ID   DDMB_STEMA              Reviewed;         105 AA.
AC   Q5S3I4;
DT   10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 63.
DE   RecName: Full=Dicamba O-demethylase, ferredoxin component {ECO:0000303|PubMed:16535584};
GN   Name=ddmB {ECO:0000303|PubMed:15855162};
OS   Stenotrophomonas maltophilia (Pseudomonas maltophilia) (Xanthomonas
OS   maltophilia).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas maltophilia group.
OX   NCBI_TaxID=40324;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBUNIT.
RC   STRAIN=DI-6 {ECO:0000312|EMBL:AAV53698.1};
RX   PubMed=15855162; DOI=10.1074/jbc.m500597200;
RA   Herman P.L., Behrens M., Chakraborty S., Chrastil B.M., Barycki J.,
RA   Weeks D.P.;
RT   "A three-component dicamba O-demethylase from Pseudomonas maltophilia,
RT   strain DI-6: gene isolation, characterization, and heterologous
RT   expression.";
RL   J. Biol. Chem. 280:24759-24767(2005).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-26, FUNCTION, COFACTOR, AND SUBUNIT.
RC   STRAIN=DI-6;
RX   PubMed=15820213; DOI=10.1016/j.abb.2005.02.024;
RA   Chakraborty S., Behrens M., Herman P.L., Arendsen A.F., Hagen W.R.,
RA   Carlson D.L., Wang X.Z., Weeks D.P.;
RT   "A three-component dicamba O-demethylase from Pseudomonas maltophilia,
RT   strain DI-6: purification and characterization.";
RL   Arch. Biochem. Biophys. 437:20-28(2005).
RN   [3]
RP   FUNCTION, AND SUBUNIT.
RC   STRAIN=DI-6;
RX   PubMed=16535584; DOI=10.1128/aem.63.4.1623-1626.1997;
RA   Wang X., Li B., Herman P.L., Weeks D.P.;
RT   "A three-component enzyme system catalyzes the O-demethylation of the
RT   herbicide dicamba in Pseudomonas maltophilia DI-6.";
RL   Appl. Environ. Microbiol. 63:1623-1626(1997).
CC   -!- FUNCTION: Component of the dicamba O-demethylase multicomponent enzyme
CC       system involved in the degradation of the herbicide dicamba
CC       (PubMed:15855162, PubMed:15820213, PubMed:16535584). In vitro,
CC       functions as an intermediate electron transfer protein
CC       (PubMed:15855162, PubMed:15820213, PubMed:16535584).
CC       {ECO:0000269|PubMed:15820213, ECO:0000269|PubMed:15855162,
CC       ECO:0000269|PubMed:16535584}.
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC         Evidence={ECO:0000269|PubMed:15820213};
CC       Note=Binds 1 [2Fe-2S] cluster. {ECO:0000250|UniProtKB:P80306};
CC   -!- SUBUNIT: Monomer (PubMed:15820213). The dicamba O-demethylase
CC       multicomponent enzyme system is composed of an oxygenase component
CC       (DdmC) and an electron transfer component formed by a ferredoxin
CC       reductase (DdmA1) and a ferredoxin (DdmB) (PubMed:15855162,
CC       PubMed:15820213, PubMed:16535584). In vitro, dicamba O-demethylase
CC       assays in which DdmA2 is substituted for DdmA1 demonstrate that the two
CC       enzymes possess nearly identical activities (PubMed:15855162).
CC       {ECO:0000269|PubMed:15820213, ECO:0000269|PubMed:15855162,
CC       ECO:0000269|PubMed:16535584}.
CC   -!- SIMILARITY: Belongs to the adrenodoxin/putidaredoxin family.
CC       {ECO:0000305}.
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DR   EMBL; AY786442; AAV53698.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q5S3I4; -.
DR   SMR; Q5S3I4; -.
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; Direct protein sequencing; Electron transport; Iron; Iron-sulfur;
KW   Metal-binding; Transport.
FT   CHAIN           1..105
FT                   /note="Dicamba O-demethylase, ferredoxin component"
FT                   /id="PRO_0000445254"
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;  11421 MW;  1091FE9A889F73C8 CRC64;
     MPQITVVNQS GEESSVEASE GRTLMEVIRD SGFDELLALC GGCCSCATCH VHIDPAFMDK
     LPEMSEDEND LLDSSDHRNE YSRLSCQIPV TGALEGIKVT IAQED