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S-adenosylmethionine synthase isoform type-1 (AdoMet synthase 1) (EC 2.5.1.6) (Methionine adenosyltransferase 1) (MAT 1) (Methionine adenosyltransferase I/III) (MAT-I/III)

 METK1_RAT               Reviewed;         397 AA.
P13444; Q5FVU2;
01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
01-NOV-1990, sequence version 2.
10-MAY-2017, entry version 151.
RecName: Full=S-adenosylmethionine synthase isoform type-1;
Short=AdoMet synthase 1;
EC=2.5.1.6 {ECO:0000269|PubMed:10873471, ECO:0000269|PubMed:1517209, ECO:0000269|PubMed:9755242};
AltName: Full=Methionine adenosyltransferase 1;
Short=MAT 1;
AltName: Full=Methionine adenosyltransferase I/III;
Short=MAT-I/III;
Name=Mat1a; Synonyms=Ams1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
STRAIN=Wistar; TISSUE=Liver;
PubMed=2806235; DOI=10.1111/j.1432-1033.1989.tb15042.x;
Horikawa S., Ishikawa M., Ozasa H., Tsukada K.;
"Isolation of a cDNA encoding the rat liver S-adenosylmethionine
synthetase.";
Eur. J. Biochem. 184:497-501(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1915866; DOI=10.1016/0014-5793(91)81245-4;
Alvarez L., Asuncion M., Corrales F., Pajares M.A., Mato J.M.;
"Analysis of the 5' non-coding region of rat liver S-
adenosylmethionine synthetase mRNA and comparison of the Mr deduced
from the cDNA sequence and the purified enzyme.";
FEBS Lett. 290:142-146(1991).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Spleen;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
SUBUNIT, CATALYTIC ACTIVITY, FUNCTION, PATHWAY, AND TISSUE
SPECIFICITY.
PubMed=1517209;
Pajares M.A., Duran C., Corrales F., Pliego M.M., Mato J.M.;
"Modulation of rat liver S-adenosylmethionine synthetase activity by
glutathione.";
J. Biol. Chem. 267:17598-17605(1992).
[5]
S-NITROSYLATION, CATALYTIC ACTIVITY, FUNCTION, SUBUNIT, AND PATHWAY.
PubMed=9755242; DOI=10.1002/hep.510280420;
Ruiz F., Corrales F.J., Miqueo C., Mato J.M.;
"Nitric oxide inactivates rat hepatic methionine adenosyltransferase
In vivo by S-nitrosylation.";
Hepatology 28:1051-1057(1998).
[6]
S-NITROSYLATION AT CYS-121.
PubMed=10358060; DOI=10.1074/jbc.274.24.17075;
Perez-Mato I., Castro C., Ruiz F.A., Corrales F.J., Mato J.M.;
"Methionine adenosyltransferase S-nitrosylation is regulated by the
basic and acidic amino acids surrounding the target thiol.";
J. Biol. Chem. 274:17075-17079(1999).
[7]
DISULFIDE BOND.
PubMed=10601859; DOI=10.1046/j.1432-1327.2000.00974.x;
Martinez-Chantar M.L., Pajares M.A.;
"Assignment of a single disulfide bridge in rat liver methionine
adenosyltransferase.";
Eur. J. Biochem. 267:132-137(2000).
[8] {ECO:0000244|PDB:1QM4}
X-RAY CRYSTALLOGRAPHY (2.66 ANGSTROMS) IN COMPLEX WITH METHIONINE
ANALOG; POTASSIUM AND MAGNESIUM, FUNCTION, CATALYTIC ACTIVITY,
PATHWAY, SUBUNIT, MUTAGENESIS OF ASP-180; LYS-182 AND PHE-251, AND
DISULFIDE BOND.
PubMed=10873471; DOI=10.1006/jmbi.2000.3858;
Gonzalez B., Pajares M.A., Hermoso J.A., Alvarez L., Garrido F.,
Sufrin J.R., Sanz-Aparicio J.;
"The crystal structure of tetrameric methionine adenosyltransferase
from rat liver reveals the methionine-binding site.";
J. Mol. Biol. 300:363-375(2000).
[9] {ECO:0000244|PDB:1O90, ECO:0000244|PDB:1O92, ECO:0000244|PDB:1O93, ECO:0000244|PDB:1O9T}
X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) IN COMPLEXES WITH ATP;
METHIONINE POTASSIUM AND MAGNESIUM, AND SUBUNIT.
PubMed=12888348; DOI=10.1016/S0022-2836(03)00728-9;
Gonzalez B., Pajares M.A., Hermoso J.A., Guillerm D., Guillerm G.,
Sanz-Aparicio J.;
"Crystal structures of methionine adenosyltransferase complexed with
substrates and products reveal the methionine-ATP recognition and give
insights into the catalytic mechanism.";
J. Mol. Biol. 331:407-416(2003).
-!- 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:0000269|PubMed:10873471,
ECO:0000269|PubMed:1517209, ECO:0000269|PubMed:9755242}.
-!- CATALYTIC ACTIVITY: ATP + L-methionine + H(2)O = phosphate +
diphosphate + S-adenosyl-L-methionine.
{ECO:0000269|PubMed:10873471, ECO:0000269|PubMed:1517209,
ECO:0000269|PubMed:9755242}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000305|PubMed:10873471};
Note=Binds 2 magnesium ions per subunit. The magnesium ions
interact primarily with the substrate.
{ECO:0000305|PubMed:10873471};
-!- COFACTOR:
Name=K(+); Xref=ChEBI:CHEBI:29103;
Evidence={ECO:0000305|PubMed:10873471};
Note=Binds 1 potassium ion per subunit. The potassium ion
interacts primarily with the substrate.
{ECO:0000305|PubMed:10873471};
-!- PATHWAY: Amino-acid biosynthesis; S-adenosyl-L-methionine
biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1.
{ECO:0000269|PubMed:10873471, ECO:0000269|PubMed:1517209,
ECO:0000269|PubMed:9755242}.
-!- SUBUNIT: Homotetramer (MAT-I); dimer of dimers (PubMed:1517209,
PubMed:9755242, PubMed:10873471, PubMed:12888348). Homodimer (MAT-
III) (PubMed:1517209, PubMed:9755242).
{ECO:0000269|PubMed:10873471, ECO:0000269|PubMed:12888348,
ECO:0000269|PubMed:1517209, ECO:0000305|PubMed:9755242}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-961260, EBI-961260;
-!- TISSUE SPECIFICITY: Detected in liver (at protein level)
(PubMed:1517209). Expressed in liver (PubMed:2806235).
{ECO:0000269|PubMed:1517209, ECO:0000269|PubMed:2806235}.
-!- PTM: S-nitrosylation of Cys-121 inactivates the enzyme.
{ECO:0000269|PubMed:10358060, ECO:0000269|PubMed:9755242}.
-!- PTM: An intrachain disulfide bond can be formed (PubMed:10601859).
The protein structure shows that the relevant Cys residues are in
a position that would permit formation of a disulfide bond
(PubMed:10873471). {ECO:0000269|PubMed:10601859,
ECO:0000269|PubMed:10873471}.
-!- SIMILARITY: Belongs to the AdoMet synthase family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X15734; CAA33754.1; -; mRNA.
EMBL; X60822; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; BC089770; AAH89770.1; -; mRNA.
PIR; S06114; S06114.
RefSeq; NP_036992.2; NM_012860.2.
UniGene; Rn.10418; -.
PDB; 1O90; X-ray; 3.10 A; A/B=1-397.
PDB; 1O92; X-ray; 3.19 A; A/B=1-397.
PDB; 1O93; X-ray; 3.49 A; A/B=1-397.
PDB; 1O9T; X-ray; 2.90 A; A/B=1-397.
PDB; 1QM4; X-ray; 2.66 A; A/B=1-397.
PDBsum; 1O90; -.
PDBsum; 1O92; -.
PDBsum; 1O93; -.
PDBsum; 1O9T; -.
PDBsum; 1QM4; -.
ProteinModelPortal; P13444; -.
SMR; P13444; -.
BioGrid; 247370; 2.
STRING; 10116.ENSRNOP00000015190; -.
BindingDB; P13444; -.
ChEMBL; CHEMBL2195; -.
iPTMnet; P13444; -.
PhosphoSitePlus; P13444; -.
PaxDb; P13444; -.
PRIDE; P13444; -.
GeneID; 25331; -.
KEGG; rno:25331; -.
UCSC; RGD:3050; rat.
CTD; 4143; -.
RGD; 3050; Mat1a.
eggNOG; KOG1506; Eukaryota.
eggNOG; COG0192; LUCA.
HOVERGEN; HBG001562; -.
InParanoid; P13444; -.
KO; K00789; -.
PhylomeDB; P13444; -.
BioCyc; MetaCyc:MONOMER-8568; -.
BRENDA; 2.5.1.6; 5301.
UniPathway; UPA00315; UER00080.
EvolutionaryTrace; P13444; -.
PRO; PR:P13444; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005829; C:cytosol; IDA:RGD.
GO; GO:0016363; C:nuclear matrix; IDA:RGD.
GO; GO:0043531; F:ADP binding; IDA:RGD.
GO; GO:0016597; F:amino acid binding; IDA:RGD.
GO; GO:0005524; F:ATP binding; IDA:RGD.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0000287; F:magnesium ion binding; IDA:RGD.
GO; GO:0004478; F:methionine adenosyltransferase activity; IDA:RGD.
GO; GO:0046983; F:protein dimerization activity; IDA:RGD.
GO; GO:0042803; F:protein homodimerization activity; IDA:RGD.
GO; GO:0009087; P:methionine catabolic process; ISS:UniProtKB.
GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
GO; GO:0051260; P:protein homooligomerization; IDA:RGD.
GO; GO:0051289; P:protein homotetramerization; IDA:RGD.
GO; GO:0051262; P:protein tetramerization; IDA:RGD.
GO; GO:0006556; P:S-adenosylmethionine biosynthetic process; IDA:RGD.
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.
1: Evidence at protein level;
3D-structure; ATP-binding; Complete proteome; Disulfide bond;
Magnesium; Metal-binding; Nucleotide-binding; One-carbon metabolism;
Potassium; Reference proteome; S-nitrosylation; Transferase.
CHAIN 1 397 S-adenosylmethionine synthase isoform
type-1.
/FTId=PRO_0000174434.
NP_BIND 180 182 ATP. {ECO:0000244|PDB:1O92,
ECO:0000244|PDB:1O9T,
ECO:0000269|PubMed:12888348}.
NP_BIND 248 251 ATP. {ECO:0000244|PDB:1QM4,
ECO:0000305|PubMed:10873471,
ECO:0000305|PubMed:12888348}.
NP_BIND 265 266 ATP. {ECO:0000244|PDB:1O9T,
ECO:0000269|PubMed:12888348}.
REGION 114 126 Flexible loop.
{ECO:0000250|UniProtKB:P0A817}.
METAL 24 24 Magnesium. {ECO:0000244|PDB:1O92,
ECO:0000244|PDB:1O9T}.
METAL 58 58 Potassium.
{ECO:0000250|UniProtKB:P0A817}.
BINDING 30 30 ATP. {ECO:0000244|PDB:1O92,
ECO:0000244|PDB:1O93,
ECO:0000244|PDB:1O9T,
ECO:0000269|PubMed:12888348}.
BINDING 71 71 Methionine.
{ECO:0000250|UniProtKB:P0A817}.
BINDING 114 114 Methionine.
{ECO:0000250|UniProtKB:P0A817}.
BINDING 259 259 ATP. {ECO:0000244|PDB:1O92}.
BINDING 259 259 Methionine; shared with neighboring
subunit. {ECO:0000250|UniProtKB:P0A817}.
BINDING 282 282 ATP; via amide nitrogen; shared with
neighboring subunit.
{ECO:0000244|PDB:1O92}.
BINDING 286 286 ATP; shared with neighboring subunit.
{ECO:0000244|PDB:1O92,
ECO:0000244|PDB:1O9T,
ECO:0000269|PubMed:12888348}.
BINDING 290 290 ATP; shared with neighboring subunit.
{ECO:0000244|PDB:1O92,
ECO:0000244|PDB:1O9T,
ECO:0000269|PubMed:12888348}.
BINDING 290 290 Methionine.
{ECO:0000250|UniProtKB:P0A817}.
MOD_RES 121 121 S-nitrosocysteine.
{ECO:0000269|PubMed:10358060}.
DISULFID 35 61 {ECO:0000269|PubMed:10601859,
ECO:0000305|PubMed:10873471}.
MUTAGEN 180 180 D->G: Loss of S-adenosylmethionine
synthase activity, but does not abolish
polyphosphatase activity.
{ECO:0000269|PubMed:10873471}.
MUTAGEN 182 182 K->G: Loss of S-adenosylmethionine
synthase activity, but does not abolish
polyphosphatase activity.
{ECO:0000269|PubMed:10873471}.
MUTAGEN 251 251 F->D,G: Loss of S-adenosylmethionine
synthase activity, but does not abolish
polyphosphatase activity.
{ECO:0000269|PubMed:10873471}.
CONFLICT 345 345 Missing (in Ref. 3; AAH89770).
{ECO:0000305}.
STRAND 19 26 {ECO:0000244|PDB:1QM4}.
HELIX 31 47 {ECO:0000244|PDB:1QM4}.
STRAND 54 61 {ECO:0000244|PDB:1QM4}.
STRAND 63 73 {ECO:0000244|PDB:1QM4}.
HELIX 80 91 {ECO:0000244|PDB:1QM4}.
TURN 96 99 {ECO:0000244|PDB:1QM4}.
TURN 102 104 {ECO:0000244|PDB:1QM4}.
STRAND 105 109 {ECO:0000244|PDB:1QM4}.
STRAND 112 114 {ECO:0000244|PDB:1QM4}.
STRAND 137 144 {ECO:0000244|PDB:1QM4}.
HELIX 153 171 {ECO:0000244|PDB:1QM4}.
STRAND 172 174 {ECO:0000244|PDB:1QM4}.
STRAND 177 190 {ECO:0000244|PDB:1QM4}.
STRAND 197 210 {ECO:0000244|PDB:1QM4}.
STRAND 212 214 {ECO:0000244|PDB:1QM4}.
HELIX 216 225 {ECO:0000244|PDB:1QM4}.
TURN 226 231 {ECO:0000244|PDB:1QM4}.
TURN 234 236 {ECO:0000244|PDB:1QM4}.
STRAND 242 246 {ECO:0000244|PDB:1QM4}.
TURN 256 259 {ECO:0000244|PDB:1QM4}.
TURN 267 274 {ECO:0000244|PDB:1QM4}.
HELIX 291 308 {ECO:0000244|PDB:1QM4}.
STRAND 313 321 {ECO:0000244|PDB:1QM4}.
STRAND 331 335 {ECO:0000244|PDB:1QM4}.
HELIX 347 354 {ECO:0000244|PDB:1QM4}.
HELIX 359 365 {ECO:0000244|PDB:1QM4}.
TURN 366 369 {ECO:0000244|PDB:1QM4}.
HELIX 373 376 {ECO:0000244|PDB:1QM4}.
STRAND 377 379 {ECO:0000244|PDB:1O9T}.
STRAND 381 383 {ECO:0000244|PDB:1QM4}.
HELIX 388 390 {ECO:0000244|PDB:1QM4}.
SEQUENCE 397 AA; 43698 MW; A847A8CCBB2007BA CRC64;
MNGPVDGLCD HSLSEEGAFM FTSESVGEGH PDKICDQISD AVLDAHLKQD PNAKVACETV
CKTGMVLLCG EITSMAMIDY QRVVRDTIKH IGYDDSAKGF DFKTCNVLVA LEQQSPDIAQ
CVHLDRNEED VGAGDQGLMF GYATDETEEC MPLTIVLAHK LNTRMADLRR SGVLPWLRPD
SKTQVTVQYV QDNGAVIPVR VHTIVISVQH NEDITLEAMR EALKEQVIKA VVPAKYLDED
TIYHLQPSGR FVIGGPQGDA GVTGRKIIVD TYGGWGAHGG GAFSGKDYTK VDRSAAYAAR
WVAKSLVKAG LCRRVLVQVS YAIGVAEPLS ISIFTYGTSK KTERDELLEV VNKNFDLRPG
VIVRDLDLKK PIYQKTACYG HFGRSEFPWE VPKKLVF


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