TFTC_BURCE
ID TFTC_BURCE Reviewed; 179 AA.
AC O87008;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=NADH:FAD oxidoreductase;
DE EC=1.5.1.37;
DE AltName: Full=Chlorophenol-4-monooxygenase component 1;
DE AltName: Full=Two component enzyme C;
GN Name=tftC;
OS Burkholderia cepacia (Pseudomonas cepacia).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=AC1100;
RX PubMed=9603818; DOI=10.1128/aem.64.6.2086-2093.1998;
RA Hubner A., Danganan C.E., Xun L., Chakrabarty A.M., Hendrickson W.;
RT "Genes for 2,4,5-trichlorophenoxyacetic acid metabolism in Burkholderia
RT cepacia AC1100: characterization of the tftC and tftD genes and locations
RT of the tft operons on multiple replicons.";
RL Appl. Environ. Microbiol. 64:2086-2093(1998).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=AC1100;
RX PubMed=12700257; DOI=10.1128/jb.185.9.2786-2792.2003;
RA Gisi M.R., Xun L.;
RT "Characterization of chlorophenol 4-monooxygenase (TftD) and NADH:flavin
RT adenine dinucleotide oxidoreductase (TftC) of Burkholderia cepacia
RT AC1100.";
RL J. Bacteriol. 185:2786-2792(2003).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH FAD AND NAD,
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=19915006; DOI=10.1074/jbc.m109.056135;
RA Webb B.N., Ballinger J.W., Kim E., Belchik S.M., Lam K.S., Youn B.,
RA Nissen M.S., Xun L., Kang C.;
RT "Characterization of chlorophenol 4-monooxygenase (TftD) and NADH:FAD
RT oxidoreductase (TftC) of Burkholderia cepacia AC1100.";
RL J. Biol. Chem. 285:2014-2027(2010).
CC -!- FUNCTION: Reductase component of a two-component system that degrades
CC 2,4,5-trichlorophenol. TftC provides the FADH(2) required by TftD. TftD
CC oxidizes 2,4,5-trichlorophenol (2,4,5-TCP) to 2,5-dichloro-p-
CC benzoquinone, which is chemically reduced to 2,5-dichloro-p-
CC hydroquinone (2,5-DiCHQ). Then, TftD oxidizes the latter to 5-chloro-2-
CC hydroxy-p-benzoquinone. {ECO:0000269|PubMed:12700257,
CC ECO:0000269|PubMed:19915006}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=FADH2 + NAD(+) = FAD + 2 H(+) + NADH; Xref=Rhea:RHEA:30147,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57692,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:58307; EC=1.5.1.37;
CC Evidence={ECO:0000269|PubMed:12700257, ECO:0000269|PubMed:19915006};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=10.3 uM for FMN (with fixed NADH concentration at 300 uM)
CC {ECO:0000269|PubMed:12700257, ECO:0000269|PubMed:19915006};
CC KM=2.0 uM for FAD {ECO:0000269|PubMed:12700257,
CC ECO:0000269|PubMed:19915006};
CC KM=4.8 uM for FAD (with fixed NADH concentration at 300 uM)
CC {ECO:0000269|PubMed:12700257, ECO:0000269|PubMed:19915006};
CC KM=45.3 uM for NADH {ECO:0000269|PubMed:12700257,
CC ECO:0000269|PubMed:19915006};
CC KM=40.1 uM for NADH (with fixed FAD concentration at 18 uM)
CC {ECO:0000269|PubMed:12700257, ECO:0000269|PubMed:19915006};
CC KM=164.0 uM for NADH (with fixed FMN concentration at 20 uM)
CC {ECO:0000269|PubMed:12700257, ECO:0000269|PubMed:19915006};
CC Vmax=120 umol/min/mg enzyme {ECO:0000269|PubMed:12700257,
CC ECO:0000269|PubMed:19915006};
CC -!- PATHWAY: Xenobiotic degradation.
CC -!- SUBUNIT: Homodimer. The chlorophenol-4-monooxygenase is composed of an
CC oxygenase component TftD and a reductase component TftC.
CC {ECO:0000269|PubMed:19915006}.
CC -!- SIMILARITY: Belongs to the non-flavoprotein flavin reductase family.
CC {ECO:0000305}.
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DR EMBL; U83405; AAC23547.1; -; Genomic_DNA.
DR PDB; 3K86; X-ray; 2.00 A; A/B=1-179.
DR PDB; 3K87; X-ray; 2.00 A; A/B=1-179.
DR PDB; 3K88; X-ray; 2.00 A; A/B=1-179.
DR PDBsum; 3K86; -.
DR PDBsum; 3K87; -.
DR PDBsum; 3K88; -.
DR AlphaFoldDB; O87008; -.
DR SMR; O87008; -.
DR PRIDE; O87008; -.
DR KEGG; ag:AAC23547; -.
DR BioCyc; MetaCyc:MON-14673; -.
DR BRENDA; 1.5.1.37; 1028.
DR SABIO-RK; O87008; -.
DR EvolutionaryTrace; O87008; -.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0016646; F:oxidoreductase activity, acting on the CH-NH group of donors, NAD or NADP as acceptor; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 2.30.110.10; -; 1.
DR InterPro; IPR002563; Flavin_Rdtase-like_dom.
DR InterPro; IPR012349; Split_barrel_FMN-bd.
DR Pfam; PF01613; Flavin_Reduct; 1.
DR SMART; SM00903; Flavin_Reduct; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aromatic hydrocarbons catabolism; FAD; Flavoprotein;
KW Monooxygenase; NAD; Nucleotide-binding; Oxidoreductase.
FT CHAIN 1..179
FT /note="NADH:FAD oxidoreductase"
FT /id="PRO_0000418739"
FT BINDING 48..51
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:19915006"
FT BINDING 54..57
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:19915006"
FT BINDING 65..71
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:19915006"
FT BINDING 99
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:19915006"
FT BINDING 104..109
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:19915006"
FT BINDING 144
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:19915006"
FT BINDING 145
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:19915006"
FT BINDING 166..169
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:19915006"
FT BINDING 166
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:19915006"
FT HELIX 19..26
FT /evidence="ECO:0007829|PDB:3K86"
FT STRAND 29..32
FT /evidence="ECO:0007829|PDB:3K86"
FT STRAND 34..38
FT /evidence="ECO:0007829|PDB:3K86"
FT STRAND 45..49
FT /evidence="ECO:0007829|PDB:3K86"
FT STRAND 52..56
FT /evidence="ECO:0007829|PDB:3K86"
FT TURN 57..60
FT /evidence="ECO:0007829|PDB:3K86"
FT STRAND 61..67
FT /evidence="ECO:0007829|PDB:3K86"
FT HELIX 71..79
FT /evidence="ECO:0007829|PDB:3K86"
FT STRAND 81..86
FT /evidence="ECO:0007829|PDB:3K86"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:3K86"
FT HELIX 92..98
FT /evidence="ECO:0007829|PDB:3K86"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:3K86"
FT HELIX 106..108
FT /evidence="ECO:0007829|PDB:3K86"
FT STRAND 119..122
FT /evidence="ECO:0007829|PDB:3K86"
FT STRAND 128..142
FT /evidence="ECO:0007829|PDB:3K86"
FT STRAND 145..156
FT /evidence="ECO:0007829|PDB:3K86"
FT STRAND 165..167
FT /evidence="ECO:0007829|PDB:3K86"
FT STRAND 170..175
FT /evidence="ECO:0007829|PDB:3K86"
SQ 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
