Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P22416

- GST_SERMA

UniProt

P22416 - GST_SERMA

(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)

Protein

Glutathione S-transferase GST-7.3

Gene
N/A
Organism
Serratia marcescens
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

GO - Molecular functioni

  1. glutathione transferase activity Source: UniProtKB-EC
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione S-transferase GST-7.3 (EC:2.5.1.18)
OrganismiSerratia marcescens
Taxonomic identifieri615 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSerratia

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – ›31›31Glutathione S-transferase GST-7.3PRO_0000185975Add
BLAST

Interactioni

Subunit structurei

Homodimer.

Family & Domainsi

Sequence similaritiesi

Belongs to the GST superfamily. Beta family.Curated

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR012336. Thioredoxin-like_fold.
[Graphical view]

Sequencei

Sequence statusi: Fragment.

P22416-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30
MKLFYKAGAC SLSPHIVLRE LGLDFTAXKV D
Length:31
Mass (Da):3,435
Last modified:August 1, 1991 - v1
Checksum:iAD993D56CD9AB0D5
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei31 – 311

Sequence databases

PIRiS14727.

Cross-referencesi

Sequence databases

PIRi S14727.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 3.40.30.10. 1 hit.
InterProi IPR012336. Thioredoxin-like_fold.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Purification and characterization of a novel glutathione transferase from Serratia marcescens."
    di Ilio C., Aceto A., Piccolomini R., Allocati N., Faraone A., Bucciarelli T., Barra D., Feferici G.
    Biochim. Biophys. Acta 1077:141-146(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE.
    Strain: CIP 6755.

Entry informationi

Entry nameiGST_SERMA
AccessioniPrimary (citable) accession number: P22416
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: August 1, 1991
Last modified: October 29, 2014
This is version 52 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3