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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
 
 
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