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S-adenosylmethionine synthase (EC 2.5.1.6)

 M1GLH9_9ASPA            Unreviewed;       396 AA.
M1GLH9;
01-MAY-2013, integrated into UniProtKB/TrEMBL.
01-MAY-2013, sequence version 1.
30-NOV-2016, entry version 15.
RecName: Full=S-adenosylmethionine synthase {ECO:0000256|RuleBase:RU000541};
EC=2.5.1.6 {ECO:0000256|RuleBase:RU000541};
Name=SAMS {ECO:0000313|EMBL:AGE15419.1};
Hosta ventricosa (blue plantain lily).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; Liliopsida; Asparagales; Asparagaceae;
Agavoideae; Hosta.
NCBI_TaxID=39527 {ECO:0000313|EMBL:AGE15419.1};
[1] {ECO:0000313|EMBL:AGE15419.1}
NUCLEOTIDE SEQUENCE.
Yang L.;
"Cloning and expression of three ethylene biosynthesis genes from
Hosta ventricosa flower.";
Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Catalyzes the formation of S-adenosylmethionine from
methionine and ATP. {ECO:0000256|RuleBase:RU000541}.
-!- CATALYTIC ACTIVITY: ATP + L-methionine + H(2)O = phosphate +
diphosphate + S-adenosyl-L-methionine.
{ECO:0000256|RuleBase:RU000541}.
-!- COFACTOR:
Name=K(+); Xref=ChEBI:CHEBI:29103;
Evidence={ECO:0000256|RuleBase:RU000541};
Note=Binds 1 potassium ion per subunit. The potassium ion
interacts primarily with the substrate.
{ECO:0000256|RuleBase:RU000541};
-!- COFACTOR:
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000256|RuleBase:RU000541};
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000256|RuleBase:RU000541};
Name=Co(2+); Xref=ChEBI:CHEBI:48828;
Evidence={ECO:0000256|RuleBase:RU000541};
Note=Binds 2 divalent ions per subunit. The metal ions interact
primarily with the substrate. Can utilize magnesium, manganese or
cobalt (in vitro). {ECO:0000256|RuleBase:RU000541};
-!- PATHWAY: Amino-acid biosynthesis; S-adenosyl-L-methionine
biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1.
{ECO:0000256|RuleBase:RU000541}.
-!- SIMILARITY: Belongs to the AdoMet synthase family.
{ECO:0000256|RuleBase:RU004462}.
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EMBL; JX274301; AGE15419.1; -; mRNA.
UniPathway; UPA00315; UER00080.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004478; F:methionine adenosyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
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.
2: Evidence at transcript level;
ATP-binding {ECO:0000256|RuleBase:RU000541};
Magnesium {ECO:0000256|RuleBase:RU000541};
Metal-binding {ECO:0000256|RuleBase:RU000541};
Nucleotide-binding {ECO:0000256|RuleBase:RU000541};
One-carbon metabolism {ECO:0000256|RuleBase:RU000541};
Potassium {ECO:0000256|RuleBase:RU000541};
Transferase {ECO:0000256|RuleBase:RU000541}.
DOMAIN 7 104 S-AdoMet_synt_N.
{ECO:0000259|Pfam:PF00438}.
DOMAIN 120 241 S-AdoMet_synt_M.
{ECO:0000259|Pfam:PF02772}.
DOMAIN 243 384 S-AdoMet_synt_C.
{ECO:0000259|Pfam:PF02773}.
SEQUENCE 396 AA; 43250 MW; 9E0D1716B779852D CRC64;
MASEDTFLFT SESVNEGHPD KLCDQTSDAV LDACLAQDPD SKVACETCSK TNMVMVFGEI
TTKANVDYEK IVRDTCRHIG FVSDDVGLDA DNCKVLVNIE QQSPDIAQGV HGHFTKSPEE
IGAGDQGHMF GYATDETPEY MPLTHVLATK LGARLTEVRK DGTCAWLRPD GKTQVTIEYR
NDNGAMVPIR VHTVLISTQH DETVTNDEIA ADLKEHVIKP VIPAQYLDEK TIFHLNPSGR
FVIGGPHGDA GLTGRKIIID TYGGWGAHGG GAFSGKDPTK VDRSGAYIVR QAAKSIVANG
LARRCIVQVS YAIGVPEPLS VFVDTYGTGK IPDKEILKIV KENFDFRPGM ITINLDLKRG
GNGRFLKTAA YGHFGRDDPD FTWETVKPLK WEKPAA


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