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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
 
 
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