DNTAD_BURSR
ID DNTAD_BURSR Reviewed; 194 AA.
AC Q45696;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=2,4-dinitrotoluene dioxygenase system, small oxygenase component {ECO:0000305};
DE AltName: Full=2,4-dinitrotoluene dioxygenase ISP beta {ECO:0000305};
DE AltName: Full=2,4-dinitrotoluene dioxygenase subunit beta {ECO:0000303|PubMed:8759857};
GN Name=dntAd {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, SUBSTRATE SPECIFICITY, AND
RP SUBUNIT.
RC STRAIN=DNT {ECO:0000312|EMBL:AAB09767.1};
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 beta subunit seems to
CC have a structural role in the holoenzyme. Also able to convert
CC naphthalene to cis-(1R,2S)-dihydroxy-1,2-dihydronaphthalene.
CC {ECO:0000269|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 beta subunit family. {ECO:0000305}.
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DR EMBL; U62430; AAB09767.1; -; Genomic_DNA.
DR AlphaFoldDB; Q45696; -.
DR SMR; Q45696; -.
DR KEGG; ag:AAB09767; -.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0071704; P:organic substance metabolic process; IEA:UniProt.
DR CDD; cd00667; ring_hydroxylating_dioxygenases_beta; 1.
DR InterPro; IPR032710; NTF2-like_dom_sf.
DR InterPro; IPR000391; Rng_hydr_dOase-bsu.
DR PANTHER; PTHR41534; PTHR41534; 1.
DR Pfam; PF00866; Ring_hydroxyl_B; 1.
DR SUPFAM; SSF54427; SSF54427; 1.
PE 1: Evidence at protein level;
KW Aromatic hydrocarbons catabolism; Dioxygenase; Oxidoreductase.
FT CHAIN 1..194
FT /note="2,4-dinitrotoluene dioxygenase system, small
FT oxygenase component"
FT /id="PRO_0000442190"
SQ SEQUENCE 194 AA; 23037 MW; F08C488CC0AA61A5 CRC64;
MMINTQEDKL VSAHDAEEFH RFFVGHDSDL QQEVTTLLTR EADLLDIQAY KAWLEHCVAP
EIKYQVISRE LRSTSERRYQ LNDAVNIYNE NYQQLKVRVE HQMDPQNWYN SPKIRFTRFV
TNVTAAKDKS APEMLHVRSN LILHRARRGN QVDVFYATRE DKWKRIEGGG IKLVERFVDY
PERSPQTHNL MIFL