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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
 
 
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