DNTAA_BURSR
ID DNTAA_BURSR Reviewed; 346 AA.
AC Q45692;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=2,4-dinitrotoluene dioxygenase system ferredoxin--NAD(+), reductase component {ECO:0000303|PubMed:8759857};
DE EC=1.18.1.3 {ECO:0000305|PubMed:8759857};
DE AltName: Full=Ferredoxin--NAD(+) reductase (2,4-dinitrotoluene dioxygenase ferredoxin-specific) {ECO:0000303|PubMed:8759857};
GN Name=dntAa {ECO:0000303|PubMed:8759857};
OS Burkholderia sp. (strain RASC).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia.
OX NCBI_TaxID=69003;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP SUBSTRATE SPECIFICITY, AND SUBUNIT.
RC STRAIN=DNT {ECO:0000312|EMBL:AAB09763.1};
RX PubMed=8759857; DOI=10.1128/jb.178.16.4926-4934.1996;
RA Suen W.C., Haigler B.E., Spain J.C.;
RT "2,4-Dinitrotoluene dioxygenase from Burkholderia sp. strain DNT:
RT similarity to naphthalene dioxygenase.";
RL J. Bacteriol. 178:4926-4934(1996).
CC -!- FUNCTION: Component of the 2,4-dinitrotoluene dioxygenase (DNTDO)
CC multicomponent enzyme system which catalyzes the incorporation of both
CC atoms of molecular oxygen into 2,4-dinitrotoluene (DNT) to form 4-
CC methyl-5-nitrocatechol (MNC) and nitrite. Ferredoxin reductase
CC catalyzes the transfer of electrons from NADH to ferredoxin (DntAb).
CC Also able to convert naphthalene to cis-(1R,2S)-dihydroxy-1,2-
CC dihydronaphthalene. {ECO:0000269|PubMed:8759857}.
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:8759857};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00465};
CC Note=Binds 1 2Fe-2S cluster. {ECO:0000255|PROSITE-ProRule:PRU00465};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000305|PubMed:8759857};
CC -!- SUBUNIT: The 2,4-dinitrotoluene dioxygenase (DNTDO) multicomponent
CC enzyme system is composed of an electron transfer component and a
CC dioxygenase component (iron sulfur protein (ISP)). The electron
CC transfer component is composed of a ferredoxin reductase (DntAa) and a
CC ferredoxin (DntAb), and the dioxygenase component is formed of a large
CC alpha subunit (DntAc) and a small beta subunit (DntAd).
CC {ECO:0000305|PubMed:8759857}.
CC -!- SIMILARITY: Belongs to the bacterial ring-hydroxylating dioxygenase
CC ferredoxin reductase component family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U62430; AAB09763.1; -; Genomic_DNA.
DR AlphaFoldDB; Q45692; -.
DR SMR; Q45692; -.
DR KEGG; ag:AAB09763; -.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; ISS:UniProtKB.
DR GO; GO:0071949; F:FAD binding; ISS:UniProtKB.
DR GO; GO:0008860; F:ferredoxin-NAD+ reductase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR CDD; cd00207; fer2; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.40.50.80; -; 1.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR006058; 2Fe2S_fd_BS.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR008333; Cbr1-like_FAD-bd_dom.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR Pfam; PF00970; FAD_binding_6; 1.
DR Pfam; PF00111; Fer2; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR SUPFAM; SSF52343; SSF52343; 1.
DR SUPFAM; SSF54292; SSF54292; 1.
DR SUPFAM; SSF63380; SSF63380; 1.
DR PROSITE; PS00197; 2FE2S_FER_1; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; Aromatic hydrocarbons catabolism; FAD; Flavoprotein; Iron;
KW Iron-sulfur; Metal-binding; NAD; Oxidoreductase.
FT CHAIN 1..346
FT /note="2,4-dinitrotoluene dioxygenase system ferredoxin--
FT NAD(+), reductase component"
FT /id="PRO_0000442196"
FT DOMAIN 1..89
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT DOMAIN 96..193
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT BINDING 35
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 40
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 43
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 73
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
SQ SEQUENCE 346 AA; 37602 MW; 0BC3F4BF22C1547B CRC64;
MELVVEPLNL HLNAETGSTL LDVLRSNEVP ISYSCMSGRC GTCRCRVIAG HLRDNGPETG
RPQAGKGAYV LACQAVLTED CTIEIPESDE IVVHPARIVK GTVTAIDEAT HDIRRLRIKL
AKPLEFSPGQ YATVQFTPEC VRPYSMAGLP SDAEMEFQIR AVPGGHVSNY VFNELSVGAS
VRISGPLGTA YLRRTHTGPM LCVGGGTGLA PVLSIVRGAL ESGMSYPIHL YFGVRSEQDI
YDEERLHALA ARFPNLKVNV VVATGPAGPG HRSGLVTDLI GRDLPNLAGW RLHPVWRSGH
GRGPEPARCS PRHSTRAHPC RCVLSQRRLS EGTMRTQFNP RIPSHE
