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S-adenosylmethionine synthase (AdoMet synthase) (EC 2.5.1.6) (MAT) (Methionine adenosyltransferase)

 A0A0P9DIR2_9CHLR        Unreviewed;       403 AA.
A0A0P9DIR2;
20-JAN-2016, integrated into UniProtKB/TrEMBL.
20-JAN-2016, sequence version 1.
28-MAR-2018, entry version 13.
RecName: Full=S-adenosylmethionine synthase {ECO:0000256|HAMAP-Rule:MF_00086};
Short=AdoMet synthase {ECO:0000256|HAMAP-Rule:MF_00086};
EC=2.5.1.6 {ECO:0000256|HAMAP-Rule:MF_00086};
AltName: Full=MAT {ECO:0000256|HAMAP-Rule:MF_00086};
AltName: Full=Methionine adenosyltransferase {ECO:0000256|HAMAP-Rule:MF_00086};
Name=metK {ECO:0000256|HAMAP-Rule:MF_00086};
ORFNames=SE17_30795 {ECO:0000313|EMBL:KPV49758.1};
Kouleothrix aurantiaca.
Bacteria; Chloroflexi; Kouleothrix.
NCBI_TaxID=186479 {ECO:0000313|EMBL:KPV49758.1, ECO:0000313|Proteomes:UP000050509};
[1] {ECO:0000313|EMBL:KPV49758.1, ECO:0000313|Proteomes:UP000050509}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=COM-B {ECO:0000313|EMBL:KPV49758.1,
ECO:0000313|Proteomes:UP000050509};
Hemp J.;
"Draft genome sequence of Kouleothrix aurantiaca JCM 19913.";
Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Catalyzes the formation of S-adenosylmethionine (AdoMet)
from methionine and ATP. The overall synthetic reaction is
composed of two sequential steps, AdoMet formation and the
subsequent tripolyphosphate hydrolysis which occurs prior to
release of AdoMet from the enzyme. {ECO:0000256|HAMAP-
Rule:MF_00086}.
-!- CATALYTIC ACTIVITY: ATP + L-methionine + H(2)O = phosphate +
diphosphate + S-adenosyl-L-methionine. {ECO:0000256|HAMAP-
Rule:MF_00086}.
-!- COFACTOR:
Name=K(+); Xref=ChEBI:CHEBI:29103;
Evidence={ECO:0000256|HAMAP-Rule:MF_00086};
Note=Binds 1 potassium ion per subunit. {ECO:0000256|HAMAP-
Rule:MF_00086};
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000256|HAMAP-Rule:MF_00086};
Note=Binds 2 divalent ions per subunit. {ECO:0000256|HAMAP-
Rule:MF_00086};
-!- PATHWAY: Amino-acid biosynthesis; S-adenosyl-L-methionine
biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1.
{ECO:0000256|HAMAP-Rule:MF_00086}.
-!- SUBUNIT: Homotetramer; dimer of dimers. {ECO:0000256|HAMAP-
Rule:MF_00086}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00086,
ECO:0000256|RuleBase:RU000542}.
-!- SIMILARITY: Belongs to the AdoMet synthase family.
{ECO:0000256|HAMAP-Rule:MF_00086, ECO:0000256|RuleBase:RU004462}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:KPV49758.1}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; LJCR01001768; KPV49758.1; -; Genomic_DNA.
EnsemblBacteria; KPV49758; KPV49758; SE17_30795.
PATRIC; fig|186479.3.peg.2925; -.
UniPathway; UPA00315; UER00080.
Proteomes; UP000050509; Unassembled WGS sequence.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
GO; GO:0004478; F:methionine adenosyltransferase activity; IEA:UniProtKB-UniRule.
GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-UniRule.
GO; GO:0006556; P:S-adenosylmethionine biosynthetic process; IEA:UniProtKB-UniPathway.
HAMAP; MF_00086; S_AdoMet_synth1; 1.
InterPro; IPR022631; ADOMET_SYNTHASE_CS.
InterPro; IPR022630; S-AdoMet_synt_C.
InterPro; IPR022629; S-AdoMet_synt_central.
InterPro; IPR022628; S-AdoMet_synt_N.
InterPro; IPR002133; S-AdoMet_synthetase.
InterPro; IPR022636; S-AdoMet_synthetase_sfam.
PANTHER; PTHR11964; PTHR11964; 1.
Pfam; PF02773; S-AdoMet_synt_C; 1.
Pfam; PF02772; S-AdoMet_synt_M; 1.
Pfam; PF00438; S-AdoMet_synt_N; 1.
PIRSF; PIRSF000497; MAT; 1.
SUPFAM; SSF55973; SSF55973; 3.
TIGRFAMs; TIGR01034; metK; 1.
PROSITE; PS00376; ADOMET_SYNTHASE_1; 1.
PROSITE; PS00377; ADOMET_SYNTHASE_2; 1.
3: Inferred from homology;
ATP-binding {ECO:0000256|HAMAP-Rule:MF_00086};
Complete proteome {ECO:0000313|Proteomes:UP000050509};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00086};
Magnesium {ECO:0000256|HAMAP-Rule:MF_00086,
ECO:0000256|RuleBase:RU000542};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_00086,
ECO:0000256|RuleBase:RU000542};
Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00086};
One-carbon metabolism {ECO:0000256|HAMAP-Rule:MF_00086};
Potassium {ECO:0000256|HAMAP-Rule:MF_00086,
ECO:0000256|RuleBase:RU000542};
Reference proteome {ECO:0000313|Proteomes:UP000050509};
Transferase {ECO:0000256|HAMAP-Rule:MF_00086,
ECO:0000313|EMBL:KPV49758.1}.
DOMAIN 11 108 S-AdoMet_synt_N.
{ECO:0000259|Pfam:PF00438}.
DOMAIN 133 249 S-AdoMet_synt_M.
{ECO:0000259|Pfam:PF02772}.
DOMAIN 252 390 S-AdoMet_synt_C.
{ECO:0000259|Pfam:PF02773}.
NP_BIND 182 184 ATP. {ECO:0000256|HAMAP-Rule:MF_00086}.
NP_BIND 248 249 ATP. {ECO:0000256|HAMAP-Rule:MF_00086}.
NP_BIND 263 264 ATP. {ECO:0000256|HAMAP-Rule:MF_00086}.
REGION 106 116 Flexible loop. {ECO:0000256|HAMAP-
Rule:MF_00086}.
METAL 24 24 Magnesium. {ECO:0000256|HAMAP-
Rule:MF_00086}.
METAL 50 50 Potassium. {ECO:0000256|HAMAP-
Rule:MF_00086}.
BINDING 22 22 ATP. {ECO:0000256|HAMAP-Rule:MF_00086}.
BINDING 63 63 Methionine. {ECO:0000256|HAMAP-
Rule:MF_00086}.
BINDING 106 106 Methionine. {ECO:0000256|HAMAP-
Rule:MF_00086}.
BINDING 257 257 ATP; shared with neighboring subunit.
{ECO:0000256|HAMAP-Rule:MF_00086}.
BINDING 257 257 Methionine; shared with neighboring
subunit. {ECO:0000256|HAMAP-
Rule:MF_00086}.
BINDING 280 280 ATP; via amide nitrogen; shared with
neighboring subunit. {ECO:0000256|HAMAP-
Rule:MF_00086}.
BINDING 284 284 ATP; shared with neighboring subunit.
{ECO:0000256|HAMAP-Rule:MF_00086}.
BINDING 288 288 Methionine. {ECO:0000256|HAMAP-
Rule:MF_00086}.
SEQUENCE 403 AA; 43503 MW; 94209C6A5AC0D4DC CRC64;
MPTSFMQSPQ LFFTSESVTE GHPDKLCDQV SDAILDAFLE KDPRSRVACE TSATTGLVLV
MGEVTTEAYV EIQEVVRRTI RDFGYTGTGV GFDADTCGVI VALHGQSADI AMGVDKALEA
KQGAMTEAEI EAVGAGDQGM MFGFACNETP ELMPLTISLA HKLTRELAVA RKSGQIAYLG
PDAKSQVTVE YSHGQPVRVD TLLISTQHAA DVSQEQIRED VIEDIFHKVV PAELIDGSTK
YYVNPTGRFV TGGPHGDAGL TGRKIIVDTY GGVARHGGGA FSGKDPTKVD RSAAYAARWV
AKNVVAAGLA DRFELQLAYA IGVARPLSVS VETFGTNKVA EETIVKLINE HFDLRPGAII
RDLDLRRPIY RQTAAYGHFG RTDVDLPWER TDRADALRRA AGL


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