ID A0A1J8PD99_9GAMM Unreviewed; 330 AA.
AC A0A1J8PD99;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=Glutathione-dependent reductase {ECO:0000313|EMBL:OJA06997.1};
GN ORFNames=QHL1GM_17170 {ECO:0000313|EMBL:OJA06997.1};
OS Halomonas sp. QHL1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=1123773 {ECO:0000313|EMBL:OJA06997.1, ECO:0000313|Proteomes:UP000183854};
RN [1] {ECO:0000313|EMBL:OJA06997.1, ECO:0000313|Proteomes:UP000183854}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QHL1 {ECO:0000313|EMBL:OJA06997.1,
RC ECO:0000313|Proteomes:UP000183854};
RA Seilhamer J.J.;
RL Submitted (AUG-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:OJA06997.1}.
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DR EMBL; MINL01000001; OJA06997.1; -; Genomic_DNA.
DR RefSeq; WP_071695585.1; NZ_MINL01000001.1.
DR AlphaFoldDB; A0A1J8PD99; -.
DR STRING; 1123773.QHL1GM_17170; -.
DR OrthoDB; 9769158at2; -.
DR Proteomes; UP000183854; 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; IPR004045; Glutathione_S-Trfase_N.
DR InterPro; IPR047047; GST_Omega-like_C.
DR InterPro; IPR016639; GST_Omega/GSH.
DR InterPro; IPR036249; Thioredoxin-like_sf.
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 Pfam; PF13409; GST_N_2; 1.
DR PIRSF; PIRSF015753; GST; 1.
DR SFLD; SFLDG01206; Xi.1; 1.
DR SFLD; SFLDG01148; Xi_(cytGST); 1.
DR SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS50405; GST_CTER; 1.
PE 4: Predicted;
FT DOMAIN 168..295
FT /note="GST C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50405"
FT REGION 308..330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 313..330
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 60
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR015753-1"
FT ACT_SITE 191
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR015753-1"
SQ SEQUENCE 330 AA; 38469 MW; C47E9BC55944E3A3 CRC64;
MGLLVNGEWQ DQWYDTKKHG GEFVRESAQL RDWVGDQPET DGDCYPAEKE RYHLYVSLAC
PWAHRTLIMR KLKGLEPLIG TSHVSPLMLD QGWTYRQDEG ASGDPINGVD FHHQLYTMTD
PNYTGRVTVP VLWDKQRSAI VNNESADLLR MFNQAFDELT GNDLDFYPED LRGVIDDVNA
DVYDHINNGV YKSGFATEQA VYEKHVKALF DALERMEARL AEHRYLAGEW LTEADIRLFT
TLIRFDAVYY GHFKCNFKRI EDYPNLSNYV REIYQWPGVA ETVNMDHIKR HYYYSHDTIN
PTRIVPTGPL LDFEQPHDRE RLPGQGVRRK
//
