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Database: UniProt
Entry: A0A1D1UW08_RAMVA
LinkDB: A0A1D1UW08_RAMVA
Original site: A0A1D1UW08_RAMVA 
ID   A0A1D1UW08_RAMVA        Unreviewed;       247 AA.
AC   A0A1D1UW08;
DT   30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2016, sequence version 1.
DT   22-FEB-2023, entry version 21.
DE   RecName: Full=Glutathione S-transferase omega {ECO:0000256|RuleBase:RU368071};
DE            Short=GSTO {ECO:0000256|RuleBase:RU368071};
DE            EC=1.20.4.2 {ECO:0000256|RuleBase:RU368071};
DE            EC=1.8.5.1 {ECO:0000256|RuleBase:RU368071};
DE            EC=2.5.1.18 {ECO:0000256|RuleBase:RU368071};
DE   AltName: Full=Glutathione-dependent dehydroascorbate reductase {ECO:0000256|RuleBase:RU368071};
DE   AltName: Full=Monomethylarsonic acid reductase {ECO:0000256|RuleBase:RU368071};
GN   Name=RvY_04767-1 {ECO:0000313|EMBL:GAU92720.1};
GN   Synonyms=RvY_04767.1 {ECO:0000313|EMBL:GAU92720.1};
GN   ORFNames=RvY_04767 {ECO:0000313|EMBL:GAU92720.1};
OS   Ramazzottius varieornatus (Water bear) (Tardigrade).
OC   Eukaryota; Metazoa; Ecdysozoa; Tardigrada; Eutardigrada; Parachela;
OC   Hypsibioidea; Ramazzottiidae; Ramazzottius.
OX   NCBI_TaxID=947166 {ECO:0000313|EMBL:GAU92720.1, ECO:0000313|Proteomes:UP000186922};
RN   [1] {ECO:0000313|EMBL:GAU92720.1, ECO:0000313|Proteomes:UP000186922}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YOKOZUNA-1 {ECO:0000313|EMBL:GAU92720.1,
RC   ECO:0000313|Proteomes:UP000186922};
RX   PubMed=27649274; DOI=10.1038/ncomms12808;
RA   Hashimoto T., Horikawa D.D., Saito Y., Kuwahara H., Kozuka-Hata H.,
RA   Shin-I T., Minakuchi Y., Ohishi K., Motoyama A., Aizu T., Enomoto A.,
RA   Kondo K., Tanaka S., Hara Y., Koshikawa S., Sagara H., Miura T.,
RA   Yokobori S., Miyagawa K., Suzuki Y., Kubo T., Oyama M., Kohara Y.,
RA   Fujiyama A., Arakawa K., Katayama T., Toyoda A., Kunieda T.;
RT   "Extremotolerant tardigrade genome and improved radiotolerance of human
RT   cultured cells by tardigrade-unique protein.";
RL   Nat. Commun. 7:12808-12808(2016).
CC   -!- FUNCTION: Exhibits glutathione-dependent thiol transferase activity.
CC       Has high dehydroascorbate reductase activity and may contribute to the
CC       recycling of ascorbic acid. Participates in the biotransformation of
CC       inorganic arsenic and reduces monomethylarsonic acid (MMA).
CC       {ECO:0000256|RuleBase:RU368071}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 glutathione + H(+) + methylarsonate = glutathione disulfide
CC         + H2O + methylarsonous acid; Xref=Rhea:RHEA:15969, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17826, ChEBI:CHEBI:33409,
CC         ChEBI:CHEBI:57925, ChEBI:CHEBI:58297; EC=1.20.4.2;
CC         Evidence={ECO:0000256|RuleBase:RU368071};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 glutathione + L-dehydroascorbate = glutathione disulfide +
CC         L-ascorbate; Xref=Rhea:RHEA:24424, ChEBI:CHEBI:38290,
CC         ChEBI:CHEBI:57925, ChEBI:CHEBI:58297, ChEBI:CHEBI:58539; EC=1.8.5.1;
CC         Evidence={ECO:0000256|RuleBase:RU368071};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glutathione + RX = a halide anion + an S-substituted
CC         glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925,
CC         ChEBI:CHEBI:90779; EC=2.5.1.18;
CC         Evidence={ECO:0000256|RuleBase:RU368071};
CC   -!- SIMILARITY: Belongs to the GST superfamily. Omega family.
CC       {ECO:0000256|ARBA:ARBA00011067, ECO:0000256|RuleBase:RU368071}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GAU92720.1}.
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DR   EMBL; BDGG01000002; GAU92720.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1D1UW08; -.
DR   STRING; 947166.A0A1D1UW08; -.
DR   Proteomes; UP000186922; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0045174; F:glutathione dehydrogenase (ascorbate) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0050610; F:methylarsonate reductase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006749; P:glutathione metabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.20.1050.10; -; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR   InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR   InterPro; IPR040079; Glutathione_S-Trfase.
DR   InterPro; IPR004045; Glutathione_S-Trfase_N.
DR   InterPro; IPR005442; GST_omega.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR43968; -; 1.
DR   PANTHER; PTHR43968:SF6; GLUTATHIONE-DEPENDENT DEHYDROASCORBATE REDUCTASE; 1.
DR   Pfam; PF13417; GST_N_3; 1.
DR   PRINTS; PR01625; GSTRNSFRASEO.
DR   SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR   SFLD; SFLDG00358; Main_(cytGST); 1.
DR   SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS51354; GLUTAREDOXIN_2; 1.
DR   PROSITE; PS50405; GST_CTER; 1.
DR   PROSITE; PS50404; GST_NTER; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU368071};
KW   Reference proteome {ECO:0000313|Proteomes:UP000186922};
KW   Transferase {ECO:0000256|RuleBase:RU368071}.
FT   DOMAIN          24..103
FT                   /note="GST N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50404"
FT   DOMAIN          101..222
FT                   /note="GST C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50405"
SQ   SEQUENCE   247 AA;  28380 MW;  11B3242755E39A0D CRC64;
     MVRKIPGKSK DFQEGSALPK INDNGVTVYS MRFCPYAERV RLMLNTKHVP YEVINIDLKS
     KPEWFLERNP LGKVPAIEEP GKKPLFESLV VAEYIDEQFK GNREVLPSDP YEKARQKVIA
     QNITTPFYGV LFKNESGDAI LKGLEDVEKM LTSEYFAGSS QGFVDLMVWP WFERLASLAD
     ARPGALQIDF SCYPKIKLWM ERKLNDPDVK DTAYSQETFT TFLKARWRGN RTRTLVFDST
     EDLAQGF
//
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