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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_HUMAN             Reviewed;         395 AA.
Q00266; D3DWD5; Q5QP09;
01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
01-OCT-1993, sequence version 2.
12-SEP-2018, entry version 192.
RecName: Full=S-adenosylmethionine synthase isoform type-1;
Short=AdoMet synthase 1;
EC=2.5.1.6 {ECO:0000269|PubMed:10677294};
AltName: Full=Methionine adenosyltransferase 1;
Short=MAT 1;
AltName: Full=Methionine adenosyltransferase I/III;
Short=MAT-I/III;
Name=MAT1A; Synonyms=AMS1, MATA1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
PubMed=8393662; DOI=10.1042/bj2930481;
Alvarez L., Corrales F., Mato J.M.;
"Characterization of a full-length cDNA encoding human liver S-
adenosylmethionine synthetase: tissue-specific gene expression and
mRNA levels in hepatopathies.";
Biochem. J. 293:481-486(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
PubMed=1772450;
Horikawa S., Tsukada K.;
"Molecular cloning and nucleotide sequence of cDNA encoding the human
liver S-adenosylmethionine synthetase.";
Biochem. Int. 25:81-90(1991).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164054; DOI=10.1038/nature02462;
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lymph;
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).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[8]
X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 14-395 IN COMPLEX WITH
S-ADENOSYL-L-METHIONINE, AND SUBUNIT.
PubMed=23425511; DOI=10.1042/BJ20121580;
Shafqat N., Muniz J.R., Pilka E.S., Papagrigoriou E., von Delft F.,
Oppermann U., Yue W.W.;
"Insight into S-adenosylmethionine biosynthesis from the crystal
structures of the human methionine adenosyltransferase catalytic and
regulatory subunits.";
Biochem. J. 452:27-36(2013).
[9]
VARIANTS MATD ASP-55; PRO-305; MET-322 AND LEU-357.
PubMed=7560086; DOI=10.1172/JCI118240;
Ubagai T., Lei K.-J., Huang S., Mudd S.H., Levy H.L., Chou J.Y.;
"Molecular mechanisms of an inborn error of methionine pathway.
Methionine adenosyltransferase deficiency.";
J. Clin. Invest. 96:1943-1947(1995).
[10]
VARIANTS MATD CYS-199; GLN-356 AND SER-378.
PubMed=8770875; DOI=10.1172/JCI118862;
Chamberlin M.E., Ubagai T., Mudd S.H., Wilson W.G., Leonard J.V.,
Chou J.Y.;
"Demyelination of the brain is associated with methionine
adenosyltransferase I/III deficiency.";
J. Clin. Invest. 98:1021-1027(1996).
[11]
VARIANT MATD HIS-264.
PubMed=9042912;
Chamberlin M.E., Ubagai T., Mudd S.H., Levy H.L., Chou J.Y.;
"Dominant inheritance of isolated hypermethioninemia is associated
with a mutation in the human methionine adenosyltransferase 1A gene.";
Am. J. Hum. Genet. 60:540-546(1997).
[12]
VARIANTS MATD ASN-38; CYS-264; HIS-264; MET-322; ARG-336 AND ALA-344,
CHARACTERIZATION OF VARIANTS MATD ASN-38; CYS-264; HIS-264; MET-322;
ARG-336 AND ALA-344, CATALYTIC ACTIVITY, FUNCTION, AND PATHWAY.
PubMed=10677294; DOI=10.1086/302752;
Chamberlin M.E., Ubagai T., Mudd S.H., Thomas J., Pao V.Y.,
Nguyen T.K., Levy H.L., Greene C., Freehauf C., Chou J.Y.;
"Methionine adenosyltransferase I/III deficiency: novel mutations and
clinical variations.";
Am. J. Hum. Genet. 66:347-355(2000).
-!- 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:10677294}.
-!- CATALYTIC ACTIVITY: ATP + L-methionine + H(2)O = phosphate +
diphosphate + S-adenosyl-L-methionine.
{ECO:0000269|PubMed:10677294}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000250|UniProtKB:P13444};
Note=Binds 2 magnesium ions per subunit. The magnesium ions
interact primarily with the substrate.
{ECO:0000250|UniProtKB:P13444};
-!- COFACTOR:
Name=K(+); Xref=ChEBI:CHEBI:29103;
Evidence={ECO:0000250|UniProtKB:P13444};
Note=Binds 1 potassium ion per subunit. The potassium ion
interacts primarily with the substrate.
{ECO:0000250|UniProtKB:P13444};
-!- PATHWAY: Amino-acid biosynthesis; S-adenosyl-L-methionine
biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1.
{ECO:0000269|PubMed:10677294}.
-!- SUBUNIT: Homotetramer (MAT-I); dimer of dimers (PubMed:23425511).
Homodimer (MAT-III) (By similarity).
{ECO:0000250|UniProtKB:P13444, ECO:0000269|PubMed:23425511}.
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-967087, EBI-967087;
P31153:MAT2A; NbExp=4; IntAct=EBI-967087, EBI-1050743;
-!- TISSUE SPECIFICITY: Expressed in liver.
{ECO:0000269|PubMed:8393662}.
-!- PTM: S-nitrosylation of Cys-120 inactivates the enzyme.
{ECO:0000250|UniProtKB:P13444}.
-!- PTM: An intrachain disulfide bond can be formed. The protein
structure shows that the relevant Cys residues are in a position
that would permit formation of a disulfide bond.
{ECO:0000250|UniProtKB:P13444}.
-!- DISEASE: Methionine adenosyltransferase deficiency (MATD)
[MIM:250850]: An inborn error of metabolism resulting in isolated
hypermethioninemia. Most patients have no clinical abnormalities,
although some neurologic symptoms may be present in rare cases
with severe loss of methionine adenosyltransferase activity.
{ECO:0000269|PubMed:10677294, ECO:0000269|PubMed:7560086,
ECO:0000269|PubMed:8770875, ECO:0000269|PubMed:9042912}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- SIMILARITY: Belongs to the AdoMet synthase family. {ECO:0000305}.
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EMBL; D49357; BAA08355.1; -; mRNA.
EMBL; X69078; CAA48822.1; -; mRNA.
EMBL; AL359195; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471142; EAW80396.1; -; Genomic_DNA.
EMBL; CH471142; EAW80397.1; -; Genomic_DNA.
EMBL; BC018359; AAH18359.1; -; mRNA.
CCDS; CCDS7365.1; -.
PIR; S27363; S27363.
RefSeq; NP_000420.1; NM_000429.2.
RefSeq; XP_005269899.1; XM_005269842.4.
UniGene; Hs.282670; -.
PDB; 2OBV; X-ray; 2.05 A; A=16-395.
PDBsum; 2OBV; -.
ProteinModelPortal; Q00266; -.
SMR; Q00266; -.
BioGrid; 110313; 14.
ComplexPortal; CPX-3168; Methionine adenosyltransferase complex variant 1.
ComplexPortal; CPX-3169; Methionine adenosyltransferase complex variant 3.
IntAct; Q00266; 1.
STRING; 9606.ENSP00000361280; -.
DrugBank; DB03191; 3-Oxiran-2ylalanine.
DrugBank; DB03611; L-2-Amino-4-Methoxy-Cis-but-3-Enoic Acid.
DrugBank; DB00134; L-Methionine.
DrugBank; DB00118; S-Adenosylmethionine.
iPTMnet; Q00266; -.
PhosphoSitePlus; Q00266; -.
BioMuta; MAT1A; -.
DMDM; 417297; -.
EPD; Q00266; -.
MaxQB; Q00266; -.
PaxDb; Q00266; -.
PeptideAtlas; Q00266; -.
PRIDE; Q00266; -.
ProteomicsDB; 57842; -.
DNASU; 4143; -.
Ensembl; ENST00000372213; ENSP00000361287; ENSG00000151224.
GeneID; 4143; -.
KEGG; hsa:4143; -.
UCSC; uc001kbw.4; human.
CTD; 4143; -.
DisGeNET; 4143; -.
EuPathDB; HostDB:ENSG00000151224.12; -.
GeneCards; MAT1A; -.
HGNC; HGNC:6903; MAT1A.
HPA; HPA048627; -.
MalaCards; MAT1A; -.
MIM; 250850; phenotype.
MIM; 610550; gene.
neXtProt; NX_Q00266; -.
OpenTargets; ENSG00000151224; -.
Orphanet; 168598; Brain demyelination due to methionine adenosyltransferase deficiency.
PharmGKB; PA30646; -.
eggNOG; KOG1506; Eukaryota.
eggNOG; COG0192; LUCA.
GeneTree; ENSGT00500000044811; -.
HOGENOM; HOG000245710; -.
HOVERGEN; HBG001562; -.
InParanoid; Q00266; -.
KO; K00789; -.
OMA; SEFPWEI; -.
OrthoDB; EOG091G08Z2; -.
PhylomeDB; Q00266; -.
TreeFam; TF300511; -.
Reactome; R-HSA-156581; Methylation.
Reactome; R-HSA-1614635; Sulfur amino acid metabolism.
Reactome; R-HSA-2408508; Metabolism of ingested SeMet, Sec, MeSec into H2Se.
Reactome; R-HSA-5579024; Defective MAT1A causes Methionine adenosyltransferase deficiency (MATD).
UniPathway; UPA00315; UER00080.
ChiTaRS; MAT1A; human.
EvolutionaryTrace; Q00266; -.
GenomeRNAi; 4143; -.
PRO; PR:Q00266; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000151224; Expressed in 89 organ(s), highest expression level in right lobe of liver.
CleanEx; HS_MAT1A; -.
ExpressionAtlas; Q00266; baseline and differential.
Genevisible; Q00266; HS.
GO; GO:0005829; C:cytosol; IBA:GO_Central.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004478; F:methionine adenosyltransferase activity; IDA:UniProtKB.
GO; GO:0098601; F:selenomethionine adenosyltransferase activity; TAS:Reactome.
GO; GO:0009087; P:methionine catabolic process; IMP:UniProtKB.
GO; GO:0032259; P:methylation; TAS:Reactome.
GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
GO; GO:0051289; P:protein homotetramerization; IDA:UniProtKB.
GO; GO:0006556; P:S-adenosylmethionine biosynthetic process; IMP:UniProtKB.
GO; GO:0001887; P:selenium compound metabolic process; TAS:Reactome.
GO; GO:0000096; P:sulfur amino acid metabolic process; TAS:Reactome.
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; Disease mutation;
Disulfide bond; Magnesium; Metal-binding; Nucleotide-binding;
One-carbon metabolism; Polymorphism; Potassium; Reference proteome;
S-nitrosylation; Transferase.
CHAIN 1 395 S-adenosylmethionine synthase isoform
type-1.
/FTId=PRO_0000174432.
NP_BIND 179 181 ATP. {ECO:0000244|PDB:2OBV,
ECO:0000305|PubMed:23425511}.
NP_BIND 247 250 ATP. {ECO:0000244|PDB:2OBV,
ECO:0000305|PubMed:23425511}.
NP_BIND 264 265 ATP. {ECO:0000250|UniProtKB:P0A817}.
REGION 113 125 Flexible loop.
{ECO:0000250|UniProtKB:P0A817}.
METAL 23 23 Magnesium.
{ECO:0000250|UniProtKB:P13444}.
METAL 57 57 Potassium.
{ECO:0000250|UniProtKB:P0A817}.
BINDING 29 29 ATP. {ECO:0000244|PDB:2OBV,
ECO:0000305|PubMed:23425511}.
BINDING 70 70 Methionine.
{ECO:0000250|UniProtKB:P0A817}.
BINDING 113 113 Methionine.
{ECO:0000250|UniProtKB:P0A817}.
BINDING 258 258 ATP. {ECO:0000244|PDB:2OBV,
ECO:0000305|PubMed:23425511}.
BINDING 258 258 Methionine; shared with neighboring
subunit. {ECO:0000250|UniProtKB:P0A817}.
BINDING 281 281 ATP; via amide nitrogen; shared with
neighboring subunit.
{ECO:0000250|UniProtKB:P0A817}.
BINDING 285 285 ATP; shared with neighboring subunit.
{ECO:0000250|UniProtKB:P0A817}.
BINDING 289 289 ATP; shared with neighboring subunit.
{ECO:0000250|UniProtKB:P13444}.
BINDING 289 289 Methionine.
{ECO:0000250|UniProtKB:P0A817}.
MOD_RES 120 120 S-nitrosocysteine.
{ECO:0000250|UniProtKB:P13444}.
DISULFID 34 60 {ECO:0000250|UniProtKB:P13444}.
VARIANT 38 38 S -> N (in MATD; abolishes enzyme
activity). {ECO:0000269|PubMed:10677294}.
/FTId=VAR_031242.
VARIANT 55 55 A -> D (in MATD; dbSNP:rs118204002).
{ECO:0000269|PubMed:7560086}.
/FTId=VAR_006935.
VARIANT 119 119 Q -> H (in dbSNP:rs1143693).
/FTId=VAR_028944.
VARIANT 199 199 R -> C (in MATD; retains 11% of wild-type
activity; dbSNP:rs773267230).
{ECO:0000269|PubMed:8770875}.
/FTId=VAR_006936.
VARIANT 264 264 R -> C (in MATD; has virtually no
enzymatic activity; dbSNP:rs118204005).
{ECO:0000269|PubMed:10677294}.
/FTId=VAR_031243.
VARIANT 264 264 R -> H (in MATD; dominant mutation;
dbSNP:rs72558181).
{ECO:0000269|PubMed:10677294,
ECO:0000269|PubMed:9042912}.
/FTId=VAR_006937.
VARIANT 305 305 L -> P (in MATD; dbSNP:rs118204004).
{ECO:0000269|PubMed:7560086}.
/FTId=VAR_006938.
VARIANT 322 322 I -> M (in MATD; diminishes but do not
completely abolishes enzyme activity; 46%
of the level of the wild-type enzyme;
dbSNP:rs118204001).
{ECO:0000269|PubMed:10677294,
ECO:0000269|PubMed:7560086}.
/FTId=VAR_006939.
VARIANT 336 336 G -> R (in MATD; retains significant
enzymatic activity; 23% of the level of
the wild-type enzyme; dbSNP:rs118204006).
{ECO:0000269|PubMed:10677294}.
/FTId=VAR_031244.
VARIANT 344 344 E -> A (in MATD; diminishes but do not
completely abolishes enzyme activity; 12%
of the level of the wild-type enzyme).
{ECO:0000269|PubMed:10677294}.
/FTId=VAR_031245.
VARIANT 356 356 R -> Q (in MATD; dbSNP:rs138742870).
{ECO:0000269|PubMed:8770875}.
/FTId=VAR_006940.
VARIANT 357 357 P -> L (in MATD; dbSNP:rs118204003).
{ECO:0000269|PubMed:7560086}.
/FTId=VAR_006941.
VARIANT 378 378 G -> S (in MATD).
{ECO:0000269|PubMed:8770875}.
/FTId=VAR_006942.
CONFLICT 272 273 GG -> AA (in Ref. 2; BAA08355).
{ECO:0000305}.
STRAND 18 25 {ECO:0000244|PDB:2OBV}.
HELIX 30 48 {ECO:0000244|PDB:2OBV}.
STRAND 53 61 {ECO:0000244|PDB:2OBV}.
STRAND 64 72 {ECO:0000244|PDB:2OBV}.
HELIX 79 90 {ECO:0000244|PDB:2OBV}.
HELIX 95 97 {ECO:0000244|PDB:2OBV}.
TURN 101 103 {ECO:0000244|PDB:2OBV}.
STRAND 105 111 {ECO:0000244|PDB:2OBV}.
HELIX 115 121 {ECO:0000244|PDB:2OBV}.
TURN 122 124 {ECO:0000244|PDB:2OBV}.
HELIX 127 129 {ECO:0000244|PDB:2OBV}.
STRAND 132 134 {ECO:0000244|PDB:2OBV}.
STRAND 136 143 {ECO:0000244|PDB:2OBV}.
HELIX 152 170 {ECO:0000244|PDB:2OBV}.
STRAND 171 173 {ECO:0000244|PDB:2OBV}.
STRAND 176 191 {ECO:0000244|PDB:2OBV}.
STRAND 194 209 {ECO:0000244|PDB:2OBV}.
STRAND 211 213 {ECO:0000244|PDB:2OBV}.
HELIX 215 224 {ECO:0000244|PDB:2OBV}.
HELIX 227 230 {ECO:0000244|PDB:2OBV}.
HELIX 233 235 {ECO:0000244|PDB:2OBV}.
STRAND 241 245 {ECO:0000244|PDB:2OBV}.
HELIX 254 256 {ECO:0000244|PDB:2OBV}.
TURN 266 273 {ECO:0000244|PDB:2OBV}.
HELIX 290 307 {ECO:0000244|PDB:2OBV}.
STRAND 312 320 {ECO:0000244|PDB:2OBV}.
STRAND 328 333 {ECO:0000244|PDB:2OBV}.
HELIX 342 352 {ECO:0000244|PDB:2OBV}.
HELIX 357 363 {ECO:0000244|PDB:2OBV}.
TURN 364 367 {ECO:0000244|PDB:2OBV}.
HELIX 371 374 {ECO:0000244|PDB:2OBV}.
STRAND 375 377 {ECO:0000244|PDB:2OBV}.
STRAND 379 381 {ECO:0000244|PDB:2OBV}.
HELIX 386 388 {ECO:0000244|PDB:2OBV}.
SEQUENCE 395 AA; 43648 MW; B3462A5670A5B0D4 CRC64;
MNGPVDGLCD HSLSEGVFMF TSESVGEGHP DKICDQISDA VLDAHLKQDP NAKVACETVC
KTGMVLLCGE ITSMAMVDYQ RVVRDTIKHI GYDDSAKGFD FKTCNVLVAL EQQSPDIAQC
VHLDRNEEDV GAGDQGLMFG YATDETEECM PLTIILAHKL NARMADLRRS GLLPWLRPDS
KTQVTVQYMQ DNGAVIPVRI HTIVISVQHN EDITLEEMRR ALKEQVIRAV VPAKYLDEDT
VYHLQPSGRF VIGGPQGDAG VTGRKIIVDT YGGWGAHGGG AFSGKDYTKV DRSAAYAARW
VAKSLVKAGL CRRVLVQVSY AIGVAEPLSI SIFTYGTSQK TERELLDVVH KNFDLRPGVI
VRDLDLKKPI YQKTACYGHF GRSEFPWEVP RKLVF


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15-288-22390A S-adenosylmethionine synthetase isoform type-2 - EC 2.5.1.6; Methionine adenosyltransferase 2; AdoMet synthetase 2; Methionine adenosyltransferase II; MAT-II Polyclonal 0.1 mg
10-288-22390F S-adenosylmethionine synthetase isoform type-2 - EC 2.5.1.6; Methionine adenosyltransferase 2; AdoMet synthetase 2; Methionine adenosyltransferase II; MAT-II 0.1 mg
10-288-22390F S-adenosylmethionine synthetase isoform type-2 - EC 2.5.1.6; Methionine adenosyltransferase 2; AdoMet synthetase 2; Methionine adenosyltransferase II; MAT-II 0.05 mg
27-079 MAT2B belongs to the methionine adenosyltransferase (MAT) family. MAT catalyzes the biosynthesis of S-adenosylmethionine from methionine and ATP. This protein is the regulatory beta subunit of MAT.The 0.05 mg
29-561 MAT1A catalyzes the formation of S-adenosylmethionine from methionine and ATP. Methionine adenosyltransferase deficiency is caused by recessive and dominant mutations, the latter identified in autosom 0.1 mg
CSB-EL013518RA Rat methionine adenosyltransferase II, beta (MAT2B) ELISA kit, Species Rat, Sample Type serum, plasma 96T
CSB-EL013517RA Rat methionine adenosyltransferase II, alpha (MAT2A) ELISA kit, Species Rat, Sample Type serum, plasma 96T
CSB-EL013516RA Rat methionine adenosyltransferase I, alpha (MAT1A) ELISA kit, Species Rat, Sample Type serum, plasma 96T
RP17932060001 Methionine Adenosyltransferase II, Alpha 1 mg
RP17932030005 Methionine Adenosyltransferase II, Alpha 5 µg
RP17932030020 Methionine Adenosyltransferase II, Alpha 20 µg
enz-320 Recombinant Human Methionine Adenosyltransferase II, Alpha 1mg
REN-493 Recombinant Human Methionine Adenosyltransferase I, Alpha 1mg
enz-320 Recombinant Human Methionine Adenosyltransferase II, Alpha 20
REN-320 Recombinant Human Methionine Adenosyltransferase II, Alpha 5
REN-461 Recombinant Human Methionine Adenosyltransferase II, Beta 5
enz-461 Recombinant Human Methionine Adenosyltransferase II, Beta 20
ENZ-493 Recombinant Human Methionine Adenosyltransferase I, Alpha 1mg
ENZ-320 Recombinant Human Methionine Adenosyltransferase II, Alpha 1mg
ARP55849_P050 MAT2B(methionine adenosyltransferase II, beta) 50 µg
enz-493 Recombinant Human Methionine Adenosyltransferase I, Alpha 10
ENZ-461 Recombinant Human Methionine Adenosyltransferase II, Beta 1mg
enz-493 Recombinant Human Methionine Adenosyltransferase I, Alpha 1mg
enz-461 Recombinant Human Methionine Adenosyltransferase II, Beta 1mg


 

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