CNDC1_RHIWD
ID CNDC1_RHIWD Reviewed; 410 AA.
AC X5CY81;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 11-JUN-2014, sequence version 1.
DT 03-AUG-2022, entry version 37.
DE RecName: Full=Chloroacetanilide N-alkylformylase, ferredoxin reductase component {ECO:0000303|PubMed:24928877};
DE AltName: Full=Ferredoxin--NAD(+) reductase {ECO:0000305|PubMed:24928877};
DE EC=1.18.1.3 {ECO:0000305|PubMed:24928877};
GN Name=cndC1 {ECO:0000303|PubMed:24928877};
GN ORFNames=HY78_15240 {ECO:0000312|EMBL:ARR54690.1};
OS Rhizorhabdus wittichii (strain DC-6 / KACC 16600) (Sphingomonas wittichii).
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, AND SUBUNIT.
RC STRAIN=DC-6 / KACC 16600;
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;
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 transfers of electrons
CC from ferredoxin (CndB1) to NADH. N-dealkylase utilizes NADH, but not
CC NADPH, as the electron donor. {ECO:0000269|PubMed:24928877}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + NAD(+) + 2 reduced [2Fe-2S]-[ferredoxin] = NADH + 2
CC oxidized [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:16521, Rhea:RHEA-
CC COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.18.1.3;
CC Evidence={ECO:0000305|PubMed:24928877};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:P16640};
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}.
CC -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase family.
CC {ECO:0000305}.
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DR EMBL; KJ020540; AHW42445.1; -; Genomic_DNA.
DR EMBL; CP021181; ARR54690.1; -; Genomic_DNA.
DR AlphaFoldDB; X5CY81; -.
DR SMR; X5CY81; -.
DR EnsemblBacteria; ARR54690; ARR54690; HY78_15240.
DR KEGG; sphd:HY78_15240; -.
DR GO; GO:0008860; F:ferredoxin-NAD+ reductase activity; IDA:UniProtKB.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; ISS:UniProtKB.
DR Gene3D; 3.30.390.30; -; 1.
DR Gene3D; 3.50.50.60; -; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR InterPro; IPR028202; Reductase_C.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF14759; Reductase_C; 1.
DR SUPFAM; SSF51905; SSF51905; 2.
DR SUPFAM; SSF55424; SSF55424; 1.
PE 1: Evidence at protein level;
KW FAD; Flavoprotein; NAD; Oxidoreductase.
FT CHAIN 1..410
FT /note="Chloroacetanilide N-alkylformylase, ferredoxin
FT reductase component"
FT /id="PRO_0000445250"
FT BINDING 14
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P16640"
FT BINDING 36
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P16640"
FT BINDING 49
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P16640"
FT BINDING 82
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P16640"
FT BINDING 130
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P16640"
FT BINDING 279
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P16640"
FT BINDING 298
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P16640"
SQ SEQUENCE 410 AA; 43440 MW; 7EB5E2BD82DF54F2 CRC64;
MAQYDVLIVG AGHGGAQAAV ALRQNKFEGT IAIVGDEPEL PYERPPLSKE YFSGEKSFDR
ILIRPATFWA ERNVDMLLGK RVASVDPAGH SVTLTDGSTI GYGKLVWATG GAPRKLACSG
HHLSGVHGVR TREDADRMLG EMERTTSVVV IGGGYIGLEA AAVLSKAGKK VTVLEALDRV
LARVAGEALS RFYEAEHRAH GVDVQLGAKV DCIVGDDQDR VTGVQMHDGS VIPADMVIVG
IGIIPAVEPL IAAGAAGGNG VDVDEYCRTS LPDIYAIGDC AMHANAFAEG ARIRLESVQN
ANDQATTAAK HILGGTDAYH AVPWFWSNQY DLRLQTMGLS IGYDETIVRG DPANRSFSVV
YLKNGRVLAL DCVNAVKDYV QGKALVTGGV SPDKASLANP EIPLKTLLPA
