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Database: UniProt
Entry: A0A1Q4DI92_9PSEU
LinkDB: A0A1Q4DI92_9PSEU
Original site: A0A1Q4DI92_9PSEU 
ID   A0A1Q4DI92_9PSEU        Unreviewed;       325 AA.
AC   A0A1Q4DI92;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=Glutathione-dependent reductase {ECO:0000313|EMBL:OJY44114.1};
GN   ORFNames=BGP03_07190 {ECO:0000313|EMBL:OJY44114.1};
OS   Pseudonocardia sp. 73-21.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Pseudonocardia.
OX   NCBI_TaxID=1895809 {ECO:0000313|EMBL:OJY44114.1, ECO:0000313|Proteomes:UP000186163};
RN   [1] {ECO:0000313|EMBL:OJY44114.1, ECO:0000313|Proteomes:UP000186163}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=73-21 {ECO:0000313|EMBL:OJY44114.1};
RA   Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA   Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT   "Genome-resolved meta-omics ties microbial dynamics to process performance
RT   in biotechnology for thiocyanate degradation.";
RL   Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
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:OJY44114.1}.
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DR   EMBL; MKVV01000061; OJY44114.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q4DI92; -.
DR   STRING; 1895809.BGP03_07190; -.
DR   Proteomes; UP000186163; Unassembled WGS sequence.
DR   GO; GO:0004364; F:glutathione transferase activity; IEA:InterPro.
DR   CDD; cd03190; GST_C_Omega_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; IPR047047; GST_Omega-like_C.
DR   InterPro; IPR016639; GST_Omega/GSH.
DR   PANTHER; PTHR32419:SF6; GLUTATHIONE S-TRANSFERASE OMEGA-LIKE 1-RELATED; 1.
DR   PANTHER; PTHR32419; GLUTATHIONYL-HYDROQUINONE REDUCTASE; 1.
DR   Pfam; PF13410; GST_C_2; 1.
DR   PIRSF; PIRSF015753; GST; 1.
DR   SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR   SFLD; SFLDG01206; Xi.1; 1.
DR   SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR   PROSITE; PS50405; GST_CTER; 1.
PE   4: Predicted;
FT   DOMAIN          146..273
FT                   /note="GST C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50405"
FT   REGION          293..325
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        308..325
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        38
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015753-1"
FT   ACT_SITE        169
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015753-1"
SQ   SEQUENCE   325 AA;  35947 MW;  169C5C4A1682083A CRC64;
     MTTFEREPVA LDERITADGS SRWPVEAGRY RLVVARACPW ANRAVIVRRL LGLEQAISMG
     IAGPLHDERS WRFHLDPDNR DPVLGIEYLG EAYRTADPGF DAGITVPAMV DLRTGGVATN
     GFQQLTLDFS TQWTAFHRSG APDLYPEALR AEIDEVNAGV YEDVNNGVYK CGFAGSQASY
     ERAYAALFAR LDALSERLAT RRYLVGDTIT EADVRLWVTL VRFDAAYHGH FKANRQKLTE
     MPVLWAYSRD LFQTPGFGDT IDFLQIKQHY YGVHLTINPT GIVPAGPDVS GWLTPHGREE
     LGGRPFGDGT PPGPPPSGER VPDIA
//
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