ID   A0A2X4TXJ0_9NOCA        Unreviewed;       459 AA.
AC   A0A2X4TXJ0;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Hydrolase {ECO:0000313|EMBL:SQI31623.1};
DE            EC=3.-.-.- {ECO:0000313|EMBL:SQI31623.1};
GN   Name=baeB {ECO:0000313|EMBL:SQI31623.1};
GN   ORFNames=NCTC10994_01976 {ECO:0000313|EMBL:SQI31623.1};
OS   Rhodococcus coprophilus.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=38310 {ECO:0000313|EMBL:SQI31623.1, ECO:0000313|Proteomes:UP000249091};
RN   [1] {ECO:0000313|EMBL:SQI31623.1, ECO:0000313|Proteomes:UP000249091}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC10994 {ECO:0000313|EMBL:SQI31623.1,
RC   ECO:0000313|Proteomes:UP000249091};
RG   Pathogen Informatics;
RA   Doyle S.;
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; LS483468; SQI31623.1; -; Genomic_DNA.
DR   RefSeq; WP_072702072.1; NZ_LS483468.1.
DR   AlphaFoldDB; A0A2X4TXJ0; -.
DR   STRING; 1219011.GCA_001895045_03070; -.
DR   KEGG; rcr:NCTC10994_01976; -.
DR   Proteomes; UP000249091; Chromosome 1.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0050313; F:sulfur dioxygenase activity; IEA:InterPro.
DR   GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
DR   CDD; cd07724; POD-like_MBL-fold; 1.
DR   CDD; cd00158; RHOD; 1.
DR   Gene3D; 3.40.250.10; Rhodanese-like domain; 2.
DR   Gene3D; 3.60.15.10; Ribonuclease Z/Hydroxyacylglutathione hydrolase-like; 1.
DR   InterPro; IPR001279; Metallo-B-lactamas.
DR   InterPro; IPR044528; POD-like_MBL-fold.
DR   InterPro; IPR001763; Rhodanese-like_dom.
DR   InterPro; IPR036873; Rhodanese-like_dom_sf.
DR   InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR   PANTHER; PTHR43084; PERSULFIDE DIOXYGENASE ETHE1; 1.
DR   PANTHER; PTHR43084:SF1; PERSULFIDE DIOXYGENASE ETHE1, MITOCHONDRIAL; 1.
DR   Pfam; PF00581; Rhodanese; 2.
DR   SMART; SM00849; Lactamase_B; 1.
DR   SMART; SM00450; RHOD; 2.
DR   SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 1.
DR   SUPFAM; SSF52821; Rhodanese/Cell cycle control phosphatase; 2.
DR   PROSITE; PS50206; RHODANESE_3; 2.
PE   4: Predicted;
KW   Hydrolase {ECO:0000313|EMBL:SQI31623.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000249091}.
FT   DOMAIN          267..293
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000259|PROSITE:PS50206"
FT   DOMAIN          373..454
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000259|PROSITE:PS50206"
SQ   SEQUENCE   459 AA;  49138 MW;  77886AD2DE10492F CRC64;
     MILEQYYIEC LSHASYLIGD ESTGRAIVVD PRRDITEYLD DAAKHHLTIE GVINTHFHAD
     FVSGHLELVD ATGAWIGFGE AAETDYPIRR LRDGERISLG DVQLEILSTP GHTWESISVL
     VREHPDAVPS AVLTGDSLFI GDVGRPDLVN LGDGSTSDLA RAMYRTVHEK LLTLPDEVTV
     MPAHGAGSSC GKNLSTELTS TIGEQRLTNP SVQPMSEDAF VALITEGQPA APTYFSADAA
     MNKRIHPLLA QDHTIPELSP AQVKAELTAG TRVLDARSVD DFADGHLRGS VNVGFDGRFA
     ETGGMVAEVG ERIVLITYPG EEQEAALRLA RIGSDNAIGY LTVPQDGSFP AELADLVEPA
     HRTSVEELDG LLAAEAVTLV DIRNPGEREQ GTIPGAVAIP LAQLRVRLEQ VPTGKPIVVH
     CAGGWRSSVA ASLLRAQGFD NVSDLVGGYN AWVEAHATV
//