DNTAC_BURSR
ID DNTAC_BURSR Reviewed; 451 AA.
AC Q45695;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=2,4-dinitrotoluene dioxygenase system, large oxygenase component {ECO:0000305};
DE EC=1.14.12.24 {ECO:0000305|PubMed:8759857};
DE AltName: Full=2,4-dinitrotoluene dioxygenase ISP alpha {ECO:0000303|PubMed:8759857};
DE AltName: Full=2,4-dinitrotoluene dioxygenase subunit alpha {ECO:0000303|PubMed:8759857};
GN Name=dntAc {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, SUBSTRATE
RP SPECIFICITY, AND SUBUNIT.
RC STRAIN=DNT {ECO:0000312|EMBL:AAB09766.1};
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. The alpha subunit has a
CC catalytic role in the holoenzyme. Also able to convert naphthalene to
CC cis-(1R,2S)-dihydroxy-1,2-dihydronaphthalene.
CC {ECO:0000269|PubMed:8759857}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2,4-dinitrotoluene + NADH + O2 = 4-methyl-5-nitrocatechol +
CC NAD(+) + nitrite; Xref=Rhea:RHEA:46760, ChEBI:CHEBI:920,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16301, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:81666; EC=1.14.12.24;
CC Evidence={ECO:0000305|PubMed:8759857};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000250|UniProtKB:P0A110,
CC ECO:0000255|PROSITE-ProRule:PRU00628};
CC Note=Binds 1 [2Fe-2S] cluster per subunit.
CC {ECO:0000250|UniProtKB:P0A110, ECO:0000255|PROSITE-ProRule:PRU00628};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000250|UniProtKB:P0A110};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250|UniProtKB:P0A110};
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 alpha subunit family. {ECO:0000305}.
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DR EMBL; U62430; AAB09766.1; -; Genomic_DNA.
DR AlphaFoldDB; Q45695; -.
DR SMR; Q45695; -.
DR KEGG; ag:AAB09766; -.
DR BioCyc; MetaCyc:MON-13335; -.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; ISS:UniProtKB.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0018625; F:naphthalene 1,2-dioxygenase activity; ISS:UniProtKB.
DR GO; GO:0016708; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of two atoms of oxygen into one donor; TAS:UniProtKB.
DR GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR CDD; cd08881; RHO_alpha_C_NDO-like; 1.
DR Gene3D; 2.102.10.10; -; 1.
DR InterPro; IPR043266; RHO_NdoB-like_C.
DR InterPro; IPR017941; Rieske_2Fe-2S.
DR InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR InterPro; IPR015881; Ring-hydroxy_dOase_2Fe2S_BS.
DR InterPro; IPR015879; Ring_hydroxy_dOase_asu_C_dom.
DR InterPro; IPR001663; Rng_hydr_dOase-A.
DR PANTHER; PTHR43756; PTHR43756; 1.
DR Pfam; PF00355; Rieske; 1.
DR Pfam; PF00848; Ring_hydroxyl_A; 1.
DR PRINTS; PR00090; RNGDIOXGNASE.
DR SUPFAM; SSF50022; SSF50022; 1.
DR PROSITE; PS51296; RIESKE; 1.
DR PROSITE; PS00570; RING_HYDROXYL_ALPHA; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; Aromatic hydrocarbons catabolism; Dioxygenase; Iron; Iron-sulfur;
KW Metal-binding; NAD; Oxidoreductase.
FT CHAIN 1..451
FT /note="2,4-dinitrotoluene dioxygenase system, large
FT oxygenase component"
FT /id="PRO_0000442188"
FT DOMAIN 42..126
FT /note="Rieske"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 84
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250|UniProtKB:P0A110,
FT ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 86
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250|UniProtKB:P0A110,
FT ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 104
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250|UniProtKB:P0A110,
FT ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 107
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250|UniProtKB:P0A110,
FT ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 211
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P0A110"
FT BINDING 216
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P0A110"
FT BINDING 365
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P0A110"
SQ SEQUENCE 451 AA; 49827 MW; 726796C29CEF9A10 CRC64;
MRQAIMSYQN LVSEAGLTQK HLIYGDKELF QHELKTIFAR NWLFLTHDSL IPSPGDYVKA
KMGVDEVIVS RQNDGSVRAF LNVCRHRGKT IVDAEAGNAK GFVCGYHGWG YGSNGELQSV
PFEKELYGDA IKKKCLGLKE VPRIESFHGF IYGCFDAEAP PLIDYLGDVA WYLEPTFKHS
GGLELVGPPA KVVVKGNWKV FAENFVGDIY HIGWTHASIL RAGQAIFAPL AGNAMLPPEG
TGLQATTKYG SGIGVSLDAY SGVQSADLVP EMMAFGGAKQ EKLAKEIGDV RARIYRSQVN
GTVFPNNCFL TGAGVFKVFN PIDENTTEAW TYAIVEKDMP EDLKRRLADA AQRSTGPAGY
WESDDNDNMV LSQNAKKYQS SNSDLIADLG FGKDVYGDEC YPGVVSKSAF SETNHRGFYR
AYQAHISSSN WAEFENTSRN WHTELTKTTD R
