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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)DescriptionActionsGraphical viewLength
    Metal bindingi2Nickel1 Publication1
    Metal bindingi3Nickel1 Publication1
    Metal bindingi4Nickel; via pros nitrogen1 Publication1
    Binding sitei34FAD1 Publication1
    Binding sitei41FAD1 Publication1
    Binding sitei50FAD1 Publication1
    Binding sitei50NAD1 Publication1
    Binding sitei230NAD; via amide nitrogen1 Publication1
    Binding sitei261NAD; via amide nitrogen1 Publication1
    Binding sitei302FAD1 Publication1
    Binding sitei308NAD; via carbonyl oxygen1 Publication1
    Binding sitei341NAD; via carbonyl oxygen1 Publication1
    Active sitei437Proton acceptor1 Publication1
    Binding sitei437FAD; via carbonyl oxygen1 Publication1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi14 – 15FAD1 Publication2
    Nucleotide bindingi113 – 114FAD1 Publication2
    Nucleotide bindingi174 – 180NAD1 Publication7
    Nucleotide bindingi197 – 198NAD1 Publication2
    Nucleotide bindingi308 – 310FAD1 Publication3

    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)DescriptionActionsGraphical viewLength
    Initiator methionineiRemoved1 Publication
    ChainiPRO_00004173712 – 463Glutathione amide reductase1 PublicationAdd BLAST462

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Disulfide bondi42 ↔ 47Redox-active1 Publication

    Keywords - PTMi

    Disulfide bond

    Interactioni

    Subunit structurei

    Homodimer.2 Publications

    Structurei

    Secondary structure

    1463
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi5 – 10Combined sources6
    Helixi14 – 25Combined sources12
    Beta strandi30 – 36Combined sources7
    Helixi40 – 45Combined sources6
    Helixi47 – 65Combined sources19
    Helixi66 – 69Combined sources4
    Helixi80 – 104Combined sources25
    Beta strandi108 – 112Combined sources5
    Beta strandi114 – 118Combined sources5
    Beta strandi121 – 124Combined sources4
    Beta strandi127 – 136Combined sources10
    Beta strandi140 – 142Combined sources3
    Helixi150 – 152Combined sources3
    Helixi156 – 161Combined sources6
    Beta strandi167 – 172Combined sources6
    Helixi176 – 187Combined sources12
    Beta strandi191 – 195Combined sources5
    Beta strandi197 – 202Combined sources6
    Helixi207 – 219Combined sources13
    Beta strandi223 – 227Combined sources5
    Beta strandi230 – 236Combined sources7
    Beta strandi239 – 244Combined sources6
    Beta strandi249 – 258Combined sources10
    Beta strandi262 – 265Combined sources4
    Helixi271 – 274Combined sources4
    Beta strandi297 – 299Combined sources3
    Helixi301 – 304Combined sources4
    Helixi310 – 325Combined sources16
    Beta strandi340 – 342Combined sources3
    Beta strandi348 – 352Combined sources5
    Helixi355 – 362Combined sources8
    Beta strandi366 – 373Combined sources8
    Helixi376 – 378Combined sources3
    Beta strandi381 – 383Combined sources3
    Beta strandi387 – 394Combined sources8
    Turni395 – 398Combined sources4
    Beta strandi399 – 407Combined sources9
    Helixi410 – 412Combined sources3
    Helixi415 – 422Combined sources8
    Helixi427 – 431Combined sources5
    Beta strandi437 – 440Combined sources4
    Helixi441 – 445Combined sources5

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2R9ZX-ray2.10A/B1-463[»]
    2RABX-ray2.50A/B1-463[»]
    ProteinModelPortaliD0VWY5.
    SMRiD0VWY5.
    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
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2R9ZX-ray2.10A/B1-463[»]
    2RABX-ray2.50A/B1-463[»]
    ProteinModelPortaliD0VWY5.
    SMRiD0VWY5.
    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 2, 2016
    This is version 36 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.