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Protein

Adenosyl-chloride synthase

Gene

salL

Organism
Salinispora tropica (strain ATCC BAA-916 / DSM 44818 / CNB-440)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the biosynthesis of the proteosome inhibitor salinosporamide A (SalA). Catalyzes the halogenation of S-adenosyl-L-methionine (SAM) with chloride to generate 5'-chloro-5'-deoxyadenosine (5'-CIDA) and L-methionine. It can also use bromide and iodide, producing halogenated 5'-deoxyadenosine (5'-XDA) and L-methionine, however no halogenase activity is detected in the presence of fluoride.1 Publication

Catalytic activityi

S-adenosyl-L-methionine + chloride = 5-deoxy-5-chloroadenosine + L-methionine.1 Publication

Kineticsi

  1. KM=1 µM for SAM (at pH 7.9 and 37 degrees Celsius)1 Publication
  2. KM=45 mM for chloride (at pH 7.9 and 37 degrees Celsius)1 Publication
  3. KM=150 mM for bromide (at pH 7.9 and 37 degrees Celsius)1 Publication
  4. KM=260 mM for iodide (at pH 7.9 and 37 degrees Celsius)1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei11Substrate1
    Binding sitei131Chloride; via amide nitrogen1

    GO - Molecular functioni

    Complete GO annotation...

    Keywords - Molecular functioni

    Transferase

    Keywords - Ligandi

    Chloride, S-adenosyl-L-methionine

    Enzyme and pathway databases

    BRENDAi2.5.1.94. 12398.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Adenosyl-chloride synthase (EC:2.5.1.94)
    Alternative name(s):
    5'-chloro-5'-deoxyadenosine synthase
    Chlorinase SalL
    Gene namesi
    Name:salL
    Ordered Locus Names:Strop_1026
    OrganismiSalinispora tropica (strain ATCC BAA-916 / DSM 44818 / CNB-440)
    Taxonomic identifieri369723 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaMicromonosporalesMicromonosporaceaeSalinispora
    Proteomesi
    • UP000000235 Componenti: Chromosome

    Pathology & Biotechi

    Disruption phenotypei

    Cells lacking this gene are not able to produce salinosporamide A (SalA), however they produce salinosporamide B.1 Publication

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi70Y → T: Results in a 2-fold reduction of chlorinase activity. 1 Publication1
    Mutagenesisi129W → F: It has a reduced activity, however, to a much lesser extent than the Y70T mutant. 1 Publication1
    Mutagenesisi131G → S: Loss of chlorinase activity. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00004242671 – 283Adenosyl-chloride synthaseAdd BLAST283

    Interactioni

    Subunit structurei

    Homotrimer.1 Publication

    Protein-protein interaction databases

    STRINGi369723.Strop_1026.

    Structurei

    Secondary structure

    1283
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi5 – 12Combined sources8
    Beta strandi14 – 17Combined sources4
    Helixi18 – 29Combined sources12
    Beta strandi34 – 40Combined sources7
    Helixi47 – 54Combined sources8
    Helixi57 – 60Combined sources4
    Beta strandi65 – 70Combined sources6
    Turni73 – 76Combined sources4
    Beta strandi81 – 86Combined sources6
    Beta strandi91 – 98Combined sources8
    Helixi101 – 106Combined sources6
    Beta strandi109 – 114Combined sources6
    Helixi118 – 120Combined sources3
    Helixi130 – 133Combined sources4
    Helixi135 – 144Combined sources10
    Helixi148 – 151Combined sources4
    Helixi157 – 159Combined sources3
    Beta strandi176 – 182Combined sources7
    Turni184 – 186Combined sources3
    Beta strandi189 – 194Combined sources6
    Helixi195 – 198Combined sources4
    Turni199 – 204Combined sources6
    Beta strandi208 – 212Combined sources5
    Turni213 – 216Combined sources4
    Beta strandi217 – 222Combined sources6
    Beta strandi224 – 227Combined sources4
    Helixi228 – 230Combined sources3
    Beta strandi236 – 240Combined sources5
    Beta strandi244 – 250Combined sources7
    Helixi255 – 258Combined sources4
    Beta strandi266 – 270Combined sources5

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2Q6IX-ray2.60A1-283[»]
    2Q6KX-ray1.55A1-283[»]
    2Q6LX-ray2.72A1-283[»]
    2Q6OX-ray2.00A/B1-283[»]
    ProteinModelPortaliA4X3Q0.
    SMRiA4X3Q0.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiA4X3Q0.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni70 – 72Substrate binding3
    Regioni128 – 131Substrate binding4

    Sequence similaritiesi

    Belongs to the SalL family.Curated

    Phylogenomic databases

    eggNOGiENOG4107V4F. Bacteria.
    COG1912. LUCA.
    HOGENOMiHOG000079692.
    KOiK09134.
    OMAiAVECHEV.
    OrthoDBiPOG091H0GBS.

    Family and domain databases

    Gene3Di2.40.30.90. 1 hit.
    InterProiIPR002747. SAM_Chlor/Fluor.
    IPR023227. SAM_OH_AdoTrfase_C.
    IPR023228. SAM_OH_AdoTrfase_N.
    [Graphical view]
    PfamiPF01887. SAM_adeno_trans. 1 hit.
    [Graphical view]
    PIRSFiPIRSF006779. UCP006779. 1 hit.
    SUPFAMiSSF101852. SSF101852. 1 hit.
    SSF102522. SSF102522. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    A4X3Q0-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MQHNLIAFLS DVGSADEAHA LCKGVMYGVA PAATIVDITH DVAPFDVREG
    60 70 80 90 100
    ALFLADVPHS FPAHTVICAY VYPETGTATH TIAVRNEKGQ LLVGPNNGLL
    110 120 130 140 150
    SFALDASPAV ECHEVLSPDV MNQPVTPTWY GKDIVAACAA HLAAGTDLAA
    160 170 180 190 200
    VGPRIDPKQI VRLPYASASE VEGGIRGEVV RIDRAFGNVW TNIPTHLIGS
    210 220 230 240 250
    MLQDGERLEV KIEALSDTVL ELPFCKTFGE VDEGQPLLYL NSRGRLALGL
    260 270 280
    NQSNFIEKWP VVPGDSITVS PRVPDSNLGP VLG
    Length:283
    Mass (Da):30,148
    Last modified:May 29, 2007 - v1
    Checksum:i1AA3B1B60D563AF9
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    CP000667 Genomic DNA. Translation: ABP53500.1.
    RefSeqiWP_011904934.1. NC_009380.1.

    Genome annotation databases

    EnsemblBacteriaiABP53500; ABP53500; Strop_1026.
    GeneIDi5057472.
    KEGGistp:Strop_1026.
    PATRICi23440977. VBISalTro43511_1048.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    CP000667 Genomic DNA. Translation: ABP53500.1.
    RefSeqiWP_011904934.1. NC_009380.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2Q6IX-ray2.60A1-283[»]
    2Q6KX-ray1.55A1-283[»]
    2Q6LX-ray2.72A1-283[»]
    2Q6OX-ray2.00A/B1-283[»]
    ProteinModelPortaliA4X3Q0.
    SMRiA4X3Q0.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi369723.Strop_1026.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiABP53500; ABP53500; Strop_1026.
    GeneIDi5057472.
    KEGGistp:Strop_1026.
    PATRICi23440977. VBISalTro43511_1048.

    Phylogenomic databases

    eggNOGiENOG4107V4F. Bacteria.
    COG1912. LUCA.
    HOGENOMiHOG000079692.
    KOiK09134.
    OMAiAVECHEV.
    OrthoDBiPOG091H0GBS.

    Enzyme and pathway databases

    BRENDAi2.5.1.94. 12398.

    Miscellaneous databases

    EvolutionaryTraceiA4X3Q0.

    Family and domain databases

    Gene3Di2.40.30.90. 1 hit.
    InterProiIPR002747. SAM_Chlor/Fluor.
    IPR023227. SAM_OH_AdoTrfase_C.
    IPR023228. SAM_OH_AdoTrfase_N.
    [Graphical view]
    PfamiPF01887. SAM_adeno_trans. 1 hit.
    [Graphical view]
    PIRSFiPIRSF006779. UCP006779. 1 hit.
    SUPFAMiSSF101852. SSF101852. 1 hit.
    SSF102522. SSF102522. 1 hit.
    ProtoNetiSearch...

    Entry informationi

    Entry nameiSALL_SALTO
    AccessioniPrimary (citable) accession number: A4X3Q0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 13, 2013
    Last sequence update: May 29, 2007
    Last modified: November 2, 2016
    This is version 59 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, Complete proteome, Reference proteome

    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.