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Database: UniProt
Entry: A0A1Q5L9X3_9ACTN
LinkDB: A0A1Q5L9X3_9ACTN
Original site: A0A1Q5L9X3_9ACTN 
ID   A0A1Q5L9X3_9ACTN        Unreviewed;       459 AA.
AC   A0A1Q5L9X3;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Hydrolase {ECO:0000313|EMBL:OKJ91672.1};
GN   ORFNames=AMK33_35165 {ECO:0000313|EMBL:OKJ91672.1};
OS   Streptomyces sp. CB02400.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1703944 {ECO:0000313|EMBL:OKJ91672.1, ECO:0000313|Proteomes:UP000185993};
RN   [1] {ECO:0000313|EMBL:OKJ91672.1, ECO:0000313|Proteomes:UP000185993}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CB02400 {ECO:0000313|EMBL:OKJ91672.1,
RC   ECO:0000313|Proteomes:UP000185993};
RX   PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA   Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA   Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA   Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT   "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL   MBio 7:e02104-e02116(2016).
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:OKJ91672.1}.
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DR   EMBL; LIWB01000023; OKJ91672.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q5L9X3; -.
DR   Proteomes; UP000185993; Unassembled WGS sequence.
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:0004792; F:thiosulfate sulfurtransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
DR   CDD; cd07724; POD-like_MBL-fold; 1.
DR   CDD; cd00158; RHOD; 2.
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   InterPro; IPR001307; Thiosulphate_STrfase_CS.
DR   PANTHER; PTHR43084; PERSULFIDE DIOXYGENASE ETHE1; 1.
DR   PANTHER; PTHR43084:SF1; PERSULFIDE DIOXYGENASE ETHE1, MITOCHONDRIAL; 1.
DR   Pfam; PF00753; Lactamase_B; 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; PS00380; RHODANESE_1; 1.
DR   PROSITE; PS50206; RHODANESE_3; 2.
PE   4: Predicted;
KW   Hydrolase {ECO:0000313|EMBL:OKJ91672.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000185993}.
FT   DOMAIN          266..357
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000259|PROSITE:PS50206"
FT   DOMAIN          372..451
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000259|PROSITE:PS50206"
SQ   SEQUENCE   459 AA;  48062 MW;  CA369A05249BF1CF CRC64;
     MGFADEHLIP LVDEGLGNSA YLLDLGDGRA LAMDAGRDLR ALREAAEQRG LTVAYAADTH
     LHADFLSGAV QLGHDTGATV LASAAGRRAF AHRALAGGDE VDLGGLTLRA LSTPGHTDEH
     LSFLLLDGGR ELGVFTGGSL IVNSAARTDL LGPERTEELA RAQYRSLRLL TELPDETAVW
     PTHGAGSFCS APPGTGRTST IGAQRQTNPL LAAPDENAFV DRLIASLGTY PTYFDRLGET
     NRRGPAVLTA QPVLPVLSAR QVQALMADGG YVVDVRPAAD YAAGHIPGSL SIPLRDQFAT
     WLGWLLPDTA PLAFVTSEGQ DLSEIVWQAY KIGYERLAGR LTGGMDAWLA DGNPQATTAF
     LTADRAVGRP YVDVRQQAEF AAGHVPGAVH LELGSLPAAA GDAPTAPVVA CGHGERAMTA
     ASLLERAGHT DIAVLDGGPD DYTAAHGRQL AQGTEGHRS
//
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