METK_MYCTU
ID METK_MYCTU Reviewed; 403 AA.
AC P9WGV1; L0T6I5; P77899;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 39.
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=Rv1392;
GN ORFNames=MTCY21B4.09;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP PUPYLATION AT LYS-345, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=20066036; DOI=10.1371/journal.pone.0008589;
RA Festa R.A., McAllister F., Pearce M.J., Mintseris J., Burns K.E.,
RA Gygi S.P., Darwin K.H.;
RT "Prokaryotic ubiquitin-like protein (Pup) proteome of Mycobacterium
RT tuberculosis.";
RL PLoS ONE 5:E8589-E8589(2010).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [4] {ECO:0007744|PDB:3TDE}
RP X-RAY CRYSTALLOGRAPHY (1.85 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; AL123456; CCP44151.1; -; Genomic_DNA.
DR PIR; F70899; F70899.
DR RefSeq; NP_215908.1; NC_000962.3.
DR RefSeq; WP_003900333.1; NZ_NVQJ01000050.1.
DR PDB; 3TDE; X-ray; 1.85 A; A/B/C/D=2-403.
DR PDBsum; 3TDE; -.
DR AlphaFoldDB; P9WGV1; -.
DR SMR; P9WGV1; -.
DR STRING; 83332.Rv1392; -.
DR PaxDb; P9WGV1; -.
DR DNASU; 886741; -.
DR GeneID; 886741; -.
DR KEGG; mtu:Rv1392; -.
DR TubercuList; Rv1392; -.
DR eggNOG; COG0192; Bacteria.
DR OMA; MPYLRPD; -.
DR PhylomeDB; P9WGV1; -.
DR UniPathway; UPA00315; UER00080.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005829; C:cytosol; HDA:MTBBASE.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
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; IBA:GO_Central.
DR GO; GO:0035375; F:zymogen binding; IPI:CAFA.
DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006556; P:S-adenosylmethionine biosynthetic process; IBA:GO_Central.
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; Isopeptide bond; Magnesium;
KW Metal-binding; Nucleotide-binding; One-carbon metabolism; Potassium;
KW Reference proteome; Transferase; Ubl conjugation.
FT CHAIN 1..403
FT /note="S-adenosylmethionine synthase"
FT /id="PRO_0000174557"
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 CROSSLNK 345
FT /note="Isoglutamyl lysine isopeptide (Lys-Gln) (interchain
FT with Q-Cter in protein Pup)"
FT /evidence="ECO:0000269|PubMed:20066036"
FT STRAND 7..13
FT /evidence="ECO:0007829|PDB:3TDE"
FT HELIX 18..36
FT /evidence="ECO:0007829|PDB:3TDE"
FT STRAND 41..49
FT /evidence="ECO:0007829|PDB:3TDE"
FT STRAND 52..60
FT /evidence="ECO:0007829|PDB:3TDE"
FT HELIX 64..68
FT /evidence="ECO:0007829|PDB:3TDE"
FT HELIX 70..81
FT /evidence="ECO:0007829|PDB:3TDE"
FT HELIX 86..88
FT /evidence="ECO:0007829|PDB:3TDE"
FT TURN 92..94
FT /evidence="ECO:0007829|PDB:3TDE"
FT STRAND 95..102
FT /evidence="ECO:0007829|PDB:3TDE"
FT STRAND 136..143
FT /evidence="ECO:0007829|PDB:3TDE"
FT HELIX 152..169
FT /evidence="ECO:0007829|PDB:3TDE"
FT STRAND 176..189
FT /evidence="ECO:0007829|PDB:3TDE"
FT STRAND 192..205
FT /evidence="ECO:0007829|PDB:3TDE"
FT TURN 211..214
FT /evidence="ECO:0007829|PDB:3TDE"
FT HELIX 215..222
FT /evidence="ECO:0007829|PDB:3TDE"
FT HELIX 224..231
FT /evidence="ECO:0007829|PDB:3TDE"
FT STRAND 242..246
FT /evidence="ECO:0007829|PDB:3TDE"
FT TURN 255..258
FT /evidence="ECO:0007829|PDB:3TDE"
FT STRAND 259..262
FT /evidence="ECO:0007829|PDB:3TDE"
FT HELIX 267..270
FT /evidence="ECO:0007829|PDB:3TDE"
FT TURN 271..274
FT /evidence="ECO:0007829|PDB:3TDE"
FT HELIX 291..308
FT /evidence="ECO:0007829|PDB:3TDE"
FT STRAND 311..321
FT /evidence="ECO:0007829|PDB:3TDE"
FT STRAND 329..334
FT /evidence="ECO:0007829|PDB:3TDE"
FT STRAND 339..341
FT /evidence="ECO:0007829|PDB:3TDE"
FT HELIX 343..353
FT /evidence="ECO:0007829|PDB:3TDE"
FT HELIX 358..364
FT /evidence="ECO:0007829|PDB:3TDE"
FT STRAND 368..370
FT /evidence="ECO:0007829|PDB:3TDE"
FT HELIX 373..376
FT /evidence="ECO:0007829|PDB:3TDE"
FT STRAND 380..382
FT /evidence="ECO:0007829|PDB:3TDE"
FT STRAND 384..386
FT /evidence="ECO:0007829|PDB:3TDE"
FT HELIX 389..391
FT /evidence="ECO:0007829|PDB:3TDE"
FT HELIX 396..402
FT /evidence="ECO:0007829|PDB:3TDE"
SQ SEQUENCE 403 AA; 43047 MW; 2E18BE05D8267972 CRC64;
MSEKGRLFTS ESVTEGHPDK ICDAISDSVL DALLAADPRS RVAVETLVTT GQVHVVGEVT
TSAKEAFADI TNTVRARILE IGYDSSDKGF DGATCGVNIG IGAQSPDIAQ GVDTAHEARV
EGAADPLDSQ GAGDQGLMFG YAINATPELM PLPIALAHRL SRRLTEVRKN GVLPYLRPDG
KTQVTIAYED NVPVRLDTVV ISTQHAADID LEKTLDPDIR EKVLNTVLDD LAHETLDAST
VRVLVNPTGK FVLGGPMGDA GLTGRKIIVD TYGGWARHGG GAFSGKDPSK VDRSAAYAMR
WVAKNVVAAG LAERVEVQVA YAIGKAAPVG LFVETFGTET EDPVKIEKAI GEVFDLRPGA
IIRDLNLLRP IYAPTAAYGH FGRTDVELPW EQLDKVDDLK RAI
