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Database: UniProt
Entry: A0A2A4KT15_9ACTN
LinkDB: A0A2A4KT15_9ACTN
Original site: A0A2A4KT15_9ACTN 
ID   A0A2A4KT15_9ACTN        Unreviewed;       452 AA.
AC   A0A2A4KT15;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=MBL fold metallo-hydrolase {ECO:0000313|EMBL:PCG87425.1};
GN   ORFNames=CIB93_03095 {ECO:0000313|EMBL:PCG87425.1};
OS   Streptomyces sp. WZ.A104.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=2023771 {ECO:0000313|EMBL:PCG87425.1, ECO:0000313|Proteomes:UP000217525};
RN   [1] {ECO:0000313|EMBL:PCG87425.1, ECO:0000313|Proteomes:UP000217525}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WZ.A104 {ECO:0000313|EMBL:PCG87425.1,
RC   ECO:0000313|Proteomes:UP000217525};
RA   Xu L., He S., Yan X.;
RT   "Isolation and Genomic Analysis of a Bioactive Actinomycete Associated with
RT   Cyanobacterium Lyngbya cf. aestuarii.";
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000217525}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WZ.A104 {ECO:0000313|Proteomes:UP000217525};
RA   Jiao Y., Han B.;
RL   Submitted (SEP-2017) 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:PCG87425.1}.
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DR   EMBL; NWVL01000004; PCG87425.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A4KT15; -.
DR   OrthoDB; 3196337at2; -.
DR   Proteomes; UP000217525; 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; 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:PCG87425.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000217525}.
FT   DOMAIN          261..352
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000259|PROSITE:PS50206"
FT   DOMAIN          365..451
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000259|PROSITE:PS50206"
SQ   SEQUENCE   452 AA;  47193 MW;  35C21C81A2BFA5AF CRC64;
     MFFVEAIELE GLGNRSYLTG GRRTAVAVDP PRDIDRVLAA AARRGVAITH VVETHIHNDY
     VTGGLELARI TGAAYLVPAD AHVSFARTAV SDGDTVIIDA ELTLTAVATP GHTPHHTSYV
     LSEAGRPVAA FTGGSLLIGT VGRPDLVEPR LTEQLARSQH ASARRLADAL PDETEVLPTH
     GFGSFCSSAQ AGGESTTIGK EKAANPALTI DVDTFVAELL AGLEDVPAYY AHMGPANAAG
     PAPVDLTAPA VADPDDIAER LAAGEWVVDL RNRIAFAEGH VAGSFNFEAD GKLATYLAWL
     IPWGKPVTLL AESAEQLAAA QRELVRVGID RPASAATGGP ADWLRAGESP ASFPRATFAE
     LAGQNRGRIV VLDVRRSSER AEGWIEGSVH IPIHQVHRRI DDVPDGTVWV HCAGGMRAGI
     AASLLDAAGR DVVAVDDGFG AAAEAGLTIV TG
//
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