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Database: UniProt
Entry: A0A0Q9MPS3_9MICC
LinkDB: A0A0Q9MPS3_9MICC
Original site: A0A0Q9MPS3_9MICC 
ID   A0A0Q9MPS3_9MICC        Unreviewed;       456 AA.
AC   A0A0Q9MPS3;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=MBL fold metallo-hydrolase {ECO:0000313|EMBL:KRE68410.1};
GN   ORFNames=ASG92_00570 {ECO:0000313|EMBL:KRE68410.1};
OS   Arthrobacter sp. Soil736.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Arthrobacter.
OX   NCBI_TaxID=1736395 {ECO:0000313|EMBL:KRE68410.1, ECO:0000313|Proteomes:UP000051775};
RN   [1] {ECO:0000313|Proteomes:UP000051775}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Soil736 {ECO:0000313|Proteomes:UP000051775};
RA   Garrido-Oter R., Bai Y.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRE68410.1, ECO:0000313|Proteomes:UP000051775}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Soil736 {ECO:0000313|EMBL:KRE68410.1,
RC   ECO:0000313|Proteomes:UP000051775};
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:KRE68410.1}.
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DR   EMBL; LMSB01000001; KRE68410.1; -; Genomic_DNA.
DR   RefSeq; WP_056622902.1; NZ_LMSB01000001.1.
DR   AlphaFoldDB; A0A0Q9MPS3; -.
DR   STRING; 1736395.ASG92_00570; -.
DR   OrthoDB; 3196337at2; -.
DR   Proteomes; UP000051775; 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: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; PF00753; Lactamase_B; 1.
DR   Pfam; PF00581; Rhodanese; 1.
DR   SMART; SM00849; Lactamase_B; 1.
DR   SMART; SM00450; RHOD; 1.
DR   SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 1.
DR   SUPFAM; SSF52821; Rhodanese/Cell cycle control phosphatase; 2.
DR   PROSITE; PS50206; RHODANESE_3; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000313|EMBL:KRE68410.1}.
FT   DOMAIN          364..450
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000259|PROSITE:PS50206"
SQ   SEQUENCE   456 AA;  48753 MW;  23A75F59EB833DA1 CRC64;
     MDVVVIETPQ LGDRSYLVHD GRVGLVIDAQ RDTDRVEEAA QQAGVEITHV AETHVHNDYL
     TGGLILARAH GAKYLVNAAD SVSFEREPIT DGQSVQIGGF SLRAVATPGH THTHLSYVVT
     DGRTQAVFSG GSLLYGSVGR TDLVGPADTA GLARDQYASV RRLADEAGPD AALFPTHGFG
     SFCSIGPATS AAASTIREQR ATNHALTDPD PEHFVAELMA NLSAYPSYYA HMAPINMTGP
     EPADLSLPES LDGAELASRL ARGEWVVDLR RRVLFASNHL DGTVSFEYGS GSSFSSYLGW
     VLPWGEKLTL VGDRKDLRSA IRDLSRIGID RPDAAVGTEP HILAPGAPVA SYPRAGWAAV
     VAEKPAGEPV LDVRRTEEFE ASHVADALNV PLHELLGRLD ELPAGRIWVH CNSGYRAAVA
     ASLLQRAGRD VVHIDARFRE AAAAGVPMHL QAAQRH
//
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