ID   R5ZS56_9STRE            Unreviewed;       397 AA.
AC   R5ZS56;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   07-APR-2021, entry version 33.
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, ECO:0000313|Proteomes:UP000017969}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:236 {ECO:0000313|Proteomes:UP000017969};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) 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:0000256|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:0000256|ARBA:ARBA00001513, ECO:0000256|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:0000256|ARBA:ARBA00005224, ECO:0000256|HAMAP-Rule:MF_00086}.
CC   -!- SUBUNIT: Homotetramer; dimer of dimers. {ECO:0000256|HAMAP-
CC       Rule:MF_00086}.
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|ARBA:ARBA00009685, ECO:0000256|HAMAP-Rule:MF_00086,
CC       ECO:0000256|RuleBase:RU004462}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:CDA39329.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CBBT010000053; CDA39329.1; -; Genomic_DNA.
DR   SMR; R5ZS56; -.
DR   EnsemblBacteria; CDA39329; CDA39329; BN551_00850.
DR   UniPathway; UPA00315; UER00080.
DR   Proteomes; UP000017969; Unassembled WGS sequence.
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   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00086}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00086};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00086};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00086};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00086};
KW   One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563, ECO:0000256|HAMAP-
KW   Rule:MF_00086};
KW   Potassium {ECO:0000256|ARBA:ARBA00022958, ECO:0000256|HAMAP-Rule:MF_00086};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00086}.
FT   DOMAIN          5..102
FT                   /note="S-AdoMet_synt_N"
FT                   /evidence="ECO:0000259|Pfam:PF00438"
FT   DOMAIN          126..243
FT                   /note="S-AdoMet_synt_M"
FT                   /evidence="ECO:0000259|Pfam:PF02772"
FT   DOMAIN          245..384
FT                   /note="S-AdoMet_synt_C"
FT                   /evidence="ECO:0000259|Pfam:PF02773"
FT   NP_BIND         175..177
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00086"
FT   NP_BIND         242..243
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00086"
FT   NP_BIND         257..258
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00086"
FT   REGION          100..110
FT                   /note="Flexible loop"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00086"
FT   METAL           18
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00086"
FT   METAL           44
FT                   /note="Potassium"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00086"
FT   BINDING         16
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00086"
FT   BINDING         57
FT                   /note="Methionine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00086"
FT   BINDING         100
FT                   /note="Methionine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00086"
FT   BINDING         251
FT                   /note="ATP; shared with neighboring subunit"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00086"
FT   BINDING         251
FT                   /note="Methionine; shared with neighboring subunit"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00086"
FT   BINDING         274
FT                   /note="ATP; via amide nitrogen; shared with neighboring
FT                   subunit"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00086"
FT   BINDING         278
FT                   /note="ATP; shared with neighboring subunit"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00086"
FT   BINDING         282
FT                   /note="Methionine"
FT                   /evidence="ECO:0000256|HAMAP-Rule: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
//