SMRiP15214. Positions 1-201.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP15214.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 8181GST N-terminalAdd
    BLAST
    Domaini87 – 203117GST C-terminalAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni51 – 522Glutathione binding
    Regioni65 – 662Glutathione binding
    Regioni106 – 1072Glutathione binding

    Sequence similaritiesi

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

    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.

    P15214-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKLYYTPGSC SLSPHIVLRE TGLDFSIERI DLRTKKTESG KDFLAINPKG    50
    QVPVLQLDNG DILTEGVAIV QYLADLKPDR NLIAPPKALE RYHQIEWLNF 100
    LASEVHKGYS PLFSSDTPES YLPVVKNKLK SKFVYINDVL SKQKCVCGDH 150
    FTVADAYLFT LSQWAPHVAL DLTDLSHLQD YLARIAQRPN VHSALVTEGL 200
    IKE 203
    Length:203
    Mass (Da):22,852
    Last modified:April 1, 1993 - v2
    Checksum:i2021F194D5CF105E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti20 – 201E → Q AA sequence (PubMed:2661269)Curated
    Sequence conflicti34 – 363TKK → RLL AA sequence (PubMed:2661269)Curated
    Sequence conflicti38 – 381Missing AA sequence (PubMed:8645008)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U38482 Genomic DNA. Translation: AAC44362.1.
    PIRiS71882.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U38482 Genomic DNA. Translation: AAC44362.1 .
    PIRi S71882.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1PMT X-ray 2.50 A 1-203 [» ]
    2PMT X-ray 2.70 A/B/C/D 1-203 [» ]
    ProteinModelPortali P15214.
    SMRi P15214. Positions 1-201.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P15214.

    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. "Molecular cloning and overexpression of a glutathione transferase gene from Proteus mirabilis."
      Perito B., Allocati N., Casalone E., Masulli M., Dragani B., Polsinelli M., Aceto A., Di Ilio C.
      Biochem. J. 318:157-162(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: AF 2924.
    2. "The amino acid sequence of glutathione transferase from Proteus mirabilis, a prototype of a new class of enzymes."
      Mignogna G., Allocati N., Aceto A., Piccolomini R., Di Ilio C., Barra D., Martini F.
      Eur. J. Biochem. 211:421-425(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE.
      Strain: AF 2924.
    3. "N-terminal region of Proteus mirabilis glutathione transferase is not homologous to mammalian and plant glutathione transferases."
      Di Ilio C., Aceto A., Piccolomini R., Allocati N., Caccuri A.M., Barra D., Feferici G.
      FEBS Lett. 250:57-59(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-38.
      Strain: AF 2924.
    4. "Purification and characterization of a heterodimeric 23/20-kDa proteolytic fragment of bacterial glutathione transferase B1-1."
      Aceto A., Dragani B., Allocati N., Masulli M., Petruzzelli R., Di Ilio C.
      Arch. Biochem. Biophys. 328:302-308(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-5 AND 36-42.
    5. "A mixed disulfide bond in bacterial glutathione transferase: functional and evolutionary implications."
      Rossjohn J., Polekhina G., Feil S.C., Allocati N., Masulli M., Di Ilio C., Parker M.W.
      Structure 6:721-734(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE.

    Entry informationi

    Entry nameiGST_PROMI
    AccessioniPrimary (citable) accession number: P15214
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: April 1, 1993
    Last modified: October 1, 2014
    This is version 84 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic 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