METK_NEIG1
ID METK_NEIG1 Reviewed; 389 AA.
AC Q5FAC0;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2006, sequence version 2.
DT 03-AUG-2022, entry version 108.
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=NGO0106;
OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=242231;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700825 / FA 1090;
RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F.,
RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C.,
RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S.,
RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.;
RT "The complete genome sequence of Neisseria gonorrhoeae.";
RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAW88867.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE004969; AAW88867.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_003704903.1; NC_002946.2.
DR RefSeq; YP_207279.2; NC_002946.2.
DR PDB; 5T8S; X-ray; 1.70 A; A/B=1-389.
DR PDB; 5T8T; X-ray; 2.10 A; A/B=1-389.
DR PDBsum; 5T8S; -.
DR PDBsum; 5T8T; -.
DR AlphaFoldDB; Q5FAC0; -.
DR SMR; Q5FAC0; -.
DR STRING; 242231.NGO_0106; -.
DR EnsemblBacteria; AAW88867; AAW88867; NGO_0106.
DR KEGG; ngo:NGO_0106; -.
DR PATRIC; fig|242231.10.peg.139; -.
DR HOGENOM; CLU_041802_1_1_4; -.
DR UniPathway; UPA00315; UER00080.
DR Proteomes; UP000000535; 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; Reference proteome;
KW Transferase.
FT CHAIN 1..389
FT /note="S-adenosylmethionine synthase"
FT /id="PRO_0000241008"
FT REGION 99..109
FT /note="Flexible loop"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00086"
FT BINDING 15
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 17
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00086"
FT BINDING 43
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00086"
FT BINDING 56
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 99
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 166..168
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 234..235
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 243
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 243
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 249..250
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 266
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 270
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 274
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 3..11
FT /evidence="ECO:0007829|PDB:5T8S"
FT HELIX 16..34
FT /evidence="ECO:0007829|PDB:5T8S"
FT STRAND 39..47
FT /evidence="ECO:0007829|PDB:5T8S"
FT STRAND 50..58
FT /evidence="ECO:0007829|PDB:5T8S"
FT HELIX 65..76
FT /evidence="ECO:0007829|PDB:5T8S"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:5T8S"
FT HELIX 87..89
FT /evidence="ECO:0007829|PDB:5T8S"
FT STRAND 91..94
FT /evidence="ECO:0007829|PDB:5T8S"
FT HELIX 101..107
FT /evidence="ECO:0007829|PDB:5T8S"
FT STRAND 111..116
FT /evidence="ECO:0007829|PDB:5T8S"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:5T8S"
FT STRAND 123..133
FT /evidence="ECO:0007829|PDB:5T8S"
FT HELIX 139..156
FT /evidence="ECO:0007829|PDB:5T8S"
FT STRAND 163..176
FT /evidence="ECO:0007829|PDB:5T8S"
FT TURN 177..179
FT /evidence="ECO:0007829|PDB:5T8S"
FT STRAND 182..194
FT /evidence="ECO:0007829|PDB:5T8S"
FT HELIX 200..210
FT /evidence="ECO:0007829|PDB:5T8S"
FT HELIX 212..215
FT /evidence="ECO:0007829|PDB:5T8S"
FT HELIX 218..220
FT /evidence="ECO:0007829|PDB:5T8S"
FT STRAND 226..230
FT /evidence="ECO:0007829|PDB:5T8S"
FT HELIX 239..242
FT /evidence="ECO:0007829|PDB:5T8S"
FT TURN 251..258
FT /evidence="ECO:0007829|PDB:5T8S"
FT HELIX 275..292
FT /evidence="ECO:0007829|PDB:5T8S"
FT STRAND 297..305
FT /evidence="ECO:0007829|PDB:5T8S"
FT STRAND 313..318
FT /evidence="ECO:0007829|PDB:5T8S"
FT HELIX 327..337
FT /evidence="ECO:0007829|PDB:5T8S"
FT HELIX 342..349
FT /evidence="ECO:0007829|PDB:5T8S"
FT STRAND 352..354
FT /evidence="ECO:0007829|PDB:5T8S"
FT HELIX 357..360
FT /evidence="ECO:0007829|PDB:5T8S"
FT STRAND 364..366
FT /evidence="ECO:0007829|PDB:5T8S"
FT HELIX 373..375
FT /evidence="ECO:0007829|PDB:5T8S"
FT HELIX 380..386
FT /evidence="ECO:0007829|PDB:5T8S"
SQ SEQUENCE 389 AA; 41942 MW; 0FB0EEDF9A564C7E CRC64;
MSEYLFTSES VSEGHPDKVA DQVSDAILDA ILAQDPKARV AAETLVNTGL CVLAGEITTT
AQVDYIKVAR ETIKRIGYNS SELGFDANGC AVGVYYDQQS PDIAQGVNEG EGIDLNQGAG
DQGLMFGYAC DETPTLMPFA IYYSHRLMQR QSELRKDGRL PWLRPDAKAQ LTVVYDSETG
KVKRIDTVVL STQHDPAISQ EELSKAVIEQ IIKPVLPPEL LTDETKYLIN PTGRFVIGGP
QGDCGLTGRK IIVDTYGGAA PHGGGAFSGK DPSKVDRSAA YACRYVAKNI VAAGLATQCQ
IQVSYAIGVA EPTSISIDTF GTGKISEEKL IALVCEHFDL RPKGIVQMLD LLRPIYGKSA
AYGHFGREEP EFTWERTDKA ASLKAAAGL
