RSAMH_PYRHO
ID RSAMH_PYRHO Reviewed; 256 AA.
AC O58212;
DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 118.
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:18551689};
DE AltName: Full=S-adenosyl-L-methionine hydrolase (adenosine-forming) {ECO:0000305};
DE Short=SAM hydrolase (adenosine-forming) {ECO:0000305};
DE AltName: Full=S-adenosyl-L-methionine:hydroxide adenosyltransferase {ECO:0000303|PubMed:18551689};
DE AltName: Full=SAM hydroxide adenosyltransferase {ECO:0000303|PubMed:18551689};
GN OrderedLocusNames=PH0463 {ECO:0000312|EMBL:BAA29549.1};
OS Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS 100139 / OT-3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=70601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT "Complete sequence and gene organization of the genome of a hyper-
RT thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL DNA Res. 5:55-76(1998).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=18551689; DOI=10.1002/anie.200800794;
RA Deng H., Botting C.H., Hamilton J.T., Russell R.J., O'Hagan D.;
RT "S-adenosyl-L-methionine:hydroxide adenosyltransferase: a SAM enzyme.";
RL Angew. Chem. Int. Ed. 47:5357-5361(2008).
RN [3] {ECO:0007744|PDB:1WU8}
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) IN COMPLEX WITH ADENOSINE.
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RA Shimizu K., Kunishima N.;
RT "Crystal structure of project ID PH0463 from Pyrococcus horikoshii OT3.";
RL Submitted (DEC-2004) to the PDB data bank.
RN [4] {ECO:0007744|PDB:2WR8}
RP X-RAY CRYSTALLOGRAPHY (1.77 ANGSTROMS) IN COMPLEX WITH
RP S-ADENOSYL-L-HOMOCYSTEINE, AND SUBUNIT.
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:18551689). Is likely
CC stereoselective, specifically hydrolyzing (R)-S-adenosyl-L-methionine
CC ((R)-SAM), the inactive form of the ubiquitous cofactor SAM, and not
CC the active form of SAM, (S)-S-adenosyl-L-methionine (By similarity).
CC Probaly plays a role in preventing accumulation of (R)-S-adenosyl-L-
CC methionine in cells; maintenance of (S)-S-denosyl-L-methionine
CC homochirality is important for cellular health given that the (R)-form
CC is largely inactive as a methyl donor and can function as an inhibitor
CC of methyltransferases (By similarity). Is unable to mediate a
CC fluorination or chlorination reaction with SAM (PubMed:18551689).
CC {ECO:0000250|UniProtKB:A4X4S2, ECO:0000269|PubMed:18551689}.
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:18551689};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67241;
CC Evidence={ECO:0000250|UniProtKB:A4X4S2};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=39.2 uM for S-adenosyl-L-methionine {ECO:0000269|PubMed:18551689};
CC Note=kcat is 0.14 sec(-1). {ECO:0000269|PubMed:18551689};
CC pH dependence:
CC Optimum pH is 8.5. {ECO:0000269|PubMed:18551689};
CC -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:19739191}.
CC -!- SIMILARITY: Belongs to the SAM hydrolase / SAM-dependent halogenase
CC family. {ECO:0000305}.
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DR EMBL; BA000001; BAA29549.1; -; Genomic_DNA.
DR PIR; H71157; H71157.
DR RefSeq; WP_010884570.1; NC_000961.1.
DR PDB; 1WU8; X-ray; 2.60 A; A/B/C=1-256.
DR PDB; 2WR8; X-ray; 1.77 A; A=1-256.
DR PDBsum; 1WU8; -.
DR PDBsum; 2WR8; -.
DR AlphaFoldDB; O58212; -.
DR SMR; O58212; -.
DR STRING; 70601.3256866; -.
DR DNASU; 1444357; -.
DR EnsemblBacteria; BAA29549; BAA29549; BAA29549.
DR GeneID; 1444357; -.
DR KEGG; pho:PH0463; -.
DR eggNOG; arCOG04309; Archaea.
DR OMA; EIPYQKA; -.
DR OrthoDB; 71537at2157; -.
DR BRENDA; 2.5.1.B21; 5244.
DR BRENDA; 3.13.1.8; 5244.
DR EvolutionaryTrace; O58212; -.
DR Proteomes; UP000000752; 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 3D-structure; Hydrolase; S-adenosyl-L-methionine.
FT CHAIN 1..256
FT /note="(R)-S-adenosyl-L-methionine hydrolase"
FT /id="PRO_0000451807"
FT BINDING 7
FT /ligand="(R)-S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:142093"
FT /evidence="ECO:0000305|Ref.3"
FT BINDING 41
FT /ligand="(R)-S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:142093"
FT /evidence="ECO:0000305|Ref.3"
FT BINDING 68..69
FT /ligand="(R)-S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:142093"
FT /evidence="ECO:0000305|Ref.3"
FT BINDING 181..183
FT /ligand="(R)-S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:142093"
FT /evidence="ECO:0000305|PubMed:19739191, ECO:0000305|Ref.3"
FT BINDING 212
FT /ligand="(R)-S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:142093"
FT /evidence="ECO:0000305|PubMed:19739191"
FT BINDING 226
FT /ligand="(R)-S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:142093"
FT /evidence="ECO:0000305|PubMed:19739191"
FT BINDING 231..236
FT /ligand="(R)-S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:142093"
FT /evidence="ECO:0000305|PubMed:19739191, ECO:0000305|Ref.3"
FT SITE 68
FT /note="Important for activity"
FT /evidence="ECO:0000305|PubMed:19739191"
FT SITE 75
FT /note="Important for activity"
FT /evidence="ECO:0000305|PubMed:19739191"
FT SITE 127
FT /note="Important for activity"
FT /evidence="ECO:0000305|PubMed:19739191"
FT STRAND 1..8
FT /evidence="ECO:0007829|PDB:2WR8"
FT STRAND 10..13
FT /evidence="ECO:0007829|PDB:2WR8"
FT HELIX 14..25
FT /evidence="ECO:0007829|PDB:2WR8"
FT STRAND 30..36
FT /evidence="ECO:0007829|PDB:2WR8"
FT HELIX 43..56
FT /evidence="ECO:0007829|PDB:2WR8"
FT STRAND 62..66
FT /evidence="ECO:0007829|PDB:2WR8"
FT TURN 69..72
FT /evidence="ECO:0007829|PDB:1WU8"
FT STRAND 77..92
FT /evidence="ECO:0007829|PDB:2WR8"
FT TURN 93..96
FT /evidence="ECO:0007829|PDB:2WR8"
FT HELIX 97..100
FT /evidence="ECO:0007829|PDB:2WR8"
FT STRAND 103..109
FT /evidence="ECO:0007829|PDB:2WR8"
FT HELIX 111..118
FT /evidence="ECO:0007829|PDB:2WR8"
FT HELIX 127..130
FT /evidence="ECO:0007829|PDB:2WR8"
FT HELIX 132..141
FT /evidence="ECO:0007829|PDB:2WR8"
FT HELIX 145..147
FT /evidence="ECO:0007829|PDB:2WR8"
FT STRAND 149..152
FT /evidence="ECO:0007829|PDB:2WR8"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:2WR8"
FT STRAND 165..167
FT /evidence="ECO:0007829|PDB:2WR8"
FT STRAND 170..178
FT /evidence="ECO:0007829|PDB:2WR8"
FT STRAND 184..187
FT /evidence="ECO:0007829|PDB:2WR8"
FT STRAND 195..199
FT /evidence="ECO:0007829|PDB:2WR8"
FT TURN 200..203
FT /evidence="ECO:0007829|PDB:2WR8"
FT STRAND 204..208
FT /evidence="ECO:0007829|PDB:2WR8"
FT HELIX 212..214
FT /evidence="ECO:0007829|PDB:2WR8"
FT STRAND 220..223
FT /evidence="ECO:0007829|PDB:2WR8"
FT STRAND 227..234
FT /evidence="ECO:0007829|PDB:2WR8"
FT HELIX 239..243
FT /evidence="ECO:0007829|PDB:2WR8"
FT STRAND 250..256
FT /evidence="ECO:0007829|PDB:2WR8"
SQ SEQUENCE 256 AA; 28615 MW; EA3B4C5EB02F0742 CRC64;
MITLTTDFGL KGPYVGEMKV AMLRINPNAK IVDVTHSVTR HSILEGSFVM EQVVKYSPKG
TVHVGVIDPG VGTERRAIVI EGDQYLVVPD NGLATLPLKH IKVKSVYEII PDKIRKFTGW
EISSTFHGRD IFGPAGALIE KGIHPEEFGR EIPVDSIVKL NVEPRKEGDV WILKVIYIDD
FGNVILNLEN YEKPRTVELL DFNLRLPYLE TYGLVEKGEM LALPGSHDYL EIAVNMGSAA
ERLNVKVGDE LRVRLL
