ID   R5ZS56_9STRE            Unreviewed;       397 AA.
AC   R5ZS56;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   01-OCT-2014, entry version 8.
DE   RecName: Full=S-adenosylmethionine synthase {ECO:0000256|HAMAP-Rule:MF_00086};
DE            Short=AdoMet synthase {ECO:0000256|HAMAP-Rule:MF_00086};
DE            EC=2.5.1.6 {ECO:0000256|HAMAP-Rule:MF_00086};
DE   AltName: Full=MAT {ECO:0000256|HAMAP-Rule:MF_00086};
DE   AltName: Full=Methionine adenosyltransferase {ECO:0000256|HAMAP-Rule:MF_00086};
GN   Name=metK {ECO:0000256|HAMAP-Rule:MF_00086};
GN   ORFNames=BN551_00850 {ECO:0000313|EMBL:CDA39329.1};
OS   Streptococcus thermophilus CAG:236.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus; environmental samples.
OX   NCBI_TaxID=1263110 {ECO:0000313|EMBL:CDA39329.1, ECO:0000313|Proteomes:UP000017969};
RN   [1] {ECO:0000313|EMBL:CDA39329.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J.,
RA   Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E.,
RA   Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J.,
RA   Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F.,
RA   Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S.,
RA   Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F.,
RA   Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E.,
RA   Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T.,
RA   MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J.,
RA   Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units
RT   of genetic variation.";
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the formation of S-adenosylmethionine from
CC       methionine and ATP. {ECO:0000256|RuleBase:RU000541}.
CC   -!- FUNCTION: Catalyzes the formation of S-adenosylmethionine from
CC       methionine and ATP. The overall synthetic reaction is composed of
CC       two sequential steps, AdoMet formation and the subsequent
CC       tripolyphosphate hydrolysis which occurs prior to release of
CC       AdoMet from the enzyme. {ECO:0000256|HAMAP-Rule:MF_00086}.
CC   -!- CATALYTIC ACTIVITY: ATP + L-methionine + H(2)O = phosphate +
CC       diphosphate + S-adenosyl-L-methionine. {ECO:0000256|HAMAP-
CC       Rule:MF_00086}.
CC   -!- COFACTOR: Binds 1 potassium ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_00086, ECO:0000256|RuleBase:RU000541}.
CC   -!- COFACTOR: Binds 2 divalent ions per subunit. Magnesium or cobalt.
CC       {ECO:0000256|HAMAP-Rule:MF_00086, ECO:0000256|RuleBase:RU000541}.
CC   -!- PATHWAY: Amino-acid biosynthesis; S-adenosyl-L-methionine
CC       biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1.
CC       {ECO:0000256|HAMAP-Rule:MF_00086}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00086,
CC       ECO:0000256|RuleBase:RU000542}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00086,
CC       ECO:0000256|RuleBase:RU000542}.
CC   -!- SIMILARITY: Belongs to the AdoMet synthase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00086, ECO:0000256|RuleBase:RU004462}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:CDA39329.1}.
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DR   EMBL; CBBT010000053; CDA39329.1; -; Genomic_DNA.
DR   ProteinModelPortal; R5ZS56; -.
DR   SMR; R5ZS56; 4-396.
DR   UniPathway; UPA00315; UER00080.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004478; F:methionine adenosyltransferase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-HAMAP.
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   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00086,
KW   ECO:0000256|RuleBase:RU000541};
KW   Cobalt {ECO:0000256|HAMAP-Rule:MF_00086};
KW   Complete proteome {ECO:0000313|Proteomes:UP000017969};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00086};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00086,
KW   ECO:0000256|RuleBase:RU000541};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00086,
KW   ECO:0000256|RuleBase:RU000541};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00086,
KW   ECO:0000256|RuleBase:RU000541};
KW   One-carbon metabolism {ECO:0000256|HAMAP-Rule:MF_00086,
KW   ECO:0000256|RuleBase:RU000541};
KW   Potassium {ECO:0000256|HAMAP-Rule:MF_00086,
KW   ECO:0000256|RuleBase:RU000541};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00086,
KW   ECO:0000256|RuleBase:RU000541}.
FT   NP_BIND     272    279       ATP. {ECO:0000256|HAMAP-Rule:MF_00086}.
FT   METAL        18     18       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00086}.
FT   METAL        44     44       Potassium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00086}.
FT   METAL       276    276       Potassium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00086}.
FT   METAL       284    284       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00086}.
SQ   SEQUENCE   397 AA;  42965 MW;  BC12D4127A5A9717 CRC64;
     MSERKLFTSE SVSEGHPDKI ADQISDAILD AILAEDPDAH VAAETAVYTG SVHIFGEVST
     TAYVDINRVV RDTIAEIGYN NAEYGFAAES VGVHPSLIEQ SPDIAQGVNE SLEVRGTGDQ
     DSLDLIGAGD QGLMFGFAID ETPEFMPLPV SLSHKLVKKL ADLRKSGEIS YLRPDAKSQV
     TVEYDENDQP VRVDTVVIST QHDPEATNDQ IRHDVIEKVI KAVIPAEYLD EDTKFFINPT
     GRFVIGGPQG DSGLTGRKII VDTYGGYSRH GGGAFSGKDA TKVDRSASYA ARYIAKNIVA
     AGLARKAEVQ LAYAIGVANP VSVRVDTFGT ATVAERKLES AVRDLFDLRP AGIIQMLDLK
     RPIYRQTAAY GHMGRTDVDL PWEKLDKVDA LKAAVEA
//