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NADH:FAD oxidoreductase (EC 1.5.1.37) (Chlorophenol-4-monooxygenase component 1) (Two component enzyme C)

 TFTC_BURCE              Reviewed;         179 AA.
O87008;
05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
01-NOV-1998, sequence version 1.
28-FEB-2018, entry version 65.
RecName: Full=NADH:FAD oxidoreductase;
EC=1.5.1.37;
AltName: Full=Chlorophenol-4-monooxygenase component 1;
AltName: Full=Two component enzyme C;
Name=tftC;
Burkholderia cepacia (Pseudomonas cepacia).
Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
NCBI_TaxID=292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=AC1100;
PubMed=9603818;
Hubner A., Danganan C.E., Xun L., Chakrabarty A.M., Hendrickson W.;
"Genes for 2,4,5-trichlorophenoxyacetic acid metabolism in
Burkholderia cepacia AC1100: characterization of the tftC and tftD
genes and locations of the tft operons on multiple replicons.";
Appl. Environ. Microbiol. 64:2086-2093(1998).
[2]
FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
STRAIN=AC1100;
PubMed=12700257; DOI=10.1128/JB.185.9.2786-2792.2003;
Gisi M.R., Xun L.;
"Characterization of chlorophenol 4-monooxygenase (TftD) and
NADH:flavin adenine dinucleotide oxidoreductase (TftC) of Burkholderia
cepacia AC1100.";
J. Bacteriol. 185:2786-2792(2003).
[3]
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH FAD AND NAD,
FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND BIOPHYSICOCHEMICAL
PROPERTIES.
PubMed=19915006; DOI=10.1074/jbc.M109.056135;
Webb B.N., Ballinger J.W., Kim E., Belchik S.M., Lam K.S., Youn B.,
Nissen M.S., Xun L., Kang C.;
"Characterization of chlorophenol 4-monooxygenase (TftD) and NADH:FAD
oxidoreductase (TftC) of Burkholderia cepacia AC1100.";
J. Biol. Chem. 285:2014-2027(2010).
-!- FUNCTION: Reductase component of a two-component system that
degrades 2,4,5-trichlorophenol. TftC provides the FADH(2) required
by TftD. TftD oxidizes 2,4,5-trichlorophenol (2,4,5-TCP) to 2,5-
dichloro-p-benzoquinone, which is chemically reduced to 2,5-
dichloro-p-hydroquinone (2,5-DiCHQ). Then, TftD oxidizes the
latter to 5-chloro-2-hydroxy-p-benzoquinone.
{ECO:0000269|PubMed:12700257, ECO:0000269|PubMed:19915006}.
-!- CATALYTIC ACTIVITY: FADH(2) + NAD(+) = FAD + NADH.
{ECO:0000269|PubMed:12700257, ECO:0000269|PubMed:19915006}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=10.3 uM for FMN (with fixed NADH concentration at 300 uM)
{ECO:0000269|PubMed:12700257, ECO:0000269|PubMed:19915006};
KM=2.0 uM for FAD {ECO:0000269|PubMed:12700257,
ECO:0000269|PubMed:19915006};
KM=4.8 uM for FAD (with fixed NADH concentration at 300 uM)
{ECO:0000269|PubMed:12700257, ECO:0000269|PubMed:19915006};
KM=45.3 uM for NADH {ECO:0000269|PubMed:12700257,
ECO:0000269|PubMed:19915006};
KM=40.1 uM for NADH (with fixed FAD concentration at 18 uM)
{ECO:0000269|PubMed:12700257, ECO:0000269|PubMed:19915006};
KM=164.0 uM for NADH (with fixed FMN concentration at 20 uM)
{ECO:0000269|PubMed:12700257, ECO:0000269|PubMed:19915006};
Vmax=120 umol/min/mg enzyme {ECO:0000269|PubMed:12700257,
ECO:0000269|PubMed:19915006};
-!- PATHWAY: Xenobiotic degradation.
-!- SUBUNIT: Homodimer. The chlorophenol-4-monooxygenase is composed
of an oxygenase component TftD and a reductase component TftC.
{ECO:0000269|PubMed:19915006}.
-!- SIMILARITY: Belongs to the non-flavoprotein flavin reductase
family. {ECO:0000305}.
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EMBL; U83405; AAC23547.1; -; Genomic_DNA.
PDB; 3K86; X-ray; 2.00 A; A/B=1-179.
PDB; 3K87; X-ray; 2.00 A; A/B=1-179.
PDB; 3K88; X-ray; 2.00 A; A/B=1-179.
PDBsum; 3K86; -.
PDBsum; 3K87; -.
PDBsum; 3K88; -.
ProteinModelPortal; O87008; -.
SMR; O87008; -.
KEGG; ag:AAC23547; -.
KO; K15245; -.
BioCyc; MetaCyc:MONOMER-14673; -.
BRENDA; 1.5.1.37; 1028.
EvolutionaryTrace; O87008; -.
GO; GO:0010181; F:FMN binding; IEA:InterPro.
GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
GO; GO:0016646; F:oxidoreductase activity, acting on the CH-NH group of donors, NAD or NADP as acceptor; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
GO; GO:0055114; P:oxidation-reduction process; IDA:UniProtKB.
Gene3D; 2.30.110.10; -; 1.
InterPro; IPR002563; Flavin_Rdtase-like_dom.
InterPro; IPR012349; Split_barrel_FMN-bd.
Pfam; PF01613; Flavin_Reduct; 1.
SMART; SM00903; Flavin_Reduct; 1.
1: Evidence at protein level;
3D-structure; Aromatic hydrocarbons catabolism; FAD; Flavoprotein;
Monooxygenase; NAD; Nucleotide-binding; Oxidoreductase.
CHAIN 1 179 NADH:FAD oxidoreductase.
/FTId=PRO_0000418739.
NP_BIND 48 51 FAD. {ECO:0000269|PubMed:19915006}.
NP_BIND 54 57 NAD. {ECO:0000269|PubMed:19915006}.
NP_BIND 65 71 FAD. {ECO:0000269|PubMed:19915006}.
NP_BIND 104 109 FAD. {ECO:0000269|PubMed:19915006}.
NP_BIND 166 169 NAD. {ECO:0000269|PubMed:19915006}.
BINDING 99 99 FAD; via carbonyl oxygen.
{ECO:0000269|PubMed:19915006}.
BINDING 144 144 FAD. {ECO:0000269|PubMed:19915006}.
BINDING 145 145 NAD. {ECO:0000269|PubMed:19915006}.
BINDING 166 166 FAD. {ECO:0000269|PubMed:19915006}.
HELIX 19 26 {ECO:0000244|PDB:3K86}.
STRAND 29 32 {ECO:0000244|PDB:3K86}.
STRAND 34 38 {ECO:0000244|PDB:3K86}.
STRAND 45 49 {ECO:0000244|PDB:3K86}.
STRAND 52 56 {ECO:0000244|PDB:3K86}.
TURN 57 60 {ECO:0000244|PDB:3K86}.
STRAND 61 67 {ECO:0000244|PDB:3K86}.
HELIX 71 79 {ECO:0000244|PDB:3K86}.
STRAND 81 86 {ECO:0000244|PDB:3K86}.
HELIX 89 91 {ECO:0000244|PDB:3K86}.
HELIX 92 98 {ECO:0000244|PDB:3K86}.
HELIX 101 103 {ECO:0000244|PDB:3K86}.
HELIX 106 108 {ECO:0000244|PDB:3K86}.
STRAND 119 122 {ECO:0000244|PDB:3K86}.
STRAND 128 142 {ECO:0000244|PDB:3K86}.
STRAND 145 156 {ECO:0000244|PDB:3K86}.
STRAND 165 167 {ECO:0000244|PDB:3K86}.
STRAND 170 175 {ECO:0000244|PDB:3K86}.
SEQUENCE 179 AA; 19028 MW; 8944587144256B80 CRC64;
MHAGEAVQQL KKAFETVASF DFRDALSKAS TPVTVVATNG PFGLAGLTCS AVCSVCDRPP
TVLLCINRKS YAAGIIKSNG VLSVNWLAAG QAVISQTFAG VGSVPMEERF ADKGWQTIAT
GAPYRMDAAV SFDCTIANIV DVGSHSVIFA EVVARNHAEE CTPLIYHRRQ YATTRSLAE


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