ID   DNHA_NOCS1              Reviewed;         328 AA.
AC   A0A096ZEC9;
DT   13-APR-2016, integrated into UniProtKB/Swiss-Prot.
DT   07-JAN-2015, sequence version 1.
DT   03-AUG-2022, entry version 22.
DE   RecName: Full=2,4-dinitroanisole O-demethylase subunit alpha {ECO:0000303|PubMed:25281383};
DE            Short=DNAN hydrolase subunit alpha {ECO:0000303|PubMed:25281383};
DE            Short=DNHA {ECO:0000303|PubMed:25281383};
DE            EC=3.3.2.14 {ECO:0000269|PubMed:25281383};
DE   Flags: Precursor;
GN   Name=dnhA {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 10-15, 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   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:P25910};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:P25910};
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; AIQ77708.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A096ZEC9; -.
DR   SMR; A0A096ZEC9; -.
DR   KEGG; ag:AIQ77708; -.
DR   BioCyc; MetaCyc:MON-19134; -.
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   SMART; SM00849; Lactamase_B; 1.
DR   SUPFAM; SSF56281; SSF56281; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Hydrolase; Metal-binding; Zinc.
FT   PROPEP          1..9
FT                   /evidence="ECO:0000269|PubMed:25281383"
FT                   /id="PRO_0000435987"
FT   CHAIN           10..328
FT                   /note="2,4-dinitroanisole O-demethylase subunit alpha"
FT                   /id="PRO_0000435988"
FT   BINDING         101
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P25910"
FT   BINDING         103
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P25910"
FT   BINDING         105
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P25910"
FT   BINDING         168
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P25910"
FT   BINDING         225
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P25910"
FT   BINDING         247
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P25910"
SQ   SEQUENCE   328 AA;  36983 MW;  9996CEBD12B4756A CRC64;
     MSVTSQTSSS GSAAVSDCHR GIIDISGPVP GYEWEPSMTT EPVRGRVWTI TDGVFRTLAI
     EGDTGVIAVD TFWSPGSARQ YRRALQSHFP RKPVHTIIYT HDHLDHTGFG ADFAPDADQI
     LAHELTAEVI ARRSSDGQLP ATRTWSGERL EVSIDGAEFE LIYPGPTHGT GNTALYFPNE
     RFLYMADTVF TGPTYNIVPD FLWTSWIPNT RRLLGLDWDL YVPGHFWRLS RREFEADFEL
     WDATAACALD ALRAGVDIDN FADVKKFTYE RMDEPFGSRT FRFDEFAAIN VLTHMVHYQT
     GGWGLRDYEP YSNEPFKTTL PQRLGSPL