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Entry version 75 (08 May 2019)
Sequence version 1 (05 Jul 2004)
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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

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

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

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>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)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>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

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionTransferase
LigandS-adenosyl-L-methionine

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
MetaCyc:MONOMER-15922

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
Q70GK9

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:flA1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiStreptomyces cattleya
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri29303 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomyces

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>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

Chemistry databases

Drug and drug target database

More...
DrugBanki
DB03716 5'-Fluoro-5'-Deoxyadenosine

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved1 Publication
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004306632 – 2995'-fluoro-5'-deoxy-adenosine synthaseAdd BLAST298

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homohexamer; dimers of trimer.7 Publications

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1299
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

More...
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[»]

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
Q70GK9

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
Q70GK9

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni21 – 23S-adenosyl-L-methionine binding6 Publications3
Regioni269 – 270S-adenosyl-L-methionine binding6 Publications2
Regioni277 – 279S-adenosyl-L-methionine binding6 Publications3

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the SalL family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG4107V4F Bacteria
COG1912 LUCA

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.40.30.90, 1 hit
3.40.50.10790, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR030978 Fluorinase
IPR002747 SAM_Chlor/Fluor
IPR023227 SAM_OH_AdoTrfase_C
IPR023228 SAM_OH_AdoTrfase_N

The PANTHER Classification System

More...
PANTHERi
PTHR35092 PTHR35092, 2 hits

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01887 SAM_adeno_trans, 2 hits

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF006779 UCP006779, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF101852 SSF101852, 1 hit
SSF102522 SSF102522, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR04507 fluorinase, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i54697A2F68121731
GO

<p>This subsection of the ‘Sequence’ section reports information derived from mass spectrometry experiments done on the entire protein or on biologically active derived peptide(s).<p><a href='/help/mass_spectrometry' target='_top'>More...</a></p>Mass spectrometryi

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

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AJ581748 Genomic DNA Translation: CAE46446.1
AM055586 Genomic DNA Translation: CAJ20006.1

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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[»]
SMRiQ70GK9
ModBaseiSearch...
MobiDBiSearch...

Chemistry databases

DrugBankiDB03716 5'-Fluoro-5'-Deoxyadenosine

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4107V4F Bacteria
COG1912 LUCA

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-15922
SABIO-RKiQ70GK9

Miscellaneous databases

EvolutionaryTraceiQ70GK9

Family and domain databases

Gene3Di2.40.30.90, 1 hit
3.40.50.10790, 1 hit
InterProiView protein in InterPro
IPR030978 Fluorinase
IPR002747 SAM_Chlor/Fluor
IPR023227 SAM_OH_AdoTrfase_C
IPR023228 SAM_OH_AdoTrfase_N
PANTHERiPTHR35092 PTHR35092, 2 hits
PfamiView protein in Pfam
PF01887 SAM_adeno_trans, 2 hits
PIRSFiPIRSF006779 UCP006779, 1 hit
SUPFAMiSSF101852 SSF101852, 1 hit
SSF102522 SSF102522, 1 hit
TIGRFAMsiTIGR04507 fluorinase, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiFLA_STRCT
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q70GK9
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 29, 2014
Last sequence update: July 5, 2004
Last modified: May 8, 2019
This is version 75 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>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
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