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Protein

Glutathione amide reductase

Gene

garB

Organism
Marichromatium gracile (Chromatium gracile)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the reduction of glutathione amide disulfide (GASSAG) to restore glutathione amide (GASH) in the presence of NADH. May play a role in GASH metabolism under anaerobic conditions as a sulfide carrier necessary for cytoplasmic sulfide oxidation.1 Publication

Catalytic activityi

2 glutathione amide + NAD+ = glutathione amide disulfide + NADH.1 Publication

Cofactori

FAD2 PublicationsNote: Binds 1 FAD per subunit.2 Publications

Kineticsi

  1. KM=97 µM for glutathione amide disulfide (GASSAG) for the reverse reaction (in the presence of 100 µM NADH)1 Publication
  2. KM=6.9 mM for glutathione disulfide (GSH) for the reverse reaction1 Publication
  3. KM=13.2 µM for NADH for the reverse reaction (in the presence of 500 µM GASSAG)1 Publication
  4. KM=1.98 mM for NADPH for the reverse reaction1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi2 – 21Nickel1 Publication
    Metal bindingi3 – 31Nickel1 Publication
    Metal bindingi4 – 41Nickel; via pros nitrogen1 Publication
    Binding sitei34 – 341FAD1 Publication
    Binding sitei41 – 411FAD1 Publication
    Binding sitei50 – 501FAD1 Publication
    Binding sitei50 – 501NAD1 Publication
    Binding sitei230 – 2301NAD; via amide nitrogen1 Publication
    Binding sitei261 – 2611NAD; via amide nitrogen1 Publication
    Binding sitei302 – 3021FAD1 Publication
    Binding sitei308 – 3081NAD; via carbonyl oxygen1 Publication
    Binding sitei341 – 3411NAD; via carbonyl oxygen1 Publication
    Active sitei437 – 4371Proton acceptor1 Publication
    Binding sitei437 – 4371FAD; via carbonyl oxygen1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi14 – 152FAD1 Publication
    Nucleotide bindingi113 – 1142FAD1 Publication
    Nucleotide bindingi174 – 1807NAD1 Publication
    Nucleotide bindingi197 – 1982NAD1 Publication
    Nucleotide bindingi308 – 3103FAD1 Publication

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    FAD, Flavoprotein, Metal-binding, NAD, Nickel, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutathione amide reductase1 Publication (EC:1.8.1.161 Publication)
    Short name:
    GAR1 Publication
    Gene namesi
    Name:garB1 Publication
    OrganismiMarichromatium gracile (Chromatium gracile)
    Taxonomic identifieri1048 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaChromatialesChromatiaceaeMarichromatium

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methionineiRemoved1 Publication
    Chaini2 – 463462Glutathione amide reductase1 PublicationPRO_0000417371Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi42 ↔ 47Redox-active1 Publication

    Keywords - PTMi

    Disulfide bond

    Interactioni

    Subunit structurei

    Homodimer.2 Publications

    Structurei

    Secondary structure

    1
    463
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 106Combined sources
    Helixi14 – 2512Combined sources
    Beta strandi30 – 367Combined sources
    Helixi40 – 456Combined sources
    Helixi47 – 6519Combined sources
    Helixi66 – 694Combined sources
    Helixi80 – 10425Combined sources
    Beta strandi108 – 1125Combined sources
    Beta strandi114 – 1185Combined sources
    Beta strandi121 – 1244Combined sources
    Beta strandi127 – 13610Combined sources
    Beta strandi140 – 1423Combined sources
    Helixi150 – 1523Combined sources
    Helixi156 – 1616Combined sources
    Beta strandi167 – 1726Combined sources
    Helixi176 – 18712Combined sources
    Beta strandi191 – 1955Combined sources
    Beta strandi197 – 2026Combined sources
    Helixi207 – 21913Combined sources
    Beta strandi223 – 2275Combined sources
    Beta strandi230 – 2367Combined sources
    Beta strandi239 – 2446Combined sources
    Beta strandi249 – 25810Combined sources
    Beta strandi262 – 2654Combined sources
    Helixi271 – 2744Combined sources
    Beta strandi297 – 2993Combined sources
    Helixi301 – 3044Combined sources
    Helixi310 – 32516Combined sources
    Beta strandi340 – 3423Combined sources
    Beta strandi348 – 3525Combined sources
    Helixi355 – 3628Combined sources
    Beta strandi366 – 3738Combined sources
    Helixi376 – 3783Combined sources
    Beta strandi381 – 3833Combined sources
    Beta strandi387 – 3948Combined sources
    Turni395 – 3984Combined sources
    Beta strandi399 – 4079Combined sources
    Helixi410 – 4123Combined sources
    Helixi415 – 4228Combined sources
    Helixi427 – 4315Combined sources
    Beta strandi437 – 4404Combined sources
    Helixi441 – 4455Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2R9ZX-ray2.10A/B1-463[»]
    2RABX-ray2.50A/B1-463[»]
    ProteinModelPortaliD0VWY5.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiD0VWY5.

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Redox-active center

    Family and domain databases

    Gene3Di3.30.390.30. 1 hit.
    3.50.50.60. 2 hits.
    InterProiIPR023753. FAD/NAD-binding_dom.
    IPR016156. FAD/NAD-linked_Rdtase_dimer.
    IPR006322. Glutathione_Rdtase_euk/bac.
    IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
    IPR012999. Pyr_OxRdtase_I_AS.
    [Graphical view]
    PfamiPF07992. Pyr_redox_2. 1 hit.
    PF02852. Pyr_redox_dim. 1 hit.
    [Graphical view]
    SUPFAMiSSF51905. SSF51905. 1 hit.
    SSF55424. SSF55424. 1 hit.
    TIGRFAMsiTIGR01421. gluta_reduc_1. 1 hit.
    PROSITEiPS00076. PYRIDINE_REDOX_1. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    D0VWY5-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MTQHFDLIAI GGGSGGLAVA EKAAAFGKRV ALIESKALGG TCVNVGCVPK
    60 70 80 90 100
    KVMWYASHLA EAVRDAPGFG VQASGGTLDW PRLVAGRDRY IGAINSFWDG
    110 120 130 140 150
    YVERLGITRV DGHARFVDAH TIEVEGQRLS ADHIVIATGG RPIVPRLPGA
    160 170 180 190 200
    ELGITSDGFF ALQQQPKRVA IIGAGYIGIE LAGLLRSFGS EVTVVALEDR
    210 220 230 240 250
    LLFQFDPLLS ATLAENMHAQ GIETHLEFAV AALERDAQGT TLVAQDGTRL
    260 270 280 290 300
    EGFDSVIWAV GRAPNTRDLG LEAAGIEVQS NGMVPTDAYQ NTNVPGVYAL
    310 320 330 340 350
    GDITGRDQLT PVAIAAGRRL AERLFDGQSE RKLDYDNIPT VVFAHPPLSK
    360 370 380 390 400
    VGLSEPEARE RLGDVLTVYE TSFTPMRYAL NEHGPKTAMK LVCAGPEQRV
    410 420 430 440 450
    VGVHVIGDGA DEMLQGFAVA VKMGATKADF DNTVAIHPGS AEELVTLKEP
    460
    VRRPGDPLPE GAA
    Length:463
    Mass (Da):49,159
    Last modified:December 15, 2009 - v1
    Checksum:i95EC9202CAD02846
    GO

    Mass spectrometryi

    Molecular mass is 49030 Da from positions 2 - 463. Determined by ESI. 1 Publication

    Cross-referencesi

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2R9ZX-ray2.10A/B1-463[»]
    2RABX-ray2.50A/B1-463[»]
    ProteinModelPortaliD0VWY5.
    ModBaseiSearch...
    MobiDBiSearch...

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Miscellaneous databases

    EvolutionaryTraceiD0VWY5.

    Family and domain databases

    Gene3Di3.30.390.30. 1 hit.
    3.50.50.60. 2 hits.
    InterProiIPR023753. FAD/NAD-binding_dom.
    IPR016156. FAD/NAD-linked_Rdtase_dimer.
    IPR006322. Glutathione_Rdtase_euk/bac.
    IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
    IPR012999. Pyr_OxRdtase_I_AS.
    [Graphical view]
    PfamiPF07992. Pyr_redox_2. 1 hit.
    PF02852. Pyr_redox_dim. 1 hit.
    [Graphical view]
    SUPFAMiSSF51905. SSF51905. 1 hit.
    SSF55424. SSF55424. 1 hit.
    TIGRFAMsiTIGR01421. gluta_reduc_1. 1 hit.
    PROSITEiPS00076. PYRIDINE_REDOX_1. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiGASHR_MARGR
    AccessioniPrimary (citable) accession number: D0VWY5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 16, 2012
    Last sequence update: December 15, 2009
    Last modified: November 11, 2015
    This is version 35 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    The active site is a redox-active disulfide bond.1 Publication

    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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.