ID   Q5QX18_IDILO            Unreviewed;       221 AA.
AC   Q5QX18;
DT   04-JAN-2005, integrated into UniProtKB/TrEMBL.
DT   04-JAN-2005, sequence version 1.
DT   27-MAR-2024, entry version 107.
DE   SubName: Full=Glutathione S-transferase related protein {ECO:0000313|EMBL:AAV81464.1};
GN   OrderedLocusNames=IL0623 {ECO:0000313|EMBL:AAV81464.1};
OS   Idiomarina loihiensis (strain ATCC BAA-735 / DSM 15497 / L2-TR).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Idiomarinaceae; Idiomarina.
OX   NCBI_TaxID=283942 {ECO:0000313|EMBL:AAV81464.1, ECO:0000313|Proteomes:UP000001171};
RN   [1] {ECO:0000313|EMBL:AAV81464.1, ECO:0000313|Proteomes:UP000001171}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-735 / DSM 15497 / L2-TR
RC   {ECO:0000313|Proteomes:UP000001171};
RX   PubMed=15596722; DOI=10.1073/pnas.0407638102;
RA   Hou S., Saw J.H., Lee K.S., Freitas T.A., Belisle C., Kawarabayasi Y.,
RA   Donachie S.P., Pikina A., Galperin M.Y., Koonin E.V., Makarova K.S.,
RA   Omelchenko M.V., Sorokin A., Wolf Y.I., Li Q.X., Keum Y.S., Campbell S.,
RA   Denery J., Aizawa S., Shibata S., Malahoff A., Alam M.;
RT   "Genome sequence of the deep-sea gamma-proteobacterium Idiomarina
RT   loihiensis reveals amino acid fermentation as a source of carbon and
RT   energy.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:18036-18041(2004).
CC   -!- SIMILARITY: Belongs to the GST superfamily.
CC       {ECO:0000256|RuleBase:RU003494}.
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DR   EMBL; AE017340; AAV81464.1; -; Genomic_DNA.
DR   RefSeq; WP_011233878.1; NC_006512.1.
DR   AlphaFoldDB; Q5QX18; -.
DR   STRING; 283942.IL0623; -.
DR   KEGG; ilo:IL0623; -.
DR   eggNOG; COG0625; Bacteria.
DR   HOGENOM; CLU_011226_14_4_6; -.
DR   OrthoDB; 9803562at2; -.
DR   Proteomes; UP000001171; Chromosome.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   CDD; cd10291; GST_C_YfcG_like; 1.
DR   CDD; cd03048; GST_N_Ure2p_like; 1.
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; IPR004046; GST_C.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR44051; GLUTATHIONE S-TRANSFERASE-RELATED; 1.
DR   PANTHER; PTHR44051:SF8; GLUTATHIONE S-TRANSFERASE-RELATED; 1.
DR   Pfam; PF00043; GST_C; 1.
DR   Pfam; PF02798; GST_N; 1.
DR   SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR   SFLD; SFLDG01150; Main.1:_Beta-like; 1.
DR   SFLD; SFLDG01151; Main.2:_Nu-like; 1.
DR   SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS50405; GST_CTER; 1.
DR   PROSITE; PS50404; GST_NTER; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000001171};
KW   Transferase {ECO:0000313|EMBL:AAV81464.1}.
FT   DOMAIN          1..83
FT                   /note="GST N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50404"
FT   DOMAIN          86..208
FT                   /note="GST C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50405"
FT   REGION          199..221
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   221 AA;  25651 MW;  A51080A910D43CF5 CRC64;
     MIELYTSATP NGYKATVTLE EMGLDYNLHH VQLQENEQKR PEFLKMNPNG RIPVIVDKNN
     DDFAVFESGA IMLYLAETYD KLNPKDPKER SRMIQWLMFQ MGGIGPMMGQ ANVFYRYFPE
     KLPSAIERYQ NESRRLFEVL NTRLGESEYL AGDNFSLADI ANWCWVRTHD WSGVSLDGLE
     NLKRWMNTIS ERPACQRGVT KPERMGDPDE LVKSAQKMVQ R
//