ID A0A0Q5VL56_9ACTN Unreviewed; 343 AA.
AC A0A0Q5VL56;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=Glutathione S-transferase {ECO:0000313|EMBL:KQS57039.1};
GN ORFNames=ASG36_18825 {ECO:0000313|EMBL:KQS57039.1};
OS Geodermatophilus sp. Leaf369.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Geodermatophilus.
OX NCBI_TaxID=1736354 {ECO:0000313|EMBL:KQS57039.1, ECO:0000313|Proteomes:UP000051830};
RN [1] {ECO:0000313|EMBL:KQS57039.1, ECO:0000313|Proteomes:UP000051830}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf369 {ECO:0000313|EMBL:KQS57039.1,
RC ECO:0000313|Proteomes:UP000051830};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQS57039.1, ECO:0000313|Proteomes:UP000051830}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf369 {ECO:0000313|EMBL:KQS57039.1,
RC ECO:0000313|Proteomes:UP000051830};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KQS57039.1}.
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DR EMBL; LMQA01000004; KQS57039.1; -; Genomic_DNA.
DR RefSeq; WP_055767551.1; NZ_LMQA01000004.1.
DR AlphaFoldDB; A0A0Q5VL56; -.
DR STRING; 1736354.ASG36_18825; -.
DR OrthoDB; 9769158at2; -.
DR Proteomes; UP000051830; 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; 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; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR SFLD; SFLDG01206; Xi.1; 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;
KW Reference proteome {ECO:0000313|Proteomes:UP000051830};
KW Transferase {ECO:0000313|EMBL:KQS57039.1}.
FT DOMAIN 156..280
FT /note="GST C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50405"
FT REGION 303..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 48
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR015753-1"
FT ACT_SITE 179
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR015753-1"
SQ SEQUENCE 343 AA; 38433 MW; 50F63340854E7AED CRC64;
MSNENGYVEP GKSFERDTNY IEDRILADGS QGWPVEADRY RLVVARACPW ANRATIVRRL
LGLESAFSMG ITGPTHDKNS WTFDLDPGGR DPVLGYERLQ EAFFARDPEY PRGITVPAMV
DLPTRAVVTN DFAQMTLDFS TEWTAFHRDG APDLYPEHLR DEMDDVMKRV FTEINNGVYR
CGFAGSQESY ASAYDRLFTA LDWVSERLET RRYLMGDTIT EADVRLFTTL ARFDAVYHGH
FKCNRQKLAE MPVLWGYARD LFQTPGFGDT TDFPQIKRHY YVVHADINPT QIVPVGPDTS
NWLTAHGREE LGGSPFGDGT PPGPVAAGEE VPASEGAGGS TSY
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