SALL_SALTO
ID SALL_SALTO Reviewed; 283 AA.
AC A4X3Q0;
DT 13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Adenosyl-chloride synthase;
DE EC=2.5.1.94;
DE AltName: Full=5'-chloro-5'-deoxyadenosine synthase;
DE AltName: Full=Chlorinase SalL;
GN Name=salL; OrderedLocusNames=Strop_1026;
OS Salinispora tropica (strain ATCC BAA-916 / DSM 44818 / CNB-440).
OC Bacteria; Actinobacteria; Micromonosporales; Micromonosporaceae;
OC Salinispora.
OX NCBI_TaxID=369723;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-916 / DSM 44818 / CNB-440;
RX PubMed=17563368; DOI=10.1073/pnas.0700962104;
RA Udwary D.W., Zeigler L., Asolkar R.N., Singan V., Lapidus A., Fenical W.,
RA Jensen P.R., Moore B.S.;
RT "Genome sequencing reveals complex secondary metabolome in the marine
RT actinomycete Salinispora tropica.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:10376-10381(2007).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF MUTANTS THR-70 AND SER-131 IN
RP COMPLEX WITH SUBSTRATE ANALOGS, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS
RP OF TYR-70; TRP-129 AND GLY-131, DISRUPTION PHENOTYPE, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBSTRATE SPECIFICITY, AND SUBUNIT.
RX PubMed=18059261; DOI=10.1038/nchembio.2007.56;
RA Eustaquio A.S., Pojer F., Noel J.P., Moore B.S.;
RT "Discovery and characterization of a marine bacterial SAM-dependent
RT chlorinase.";
RL Nat. Chem. Biol. 4:69-74(2008).
CC -!- FUNCTION: Involved in the biosynthesis of the proteosome inhibitor
CC salinosporamide A (SalA). Catalyzes the halogenation of S-adenosyl-L-
CC methionine (SAM) with chloride to generate 5'-chloro-5'-deoxyadenosine
CC (5'-CIDA) and L-methionine. It can also use bromide and iodide,
CC producing halogenated 5'-deoxyadenosine (5'-XDA) and L-methionine,
CC however no halogenase activity is detected in the presence of fluoride.
CC {ECO:0000269|PubMed:18059261}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chloride + S-adenosyl-L-methionine = 5'-chloro-5'-
CC deoxyadenosine + L-methionine; Xref=Rhea:RHEA:28110,
CC ChEBI:CHEBI:17996, ChEBI:CHEBI:47133, ChEBI:CHEBI:57844,
CC ChEBI:CHEBI:59789; EC=2.5.1.94;
CC Evidence={ECO:0000269|PubMed:18059261};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1 uM for SAM (at pH 7.9 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:18059261};
CC KM=45 mM for chloride (at pH 7.9 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:18059261};
CC KM=150 mM for bromide (at pH 7.9 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:18059261};
CC KM=260 mM for iodide (at pH 7.9 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:18059261};
CC -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:18059261}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene are not able to produce
CC salinosporamide A (SalA), however they produce salinosporamide B.
CC {ECO:0000269|PubMed:18059261}.
CC -!- SIMILARITY: Belongs to the SAM hydrolase / SAM-dependent halogenase
CC family. {ECO:0000305}.
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DR EMBL; CP000667; ABP53500.1; -; Genomic_DNA.
DR RefSeq; WP_011904934.1; NC_009380.1.
DR PDB; 2Q6I; X-ray; 2.60 A; A=1-283.
DR PDB; 2Q6K; X-ray; 1.55 A; A=1-283.
DR PDB; 2Q6L; X-ray; 2.72 A; A=1-283.
DR PDB; 2Q6O; X-ray; 2.00 A; A/B=1-283.
DR PDB; 6RYZ; X-ray; 1.50 A; A/B/C=1-283.
DR PDB; 6RZ2; X-ray; 1.77 A; A/B/C=1-283.
DR PDBsum; 2Q6I; -.
DR PDBsum; 2Q6K; -.
DR PDBsum; 2Q6L; -.
DR PDBsum; 2Q6O; -.
DR PDBsum; 6RYZ; -.
DR PDBsum; 6RZ2; -.
DR AlphaFoldDB; A4X3Q0; -.
DR SMR; A4X3Q0; -.
DR STRING; 369723.Strop_1026; -.
DR ChEMBL; CHEMBL4296303; -.
DR EnsemblBacteria; ABP53500; ABP53500; Strop_1026.
DR KEGG; stp:Strop_1026; -.
DR PATRIC; fig|369723.5.peg.1048; -.
DR eggNOG; COG1912; Bacteria.
DR HOGENOM; CLU_059734_0_0_11; -.
DR BRENDA; 2.5.1.94; 12398.
DR EvolutionaryTrace; A4X3Q0; -.
DR Proteomes; UP000000235; Chromosome.
DR GO; GO:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; IDA:UniProtKB.
DR Gene3D; 2.40.30.90; -; 1.
DR Gene3D; 3.40.50.10790; -; 1.
DR InterPro; IPR002747; SAM_Chlor/Fluor.
DR InterPro; IPR023227; SAM_OH_AdoTrfase_C.
DR InterPro; IPR023228; SAM_OH_AdoTrfase_N.
DR PANTHER; PTHR35092; PTHR35092; 1.
DR Pfam; PF01887; SAM_adeno_trans; 1.
DR PIRSF; PIRSF006779; UCP006779; 1.
DR SUPFAM; SSF101852; SSF101852; 1.
DR SUPFAM; SSF102522; SSF102522; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chloride; Reference proteome; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..283
FT /note="Adenosyl-chloride synthase"
FT /id="PRO_0000424267"
FT BINDING 11
FT /ligand="substrate"
FT BINDING 70..72
FT /ligand="substrate"
FT BINDING 128..131
FT /ligand="substrate"
FT BINDING 131
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT MUTAGEN 70
FT /note="Y->T: Results in a 2-fold reduction of chlorinase
FT activity."
FT /evidence="ECO:0000269|PubMed:18059261"
FT MUTAGEN 129
FT /note="W->F: It has a reduced activity, however, to a much
FT lesser extent than the Y70T mutant."
FT /evidence="ECO:0000269|PubMed:18059261"
FT MUTAGEN 131
FT /note="G->S: Loss of chlorinase activity."
FT /evidence="ECO:0000269|PubMed:18059261"
FT STRAND 5..12
FT /evidence="ECO:0007829|PDB:6RYZ"
FT STRAND 14..17
FT /evidence="ECO:0007829|PDB:6RYZ"
FT HELIX 18..29
FT /evidence="ECO:0007829|PDB:6RYZ"
FT STRAND 34..40
FT /evidence="ECO:0007829|PDB:6RYZ"
FT HELIX 47..54
FT /evidence="ECO:0007829|PDB:6RYZ"
FT HELIX 57..60
FT /evidence="ECO:0007829|PDB:6RYZ"
FT STRAND 65..70
FT /evidence="ECO:0007829|PDB:6RYZ"
FT TURN 73..76
FT /evidence="ECO:0007829|PDB:6RYZ"
FT STRAND 81..86
FT /evidence="ECO:0007829|PDB:6RYZ"
FT STRAND 91..98
FT /evidence="ECO:0007829|PDB:6RYZ"
FT HELIX 101..106
FT /evidence="ECO:0007829|PDB:6RYZ"
FT STRAND 109..114
FT /evidence="ECO:0007829|PDB:6RYZ"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:6RYZ"
FT HELIX 130..133
FT /evidence="ECO:0007829|PDB:6RYZ"
FT HELIX 135..143
FT /evidence="ECO:0007829|PDB:6RYZ"
FT HELIX 148..151
FT /evidence="ECO:0007829|PDB:6RYZ"
FT HELIX 157..159
FT /evidence="ECO:0007829|PDB:6RYZ"
FT STRAND 169..171
FT /evidence="ECO:0007829|PDB:6RYZ"
FT STRAND 174..182
FT /evidence="ECO:0007829|PDB:6RYZ"
FT TURN 184..186
FT /evidence="ECO:0007829|PDB:6RYZ"
FT STRAND 189..194
FT /evidence="ECO:0007829|PDB:6RYZ"
FT HELIX 195..199
FT /evidence="ECO:0007829|PDB:6RYZ"
FT STRAND 207..213
FT /evidence="ECO:0007829|PDB:6RYZ"
FT STRAND 219..227
FT /evidence="ECO:0007829|PDB:6RYZ"
FT HELIX 228..230
FT /evidence="ECO:0007829|PDB:6RYZ"
FT STRAND 236..240
FT /evidence="ECO:0007829|PDB:6RYZ"
FT STRAND 244..250
FT /evidence="ECO:0007829|PDB:6RYZ"
FT HELIX 255..258
FT /evidence="ECO:0007829|PDB:6RYZ"
FT STRAND 266..270
FT /evidence="ECO:0007829|PDB:6RYZ"
SQ SEQUENCE 283 AA; 30148 MW; 1AA3B1B60D563AF9 CRC64;
MQHNLIAFLS DVGSADEAHA LCKGVMYGVA PAATIVDITH DVAPFDVREG ALFLADVPHS
FPAHTVICAY VYPETGTATH TIAVRNEKGQ LLVGPNNGLL SFALDASPAV ECHEVLSPDV
MNQPVTPTWY GKDIVAACAA HLAAGTDLAA VGPRIDPKQI VRLPYASASE VEGGIRGEVV
RIDRAFGNVW TNIPTHLIGS MLQDGERLEV KIEALSDTVL ELPFCKTFGE VDEGQPLLYL
NSRGRLALGL NQSNFIEKWP VVPGDSITVS PRVPDSNLGP VLG
