ID   DNHB_NOCS1              Reviewed;         318 AA.
AC   A0A096ZED0;
DT   13-APR-2016, integrated into UniProtKB/Swiss-Prot.
DT   07-JAN-2015, sequence version 1.
DT   03-AUG-2022, entry version 24.
DE   RecName: Full=2,4-dinitroanisole O-demethylase subunit beta {ECO:0000303|PubMed:25281383};
DE            Short=DNAN hydrolase subunit beta {ECO:0000303|PubMed:25281383};
DE            Short=DNHB {ECO:0000303|PubMed:25281383};
DE            EC=3.3.2.14 {ECO:0000269|PubMed:25281383};
GN   Name=dnhB {ECO:0000303|PubMed:25281383};
OS   Nocardioides sp. (strain JS1661).
OC   Bacteria; Actinobacteria; Propionibacteriales; Nocardioidaceae;
OC   Nocardioides.
OX   NCBI_TaxID=1517491;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-7, FUNCTION,
RP   CATALYTIC ACTIVITY, INDUCTION, AND SUBUNIT.
RC   STRAIN=JS1661;
RX   PubMed=25281383; DOI=10.1128/aem.02752-14;
RA   Fida T.T., Palamuru S., Pandey G., Spain J.C.;
RT   "Aerobic biodegradation of 2,4-dinitroanisole by Nocardioides sp. strain
RT   JS1661.";
RL   Appl. Environ. Microbiol. 80:7725-7731(2014).
CC   -!- FUNCTION: Involved in the degradation of 2,4-dinitroanisole (DNAN), an
CC       insensitive munition ingredient used in explosive formulations as a
CC       replacement for 2,4,6-trinitrotoluene (TNT). Catalyzes the removal of
CC       the methyl group from 2,4-dinitroanisole (DNAN) to yield 2,4-
CC       dinitrophenol (2,4-DNP) and methanol. {ECO:0000269|PubMed:25281383}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2,4-dinitroanisole + H2O = 2,4-dinitrophenol + H(+) +
CC         methanol; Xref=Rhea:RHEA:44636, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17790, ChEBI:CHEBI:84559, ChEBI:CHEBI:84561; EC=3.3.2.14;
CC         Evidence={ECO:0000269|PubMed:25281383};
CC   -!- SUBUNIT: Part of the complex DnhAB composed of the 2,4-dinitroanisole
CC       O-demethylase alpha (DnhA) and beta (DnhB) subunits.
CC       {ECO:0000305|PubMed:25281383}.
CC   -!- INDUCTION: Constitutively expressed. {ECO:0000269|PubMed:25281383}.
CC   -!- MISCELLANEOUS: Unlike other known O-demethylases, it does not require
CC       oxygen or electron donors. {ECO:0000269|PubMed:25281383}.
CC   -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily.
CC       {ECO:0000305}.
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DR   EMBL; KM213001; AIQ77709.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A096ZED0; -.
DR   SMR; A0A096ZED0; -.
DR   KEGG; ag:AIQ77709; -.
DR   BioCyc; MetaCyc:MON-19135; -.
DR   BRENDA; 3.3.2.14; 4363.
DR   GO; GO:0016803; F:ether hydrolase activity; IDA:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR   Gene3D; 3.60.15.10; -; 1.
DR   InterPro; IPR001279; Metallo-B-lactamas.
DR   InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR   Pfam; PF00753; Lactamase_B; 1.
DR   SUPFAM; SSF56281; SSF56281; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Hydrolase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:25281383"
FT   CHAIN           2..318
FT                   /note="2,4-dinitroanisole O-demethylase subunit beta"
FT                   /id="PRO_0000435989"
SQ   SEQUENCE   318 AA;  35021 MW;  FA555A5D5AED7B38 CRC64;
     MTGRQRTTVV APDRPVQDAT ISQLTTRVWT VAIDGYRTIV VEGETGIVAI NSFGTPSAQT
     KYRELITQTF GDKPVVAVVA SIDHLDHTGR LGPFANGAEV IGHELGQAIA FGRGLPEQKL
     ADTVVTGPVT EIERAGVRLV LRYPAPTVGT GNLAVDLPDD DVVFMVGLQS GARYGIFPDF
     HFKHFLRATS EIAALGRRYF VPGRSEVMDA GQVRQALEYV NDFQNACQRC LAGGEVPHWL
     LEPTTAYLHD ELSSKWSHLE GYDPVAVGLG GLRVVCHYYM GGWWLDDTDH HELLYDHLTV
     RTYREYRERL ATAGTGRA