METK_COXB1
ID METK_COXB1 Reviewed; 393 AA.
AC B6J6H0;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=S-adenosylmethionine synthase {ECO:0000255|HAMAP-Rule:MF_00086};
DE Short=AdoMet synthase {ECO:0000255|HAMAP-Rule:MF_00086};
DE EC=2.5.1.6 {ECO:0000255|HAMAP-Rule:MF_00086};
DE AltName: Full=MAT {ECO:0000255|HAMAP-Rule:MF_00086};
DE AltName: Full=Methionine adenosyltransferase {ECO:0000255|HAMAP-Rule:MF_00086};
GN Name=metK {ECO:0000255|HAMAP-Rule:MF_00086}; OrderedLocusNames=CbuK_2082;
OS Coxiella burnetii (strain CbuK_Q154) (Coxiella burnetii (strain Q154)).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC Coxiella.
OX NCBI_TaxID=434924;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CbuK_Q154;
RX PubMed=19047403; DOI=10.1128/iai.01141-08;
RA Beare P.A., Unsworth N., Andoh M., Voth D.E., Omsland A., Gilk S.D.,
RA Williams K.P., Sobral B.W., Kupko J.J. III, Porcella S.F., Samuel J.E.,
RA Heinzen R.A.;
RT "Comparative genomics reveal extensive transposon-mediated genomic
RT plasticity and diversity among potential effector proteins within the genus
RT Coxiella.";
RL Infect. Immun. 77:642-656(2009).
CC -!- FUNCTION: Catalyzes the formation of S-adenosylmethionine (AdoMet) from
CC methionine and ATP. The overall synthetic reaction is composed of two
CC sequential steps, AdoMet formation and the subsequent tripolyphosphate
CC hydrolysis which occurs prior to release of AdoMet from the enzyme.
CC {ECO:0000255|HAMAP-Rule:MF_00086}.
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:0000255|HAMAP-Rule:MF_00086};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00086};
CC Note=Binds 2 divalent ions per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_00086};
CC -!- COFACTOR:
CC Name=K(+); Xref=ChEBI:CHEBI:29103;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00086};
CC Note=Binds 1 potassium ion per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_00086};
CC -!- PATHWAY: Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis;
CC S-adenosyl-L-methionine from L-methionine: step 1/1.
CC {ECO:0000255|HAMAP-Rule:MF_00086}.
CC -!- SUBUNIT: Homotetramer; dimer of dimers. {ECO:0000255|HAMAP-
CC Rule:MF_00086}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00086}.
CC -!- SIMILARITY: Belongs to the AdoMet synthase family. {ECO:0000255|HAMAP-
CC Rule:MF_00086}.
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DR EMBL; CP001020; ACJ21180.1; -; Genomic_DNA.
DR RefSeq; WP_005769816.1; NC_011528.1.
DR AlphaFoldDB; B6J6H0; -.
DR SMR; B6J6H0; -.
DR KEGG; cbc:CbuK_2082; -.
DR HOGENOM; CLU_041802_1_1_6; -.
DR OMA; MPYLRPD; -.
DR UniPathway; UPA00315; UER00080.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004478; F:methionine adenosyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006556; P:S-adenosylmethionine biosynthetic process; IEA:UniProtKB-UniPathway.
DR HAMAP; MF_00086; S_AdoMet_synth1; 1.
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 TIGRFAMs; TIGR01034; metK; 1.
DR PROSITE; PS00376; ADOMET_SYNTHASE_1; 1.
DR PROSITE; PS00377; ADOMET_SYNTHASE_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Magnesium; Metal-binding; Nucleotide-binding;
KW One-carbon metabolism; Potassium; Transferase.
FT CHAIN 1..393
FT /note="S-adenosylmethionine synthase"
FT /id="PRO_1000093041"
FT REGION 100..110
FT /note="Flexible loop"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00086"
FT BINDING 16
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:0000255|HAMAP-Rule:MF_00086"
FT BINDING 18
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00086"
FT BINDING 44
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00086"
FT BINDING 57
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:0000255|HAMAP-Rule:MF_00086"
FT BINDING 100
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:0000255|HAMAP-Rule:MF_00086"
FT BINDING 165..167
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:0000255|HAMAP-Rule:MF_00086"
FT BINDING 231..232
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:0000255|HAMAP-Rule:MF_00086"
FT BINDING 240
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00086"
FT BINDING 240
FT /ligand="L-methionine"
FT /ligand_id="ChEBI:CHEBI:57844"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00086"
FT BINDING 246..247
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:0000255|HAMAP-Rule:MF_00086"
FT BINDING 267
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00086"
FT BINDING 271
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:0000255|HAMAP-Rule:MF_00086"
SQ SEQUENCE 393 AA; 42748 MW; 83448409BC8EFD3C CRC64;
MTHTTLFTSE SVSEGHPDKV ADQISDAVLD ALIGQDPNCR VACEAVVKSG MVFVAGEITT
NAWADVEQIT RNTVLQIGYN DPHLGFDGEA CAVVTAIGKQ SPDIVMGVDG REDQELGAGD
QGLMFGYASR ETDVFMPAPI TYAHRLVRQQ ALLRKNGRLP WLRPDAKSQV TLRYENGKPV
AADCIVLSTQ HSPEISQESL REAVIDEIIK PIMPPHWLDK HTRFLVNPTG RFVIGGPVGD
CGLTGRKIIV DTYGGMARHG GGCFSGKDPS KVDRSGAYAA RYVAKNIVAG GLADRCEIQV
SYAIGVAEPT SISVETFGTG KIDEVRIQQL IKEHFDLRPG KIIEELNLLR SIYKATATYG
HFGREEPEFT WERTDKAEIL REAAGLAAAN VTN
