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S-adenosylmethionine synthase 1 (AdoMet synthase 1) (EC 2.5.1.6) (Methionine adenosyltransferase 1) (MAT 1)

 METK1_ORYSI             Reviewed;         396 AA.
A2Y053; P46611; Q6AVZ2; Q8VXC5;
11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
11-SEP-2007, sequence version 2.
22-NOV-2017, entry version 62.
RecName: Full=S-adenosylmethionine synthase 1;
Short=AdoMet synthase 1;
EC=2.5.1.6 {ECO:0000250|UniProtKB:Q96551};
AltName: Full=Methionine adenosyltransferase 1;
Short=MAT 1;
Name=SAM1; Synonyms=SAMS; ORFNames=OsI_017696;
Oryza sativa subsp. indica (Rice).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BOP clade;
Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
NCBI_TaxID=39946;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=cv. Taichung native 1;
PubMed=7972513; DOI=10.1104/pp.105.4.1463;
van Breusegem F., Dekeyser R., Gielen J., van Montagu M., Caplan A.;
"Characterization of a S-adenosylmethionine synthetase gene in rice.";
Plant Physiol. 105:1463-1464(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Pusa Basmati; TISSUE=Root;
Mukhopadhyay A., Sharma S., Tyagi A.K.;
"Isolation and characterization of a new member of the rice S-
adenosyl-L-methionine synthetase family.";
Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. 93-11;
PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H.,
Cong L., Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J.,
Wang J., Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X.,
Wang J., Wang X., Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y.,
Zhang Z., Bao J., Han Y., Dong L., Ji J., Chen P., Wu S., Liu J.,
Xiao Y., Bu D., Tan J., Yang L., Ye C., Zhang J., Xu J., Zhou Y.,
Yu Y., Zhang B., Zhuang S., Wei H., Liu B., Lei M., Yu H., Li Y.,
Xu H., Wei S., He X., Fang L., Zhang Z., Zhang Y., Huang X., Su Z.,
Tong W., Li J., Tong Z., Li S., Ye J., Wang L., Fang L., Lei T.,
Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F., Xu H.,
Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q., Li W.,
Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J., Gao L.,
Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M., McDermott J.,
Samudrala R., Wang J., Wong G.K.-S., Yang H.;
"The genomes of Oryza sativa: a history of duplications.";
PLoS Biol. 3:266-281(2005).
-!- FUNCTION: Catalyzes the formation of S-adenosylmethionine from
methionine and ATP. The reaction comprises two steps that are both
catalyzed by the same enzyme: formation of S-adenosylmethionine
(AdoMet) and triphosphate, and subsequent hydrolysis of the
triphosphate. {ECO:0000250|UniProtKB:Q96551}.
-!- CATALYTIC ACTIVITY: ATP + L-methionine + H(2)O = phosphate +
diphosphate + S-adenosyl-L-methionine.
{ECO:0000250|UniProtKB:Q96551}.
-!- COFACTOR:
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000250|UniProtKB:Q96551};
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000250|UniProtKB:Q96551};
Name=Co(2+); Xref=ChEBI:CHEBI:48828;
Evidence={ECO:0000250|UniProtKB:Q96551};
Note=Binds 2 divalent ions per subunit. The metal ions interact
primarily with the substrate (By similarity). Can utilize
magnesium, manganese or cobalt (in vitro) (By similarity).
{ECO:0000250|UniProtKB:P13444, ECO:0000250|UniProtKB:Q96551};
-!- COFACTOR:
Name=K(+); Xref=ChEBI:CHEBI:29103;
Evidence={ECO:0000250|UniProtKB:Q96551};
Note=Binds 1 potassium ion per subunit. The potassium ion
interacts primarily with the substrate (By similarity).
{ECO:0000250|UniProtKB:P13444};
-!- PATHWAY: Amino-acid biosynthesis; S-adenosyl-L-methionine
biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1.
{ECO:0000250|UniProtKB:Q96551}.
-!- SUBUNIT: Homotetramer. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
-!- SIMILARITY: Belongs to the AdoMet synthase family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=EAY96463.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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EMBL; Z26867; CAA81481.1; -; Genomic_DNA.
EMBL; AJ296743; CAC82203.1; -; mRNA.
EMBL; CM000130; EAY96463.1; ALT_SEQ; Genomic_DNA.
ProteinModelPortal; A2Y053; -.
SMR; A2Y053; -.
STRING; 39946.BGIOSGA019139-PA; -.
EnsemblPlants; OS05T0135700-01; OS05T0135700-01; OS05G0135700.
Gramene; OS05T0135700-01; OS05T0135700-01; OS05G0135700.
eggNOG; KOG1506; Eukaryota.
eggNOG; COG0192; LUCA.
HOGENOM; HOG000245710; -.
UniPathway; UPA00315; UER00080.
Proteomes; UP000007015; Chromosome 5.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; Cobalt; Complete proteome; Cytoplasm; Magnesium;
Metal-binding; Nucleotide-binding; One-carbon metabolism; Potassium;
Reference proteome; Transferase.
CHAIN 1 396 S-adenosylmethionine synthase 1.
/FTId=PRO_0000302887.
NP_BIND 170 172 ATP. {ECO:0000250|UniProtKB:Q00266}.
NP_BIND 238 241 ATP. {ECO:0000250|UniProtKB:Q00266}.
NP_BIND 255 256 ATP. {ECO:0000250|UniProtKB:P0A817}.
METAL 12 12 Magnesium.
{ECO:0000250|UniProtKB:P13444}.
METAL 46 46 Potassium.
{ECO:0000250|UniProtKB:P0A817}.
BINDING 18 18 ATP. {ECO:0000250|UniProtKB:Q00266}.
BINDING 59 59 Methionine.
{ECO:0000250|UniProtKB:P0A817}.
BINDING 102 102 Methionine.
{ECO:0000250|UniProtKB:P0A817}.
BINDING 249 249 ATP. {ECO:0000250|UniProtKB:Q00266}.
BINDING 249 249 Methionine; shared with neighboring
subunit. {ECO:0000250|UniProtKB:P0A817}.
BINDING 272 272 ATP; via amide nitrogen; shared with
neighboring subunit.
{ECO:0000250|UniProtKB:P0A817}.
BINDING 276 276 ATP; shared with neighboring subunit.
{ECO:0000250|UniProtKB:P0A817}.
BINDING 280 280 ATP; shared with neighboring subunit.
{ECO:0000250|UniProtKB:P13444}.
BINDING 280 280 Methionine.
{ECO:0000250|UniProtKB:P0A817}.
CONFLICT 157 157 E -> K (in Ref. 2; CAC82203).
{ECO:0000305}.
SEQUENCE 396 AA; 43220 MW; 16FE43474045FEB9 CRC64;
MAALDTFLFT SESVNEGHPD KLCDQVSDAV LDACLAEDPD SKVACETCTK TNMVMVFGEI
TTKANVDYEK IVRETCRNIG FVSADVGLDA DHCKVLVNIE QQSPDIAQGV HGHFTKRPEE
IGAGDQGHMF GYATDETPEL MPLSHVLATK LGARLTEVRK NGTCAWLRPD GKTQVTVEYR
NESGARVPVR VHTVLISTQH DETVTNDEIA ADLKEHVIKP VIPEQYLDEK TIFHLNPSGR
FVIGGPHGDA GLTGRKIIID TYGGWGAHGG GAFSGKDPTK VDRSGAYVAR QAAKSIVASG
LARRCIVQVS YAIGVPEPLS VFVDTYGTGR IPDKEILKIV KENFDFRPGM IIINLDLKKG
GNGRYLKTAA YGHFGRDDPD FTWEVVKPLK WEKPSA


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