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Protein

5'-fluoro-5'-deoxy-adenosine synthase

Gene

flA

Organism
Streptomyces cattleya
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.6 Publications

Catalytic activityi

S-adenosyl-L-methionine + fluoride = 5'-deoxy-5'-fluoroadenosine + L-methionine.3 Publications

Enzyme regulationi

Competitively inhibited by S-adenosyl-L-homocysteine (AdoHcy) and S-adenosyl-L-homocysteine (SAH). Sinefungin is only weakly inhibitory.1 Publication

Kineticsi

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).2 Publications

  1. KM=6.5 µM for SAM (at pH 7.8 and degrees Celsius)1 Publication
  2. KM=74 µM for SAM (at pH 7.9 and 37 degrees Celsius)1 Publication
  3. KM=0.42 mM for SAM (at pH 7.8 and 25 degrees Celsius)1 Publication
  4. KM=2 mM for fluoride (at pH 7.9 and 37 degrees Celsius)1 Publication
  5. KM=8.56 mM for fluoride (at pH 7.8 and 25 degrees Celsius)1 Publication
  6. KM=10.2 mM for fluoride (at pH 7.8 and degrees Celsius)1 Publication
  1. Vmax=1.28 µmol/min/mg enzyme toward SAM (at pH 7.8 and 25 degrees Celsius)1 Publication
  2. Vmax=1.59 µmol/min/mg enzyme toward fluoride (at pH 7.8 and 25 degrees Celsius)1 Publication

Temperature dependencei

Optimum temperature is 55 degrees Celsius.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei16 – 161S-adenosyl-L-methionine6 Publications
Binding sitei77 – 771S-adenosyl-L-methionine6 Publications
Binding sitei158 – 1581S-adenosyl-L-methionine6 Publications
Binding sitei210 – 2101S-adenosyl-L-methionine6 Publications
Binding sitei215 – 2151S-adenosyl-L-methionine6 Publications

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Ligandi

S-adenosyl-L-methionine

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-15922.
SABIO-RKQ70GK9.

Names & Taxonomyi

Protein namesi
Recommended name:
5'-fluoro-5'-deoxy-adenosine synthase1 Publication (EC:2.5.1.633 Publications)
Short name:
5'-FDAS1 Publication
Alternative name(s):
5'-fluorodeoxyadenosine synthase1 Publication
Fluorinase1 Publication
Gene namesi
Name:flA1 Publication
OrganismiStreptomyces cattleya
Taxonomic identifieri29303 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomyces

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi16 – 161D → A: Loss of 5'-FDA synthase activity. 1 Publication
Mutagenesisi16 – 161D → N: Loss of 5'-FDA synthase activity. 1 Publication
Mutagenesisi16 – 161D → S: Loss of 5'-FDA synthase activity. 1 Publication
Mutagenesisi80 – 801T → 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. 1 Publication
Mutagenesisi80 – 801T → S: The 5'-FDA synthase activity and the affinity binding for S-adenosyl-L-methionine and fuoride are similar to the wild-type. 1 Publication
Mutagenesisi156 – 1561F → A: Weak 5'-FDA synthase activity. 1 Publication
Mutagenesisi156 – 1561F → V: Weak 5'-FDA synthase activity. 1 Publication
Mutagenesisi158 – 1581S → 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. 1 Publication
Mutagenesisi158 – 1581S → G: Weak 5'-FDA synthase activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 2992985'-fluoro-5'-deoxy-adenosine synthasePRO_0000430663Add
BLAST

Interactioni

Subunit structurei

Homohexamer; dimers of trimer.7 Publications

Protein-protein interaction databases

STRINGi1003195.SCAT_4165.

Structurei

Secondary structure

1
299
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi10 – 178Combined sources
Beta strandi19 – 224Combined sources
Helixi23 – 3412Combined sources
Beta strandi39 – 457Combined sources
Helixi52 – 576Combined sources
Turni58 – 614Combined sources
Helixi63 – 653Combined sources
Beta strandi71 – 755Combined sources
Turni78 – 814Combined sources
Beta strandi87 – 926Combined sources
Turni98 – 1014Combined sources
Beta strandi105 – 1073Combined sources
Beta strandi118 – 1214Combined sources
Beta strandi123 – 1253Combined sources
Helixi128 – 1347Combined sources
Beta strandi136 – 1416Combined sources
Turni145 – 1473Combined sources
Beta strandi148 – 1514Combined sources
Helixi157 – 1604Combined sources
Helixi163 – 1708Combined sources
Helixi175 – 1773Combined sources
Beta strandi178 – 1814Combined sources
Helixi184 – 1863Combined sources
Beta strandi196 – 1983Combined sources
Beta strandi201 – 21010Combined sources
Turni211 – 2144Combined sources
Beta strandi215 – 2217Combined sources
Helixi222 – 2265Combined sources
Turni227 – 2293Combined sources
Beta strandi235 – 2406Combined sources
Turni241 – 2433Combined sources
Beta strandi244 – 25310Combined sources
Helixi254 – 2574Combined sources
Beta strandi263 – 2675Combined sources
Beta strandi271 – 2777Combined sources
Helixi283 – 2864Combined sources
Beta strandi293 – 2975Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RQPX-ray1.80A/B/C1-299[»]
1RQRX-ray2.67A/B/C1-299[»]
2C2WX-ray2.00A/B/C1-299[»]
2C4TX-ray2.30A/B/C1-299[»]
2C4UX-ray2.50A/B/C/D/E/F1-299[»]
2C5BX-ray2.50A/B/C1-299[»]
2C5HX-ray2.70A/B/C1-299[»]
2CBXX-ray2.00A/B/C1-299[»]
2CC2X-ray2.00A/B/C1-299[»]
2V7TX-ray2.15A/B/C1-299[»]
2V7UX-ray2.00A/B/C1-299[»]
2V7VX-ray1.94A/B/C1-299[»]
2V7WX-ray1.90A/B/C1-299[»]
2V7XX-ray1.96A/B/C1-299[»]
4CQJX-ray2.44A/B/C1-299[»]
5FIUX-ray1.84A/B/C1-299[»]
ProteinModelPortaliQ70GK9.
SMRiQ70GK9. Positions 8-298.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ70GK9.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni21 – 233S-adenosyl-L-methionine binding6 Publications
Regioni269 – 2702S-adenosyl-L-methionine binding6 Publications
Regioni277 – 2793S-adenosyl-L-methionine binding6 Publications

Sequence similaritiesi

Belongs to the SalL family.Curated

Phylogenomic databases

eggNOGiENOG4107V4F. Bacteria.
COG1912. LUCA.

Family and domain databases

Gene3Di2.40.30.90. 1 hit.
InterProiIPR030978. Fluorinase.
IPR002747. SAM_Chlor/Fluor.
IPR023227. SAM_OH_AdoTrfase_C.
IPR023228. SAM_OH_AdoTrfase_N.
[Graphical view]
PfamiPF01887. SAM_adeno_trans. 2 hits.
[Graphical view]
SUPFAMiSSF101852. SSF101852. 1 hit.
SSF102522. SSF102522. 1 hit.
TIGRFAMsiTIGR04507. fluorinase. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q70GK9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAANSTRRPI IAFMSDLGTT DDSVAQCKGL MYSICPDVTV VDVCHSMTPW
60 70 80 90 100
DVEEGARYIV DLPRFFPEGT VFATTTYPAT GTTTRSVAVR IKQAAKGGAR
110 120 130 140 150
GQWAGSGAGF ERAEGSYIYI APNNGLLTTV LEEHGYLEAY EVTSPKVIPE
160 170 180 190 200
QPEPTFYSRE MVAIPSAHLA AGFPLSEVGR PLEDHEIVRF NRPAVEQDGE
210 220 230 240 250
ALVGVVSAID HPFGNVWTNI HRTDLEKAGI GYGARLRLTL DGVLPFEAPL
260 270 280 290
TPTFADAGEI GNIAIYLNSR GYLSIARNAA SLAYPYHLKE GMSARVEAR
Length:299
Mass (Da):32,370
Last modified:July 5, 2004 - v1
Checksum:i54697A2F68121731
GO

Mass spectrometryi

Molecular mass is 32200 Da from positions 2 - 299. Determined by ESI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ581748 Genomic DNA. Translation: CAE46446.1.
AM055586 Genomic DNA. Translation: CAJ20006.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ581748 Genomic DNA. Translation: CAE46446.1.
AM055586 Genomic DNA. Translation: CAJ20006.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RQPX-ray1.80A/B/C1-299[»]
1RQRX-ray2.67A/B/C1-299[»]
2C2WX-ray2.00A/B/C1-299[»]
2C4TX-ray2.30A/B/C1-299[»]
2C4UX-ray2.50A/B/C/D/E/F1-299[»]
2C5BX-ray2.50A/B/C1-299[»]
2C5HX-ray2.70A/B/C1-299[»]
2CBXX-ray2.00A/B/C1-299[»]
2CC2X-ray2.00A/B/C1-299[»]
2V7TX-ray2.15A/B/C1-299[»]
2V7UX-ray2.00A/B/C1-299[»]
2V7VX-ray1.94A/B/C1-299[»]
2V7WX-ray1.90A/B/C1-299[»]
2V7XX-ray1.96A/B/C1-299[»]
4CQJX-ray2.44A/B/C1-299[»]
5FIUX-ray1.84A/B/C1-299[»]
ProteinModelPortaliQ70GK9.
SMRiQ70GK9. Positions 8-298.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi1003195.SCAT_4165.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4107V4F. Bacteria.
COG1912. LUCA.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-15922.
SABIO-RKQ70GK9.

Miscellaneous databases

EvolutionaryTraceiQ70GK9.

Family and domain databases

Gene3Di2.40.30.90. 1 hit.
InterProiIPR030978. Fluorinase.
IPR002747. SAM_Chlor/Fluor.
IPR023227. SAM_OH_AdoTrfase_C.
IPR023228. SAM_OH_AdoTrfase_N.
[Graphical view]
PfamiPF01887. SAM_adeno_trans. 2 hits.
[Graphical view]
SUPFAMiSSF101852. SSF101852. 1 hit.
SSF102522. SSF102522. 1 hit.
TIGRFAMsiTIGR04507. fluorinase. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Crystal structure and mechanism of a bacterial fluorinating enzyme."
    Dong C., Huang F., Deng H., Schaffrath C., Spencer J.B., O'Hagan D., Naismith J.H.
    Nature 427:561-565(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH SUBSTRATES, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
  2. "The gene cluster for fluorometabolite biosynthesis in Streptomyces cattleya: a thioesterase confers resistance to fluoroacetyl-coenzyme A."
    Huang F., Haydock S.F., Spiteller D., Mironenko T., Li T.-L., O'Hagan D., Leadlay P.F., Spencer J.B.
    Chem. Biol. 13:475-484(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, ENZYME REGULATION.
  3. "Isolation and characterisation of 5'-fluorodeoxyadenosine synthase, a fluorination enzyme from Streptomyces cattleya."
    Schaffrath C., Deng H., O'Hagan D.
    FEBS Lett. 547:111-114(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-25, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, MASS SPECTROMETRY.
  4. "Substrates and inhibitors of the fluorinase from Streptomyces cattleya."
    Mcewan A.R., Deng H., Mcglinchey R.P., Robinson D.R., O'Hagan D., Naismith J.H.
    Submitted (OCT-2005) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS, SUBUNIT.
  5. Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS, FUNCTION, SUBUNIT.
  6. "Substrate specificity in enzymatic fluorination. The fluorinase from Streptomyces cattleya accepts 2'-deoxyadenosine substrates."
    Cobb S.L., Deng H., McEwan A.R., Naismith J.H., O'Hagan D., Robinson D.A.
    Org. Biomol. Chem. 4:1458-1460(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS)IN COMLEX WITH SUBSTRATE ANALOGS, FUNCTION, SUBSTRATE SPECIFICITY, SUBUNIT.
  7. "Mechanism of enzymatic fluorination in Streptomyces cattleya."
    Zhu X., Robinson D.A., McEwan A.R., O'Hagan D., Naismith J.H.
    J. Am. Chem. Soc. 129:14597-14604(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: 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, SUBUNIT.
  8. "Structure of a bacterial fluorinating enzyme with."
    Thomson S., Mcmahon S.A., Naismith J.H., O'Hagan D.
    Submitted (FEB-2014) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.44 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS, SUBUNIT.

Entry informationi

Entry nameiFLA_STRCT
AccessioniPrimary (citable) accession number: Q70GK9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 29, 2014
Last sequence update: July 5, 2004
Last modified: February 17, 2016
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.