ID Q3SSA4_NITWN Unreviewed; 290 AA.
AC Q3SSA4;
DT 11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT 11-OCT-2005, sequence version 1.
DT 27-MAR-2024, entry version 108.
DE SubName: Full=Glutathione S-transferase {ECO:0000313|EMBL:ABA04837.1};
DE EC=2.5.1.18 {ECO:0000313|EMBL:ABA04837.1};
GN OrderedLocusNames=Nwi_1576 {ECO:0000313|EMBL:ABA04837.1};
OS Nitrobacter winogradskyi (strain ATCC 25391 / DSM 10237 / CIP 104748 /
OS NCIMB 11846 / Nb-255).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Nitrobacter.
OX NCBI_TaxID=323098 {ECO:0000313|EMBL:ABA04837.1, ECO:0000313|Proteomes:UP000002531};
RN [1] {ECO:0000313|EMBL:ABA04837.1, ECO:0000313|Proteomes:UP000002531}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25391 / DSM 10237 / CIP 104748 / NCIMB 11846 / Nb-255
RC {ECO:0000313|Proteomes:UP000002531};
RX PubMed=16517654; DOI=10.1128/AEM.72.3.2050-2063.2006;
RA Starkenburg S.R., Chain P.S., Sayavedra-Soto L.A., Hauser L., Land M.L.,
RA Larimer F.W., Malfatti S.A., Klotz M.G., Bottomley P.J., Arp D.J.,
RA Hickey W.J.;
RT "Genome sequence of the chemolithoautotrophic nitrite-oxidizing bacterium
RT Nitrobacter winogradskyi Nb-255.";
RL Appl. Environ. Microbiol. 72:2050-2063(2006).
CC -!- SIMILARITY: Belongs to the GST superfamily.
CC {ECO:0000256|RuleBase:RU003494}.
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DR EMBL; CP000115; ABA04837.1; -; Genomic_DNA.
DR RefSeq; WP_011314843.1; NC_007406.1.
DR AlphaFoldDB; Q3SSA4; -.
DR STRING; 323098.Nwi_1576; -.
DR KEGG; nwi:Nwi_1576; -.
DR eggNOG; COG0625; Bacteria.
DR HOGENOM; CLU_011226_14_4_5; -.
DR OrthoDB; 9803562at2; -.
DR Proteomes; UP000002531; Chromosome.
DR GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC.
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; 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; 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 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000002531};
KW Transferase {ECO:0000313|EMBL:ABA04837.1}.
FT DOMAIN 46..132
FT /note="GST N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50404"
FT DOMAIN 135..269
FT /note="GST C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50405"
FT REGION 257..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 266..290
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 290 AA; 32750 MW; 5967E667CC7F70F8 CRC64;
MTDAPYMPPK VWTFDKENGG RFASVNRPTA GATHEKVLPV GKHPFQLYSR GTPNGQKVTI
MFEELLARGH AGAEYDAWLI QIDGEQFGSG FVEVNPNSKI PALVDRSRPV PFRVFESGAI
LLHLADKFRE FIPRATAARA ECLSWLFWQM GSAPYLGGGF GHFYHYAPEK IEYAINRFAM
ETKRQMDVLD RRLKDNEYLA GNEYTIADMA VWPWYGGLAE GRLYGDSATF LDVQSYKNVQ
RWTAQIAARP AVKRGRIVNR TSGDPASQLH ERHDASDFET RTQDKLAKQG
//
