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Adenosyl-chloride synthase (EC 2.5.1.94) (5'-chloro-5'-deoxyadenosine synthase) (Chlorinase SalL)

 SALL_SALTO              Reviewed;         283 AA.
A4X3Q0;
13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
29-MAY-2007, sequence version 1.
22-NOV-2017, entry version 64.
RecName: Full=Adenosyl-chloride synthase;
EC=2.5.1.94;
AltName: Full=5'-chloro-5'-deoxyadenosine synthase;
AltName: Full=Chlorinase SalL;
Name=salL; OrderedLocusNames=Strop_1026;
Salinispora tropica (strain ATCC BAA-916 / DSM 44818 / CNB-440).
Bacteria; Actinobacteria; Micromonosporales; Micromonosporaceae;
Salinispora.
NCBI_TaxID=369723;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC BAA-916 / DSM 44818 / CNB-440;
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
Dalin E., Tice H., Pitluck S., Sun H., Schmutz J., Larimer F.,
Land M., Hauser L., Kyrpides N., Kim E., Jensen P.R., Moore B.S.,
Udwary D.W., Richardson P.;
"Complete sequence of Salinispora tropica CNB-440.";
Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
[2]
X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF MUTANTS THR-70 AND SER-131
IN COMPLEX WITH SUBSTRATE ANALOGS, FUNCTION, CATALYTIC ACTIVITY,
MUTAGENESIS OF TYR-70; TRP-129 AND GLY-131, DISRUPTION PHENOTYPE,
BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, AND SUBUNIT.
PubMed=18059261; DOI=10.1038/nchembio.2007.56;
Eustaquio A.S., Pojer F., Noel J.P., Moore B.S.;
"Discovery and characterization of a marine bacterial SAM-dependent
chlorinase.";
Nat. Chem. Biol. 4:69-74(2008).
-!- FUNCTION: 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. {ECO:0000269|PubMed:18059261}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + chloride = 5-deoxy-
5-chloroadenosine + L-methionine. {ECO:0000269|PubMed:18059261}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=1 uM for SAM (at pH 7.9 and 37 degrees Celsius)
{ECO:0000269|PubMed:18059261};
KM=45 mM for chloride (at pH 7.9 and 37 degrees Celsius)
{ECO:0000269|PubMed:18059261};
KM=150 mM for bromide (at pH 7.9 and 37 degrees Celsius)
{ECO:0000269|PubMed:18059261};
KM=260 mM for iodide (at pH 7.9 and 37 degrees Celsius)
{ECO:0000269|PubMed:18059261};
-!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:18059261}.
-!- DISRUPTION PHENOTYPE: Cells lacking this gene are not able to
produce salinosporamide A (SalA), however they produce
salinosporamide B. {ECO:0000269|PubMed:18059261}.
-!- SIMILARITY: Belongs to the SalL family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; CP000667; ABP53500.1; -; Genomic_DNA.
RefSeq; WP_011904934.1; NC_009380.1.
PDB; 2Q6I; X-ray; 2.60 A; A=1-283.
PDB; 2Q6K; X-ray; 1.55 A; A=1-283.
PDB; 2Q6L; X-ray; 2.72 A; A=1-283.
PDB; 2Q6O; X-ray; 2.00 A; A/B=1-283.
PDBsum; 2Q6I; -.
PDBsum; 2Q6K; -.
PDBsum; 2Q6L; -.
PDBsum; 2Q6O; -.
ProteinModelPortal; A4X3Q0; -.
SMR; A4X3Q0; -.
STRING; 369723.Strop_1026; -.
EnsemblBacteria; ABP53500; ABP53500; Strop_1026.
GeneID; 5057472; -.
KEGG; stp:Strop_1026; -.
PATRIC; fig|369723.5.peg.1048; -.
eggNOG; ENOG4107V4F; Bacteria.
eggNOG; COG1912; LUCA.
HOGENOM; HOG000079692; -.
KO; K21153; -.
OrthoDB; POG091H0GBS; -.
BRENDA; 2.5.1.94; 12398.
EvolutionaryTrace; A4X3Q0; -.
Proteomes; UP000000235; Chromosome.
GO; GO:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; IDA:UniProtKB.
Gene3D; 2.40.30.90; -; 1.
Gene3D; 3.40.50.10790; -; 1.
InterPro; IPR002747; SAM_Chlor/Fluor.
InterPro; IPR023227; SAM_OH_AdoTrfase_C.
InterPro; IPR023228; SAM_OH_AdoTrfase_N.
PANTHER; PTHR35092; PTHR35092; 1.
Pfam; PF01887; SAM_adeno_trans; 1.
PIRSF; PIRSF006779; UCP006779; 1.
SUPFAM; SSF101852; SSF101852; 1.
SUPFAM; SSF102522; SSF102522; 1.
1: Evidence at protein level;
3D-structure; Chloride; Complete proteome; Reference proteome;
S-adenosyl-L-methionine; Transferase.
CHAIN 1 283 Adenosyl-chloride synthase.
/FTId=PRO_0000424267.
REGION 70 72 Substrate binding.
REGION 128 131 Substrate binding.
BINDING 11 11 Substrate.
BINDING 131 131 Chloride; via amide nitrogen.
MUTAGEN 70 70 Y->T: Results in a 2-fold reduction of
chlorinase activity.
{ECO:0000269|PubMed:18059261}.
MUTAGEN 129 129 W->F: It has a reduced activity, however,
to a much lesser extent than the Y70T
mutant. {ECO:0000269|PubMed:18059261}.
MUTAGEN 131 131 G->S: Loss of chlorinase activity.
{ECO:0000269|PubMed:18059261}.
STRAND 5 12 {ECO:0000244|PDB:2Q6K}.
STRAND 14 17 {ECO:0000244|PDB:2Q6K}.
HELIX 18 29 {ECO:0000244|PDB:2Q6K}.
STRAND 34 40 {ECO:0000244|PDB:2Q6K}.
HELIX 47 54 {ECO:0000244|PDB:2Q6K}.
HELIX 57 60 {ECO:0000244|PDB:2Q6K}.
STRAND 65 70 {ECO:0000244|PDB:2Q6K}.
TURN 73 76 {ECO:0000244|PDB:2Q6K}.
STRAND 81 86 {ECO:0000244|PDB:2Q6K}.
STRAND 91 98 {ECO:0000244|PDB:2Q6K}.
HELIX 101 106 {ECO:0000244|PDB:2Q6K}.
STRAND 109 114 {ECO:0000244|PDB:2Q6K}.
HELIX 118 120 {ECO:0000244|PDB:2Q6K}.
HELIX 130 133 {ECO:0000244|PDB:2Q6K}.
HELIX 135 144 {ECO:0000244|PDB:2Q6K}.
HELIX 148 151 {ECO:0000244|PDB:2Q6K}.
HELIX 157 159 {ECO:0000244|PDB:2Q6K}.
STRAND 176 182 {ECO:0000244|PDB:2Q6K}.
TURN 184 186 {ECO:0000244|PDB:2Q6K}.
STRAND 189 194 {ECO:0000244|PDB:2Q6K}.
HELIX 195 198 {ECO:0000244|PDB:2Q6K}.
TURN 199 204 {ECO:0000244|PDB:2Q6O}.
STRAND 208 212 {ECO:0000244|PDB:2Q6K}.
TURN 213 216 {ECO:0000244|PDB:2Q6I}.
STRAND 217 222 {ECO:0000244|PDB:2Q6K}.
STRAND 224 227 {ECO:0000244|PDB:2Q6O}.
HELIX 228 230 {ECO:0000244|PDB:2Q6K}.
STRAND 236 240 {ECO:0000244|PDB:2Q6K}.
STRAND 244 250 {ECO:0000244|PDB:2Q6K}.
HELIX 255 258 {ECO:0000244|PDB:2Q6K}.
STRAND 266 270 {ECO:0000244|PDB:2Q6K}.
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


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