RSAMH_SALAI
ID RSAMH_SALAI Reviewed; 261 AA.
AC A8M783;
DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=(R)-S-adenosyl-L-methionine hydrolase {ECO:0000250|UniProtKB:A4X4S2};
DE EC=3.13.1.8 {ECO:0000250|UniProtKB:A4X4S2, ECO:0000305|PubMed:18720493, ECO:0000305|PubMed:19739191};
DE AltName: Full=S-adenosyl-L-methionine hydrolase (adenosine-forming) {ECO:0000303|PubMed:18720493};
DE Short=SAM hydrolase (adenosine-forming) {ECO:0000303|PubMed:18720493};
DE AltName: Full=S-adenosyl-L-methionine:hydroxide adenosyltransferase {ECO:0000250|UniProtKB:O58212};
DE AltName: Full=SAM hydroxide adenosyltransferase {ECO:0000303|PubMed:19739191};
GN OrderedLocusNames=Sare_1364 {ECO:0000312|EMBL:ABV97265.1};
OS Salinispora arenicola (strain CNS-205).
OC Bacteria; Actinobacteria; Micromonosporales; Micromonosporaceae;
OC Salinispora.
OX NCBI_TaxID=391037;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CNS-205;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Foster B., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Jensen P.R., Moore B.S., Penn K., Jenkins C.,
RA Udwary D., Xiang L., Gontang E., Richardson P.;
RT "Complete sequence of Salinispora arenicola CNS-205.";
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RC STRAIN=CNS-205;
RX PubMed=18720493; DOI=10.1002/cbic.200800341;
RA Eustaquio A.S., Haerle J., Noel J.P., Moore B.S.;
RT "S-Adenosyl-L-methionine hydrolase (adenosine-forming), a conserved
RT bacterial and archaeal protein related to SAM-dependent halogenases.";
RL ChemBioChem 9:2215-2219(2008).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP MUTAGENESIS OF ASP-72; ARG-79 AND HIS-130.
RX PubMed=19739191; DOI=10.1002/cbic.200900369;
RA Deng H., McMahon S.A., Eustaquio A.S., Moore B.S., Naismith J.H.,
RA O'Hagan D.;
RT "Mechanistic insights into water activation in SAM hydroxide
RT adenosyltransferase (duf-62).";
RL ChemBioChem 10:2455-2459(2009).
CC -!- FUNCTION: Catalyzes the hydrolysis of S-adenosyl-L-methionine (SAM)
CC into adenosine and L-methionine (PubMed:18720493, PubMed:19739191). Is
CC likely stereoselective, specifically hydrolyzing (R)-S-adenosyl-L-
CC methionine ((R)-SAM), the inactive form of the ubiquitous cofactor SAM,
CC and not the active form of SAM, (S)-S-adenosyl-L-methionine (By
CC similarity). Probaly plays a role in preventing accumulation of (R)-S-
CC adenosyl-L-methionine in cells; maintenance of (S)-S-denosyl-L-
CC methionine homochirality is important for cellular health given that
CC the (R)-form is largely inactive as a methyl donor and can function as
CC an inhibitor of methyltransferases (By similarity). Shows very slow
CC iodinase activity in vitro (PubMed:18720493).
CC {ECO:0000250|UniProtKB:A4X4S2, ECO:0000269|PubMed:18720493,
CC ECO:0000269|PubMed:19739191}.
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:0000250|UniProtKB:A4X4S2, ECO:0000305|PubMed:18720493,
CC ECO:0000305|PubMed:19739191};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67241;
CC Evidence={ECO:0000250|UniProtKB:A4X4S2};
CC -!- ACTIVITY REGULATION: Activity is inhibited by chloride.
CC {ECO:0000269|PubMed:18720493}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.6 uM for S-adenosyl-L-methionine {ECO:0000269|PubMed:18720493};
CC KM=1 uM for S-adenosyl-L-methionine {ECO:0000269|PubMed:19739191};
CC Note=kcat is 0.5 min(-1) (PubMed:18720493). kcat is 0.45 min(-1)
CC (PubMed:19739191). {ECO:0000269|PubMed:18720493,
CC ECO:0000269|PubMed:19739191};
CC pH dependence:
CC Optimum pH is 8. {ECO:0000269|PubMed:18720493};
CC -!- SIMILARITY: Belongs to the SAM hydrolase / SAM-dependent halogenase
CC family. {ECO:0000305}.
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DR EMBL; CP000850; ABV97265.1; -; Genomic_DNA.
DR RefSeq; WP_012181573.1; NC_009953.1.
DR AlphaFoldDB; A8M783; -.
DR SMR; A8M783; -.
DR STRING; 391037.Sare_1364; -.
DR EnsemblBacteria; ABV97265; ABV97265; Sare_1364.
DR GeneID; 5707283; -.
DR KEGG; saq:Sare_1364; -.
DR PATRIC; fig|391037.6.peg.1387; -.
DR eggNOG; COG1912; Bacteria.
DR HOGENOM; CLU_059734_1_0_11; -.
DR OMA; EIPYQKA; -.
DR OrthoDB; 1262717at2; -.
DR BioCyc; MetaCyc:MON-20362; -.
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; S-adenosyl-L-methionine.
FT CHAIN 1..261
FT /note="(R)-S-adenosyl-L-methionine hydrolase"
FT /id="PRO_0000451806"
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"
FT SITE 72
FT /note="Important for activity"
FT /evidence="ECO:0000305|PubMed:19739191"
FT SITE 79
FT /note="Important for activity"
FT /evidence="ECO:0000305|PubMed:19739191"
FT SITE 130
FT /note="Important for activity"
FT /evidence="ECO:0000305|PubMed:19739191"
FT MUTAGEN 72
FT /note="D->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:19739191"
FT MUTAGEN 79
FT /note="R->A: Almost loss of activity."
FT /evidence="ECO:0000269|PubMed:19739191"
FT MUTAGEN 130
FT /note="H->A: 75% decrease in catalytic efficiency."
FT /evidence="ECO:0000269|PubMed:19739191"
FT MUTAGEN 130
FT /note="H->Y: 95% decrease in catalytic efficiency."
FT /evidence="ECO:0000269|PubMed:19739191"
SQ SEQUENCE 261 AA; 26346 MW; 3E86E2CD9A4ECF2C CRC64;
MASTPWISFT TDYGLADGFV AACHGVLARL APTARVIDVT HLVPPGDVRR GAAVLAQTVP
YLPAAVHVAV VDPGVGTARR AIALTAGNGL LVGPDNGLLL DAATALGGVD AAVELTNPDW
LGARMSATFH GRDVFAPVAA RLALGAPLAD AGPAVEPGAL VRLPTPLVQP ETDGFTAEVL
TVDHFGNVQL AATGALLESL PRSLRVAHRP AVHARTFDDA PPGGLLVHVD SAGLVAVAVN
GGRAADLLAV TPGDQLRVTA G
