CNDA_RHIWD
ID CNDA_RHIWD Reviewed; 348 AA.
AC A0A059WLZ7;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 03-SEP-2014, sequence version 1.
DT 03-AUG-2022, entry version 34.
DE RecName: Full=Chloroacetanilide N-alkylformylase, oxygenase component {ECO:0000303|PubMed:24928877};
DE EC=1.14.15.23 {ECO:0000269|PubMed:24928877};
DE AltName: Full=Three-component Rieske non-heme iron oxygenase system {ECO:0000303|PubMed:24928877};
DE Short=RHO {ECO:0000303|PubMed:24928877};
GN Name=cndA {ECO:0000303|PubMed:24928877};
GN ORFNames=HY78_30640 {ECO:0000312|EMBL:ARR57849.1};
OS Rhizorhabdus wittichii (strain DC-6 / KACC 16600) (Sphingomonas wittichii).
OG Plasmid pDC05.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Rhizorhabdus.
OX NCBI_TaxID=1283312;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], FUNCTION, CATALYTIC
RP ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE
RP SPECIFICITY, AND SUBUNIT.
RC STRAIN=DC-6 / KACC 16600; PLASMID=pDC05 {ECO:0000312|EMBL:ARR57849.1};
RX PubMed=24928877; DOI=10.1128/aem.00659-14;
RA Chen Q., Wang C.H., Deng S.K., Wu Y.D., Li Y., Yao L., Jiang J.D., Yan X.,
RA He J., Li S.P.;
RT "Novel three-component Rieske non-heme iron oxygenase system catalyzing the
RT N-dealkylation of chloroacetanilide herbicides in sphingomonads DC-6 and
RT DC-2.";
RL Appl. Environ. Microbiol. 80:5078-5085(2014).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DC-6 / KACC 16600; PLASMID=pDC05 {ECO:0000312|EMBL:ARR57849.1};
RA Cheng M., Chen Q., Qiu J., Yan X., He J.;
RT "Comparative genome analysis reveals the molecular basis of
RT chloroacetanilide herbicide mineralization in Sphingomonas wittichii DC-
RT 6.";
RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the chloroacetanilide N-alkylformylase
CC multicomponent enzyme system involved in the degradation of
CC chloroacetanilide herbicides (N-alkoxyalkyl-N-chloroacetyl-substituted
CC aniline derivatives). In vitro, catalyzes the N-dealkylation of
CC butachlor, alachlor and acetochlor to yield 2-chloro-N-(2,6-
CC diethylphenyl)acetamide (CDEPA) (for alachlor and butachlor) and 2-
CC chloro-N-(2-methyl-6-ethylphenyl)acetamide (CMEPA) (for acetochlor).
CC {ECO:0000269|PubMed:24928877}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=butachlor + 2 H(+) + O2 + 2 reduced [2Fe-2S]-[ferredoxin] =
CC butyl formate + H2O + N-(2,6-diethylphenyl)-2-chloroacetamide + 2
CC oxidized [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:52204, Rhea:RHEA-
CC COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:3230,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:88514,
CC ChEBI:CHEBI:136492; EC=1.14.15.23;
CC Evidence={ECO:0000269|PubMed:24928877};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alachlor + 2 H(+) + O2 + 2 reduced [2Fe-2S]-[ferredoxin] = H2O
CC + methyl formate + N-(2,6-diethylphenyl)-2-chloroacetamide + 2
CC oxidized [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:52208, Rhea:RHEA-
CC COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:2533,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:77699,
CC ChEBI:CHEBI:136492; Evidence={ECO:0000269|PubMed:24928877};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetochlor + 2 H(+) + O2 + 2 reduced [2Fe-2S]-[ferredoxin] =
CC ethyl formate + H2O + N-(2-ethyl-6-methylphenyl)-2-chloroacetamide +
CC 2 oxidized [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:52212, Rhea:RHEA-
CC COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:2394,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:52342,
CC ChEBI:CHEBI:136494; Evidence={ECO:0000269|PubMed:24928877};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000250|UniProtKB:Q5S3I3};
CC Note=Binds 1 [2Fe-2S] cluster per subunit.
CC {ECO:0000250|UniProtKB:Q5S3I3};
CC -!- ACTIVITY REGULATION: Activity enhanced by Fe(2+) and Mg(2+) ions.
CC Divalent cations such as Ca(2+), Cr(2+), Co(2+), and Mn(2+) show
CC moderate inhibition of the enzyme, whereas heavy metal ions such as
CC Ag(+), Cu(2+), Pb(2+), Hg(2+), Ni(2+) and Zn(2+) severely inhibit the
CC activity. {ECO:0000269|PubMed:24928877}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7. {ECO:0000269|PubMed:24928877};
CC Temperature dependence:
CC Optimum temperature is 35 degrees Celsius.
CC {ECO:0000269|PubMed:24928877};
CC -!- SUBUNIT: The chloroacetanilide N-alkylformylase multicomponent enzyme
CC system is composed of an oxygenase component (CndA) and an electron
CC transfer component formed by a ferredoxin reductase (CndC1) and a
CC ferredoxin (CndB1). In vitro, chloroacetanilide N-alkylformylase assays
CC in which CndB1 is substituted for CndB2 demonstrate that the two
CC enzymes possess nearly identical activities.
CC {ECO:0000269|PubMed:24928877}.
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DR EMBL; KJ461679; AIA08943.1; -; Genomic_DNA.
DR EMBL; CP021186; ARR57849.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A059WLZ7; -.
DR SMR; A0A059WLZ7; -.
DR EnsemblBacteria; ARR57849; ARR57849; HY78_30640.
DR KEGG; ag:AIA08943; -.
DR KEGG; sphd:HY78_30640; -.
DR BioCyc; MetaCyc:MON-19784; -.
DR BRENDA; 1.14.15.23; 13073.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 2.102.10.10; -; 1.
DR InterPro; IPR017941; Rieske_2Fe-2S.
DR InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR InterPro; IPR044043; VanA_C_cat.
DR Pfam; PF00355; Rieske; 1.
DR Pfam; PF19112; VanA_C; 1.
DR SUPFAM; SSF50022; SSF50022; 1.
DR PROSITE; PS51296; RIESKE; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; Aromatic hydrocarbons catabolism; Iron; Iron-sulfur; Metal-binding;
KW Oxidoreductase; Plasmid.
FT CHAIN 1..348
FT /note="Chloroacetanilide N-alkylformylase, oxygenase
FT component"
FT /id="PRO_0000445251"
FT DOMAIN 7..108
FT /note="Rieske"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 47
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250|UniProtKB:Q5S3I3"
FT BINDING 49
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250|UniProtKB:Q5S3I3"
FT BINDING 66
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250|UniProtKB:Q5S3I3"
FT BINDING 69
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250|UniProtKB:Q5S3I3"
FT BINDING 159
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:Q5S3I3"
FT BINDING 164
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:Q5S3I3"
FT BINDING 250
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q5S3I3"
FT BINDING 293
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:Q5S3I3"
FT SITE 153
FT /note="Plays a role in the stabilization the metal
FT coordination"
FT /evidence="ECO:0000250|UniProtKB:Q5S3I3"
SQ SEQUENCE 348 AA; 38664 MW; 2DD4F4D52883F55C CRC64;
MFLQNAWYAV AWCDEVTDGI VTRKVLGREL ALFRDGEGQP RAILNRCPHR FAPLSLGKRI
GDAIQCPYHG LHFGPDGRCV HNPHGDGVVP DVATPTFPAR ERHKLIWAWM GDPALATDDI
AGGEYGYLDD VELDLLPRGH LHLDCDYRLV IDNLMDPAHV AVLHDSALAS EALIRAVPRV
WREEDVIRVE SWAPDSKPSF LFGAWLGNHD DPVDHWVASR WQAAGLLSVE GGVVAVGGDR
EDGLRVRGAH MITPETETSA HYFWAVVRNF REDDAEQSEQ IRATTAAIFT GEDKWMLEAI
ERSMDGEEFW SLRPAILGTD RAAVMVRRAL ESEIKAEGRP KVVAVSAG
