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5'-fluoro-5'-deoxy-adenosine synthase (5'-FDAS) (EC 2.5.1.63) (5'-fluorodeoxyadenosine synthase) (Fluorinase)

 FLA_STRCT               Reviewed;         299 AA.
Q70GK9;
29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
22-NOV-2017, entry version 70.
RecName: Full=5'-fluoro-5'-deoxy-adenosine synthase {ECO:0000303|PubMed:14765200};
Short=5'-FDAS {ECO:0000303|PubMed:14765200};
EC=2.5.1.63 {ECO:0000269|PubMed:12860396, ECO:0000269|PubMed:14765200, ECO:0000269|PubMed:17985882};
AltName: Full=5'-fluorodeoxyadenosine synthase {ECO:0000303|PubMed:12860396};
AltName: Full=Fluorinase {ECO:0000303|PubMed:16370017};
Name=flA {ECO:0000303|PubMed:14765200};
Streptomyces cattleya.
Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
Streptomyces.
NCBI_TaxID=29303;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (1.8
ANGSTROMS) IN COMPLEX WITH SUBSTRATES, FUNCTION, CATALYTIC ACTIVITY,
BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
PubMed=14765200; DOI=10.1038/nature02280;
Dong C., Huang F., Deng H., Schaffrath C., Spencer J.B., O'Hagan D.,
Naismith J.H.;
"Crystal structure and mechanism of a bacterial fluorinating enzyme.";
Nature 427:561-565(2004).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND ENZYME REGULATION.
PubMed=16720268; DOI=10.1016/j.chembiol.2006.02.014;
Huang F., Haydock S.F., Spiteller D., Mironenko T., Li T.-L.,
O'Hagan D., Leadlay P.F., Spencer J.B.;
"The gene cluster for fluorometabolite biosynthesis in Streptomyces
cattleya: a thioesterase confers resistance to fluoroacetyl-coenzyme
A.";
Chem. Biol. 13:475-484(2006).
[3]
PROTEIN SEQUENCE OF 2-25, FUNCTION, CATALYTIC ACTIVITY,
BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND MASS SPECTROMETRY.
PubMed=12860396; DOI=10.1016/S0014-5793(03)00688-4;
Schaffrath C., Deng H., O'Hagan D.;
"Isolation and characterisation of 5'-fluorodeoxyadenosine synthase, a
fluorination enzyme from Streptomyces cattleya.";
FEBS Lett. 547:111-114(2003).
[4]
X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH SUBSTRATE
ANALOGS, AND SUBUNIT.
Mcewan A.R., Deng H., Mcglinchey R.P., Robinson D.R., O'Hagan D.,
Naismith J.H.;
"Substrates and inhibitors of the fluorinase from Streptomyces
cattleya.";
Submitted (OCT-2005) to the PDB data bank.
[5]
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH SUBSTRATE
ANALOGS, FUNCTION, AND SUBUNIT.
PubMed=16370017; DOI=10.1002/anie.200503582;
Deng H., Cobb S.L., McEwan A.R., McGlinchey R.P., Naismith J.H.,
O'Hagan D., Robinson D.A., Spencer J.B.;
"The fluorinase from Streptomyces cattleya is also a chlorinase.";
Angew. Chem. Int. Ed. 45:759-762(2006).
[6]
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS)IN COMPLEX WITH SUBSTRATE
ANALOGS, FUNCTION, SUBSTRATE SPECIFICITY, AND SUBUNIT.
PubMed=16604208; DOI=10.1039/b600574h;
Cobb S.L., Deng H., McEwan A.R., Naismith J.H., O'Hagan D.,
Robinson D.A.;
"Substrate specificity in enzymatic fluorination. The fluorinase from
Streptomyces cattleya accepts 2'-deoxyadenosine substrates.";
Org. Biomol. Chem. 4:1458-1460(2006).
[7]
X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH SAM AND
SUBSTRATE ANALOGS, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF
ASP-16; THR-80; PHE-156 AND SER-158, BIOPHYSICOCHEMICAL PROPERTIES,
AND SUBUNIT.
PubMed=17985882; DOI=10.1021/ja0731569;
Zhu X., Robinson D.A., McEwan A.R., O'Hagan D., Naismith J.H.;
"Mechanism of enzymatic fluorination in Streptomyces cattleya.";
J. Am. Chem. Soc. 129:14597-14604(2007).
[8]
X-RAY CRYSTALLOGRAPHY (2.44 ANGSTROMS) IN COMPLEX WITH SUBSTRATE
ANALOGS, AND SUBUNIT.
Thomson S., Mcmahon S.A., Naismith J.H., O'Hagan D.;
"Structure of a bacterial fluorinating enzyme with.";
Submitted (FEB-2014) to the PDB data bank.
-!- FUNCTION: Involved in the biosynthesis of fluorometabolites.
Catalyzes the formation of a C-F bond by combining S-adenosyl-L-
methionine (SAM) and fluoride to generate 5'-fluoro-5'-
deoxyadenosine (5'-FDA) and L-methionine. It can also use 2'-
deoxyadenosine in place of adenosine as substrate.
{ECO:0000269|PubMed:12860396, ECO:0000269|PubMed:14765200,
ECO:0000269|PubMed:16370017, ECO:0000269|PubMed:16604208,
ECO:0000269|PubMed:16720268, ECO:0000269|PubMed:17985882}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + fluoride = 5'-deoxy-
5'-fluoroadenosine + L-methionine. {ECO:0000269|PubMed:12860396,
ECO:0000269|PubMed:14765200, ECO:0000269|PubMed:17985882}.
-!- ENZYME REGULATION: Competitively inhibited by S-adenosyl-L-
homocysteine (AdoHcy) and S-adenosyl-L-homocysteine (SAH).
Sinefungin is only weakly inhibitory.
{ECO:0000269|PubMed:16720268}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=6.5 uM for SAM (at pH 7.8 and degrees Celsius)
{ECO:0000269|PubMed:17985882};
KM=74 uM for SAM (at pH 7.9 and 37 degrees Celsius)
{ECO:0000269|PubMed:14765200};
KM=0.42 mM for SAM (at pH 7.8 and 25 degrees Celsius)
{ECO:0000269|PubMed:12860396};
KM=2 mM for fluoride (at pH 7.9 and 37 degrees Celsius)
{ECO:0000269|PubMed:14765200};
KM=8.56 mM for fluoride (at pH 7.8 and 25 degrees Celsius)
{ECO:0000269|PubMed:12860396};
KM=10.2 mM for fluoride (at pH 7.8 and degrees Celsius)
{ECO:0000269|PubMed:17985882};
Vmax=1.28 umol/min/mg enzyme toward SAM (at pH 7.8 and 25
degrees Celsius) {ECO:0000269|PubMed:12860396};
Vmax=1.59 umol/min/mg enzyme toward fluoride (at pH 7.8 and 25
degrees Celsius) {ECO:0000269|PubMed:12860396};
Note=Kcat is 0.07 sec(-1) for 5'-FDA synthase activity with SAM
as substrate(at pH 7.9 and 37 degrees Celsius). Kcat is 0.06
sec(-1) for 5'-FDA synthase activity with fluoride as substrate
(at pH 7.9 and 37 degrees Celsius).
{ECO:0000269|PubMed:14765200, ECO:0000269|PubMed:17985882};
Temperature dependence:
Optimum temperature is 55 degrees Celsius.
{ECO:0000269|PubMed:12860396};
-!- SUBUNIT: Homohexamer; dimers of trimer.
{ECO:0000269|PubMed:12860396, ECO:0000269|PubMed:14765200,
ECO:0000269|PubMed:16370017, ECO:0000269|PubMed:16604208,
ECO:0000269|PubMed:17985882, ECO:0000269|Ref.4,
ECO:0000269|Ref.8}.
-!- MASS SPECTROMETRY: Mass=32200; Method=Electrospray; Range=2-299;
Evidence={ECO:0000269|PubMed:12860396};
-!- SIMILARITY: Belongs to the SalL family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AJ581748; CAE46446.1; -; Genomic_DNA.
EMBL; AM055586; CAJ20006.1; -; Genomic_DNA.
PDB; 1RQP; X-ray; 1.80 A; A/B/C=1-299.
PDB; 1RQR; X-ray; 2.67 A; A/B/C=1-299.
PDB; 2C2W; X-ray; 2.00 A; A/B/C=1-299.
PDB; 2C4T; X-ray; 2.30 A; A/B/C=1-299.
PDB; 2C4U; X-ray; 2.50 A; A/B/C/D/E/F=1-299.
PDB; 2C5B; X-ray; 2.50 A; A/B/C=1-299.
PDB; 2C5H; X-ray; 2.70 A; A/B/C=1-299.
PDB; 2CBX; X-ray; 2.00 A; A/B/C=1-299.
PDB; 2CC2; X-ray; 2.00 A; A/B/C=1-299.
PDB; 2V7T; X-ray; 2.15 A; A/B/C=1-299.
PDB; 2V7U; X-ray; 2.00 A; A/B/C=1-299.
PDB; 2V7V; X-ray; 1.94 A; A/B/C=1-299.
PDB; 2V7W; X-ray; 1.90 A; A/B/C=1-299.
PDB; 2V7X; X-ray; 1.96 A; A/B/C=1-299.
PDB; 4CQJ; X-ray; 2.44 A; A/B/C=1-299.
PDB; 5FIU; X-ray; 1.84 A; A/B/C=1-299.
PDBsum; 1RQP; -.
PDBsum; 1RQR; -.
PDBsum; 2C2W; -.
PDBsum; 2C4T; -.
PDBsum; 2C4U; -.
PDBsum; 2C5B; -.
PDBsum; 2C5H; -.
PDBsum; 2CBX; -.
PDBsum; 2CC2; -.
PDBsum; 2V7T; -.
PDBsum; 2V7U; -.
PDBsum; 2V7V; -.
PDBsum; 2V7W; -.
PDBsum; 2V7X; -.
PDBsum; 4CQJ; -.
PDBsum; 5FIU; -.
ProteinModelPortal; Q70GK9; -.
SMR; Q70GK9; -.
DrugBank; DB03716; 5'-Fluoro-5'-Deoxyadenosine.
eggNOG; ENOG4107V4F; Bacteria.
eggNOG; COG1912; LUCA.
BioCyc; MetaCyc:MONOMER-15922; -.
SABIO-RK; Q70GK9; -.
EvolutionaryTrace; Q70GK9; -.
GO; GO:0033846; F:adenosyl-fluoride synthase activity; IEA:UniProtKB-EC.
Gene3D; 2.40.30.90; -; 1.
Gene3D; 3.40.50.10790; -; 1.
InterPro; IPR030978; Fluorinase.
InterPro; IPR002747; SAM_Chlor/Fluor.
InterPro; IPR023227; SAM_OH_AdoTrfase_C.
InterPro; IPR023228; SAM_OH_AdoTrfase_N.
PANTHER; PTHR35092; PTHR35092; 2.
Pfam; PF01887; SAM_adeno_trans; 2.
PIRSF; PIRSF006779; UCP006779; 1.
SUPFAM; SSF101852; SSF101852; 1.
SUPFAM; SSF102522; SSF102522; 1.
TIGRFAMs; TIGR04507; fluorinase; 1.
1: Evidence at protein level;
3D-structure; Direct protein sequencing; S-adenosyl-L-methionine;
Transferase.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:12860396}.
CHAIN 2 299 5'-fluoro-5'-deoxy-adenosine synthase.
/FTId=PRO_0000430663.
REGION 21 23 S-adenosyl-L-methionine binding.
{ECO:0000269|PubMed:14765200,
ECO:0000269|PubMed:16370017,
ECO:0000269|PubMed:16604208,
ECO:0000269|PubMed:17985882,
ECO:0000269|Ref.4, ECO:0000269|Ref.8}.
REGION 269 270 S-adenosyl-L-methionine binding.
{ECO:0000269|PubMed:14765200,
ECO:0000269|PubMed:16370017,
ECO:0000269|PubMed:16604208,
ECO:0000269|PubMed:17985882,
ECO:0000269|Ref.4, ECO:0000269|Ref.8}.
REGION 277 279 S-adenosyl-L-methionine binding.
{ECO:0000269|PubMed:14765200,
ECO:0000269|PubMed:16370017,
ECO:0000269|PubMed:16604208,
ECO:0000269|PubMed:17985882,
ECO:0000269|Ref.4, ECO:0000269|Ref.8}.
BINDING 16 16 S-adenosyl-L-methionine.
{ECO:0000269|PubMed:14765200,
ECO:0000269|PubMed:16370017,
ECO:0000269|PubMed:16604208,
ECO:0000269|PubMed:17985882,
ECO:0000269|Ref.4, ECO:0000269|Ref.8}.
BINDING 77 77 S-adenosyl-L-methionine.
{ECO:0000269|PubMed:14765200,
ECO:0000269|PubMed:16370017,
ECO:0000269|PubMed:16604208,
ECO:0000269|PubMed:17985882,
ECO:0000269|Ref.4, ECO:0000269|Ref.8}.
BINDING 158 158 S-adenosyl-L-methionine.
{ECO:0000269|PubMed:14765200,
ECO:0000269|PubMed:16370017,
ECO:0000269|PubMed:16604208,
ECO:0000269|PubMed:17985882,
ECO:0000269|Ref.4, ECO:0000269|Ref.8}.
BINDING 210 210 S-adenosyl-L-methionine.
{ECO:0000269|PubMed:14765200,
ECO:0000269|PubMed:16370017,
ECO:0000269|PubMed:16604208,
ECO:0000269|PubMed:17985882,
ECO:0000269|Ref.4, ECO:0000269|Ref.8}.
BINDING 215 215 S-adenosyl-L-methionine.
{ECO:0000269|PubMed:14765200,
ECO:0000269|PubMed:16370017,
ECO:0000269|PubMed:16604208,
ECO:0000269|PubMed:17985882,
ECO:0000269|Ref.4, ECO:0000269|Ref.8}.
MUTAGEN 16 16 D->A: Loss of 5'-FDA synthase activity.
{ECO:0000269|PubMed:17985882}.
MUTAGEN 16 16 D->N: Loss of 5'-FDA synthase activity.
{ECO:0000269|PubMed:17985882}.
MUTAGEN 16 16 D->S: Loss of 5'-FDA synthase activity.
{ECO:0000269|PubMed:17985882}.
MUTAGEN 80 80 T->A: Weak 5'-FDA synthase activity. 2-
fold increase of the affinity binding for
S-adenosyl-L-methionine and 4-fold
decrease of the affinity binding for
fluoride. {ECO:0000269|PubMed:17985882}.
MUTAGEN 80 80 T->S: The 5'-FDA synthase activity and
the affinity binding for S-adenosyl-L-
methionine and fuoride are similar to the
wild-type. {ECO:0000269|PubMed:17985882}.
MUTAGEN 156 156 F->A: Weak 5'-FDA synthase activity.
{ECO:0000269|PubMed:17985882}.
MUTAGEN 156 156 F->V: Weak 5'-FDA synthase activity.
{ECO:0000269|PubMed:17985882}.
MUTAGEN 158 158 S->A: The 5'-FDA synthase activity is 40%
of the wild-type. 2-fold increase of the
affinity binding for fluoride and 1.5-
fold decrease of the affinity binding for
S-adenosyl-L-methionine.
{ECO:0000269|PubMed:17985882}.
MUTAGEN 158 158 S->G: Weak 5'-FDA synthase activity.
{ECO:0000269|PubMed:17985882}.
STRAND 10 17 {ECO:0000244|PDB:1RQP}.
STRAND 19 22 {ECO:0000244|PDB:1RQP}.
HELIX 23 34 {ECO:0000244|PDB:1RQP}.
STRAND 39 45 {ECO:0000244|PDB:1RQP}.
HELIX 52 57 {ECO:0000244|PDB:1RQP}.
TURN 58 61 {ECO:0000244|PDB:1RQP}.
HELIX 63 65 {ECO:0000244|PDB:1RQP}.
STRAND 71 75 {ECO:0000244|PDB:1RQP}.
TURN 78 81 {ECO:0000244|PDB:1RQP}.
STRAND 87 92 {ECO:0000244|PDB:1RQP}.
TURN 98 101 {ECO:0000244|PDB:1RQP}.
STRAND 105 107 {ECO:0000244|PDB:1RQP}.
STRAND 118 121 {ECO:0000244|PDB:1RQP}.
STRAND 123 125 {ECO:0000244|PDB:1RQP}.
HELIX 128 134 {ECO:0000244|PDB:1RQP}.
STRAND 136 141 {ECO:0000244|PDB:1RQP}.
TURN 145 147 {ECO:0000244|PDB:1RQP}.
STRAND 148 151 {ECO:0000244|PDB:1RQP}.
HELIX 157 160 {ECO:0000244|PDB:1RQP}.
HELIX 163 170 {ECO:0000244|PDB:1RQP}.
HELIX 175 177 {ECO:0000244|PDB:1RQP}.
STRAND 178 181 {ECO:0000244|PDB:2C5B}.
HELIX 184 186 {ECO:0000244|PDB:1RQP}.
STRAND 196 198 {ECO:0000244|PDB:1RQP}.
STRAND 201 210 {ECO:0000244|PDB:1RQP}.
TURN 211 214 {ECO:0000244|PDB:1RQP}.
STRAND 215 221 {ECO:0000244|PDB:1RQP}.
HELIX 222 226 {ECO:0000244|PDB:1RQP}.
TURN 227 229 {ECO:0000244|PDB:1RQP}.
STRAND 235 240 {ECO:0000244|PDB:1RQP}.
TURN 241 243 {ECO:0000244|PDB:1RQP}.
STRAND 244 253 {ECO:0000244|PDB:1RQP}.
HELIX 254 257 {ECO:0000244|PDB:1RQP}.
STRAND 263 267 {ECO:0000244|PDB:1RQP}.
STRAND 271 277 {ECO:0000244|PDB:1RQP}.
HELIX 283 286 {ECO:0000244|PDB:1RQP}.
STRAND 293 297 {ECO:0000244|PDB:1RQP}.
SEQUENCE 299 AA; 32370 MW; 54697A2F68121731 CRC64;
MAANSTRRPI IAFMSDLGTT DDSVAQCKGL MYSICPDVTV VDVCHSMTPW DVEEGARYIV
DLPRFFPEGT VFATTTYPAT GTTTRSVAVR IKQAAKGGAR GQWAGSGAGF ERAEGSYIYI
APNNGLLTTV LEEHGYLEAY EVTSPKVIPE QPEPTFYSRE MVAIPSAHLA AGFPLSEVGR
PLEDHEIVRF NRPAVEQDGE ALVGVVSAID HPFGNVWTNI HRTDLEKAGI GYGARLRLTL
DGVLPFEAPL TPTFADAGEI GNIAIYLNSR GYLSIARNAA SLAYPYHLKE GMSARVEAR


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