METK_MYCA1
ID METK_MYCA1 Reviewed; 403 AA.
AC A0QI26;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 88.
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=MAV_3382;
OS Mycobacterium avium (strain 104).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium avium complex (MAC).
OX NCBI_TaxID=243243;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=104;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0007744|PDB:3S82}
RP X-RAY CRYSTALLOGRAPHY (1.73 ANGSTROMS).
RX PubMed=25613812; DOI=10.1016/j.tube.2014.12.003;
RA Baugh L., Phan I., Begley D.W., Clifton M.C., Armour B., Dranow D.M.,
RA Taylor B.M., Muruthi M.M., Abendroth J., Fairman J.W., Fox D. III,
RA Dieterich S.H., Staker B.L., Gardberg A.S., Choi R., Hewitt S.N.,
RA Napuli A.J., Myers J., Barrett L.K., Zhang Y., Ferrell M., Mundt E.,
RA Thompkins K., Tran N., Lyons-Abbott S., Abramov A., Sekar A.,
RA Serbzhinskiy D., Lorimer D., Buchko G.W., Stacy R., Stewart L.J.,
RA Edwards T.E., Van Voorhis W.C., Myler P.J.;
RT "Increasing the structural coverage of tuberculosis drug targets.";
RL Tuberculosis 95:142-148(2015).
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; CP000479; ABK67721.1; -; Genomic_DNA.
DR RefSeq; WP_008258192.1; NC_008595.1.
DR PDB; 3S82; X-ray; 1.73 A; A/B=1-403.
DR PDBsum; 3S82; -.
DR AlphaFoldDB; A0QI26; -.
DR SMR; A0QI26; -.
DR EnsemblBacteria; ABK67721; ABK67721; MAV_3382.
DR GeneID; 66745926; -.
DR KEGG; mav:MAV_3382; -.
DR HOGENOM; CLU_041802_1_1_11; -.
DR OMA; MPYLRPD; -.
DR OrthoDB; 1024388at2; -.
DR UniPathway; UPA00315; UER00080.
DR EvolutionaryTrace; A0QI26; -.
DR Proteomes; UP000001574; Chromosome.
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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Magnesium; Metal-binding;
KW Nucleotide-binding; One-carbon metabolism; Potassium; Transferase.
FT CHAIN 1..403
FT /note="S-adenosylmethionine synthase"
FT /id="PRO_0000302939"
FT REGION 104..114
FT /note="Flexible loop"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00086"
FT BINDING 17
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 19
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00086"
FT BINDING 45
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00086"
FT BINDING 58
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 104
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 179..181
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 250..251
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 259
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 259
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 265..266
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 282
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 286
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 290
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 STRAND 6..13
FT /evidence="ECO:0007829|PDB:3S82"
FT HELIX 18..36
FT /evidence="ECO:0007829|PDB:3S82"
FT STRAND 41..49
FT /evidence="ECO:0007829|PDB:3S82"
FT STRAND 52..60
FT /evidence="ECO:0007829|PDB:3S82"
FT HELIX 64..68
FT /evidence="ECO:0007829|PDB:3S82"
FT HELIX 70..81
FT /evidence="ECO:0007829|PDB:3S82"
FT HELIX 86..88
FT /evidence="ECO:0007829|PDB:3S82"
FT TURN 92..94
FT /evidence="ECO:0007829|PDB:3S82"
FT STRAND 95..104
FT /evidence="ECO:0007829|PDB:3S82"
FT STRAND 136..143
FT /evidence="ECO:0007829|PDB:3S82"
FT HELIX 152..169
FT /evidence="ECO:0007829|PDB:3S82"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:3S82"
FT STRAND 176..189
FT /evidence="ECO:0007829|PDB:3S82"
FT STRAND 192..205
FT /evidence="ECO:0007829|PDB:3S82"
FT TURN 211..214
FT /evidence="ECO:0007829|PDB:3S82"
FT HELIX 215..222
FT /evidence="ECO:0007829|PDB:3S82"
FT HELIX 224..231
FT /evidence="ECO:0007829|PDB:3S82"
FT STRAND 242..246
FT /evidence="ECO:0007829|PDB:3S82"
FT TURN 255..258
FT /evidence="ECO:0007829|PDB:3S82"
FT STRAND 259..262
FT /evidence="ECO:0007829|PDB:3S82"
FT TURN 267..274
FT /evidence="ECO:0007829|PDB:3S82"
FT HELIX 291..308
FT /evidence="ECO:0007829|PDB:3S82"
FT STRAND 313..321
FT /evidence="ECO:0007829|PDB:3S82"
FT STRAND 329..334
FT /evidence="ECO:0007829|PDB:3S82"
FT HELIX 343..353
FT /evidence="ECO:0007829|PDB:3S82"
FT HELIX 358..364
FT /evidence="ECO:0007829|PDB:3S82"
FT STRAND 368..370
FT /evidence="ECO:0007829|PDB:3S82"
FT HELIX 373..375
FT /evidence="ECO:0007829|PDB:3S82"
FT STRAND 376..378
FT /evidence="ECO:0007829|PDB:3S82"
FT STRAND 380..382
FT /evidence="ECO:0007829|PDB:3S82"
FT STRAND 384..386
FT /evidence="ECO:0007829|PDB:3S82"
FT HELIX 389..391
FT /evidence="ECO:0007829|PDB:3S82"
FT HELIX 396..402
FT /evidence="ECO:0007829|PDB:3S82"
SQ SEQUENCE 403 AA; 43306 MW; 8BB763DF835F67E3 CRC64;
MSEKGRLFTS ESVTEGHPDK ICDAISDSVL DALLAQDPRS RVAVETLVTT GQVHVVGEVT
TTAKEAFADI TNTVRERILD IGYDSSDKGF DGASCGVNIG IGAQSPDIAQ GVDTAHETRV
EGAADPLDAQ GAGDQGLMFG YAINDTPERM PLPIALAHRL SRRLTEVRKN GVLPYLRPDG
KTQVTIEFED DVPVRLDTVV ISTQHAADID LENTLTPDIR EKVLNTVLND LAHDTLDTSS
TRLLVNPTGK FVVGGPMGDA GLTGRKIIVD TYGGWARHGG GAFSGKDPSK VDRSAAYAMR
WVAKNIVAAG LAERVEVQVA YAIGKAAPVG LFIETFGTAT VDPVKIEKIV PEVFDLRPGA
IIRDLDLLRP IYAQTAAYGH FGRTDVELPW EQLNKVDDLK RAI
