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Q8Y3R3

- GSHAB_LISMO

UniProt

Q8Y3R3 - GSHAB_LISMO

Protein

Glutathione biosynthesis bifunctional protein GshAB

Gene

gshAB

Organism
Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 77 (01 Oct 2014)
      Sequence version 2 (05 Jul 2005)
      Previous versions | rss
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    Functioni

    Synthesizes glutathione from L-glutamate and L-cysteine via gamma-L-glutamyl-L-cysteine.

    Catalytic activityi

    ATP + L-glutamate + L-cysteine = ADP + phosphate + gamma-L-glutamyl-L-cysteine.UniRule annotation
    ATP + gamma-L-glutamyl-L-cysteine + glycine = ADP + phosphate + glutathione.UniRule annotation

    Cofactori

    Binds 2 magnesium or manganese ions per subunit.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi721 – 7211Magnesium or manganese 1UniRule annotation
    Metal bindingi738 – 7381Magnesium or manganese 1UniRule annotation
    Metal bindingi738 – 7381Magnesium or manganese 2UniRule annotation
    Metal bindingi740 – 7401Magnesium or manganese 2UniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi541 – 59959ATPUniRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-HAMAP
    2. glutamate-cysteine ligase activity Source: UniProtKB-HAMAP
    3. glutathione synthase activity Source: UniProtKB-HAMAP
    4. magnesium ion binding Source: UniProtKB-HAMAP
    5. manganese ion binding Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Glutathione biosynthesis

    Keywords - Ligandi

    ATP-binding, Magnesium, Manganese, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciLMON169963:LMO2770-MONOMER.
    UniPathwayiUPA00142; UER00209.
    UPA00142; UER00210.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutathione biosynthesis bifunctional protein GshABUniRule annotation
    Alternative name(s):
    Gamma-GCS-GSUniRule annotation
    Short name:
    GCS-GSUniRule annotation
    Including the following 2 domains:
    Glutamate--cysteine ligaseUniRule annotation (EC:6.3.2.2UniRule annotation)
    Alternative name(s):
    Gamma-ECSUniRule annotation
    Short name:
    GCSUniRule annotation
    Gamma-glutamylcysteine synthetaseUniRule annotation
    Glutathione synthetaseUniRule annotation (EC:6.3.2.3UniRule annotation)
    Alternative name(s):
    GSH synthetaseUniRule annotation
    Short name:
    GSUniRule annotation
    Short name:
    GSH-SUniRule annotation
    Short name:
    GSHaseUniRule annotation
    Glutathione synthaseUniRule annotation
    Gene namesi
    Name:gshABUniRule annotation
    Synonyms:gshFUniRule annotation
    Ordered Locus Names:lmo2770
    OrganismiListeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)
    Taxonomic identifieri169963 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesListeriaceaeListeria
    ProteomesiUP000000817: Chromosome

    Organism-specific databases

    GenoListiLMO2770.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 769769Glutathione biosynthesis bifunctional protein GshABPRO_0000192555Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.UniRule annotation

    Protein-protein interaction databases

    STRINGi169963.lmo2770.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8Y3R3.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini514 – 768255ATP-graspUniRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 347347Glutamate--cysteine ligaseAdd
    BLAST

    Sequence similaritiesi

    In the N-terminal section; belongs to the glutamate--cysteine ligase type 1 family. Type 2 subfamily.UniRule annotation
    Contains 1 ATP-grasp domain.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG1181.
    HOGENOMiHOG000156471.
    KOiK01919.
    OrthoDBiEOG6BKJ7H.

    Family and domain databases

    Gene3Di3.30.1490.20. 1 hit.
    3.30.470.20. 3 hits.
    HAMAPiMF_00782. Glut_biosynth.
    InterProiIPR011761. ATP-grasp.
    IPR013815. ATP_grasp_subdomain_1.
    IPR013816. ATP_grasp_subdomain_2.
    IPR007370. Glu_cys_ligase.
    IPR006335. Glut_biosynth.
    IPR020561. PRibGlycinamid_synth_ATP-grasp.
    [Graphical view]
    PfamiPF01071. GARS_A. 1 hit.
    PF04262. Glu_cys_ligase. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR01435. glu_cys_lig_rel. 1 hit.
    PROSITEiPS50975. ATP_GRASP. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q8Y3R3-1 [UniParc]FASTAAdd to Basket

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    MLDSFKEDPN LRKLLFSGHF GLEKENIRVT SDGKLALTPH PAIFGPKEDN    50
    PYIKTDFSES QIEMITPVTD SIDSVYEWLE NLHNIVSLRS ENELLWPSSN 100
    PPILPAEEDI PIAEYKTPDS PDRKYREHLA KGYGKKIQLL SGIHYNFSFP 150
    EALIDGLYAN ISLPEESKQD FKNRLYLKVA KYFMKNRWLL IYLTGASPVY 200
    LADFSKTKHE ESLPDGSSAL RDGISLRNSN AGYKNKEALF VDYNSFDAYI 250
    SSISNYIEAG KIESMREFYN PIRLKNAHTD QTVESLAEHG VEYLEIRSID 300
    LNPLEPNGIS KDELDFIHLF LIKGLLSEDR ELCANNQQLA DENENNIALN 350
    GLAQPSIKNC DNEDIPLADA GLLELDKMSD FIKSLRPEDT KLRAIIEKQK 400
    ERLLHPEKTI AAQVKQQVTK EGYVDFHLNQ AKTYMEETEA LAYKLIGAED 450
    MELSTQIIWK DAIARGIKVD VLDRAENFLR FQKGDHIEYV KQASKTSKDN 500
    YVSVLMMENK VVTKLVLAEH DIRVPFGDSF SDQALALEAF SLFEDKQIVV 550
    KPKSTNYGWG ISIFKNKFTL EDYQEALNIA FSYDSSVIIE EFIPGDEFRF 600
    LVINDKVEAV LKRVPANVTG DGIHTVRELV EEKNTDPLRG TDHLKPLEKI 650
    RTGPEETLML SMQNLSWDSI PKAEEIIYLR ENSNVSTGGD SIDYTEEMDD 700
    YFKEIAIRAT QVLDAKICGV DIIVPRETID RDKHAIIELN FNPAMHMHCF 750
    PYQGEQKKIG DKILDFLFD 769
    Length:769
    Mass (Da):87,728
    Last modified:July 5, 2005 - v2
    Checksum:iB60DA05A3D8B43FD
    GO

    Sequence cautioni

    The sequence CAD00983.1 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL591984 Genomic DNA. Translation: CAD00983.1. Different initiation.
    PIRiAI1420.
    RefSeqiNP_466292.1. NC_003210.1.

    Genome annotation databases

    EnsemblBacteriaiCAD00983; CAD00983; CAD00983.
    GeneIDi986798.
    KEGGilmo:lmo2770.
    PATRICi20314847. VBILisMon69206_2839.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL591984 Genomic DNA. Translation: CAD00983.1 . Different initiation.
    PIRi AI1420.
    RefSeqi NP_466292.1. NC_003210.1.

    3D structure databases

    ProteinModelPortali Q8Y3R3.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 169963.lmo2770.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAD00983 ; CAD00983 ; CAD00983 .
    GeneIDi 986798.
    KEGGi lmo:lmo2770.
    PATRICi 20314847. VBILisMon69206_2839.

    Organism-specific databases

    GenoListi LMO2770.

    Phylogenomic databases

    eggNOGi COG1181.
    HOGENOMi HOG000156471.
    KOi K01919.
    OrthoDBi EOG6BKJ7H.

    Enzyme and pathway databases

    UniPathwayi UPA00142 ; UER00209 .
    UPA00142 ; UER00210 .
    BioCyci LMON169963:LMO2770-MONOMER.

    Family and domain databases

    Gene3Di 3.30.1490.20. 1 hit.
    3.30.470.20. 3 hits.
    HAMAPi MF_00782. Glut_biosynth.
    InterProi IPR011761. ATP-grasp.
    IPR013815. ATP_grasp_subdomain_1.
    IPR013816. ATP_grasp_subdomain_2.
    IPR007370. Glu_cys_ligase.
    IPR006335. Glut_biosynth.
    IPR020561. PRibGlycinamid_synth_ATP-grasp.
    [Graphical view ]
    Pfami PF01071. GARS_A. 1 hit.
    PF04262. Glu_cys_ligase. 1 hit.
    [Graphical view ]
    TIGRFAMsi TIGR01435. glu_cys_lig_rel. 1 hit.
    PROSITEi PS50975. ATP_GRASP. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC BAA-679 / EGD-e.
    2. "A multidomain fusion protein in Listeria monocytogenes catalyzes the two primary activities for glutathione biosynthesis."
      Gopal S., Borovok I., Ofer A., Yanku M., Cohen G., Goebel W., Kreft J., Aharonowitz Y.
      J. Bacteriol. 187:3839-3847(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
      Strain: ATCC BAA-679 / EGD-e.

    Entry informationi

    Entry nameiGSHAB_LISMO
    AccessioniPrimary (citable) accession number: Q8Y3R3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 30, 2002
    Last sequence update: July 5, 2005
    Last modified: October 1, 2014
    This is version 77 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

    Complete proteome, Multifunctional enzyme, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3