ID A0A0W0VFX9_9GAMM Unreviewed; 209 AA.
AC A0A0W0VFX9;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=Glutathione S-transferase (Maleylacetoacetate isomerase) {ECO:0000313|EMBL:KTD19024.1};
GN ORFNames=Ljor_0247 {ECO:0000313|EMBL:KTD19024.1};
OS Legionella jordanis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=456 {ECO:0000313|EMBL:KTD19024.1, ECO:0000313|Proteomes:UP000055035};
RN [1] {ECO:0000313|EMBL:KTD19024.1, ECO:0000313|Proteomes:UP000055035}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BL-540 {ECO:0000313|EMBL:KTD19024.1,
RC ECO:0000313|Proteomes:UP000055035};
RA Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA Pupko T., Shuman H.A., Segal G.;
RT "Genomic analysis of 38 Legionella species identifies large and diverse
RT effector repertoires.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the GST superfamily. Zeta family.
CC {ECO:0000256|ARBA:ARBA00010007}.
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:KTD19024.1}.
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DR EMBL; LNYJ01000003; KTD19024.1; -; Genomic_DNA.
DR RefSeq; WP_058469829.1; NZ_RDQQ01000006.1.
DR AlphaFoldDB; A0A0W0VFX9; -.
DR STRING; 456.Ljor_0247; -.
DR PATRIC; fig|456.5.peg.263; -.
DR OrthoDB; 509852at2; -.
DR Proteomes; UP000055035; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0009072; P:aromatic amino acid metabolic process; IEA:InterPro.
DR CDD; cd03191; GST_C_Zeta; 1.
DR CDD; cd03042; GST_N_Zeta; 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; IPR005955; GST_Zeta.
DR InterPro; IPR034330; GST_Zeta_C.
DR InterPro; IPR034333; GST_Zeta_N.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR NCBIfam; TIGR01262; maiA; 1.
DR PANTHER; PTHR42673; MALEYLACETOACETATE ISOMERASE; 1.
DR PANTHER; PTHR42673:SF4; MALEYLACETOACETATE ISOMERASE; 1.
DR Pfam; PF13417; GST_N_3; 1.
DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 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 Isomerase {ECO:0000313|EMBL:KTD19024.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000055035};
KW Transferase {ECO:0000313|EMBL:KTD19024.1}.
FT DOMAIN 1..82
FT /note="GST N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50404"
FT DOMAIN 87..209
FT /note="GST C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50405"
SQ SEQUENCE 209 AA; 24065 MW; C76582E46C861F0B CRC64;
MKLYDYYRST ASYRVRIALN IKNISYEKIP VHLVKEGGEQ HRPEYLKLNP QGLVPTLDEN
GHILTQSLAI IEYLDEINPT PALLPTNPFA RAQIRSMALT VACDMHPLNN LRVLNRLKDQ
FKANDEEVMD WYHHWLKLGF DSLEAKLQSL PHKNQVCYGT EVSLADICLI PQVYNAQRFG
FSMNNYPIIN QINEYCLSLS AFKDAVPLE
//
