METK_AMOPR
ID METK_AMOPR Reviewed; 426 AA.
AC O09486;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2004, sequence version 2.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=S-adenosylmethionine synthase;
DE Short=AdoMet synthase;
DE EC=2.5.1.6 {ECO:0000250|UniProtKB:Q00266};
DE AltName: Full=Methionine adenosyltransferase;
DE Short=MAT;
GN Name=metK; Synonyms=sams;
OS Amoeba proteus (Amoeba) (Chaos diffluens).
OC Eukaryota; Amoebozoa; Tubulinea; Elardia; Euamoebida; Amoebidae; Amoeba.
OX NCBI_TaxID=5775;
RN [1]
RP NUCLEOTIDE SEQUENCE OF 1-6, AND INDUCTION.
RC STRAIN=D, and xD;
RX PubMed=12674481; DOI=10.1111/j.1550-7408.2003.tb00107.x;
RA Jeon T.J., Jeon K.W.;
RT "Characterization of sams genes of Amoeba proteus and the endosymbiotic X-
RT bacteria.";
RL J. Eukaryot. Microbiol. 50:61-69(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 7-426.
RC STRAIN=D, and xD;
RX PubMed=9304810; DOI=10.1111/j.1550-7408.1997.tb05717.x;
RA Choi J.Y., Lee T.W., Jeon K.W., Ahn T.I.;
RT "Evidence for symbiont-induced alteration of a host's gene expression:
RT irreversible loss of SAM synthetase from Amoeba proteus.";
RL J. Eukaryot. Microbiol. 44:412-419(1997).
CC -!- FUNCTION: Catalyzes the formation of S-adenosylmethionine from
CC methionine and ATP. The reaction comprises two steps that are both
CC catalyzed by the same enzyme: formation of S-adenosylmethionine
CC (AdoMet) and triphosphate, and subsequent hydrolysis of the
CC triphosphate. {ECO:0000250|UniProtKB:Q00266}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + L-methionine = diphosphate + phosphate + S-
CC adenosyl-L-methionine; Xref=Rhea:RHEA:21080, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57844, ChEBI:CHEBI:59789; EC=2.5.1.6;
CC Evidence={ECO:0000250|UniProtKB:Q00266};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P13444};
CC Note=Binds 2 magnesium ions per subunit. The magnesium ions interact
CC primarily with the substrate. {ECO:0000250|UniProtKB:P13444};
CC -!- COFACTOR:
CC Name=K(+); Xref=ChEBI:CHEBI:29103;
CC Evidence={ECO:0000250|UniProtKB:P13444};
CC Note=Binds 1 potassium ion per subunit. The potassium ion interacts
CC primarily with the substrate. {ECO:0000250|UniProtKB:P13444};
CC -!- PATHWAY: Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis;
CC S-adenosyl-L-methionine from L-methionine: step 1/1.
CC {ECO:0000250|UniProtKB:Q00266}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- INDUCTION: Repressed in strain X by infection with X-bacteria. Removal
CC of bacteria does not restore expression. {ECO:0000269|PubMed:12674481}.
CC -!- MISCELLANEOUS: Strain xD contains the sams gene. However, due to
CC infection by bacterial endosymbionts, it does not produce its own S-
CC adenosylmethionine synthase but is dependent on the bacteria for enzyme
CC production.
CC -!- SIMILARITY: Belongs to the AdoMet synthase family. {ECO:0000305}.
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DR EMBL; AY575678; AAS68367.1; -; Genomic_DNA.
DR EMBL; U91602; AAB50563.3; -; mRNA.
DR AlphaFoldDB; O09486; -.
DR SMR; O09486; -.
DR UniPathway; UPA00315; UER00080.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004478; F:methionine adenosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006556; P:S-adenosylmethionine biosynthetic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR022631; ADOMET_SYNTHASE_CS.
DR InterPro; IPR022630; S-AdoMet_synt_C.
DR InterPro; IPR022629; S-AdoMet_synt_central.
DR InterPro; IPR022628; S-AdoMet_synt_N.
DR InterPro; IPR002133; S-AdoMet_synthetase.
DR InterPro; IPR022636; S-AdoMet_synthetase_sfam.
DR PANTHER; PTHR11964; PTHR11964; 1.
DR Pfam; PF02773; S-AdoMet_synt_C; 1.
DR Pfam; PF02772; S-AdoMet_synt_M; 1.
DR Pfam; PF00438; S-AdoMet_synt_N; 1.
DR PIRSF; PIRSF000497; MAT; 1.
DR SUPFAM; SSF55973; SSF55973; 3.
DR PROSITE; PS00376; ADOMET_SYNTHASE_1; 1.
DR PROSITE; PS00377; ADOMET_SYNTHASE_2; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cytoplasm; Magnesium; Metal-binding; Nucleotide-binding;
KW One-carbon metabolism; Potassium; Transferase.
FT CHAIN 1..426
FT /note="S-adenosylmethionine synthase"
FT /id="PRO_0000174441"
FT BINDING 12
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P13444"
FT BINDING 18
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:Q00266"
FT BINDING 50
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250|UniProtKB:P0A817"
FT BINDING 63
FT /ligand="L-methionine"
FT /ligand_id="ChEBI:CHEBI:57844"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P0A817"
FT BINDING 106
FT /ligand="L-methionine"
FT /ligand_id="ChEBI:CHEBI:57844"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P0A817"
FT BINDING 202..204
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:Q00266"
FT BINDING 286
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:Q00266"
FT BINDING 286
FT /ligand="L-methionine"
FT /ligand_id="ChEBI:CHEBI:57844"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0000250|UniProtKB:P0A817"
FT BINDING 292..293
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P0A817"
FT BINDING 309
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0000250|UniProtKB:P0A817"
FT BINDING 313
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0000250|UniProtKB:P0A817"
FT BINDING 317
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0000250|UniProtKB:P13444"
FT BINDING 317
FT /ligand="L-methionine"
FT /ligand_id="ChEBI:CHEBI:57844"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P0A817"
SQ SEQUENCE 426 AA; 47920 MW; AE6DFF025E052752 CRC64;
MQQNTRYLFA SEAVSRGHPD KACDQVSDRV LDYCLQAEKK CKKASRVALE TTIKGNVVGL
FGEVTCQKTF PTISWFRELV TEIGYSREDL DLDPTTCSVH INVRGQEAEI RGVVHNQERA
AKETLGAGDQ GLMFGYATDE TPERCPCLWF LLRRFKLALR SKFEEARKKK IELAVAKGIK
VSQVDATPEL RDTIDFWWLH TDAKSQVIIE YEDDSGALKP ITARVAVLSV QHSKFVTHDQ
YEDRLPQLVK GVLDEYGMHS EATEYLINIK QKTSGYGWTV GGPNADAGTT GRKIIVDTYG
GHGAHGGGAF SGKDPSKVDR SAAYYARYVA QNLVRAKLCR RVLVQVSYVI GKPEPLNIYV
NTYGTGTHSD SELLEIINKN FDFRPGFIIE ELDLLNPDRI KYVETAYHGH FGRPEFPWEQ
EKTLTL
