ID   CNDB2_RHIWD             Reviewed;         105 AA.
AC   X5CWH9;
DT   10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT   11-JUN-2014, sequence version 1.
DT   03-AUG-2022, entry version 33.
DE   RecName: Full=Chloroacetanilide N-alkylformylase 2, ferredoxin component {ECO:0000303|PubMed:24928877};
DE   AltName: Full=Ferredoxin CndB2 {ECO:0000305|PubMed:24928877};
GN   Name=cndB2 {ECO:0000303|PubMed:24928877};
GN   ORFNames=HY78_13385 {ECO:0000312|EMBL:ARR54349.1};
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, 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, functions as an intermediate electron
CC       transfer protein. {ECO:0000269|PubMed:24928877}.
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC         Evidence={ECO:0000250|UniProtKB:P80306};
CC       Note=Binds 1 [2Fe-2S] cluster. {ECO:0000250|UniProtKB:P80306};
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 adrenodoxin/putidaredoxin family.
CC       {ECO:0000305}.
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DR   EMBL; KJ020543; AHW42449.1; -; Genomic_DNA.
DR   EMBL; CP021181; ARR54349.1; -; Genomic_DNA.
DR   AlphaFoldDB; X5CWH9; -.
DR   SMR; X5CWH9; -.
DR   EnsemblBacteria; ARR54349; ARR54349; HY78_13385.
DR   KEGG; sphd:HY78_13385; -.
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:0140647; P:P450-containing electron transport chain; IEA:InterPro.
DR   CDD; cd00207; fer2; 1.
DR   Gene3D; 3.10.20.30; -; 1.
DR   InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR   InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR   InterPro; IPR001055; Adrenodoxin.
DR   InterPro; IPR012675; Beta-grasp_dom_sf.
DR   PANTHER; PTHR23426; PTHR23426; 1.
DR   Pfam; PF00111; Fer2; 1.
DR   PRINTS; PR00355; ADRENODOXIN.
DR   SUPFAM; SSF54292; SSF54292; 1.
DR   PROSITE; PS51085; 2FE2S_FER_2; 1.
PE   1: Evidence at protein level;
KW   2Fe-2S; Electron transport; Iron; Iron-sulfur; Metal-binding; Transport.
FT   CHAIN           1..105
FT                   /note="Chloroacetanilide N-alkylformylase 2, ferredoxin
FT                   component"
FT                   /id="PRO_0000445253"
FT   DOMAIN          2..105
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   BINDING         40
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000250|UniProtKB:P80306"
FT   BINDING         46
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000250|UniProtKB:P80306"
FT   BINDING         49
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000250|UniProtKB:P80306"
FT   BINDING         86
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000250|UniProtKB:P80306"
SQ   SEQUENCE   105 AA;  11333 MW;  4EC69B921E19FE63 CRC64;
     MPKLVVVTRE GEESVIEAET GLSVMEVIRD AGIDELLALC GGCCSCATCH VFVDPAFNGL
     LPDMSDDEND LLDSSDHRDD RSRLSCQLTM TDELDGLTVT IAPED