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A0AMA3

- GSHAB_LISW6

UniProt

A0AMA3 - GSHAB_LISW6

Protein

Glutathione biosynthesis bifunctional protein GshAB

Gene

gshAB

Organism
Listeria welshimeri serovar 6b (strain ATCC 35897 / DSM 20650 / SLCC5334)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 60 (01 Oct 2014)
      Sequence version 1 (28 Nov 2006)
      Previous versions | rss
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    Functioni

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

    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 bindingi728 – 7281Magnesium or manganese 1UniRule annotation
    Metal bindingi745 – 7451Magnesium or manganese 1UniRule annotation
    Metal bindingi745 – 7451Magnesium or manganese 2UniRule annotation
    Metal bindingi747 – 7471Magnesium or manganese 2UniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi548 – 60659ATPUniRule 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

    BioCyciLWEL386043:GI5X-2800-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:lwe2717
    OrganismiListeria welshimeri serovar 6b (strain ATCC 35897 / DSM 20650 / SLCC5334)
    Taxonomic identifieri386043 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesListeriaceaeListeria
    ProteomesiUP000000779: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 776776Glutathione biosynthesis bifunctional protein GshABPRO_1000133720Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.UniRule annotation

    Protein-protein interaction databases

    STRINGi386043.lwe2717.

    Structurei

    3D structure databases

    ProteinModelPortaliA0AMA3.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini521 – 775255ATP-graspUniRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 354354Glutamate--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.
    OMAiHVEYVKN.
    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.

    A0AMA3-1 [UniParc]FASTAAdd to Basket

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    MIKLDMTILD SLKENKALRK LLFSGHFGLE KENIRVTSDG KLALTPHPAI    50
    FGPKEDNPYI KTDFSESQIE MITPVTDSID DVYNWLENLH NIVSLRSKNE 100
    LLWPSSNPPI LPAEKDIPIA EYKTPDSPDR KYREHLAQGY GKKIQLLSGI 150
    HYNFSFPEAL IDGLYDEISL PNESKRDFKN RLYLKVAKYF MKNRWLLIYL 200
    TGASPVYLAD FTKTKQEEKL RDGSSALHDG ISLRNSNAGY KNKESLYVDY 250
    NSFDAYISSI SNYIEAGKIE SMREFYNPIR LKNAHTDQTV ESLAKHGVEY 300
    LEIRSIDLNP LEPNGISKEA LHFIHLFLIK GLLSEDRELC ENNQQLADEN 350
    ENNIALNGLS KPAIKNCDNE EMALADAGLL ELDKMNDFIQ SLRPEDTYFQ 400
    AIIEKQKERL LHPEKTIAAQ VKEQSATAGF IEFHLNQAKT YMEETEALAY 450
    KLIGAEDMEL STQIIWKDAI ARGIKVDVLD RAENFLRFQK GDHVEYVKQA 500
    SKTSKDNYVS VLMMENKVVT KLVLAENNIR VPFGDSFSDQ ALALEAFSLF 550
    KDKQIVVKPK STNYGWGISI FKNKFTTEDY QEALNIAFSY DSSVIIEEFI 600
    PGDEFRFLVI NDKVEAVLKR VPANVTGDGI HTVRELVEEK NMDPLRGTDH 650
    LKPLEKIRTG PEETLMLSMQ KLSWDSIPKA NETIYLRENS NVSTGGDSID 700
    YTAEMDDYFK EIAIRATQVL DAKICGVDII VPRETIDRDK HAIIELNFNP 750
    AMHMHCFPYQ GEQKKIGDKI LDFLFE 776
    Length:776
    Mass (Da):88,615
    Last modified:November 28, 2006 - v1
    Checksum:i9DDA45402F88588D
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM263198 Genomic DNA. Translation: CAK22135.1.
    RefSeqiYP_850914.1. NC_008555.1.

    Genome annotation databases

    EnsemblBacteriaiCAK22135; CAK22135; lwe2717.
    GeneIDi4466025.
    KEGGilwe:lwe2717.
    PATRICi20332701. VBILisWel39304_2724.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM263198 Genomic DNA. Translation: CAK22135.1 .
    RefSeqi YP_850914.1. NC_008555.1.

    3D structure databases

    ProteinModelPortali A0AMA3.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 386043.lwe2717.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAK22135 ; CAK22135 ; lwe2717 .
    GeneIDi 4466025.
    KEGGi lwe:lwe2717.
    PATRICi 20332701. VBILisWel39304_2724.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00142 ; UER00209 .
    UPA00142 ; UER00210 .
    BioCyci LWEL386043:GI5X-2800-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. "Whole-genome sequence of Listeria welshimeri reveals common steps in genome reduction with Listeria innocua as compared to Listeria monocytogenes."
      Hain T., Steinweg C., Kuenne C.T., Billion A., Ghai R., Chatterjee S.S., Domann E., Kaerst U., Goesmann A., Bekel T., Bartels D., Kaiser O., Meyer F., Puehler A., Weisshaar B., Wehland J., Liang C., Dandekar T.
      , Lampidis R., Kreft J., Goebel W., Chakraborty T.
      J. Bacteriol. 188:7405-7415(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 35897 / DSM 20650 / SLCC5334.

    Entry informationi

    Entry nameiGSHAB_LISW6
    AccessioniPrimary (citable) accession number: A0AMA3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 14, 2009
    Last sequence update: November 28, 2006
    Last modified: October 1, 2014
    This is version 60 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

    Complete proteome, Multifunctional enzyme

    Documents

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

    External Data

    Dasty 3