ID   RSAMH_SALTO             Reviewed;         261 AA.
AC   A4X4S2;
DT   25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=(R)-S-adenosyl-L-methionine hydrolase {ECO:0000303|PubMed:32776704};
DE            EC=3.13.1.8 {ECO:0000269|PubMed:32776704};
GN   OrderedLocusNames=Strop_1405 {ECO:0000312|EMBL:ABP53872.1};
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   FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=ATCC BAA-916 / DSM 44818 / CNB-440;
RX   PubMed=32776704; DOI=10.1002/cbic.202000349;
RA   Kornfuehrer T., Romanowski S., de Crecy-Lagard V., Hanson A.D.,
RA   Eustaquio A.S.;
RT   "An Enzyme Containing the Conserved Domain of Unknown Function DUF62 Acts
RT   as a Stereoselective (Rs,Sc)-S-Adenosylmethionine Hydrolase.";
RL   ChemBioChem 21:3495-3499(2020).
CC   -!- FUNCTION: Specifically hydrolyzes (R)-S-adenosyl-L-methionine ((R)-
CC       SAM), the inactive form of the ubiquitous cofactor SAM, into adenosine
CC       and L-methionine. Is stereoselective as it cannot use the active form
CC       of SAM, (S)-S-adenosyl-L-methionine, as substrate. Likely plays a role
CC       in preventing accumulation of (R)-S-adenosyl-L-methionine in cells;
CC       maintenance of (S)-S-denosyl-L-methionine homochirality is important
CC       for cellular health given that the (R)-form is largely inactive as a
CC       methyl donor and can function as an inhibitor of methyltransferases.
CC       {ECO:0000269|PubMed:32776704}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-S-adenosyl-L-methionine + H2O = adenosine + H(+) + L-
CC         methionine; Xref=Rhea:RHEA:67240, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16335, ChEBI:CHEBI:57844,
CC         ChEBI:CHEBI:142093; EC=3.13.1.8;
CC         Evidence={ECO:0000269|PubMed:32776704};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67241;
CC         Evidence={ECO:0000305|PubMed:32776704};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.63 uM for (R)-S-adenosyl-L-methionine
CC         {ECO:0000269|PubMed:32776704};
CC         Note=kcat is 0.0045 sec(-1). {ECO:0000269|PubMed:32776704};
CC   -!- SIMILARITY: Belongs to the SAM hydrolase / SAM-dependent halogenase
CC       family. {ECO:0000305}.
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DR   EMBL; CP000667; ABP53872.1; -; Genomic_DNA.
DR   RefSeq; WP_011905304.1; NC_009380.1.
DR   STRING; 369723.Strop_1405; -.
DR   EnsemblBacteria; ABP53872; ABP53872; Strop_1405.
DR   KEGG; stp:Strop_1405; -.
DR   PATRIC; fig|369723.5.peg.1432; -.
DR   eggNOG; COG1912; Bacteria.
DR   HOGENOM; CLU_059734_1_0_11; -.
DR   OMA; EIPYQKA; -.
DR   Proteomes; UP000000235; Chromosome.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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   Hydrolase; Reference proteome; S-adenosyl-L-methionine.
FT   CHAIN           1..261
FT                   /note="(R)-S-adenosyl-L-methionine hydrolase"
FT                   /id="PRO_0000455605"
FT   BINDING         12
FT                   /ligand="(R)-S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:142093"
FT                   /evidence="ECO:0000250|UniProtKB:O58212"
FT   BINDING         72..73
FT                   /ligand="(R)-S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:142093"
FT                   /evidence="ECO:0000250|UniProtKB:O58212"
FT   BINDING         185..187
FT                   /ligand="(R)-S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:142093"
FT                   /evidence="ECO:0000250|UniProtKB:O58212"
FT   BINDING         231
FT                   /ligand="(R)-S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:142093"
FT                   /evidence="ECO:0000250|UniProtKB:O58212"
FT   BINDING         236..241
FT                   /ligand="(R)-S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:142093"
FT                   /evidence="ECO:0000250|UniProtKB:O58212"
SQ   SEQUENCE   261 AA;  26602 MW;  DA8EFBCAB9EB86F6 CRC64;
     MAPTPWISFT TDYGLADGFV AACHGVLARL TPTTRVIDVT HLVPPGDVRR GAAVLAQAVP
     YLPAAVHLAV VDPGVGTARR AIALAAGDGL LVGPDNGLLL DAAAALGGVR AAVELTNRDW
     LGADVSATFH GRDIFAPVAA RLALGAPLAD AGPAVEPSTL VRLPVPLVRP EADGFTAEVL
     TVDHFGNVQL AASGSLLEPL PRSLRVERQP AVRVHTFGDV APGELLVHVD STGQVAVAVN
     GGRAADLLGV TPGDRLRVTA G