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Q8DW15

- GSHAB_STRMU

UniProt

Q8DW15 - GSHAB_STRMU

Protein

Glutathione biosynthesis bifunctional protein GshAB

Gene

gshAB

Organism
Streptococcus mutans serotype c (strain ATCC 700610 / UA159)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 84 (01 Oct 2014)
      Sequence version 1 (01 Mar 2003)
      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 bindingi696 – 6961Magnesium or manganese 1UniRule annotation
    Metal bindingi717 – 7171Magnesium or manganese 1UniRule annotation
    Metal bindingi717 – 7171Magnesium or manganese 2UniRule annotation
    Metal bindingi719 – 7191Magnesium or manganese 2UniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi516 – 57459ATPUniRule 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

    BioCyciSMUT210007:GC7Z-281-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:SMU_267c
    OrganismiStreptococcus mutans serotype c (strain ATCC 700610 / UA159)
    Taxonomic identifieri210007 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus
    ProteomesiUP000002512: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 754754Glutathione biosynthesis bifunctional protein GshABPRO_0000192560Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.UniRule annotation

    Protein-protein interaction databases

    STRINGi210007.SMU.267c.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8DW15.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini489 – 752264ATP-graspUniRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 333333Glutamate--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.
    KOiK01919.
    OMAiHVEYVKN.
    OrthoDBiEOG6BKJ7H.
    PhylomeDBiQ8DW15.

    Family and domain databases

    Gene3Di3.30.1490.20. 1 hit.
    HAMAPiMF_00782. Glut_biosynth.
    InterProiIPR011761. ATP-grasp.
    IPR013815. ATP_grasp_subdomain_1.
    IPR007370. Glu_cys_ligase.
    IPR006335. Glut_biosynth.
    [Graphical view]
    PfamiPF04262. 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.

    Q8DW15-1 [UniParc]FASTAAdd to Basket

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    MHINQLLQHA NSDLPLLQAN FGLERESLRI NKTNHRLAQT PHPTALGSRQ    50
    FHPYIQTDYS ESQMELITPV AHSSKEVLRF LGAITDVAER SIDQNQYLWP 100
    LSMPPQITED EIEIAQLEDD FEFSYRQYLD KKYGKILQSI SGIHYNMELG 150
    ADLMNELFEL SGYQSFIDFK NDLYLKVAQN FLNYRWFLTY LYGASPLAEK 200
    GFLNEELSQT VRSIRNSHLG YVNTDDIKVP FDSLENYISS IEHYVKSGAL 250
    SAEKEFYSAV RLRGSKHNRD YLTKGITYLE FRCFDLNPFN NRGITQETID 300
    SVHLFILAML WLDTPKKLNQ ALDKAQKLND KIALSHPLEK LPKENSASLI 350
    IEAMEALIKH FKLPSYYDDL LIAIKKQVEN PKLTLSGRLF EHIKHASLEH 400
    FGQKKGQDYH NYAWQNYYAL KGYENMELST QMLLFDTIQK GIHFEILDEN 450
    DQFLKLWHND HIEYVKNGNM TSKDNYVIPL AMANKVVTKK ILRENGYPVP 500
    AGAEFDNKDE ALRYYSQIKN KPIVVKPKTT NFGLGISIFE TAASHNDYEK 550
    ALDIAFIEDY SVLVEEFIPG TEYRFFILDG KCEAVLLRVA ANVVGDGHST 600
    VRQLVAQKNR DPLRGREHRS PLEIIDLGDI ELLMLQQEGY TLEDILPKGK 650
    KVNLRGNSNI STGGDSIDVT ETMDPSYKQL AANMATAMGA WVCGVDLIIP 700
    DTNLKASKGK PNCTCIELNF NPSMYMHTYC YQGPGQVITG KILAKLFPEI 750
    STKI 754
    Length:754
    Mass (Da):86,187
    Last modified:March 1, 2003 - v1
    Checksum:i103479A8536A10CB
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE014133 Genomic DNA. Translation: AAN58035.1.
    RefSeqiNP_720729.1. NC_004350.2.

    Genome annotation databases

    EnsemblBacteriaiAAN58035; AAN58035; SMU_267c.
    GeneIDi1027852.
    KEGGismu:SMU_267c.
    PATRICi19662795. VBIStrMut61772_0233.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE014133 Genomic DNA. Translation: AAN58035.1 .
    RefSeqi NP_720729.1. NC_004350.2.

    3D structure databases

    ProteinModelPortali Q8DW15.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 210007.SMU.267c.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAN58035 ; AAN58035 ; SMU_267c .
    GeneIDi 1027852.
    KEGGi smu:SMU_267c.
    PATRICi 19662795. VBIStrMut61772_0233.

    Phylogenomic databases

    eggNOGi COG1181.
    KOi K01919.
    OMAi HVEYVKN.
    OrthoDBi EOG6BKJ7H.
    PhylomeDBi Q8DW15.

    Enzyme and pathway databases

    UniPathwayi UPA00142 ; UER00209 .
    UPA00142 ; UER00210 .
    BioCyci SMUT210007:GC7Z-281-MONOMER.

    Family and domain databases

    Gene3Di 3.30.1490.20. 1 hit.
    HAMAPi MF_00782. Glut_biosynth.
    InterProi IPR011761. ATP-grasp.
    IPR013815. ATP_grasp_subdomain_1.
    IPR007370. Glu_cys_ligase.
    IPR006335. Glut_biosynth.
    [Graphical view ]
    Pfami 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 700610 / UA159.

    Entry informationi

    Entry nameiGSHAB_STRMU
    AccessioniPrimary (citable) accession number: Q8DW15
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 24, 2004
    Last sequence update: March 1, 2003
    Last modified: October 1, 2014
    This is version 84 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, 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