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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

Manual assertion based on experiment ini

  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)DescriptionActionsGraphical viewLength
Binding sitei16S-adenosyl-L-methionine6 Publications1
Binding sitei77S-adenosyl-L-methionine6 Publications1
Binding sitei158S-adenosyl-L-methionine6 Publications1
Binding sitei210S-adenosyl-L-methionine6 Publications1
Binding sitei215S-adenosyl-L-methionine6 Publications1

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)DescriptionActionsGraphical viewLength
Mutagenesisi16D → A: Loss of 5'-FDA synthase activity. 1 Publication1
Mutagenesisi16D → N: Loss of 5'-FDA synthase activity. 1 Publication1
Mutagenesisi16D → S: Loss of 5'-FDA synthase activity. 1 Publication1
Mutagenesisi80T → 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 Publication1
Mutagenesisi80T → S: The 5'-FDA synthase activity and the affinity binding for S-adenosyl-L-methionine and fuoride are similar to the wild-type. 1 Publication1
Mutagenesisi156F → A: Weak 5'-FDA synthase activity. 1 Publication1
Mutagenesisi156F → V: Weak 5'-FDA synthase activity. 1 Publication1
Mutagenesisi158S → 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 Publication1
Mutagenesisi158S → G: Weak 5'-FDA synthase activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00004306632 – 2995'-fluoro-5'-deoxy-adenosine synthaseAdd BLAST298

Interactioni

Subunit structurei

Homohexamer; dimers of trimer.7 Publications

Protein-protein interaction databases

STRINGi1003195.SCAT_4165.

Structurei

Secondary structure

1299
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi10 – 17Combined sources8
Beta strandi19 – 22Combined sources4
Helixi23 – 34Combined sources12
Beta strandi39 – 45Combined sources7
Helixi52 – 57Combined sources6
Turni58 – 61Combined sources4
Helixi63 – 65Combined sources3
Beta strandi71 – 75Combined sources5
Turni78 – 81Combined sources4
Beta strandi87 – 92Combined sources6
Turni98 – 101Combined sources4
Beta strandi105 – 107Combined sources3
Beta strandi118 – 121Combined sources4
Beta strandi123 – 125Combined sources3
Helixi128 – 134Combined sources7
Beta strandi136 – 141Combined sources6
Turni145 – 147Combined sources3
Beta strandi148 – 151Combined sources4
Helixi157 – 160Combined sources4
Helixi163 – 170Combined sources8
Helixi175 – 177Combined sources3
Beta strandi178 – 181Combined sources4
Helixi184 – 186Combined sources3
Beta strandi196 – 198Combined sources3
Beta strandi201 – 210Combined sources10
Turni211 – 214Combined sources4
Beta strandi215 – 221Combined sources7
Helixi222 – 226Combined sources5
Turni227 – 229Combined sources3
Beta strandi235 – 240Combined sources6
Turni241 – 243Combined sources3
Beta strandi244 – 253Combined sources10
Helixi254 – 257Combined sources4
Beta strandi263 – 267Combined sources5
Beta strandi271 – 277Combined sources7
Helixi283 – 286Combined sources4
Beta strandi293 – 297Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ70GK9.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni21 – 23S-adenosyl-L-methionine binding6 Publications3
Regioni269 – 270S-adenosyl-L-methionine binding6 Publications2
Regioni277 – 279S-adenosyl-L-methionine binding6 Publications3

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
PDB 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.
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...

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: November 2, 2016
This is version 64 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.