ID A0A0Q5HIB2_9BURK Unreviewed; 280 AA.
AC A0A0Q5HIB2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=S-transferase {ECO:0000313|EMBL:KQQ88913.1};
GN ORFNames=ASF77_09365 {ECO:0000313|EMBL:KQQ88913.1};
OS Massilia sp. Leaf139.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Massilia.
OX NCBI_TaxID=1736272 {ECO:0000313|EMBL:KQQ88913.1, ECO:0000313|Proteomes:UP000051760};
RN [1] {ECO:0000313|EMBL:KQQ88913.1, ECO:0000313|Proteomes:UP000051760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf139 {ECO:0000313|EMBL:KQQ88913.1,
RC ECO:0000313|Proteomes:UP000051760};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQQ88913.1, ECO:0000313|Proteomes:UP000051760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf139 {ECO:0000313|EMBL:KQQ88913.1,
RC ECO:0000313|Proteomes:UP000051760};
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:KQQ88913.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LMOJ01000022; KQQ88913.1; -; Genomic_DNA.
DR RefSeq; WP_056339288.1; NZ_LMOJ01000022.1.
DR AlphaFoldDB; A0A0Q5HIB2; -.
DR STRING; 1736272.ASF77_09365; -.
DR OrthoDB; 81087at2; -.
DR Proteomes; UP000051760; Unassembled WGS sequence.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR CDD; cd10292; GST_C_YghU_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; IPR004045; Glutathione_S-Trfase_N.
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; PF13410; GST_C_2; 1.
DR Pfam; PF02798; GST_N; 1.
DR SFLD; SFLDG01151; Main.2:_Nu-like; 1.
DR SFLD; SFLDG00358; Main_(cytGST); 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 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000051760};
KW Transferase {ECO:0000313|EMBL:KQQ88913.1}.
FT DOMAIN 47..134
FT /note="GST N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50404"
FT DOMAIN 137..266
FT /note="GST C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50405"
SQ SEQUENCE 280 AA; 31283 MW; B95A2DADD9645A56 CRC64;
MPEQSNYVPA KVWTPPASNG GMFANINRPV AGPTHEAELP VGKHPLQLYS LATPNGQKVT
ILLEELLAAG HAGAEYDAWL IKINEGAQFS SGFVEVNPNS KIPALMDRSG PEPLRVFESG
AILLYLAEKF GAFLPTELRA RTETLNWLFW QMGSAPMLGG GFGHFYAYAP EKLEYPIDRY
AMEVKRQLDV LDRQLADNRY VAGGEYTIAD MAIWPWYGAL VQGEIYEAGE FLSVHEYTHV
RRWADEIAAR PAVIRGRRVN RVRGKPEEQL AERHDASDLD
//