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Protein

S-adenosylmethionine synthase isoform type-2

Gene

Mat2a

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the formation of S-adenosylmethionine from methionine and ATP.By similarity

Catalytic activityi

ATP + L-methionine + H2O = phosphate + diphosphate + S-adenosyl-L-methionine.

Cofactori

Protein has several cofactor binding sites:
  • Mg2+By similarity, Co2+By similarityNote: Binds 2 divalent ions per subunit. Magnesium or cobalt.By similarity
  • K+By similarityNote: Binds 1 potassium ion per subunit.By similarity

Pathwayi: S-adenosyl-L-methionine biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes S-adenosyl-L-methionine from L-methionine.
Proteins known to be involved in this subpathway in this organism are:
  1. S-adenosylmethionine synthase isoform type-2 (Mat2a), Methionine adenosyltransferase 2 subunit beta (Mat2b), S-adenosylmethionine synthase isoform type-1 (Mat1a), S-adenosylmethionine synthase (Mat2a), S-adenosylmethionine synthase (Mat2a)
This subpathway is part of the pathway S-adenosyl-L-methionine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes S-adenosyl-L-methionine from L-methionine, the pathway S-adenosyl-L-methionine biosynthesis and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi31 – 311MagnesiumBy similarity
Metal bindingi57 – 571PotassiumBy similarity
Binding sitei159 – 1591ATPSequence analysis
Metal bindingi283 – 2831PotassiumBy similarity
Metal bindingi291 – 2911MagnesiumBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi131 – 1366ATPSequence analysis

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • metal ion binding Source: UniProtKB-KW
  • methionine adenosyltransferase activity Source: MGI

GO - Biological processi

  • one-carbon metabolic process Source: UniProtKB-KW
  • S-adenosylmethionine biosynthetic process Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

One-carbon metabolism

Keywords - Ligandi

ATP-binding, Cobalt, Magnesium, Metal-binding, Nucleotide-binding, Potassium

Enzyme and pathway databases

ReactomeiR-MMU-156581. Methylation.
UniPathwayiUPA00315; UER00080.

Names & Taxonomyi

Protein namesi
Recommended name:
S-adenosylmethionine synthase isoform type-2 (EC:2.5.1.6)
Short name:
AdoMet synthase 2
Alternative name(s):
Methionine adenosyltransferase 2
Short name:
MAT 2
Gene namesi
Name:Mat2a
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 6

Organism-specific databases

MGIiMGI:2443731. Mat2a.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 395395S-adenosylmethionine synthase isoform type-2PRO_0000174437Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei81 – 811N6-acetyllysineBy similarity
Modified residuei114 – 1141PhosphoserineBy similarity

Post-translational modificationi

The alpha' subunit is a post-translationally modified version of MAT2A.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ3THS6.
PaxDbiQ3THS6.
PRIDEiQ3THS6.

PTM databases

iPTMnetiQ3THS6.
PhosphoSiteiQ3THS6.

Expressioni

Gene expression databases

BgeeiQ3THS6.
CleanExiMM_MAT2A.
ExpressionAtlasiQ3THS6. baseline and differential.
GenevisibleiQ3THS6. MM.

Interactioni

Subunit structurei

Heterotetramer composed of 2 catalytic alpha subunits (alpha and alpha') (MAT2A) and 1 copy of beta subunit (MAT2B).By similarity

Protein-protein interaction databases

DIPiDIP-59526N.
IntActiQ3THS6. 1 interaction.
STRINGi10090.ENSMUSP00000087118.

Structurei

3D structure databases

ProteinModelPortaliQ3THS6.
SMRiQ3THS6. Positions 13-395.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the AdoMet synthase family.Curated

Phylogenomic databases

eggNOGiKOG1506. Eukaryota.
COG0192. LUCA.
HOGENOMiHOG000245710.
HOVERGENiHBG001562.
InParanoidiQ3THS6.
KOiK00789.
OMAiGQMNGFH.
OrthoDBiEOG7TF79H.
PhylomeDBiQ3THS6.
TreeFamiTF300511.

Family and domain databases

HAMAPiMF_00086. S_AdoMet_synth1.
InterProiIPR022631. ADOMET_SYNTHASE_CS.
IPR022630. S-AdoMet_synt_C.
IPR022629. S-AdoMet_synt_central.
IPR022628. S-AdoMet_synt_N.
IPR002133. S-AdoMet_synthetase.
IPR022636. S-AdoMet_synthetase_sfam.
[Graphical view]
PANTHERiPTHR11964. PTHR11964. 1 hit.
PfamiPF02773. S-AdoMet_synt_C. 1 hit.
PF02772. S-AdoMet_synt_M. 1 hit.
PF00438. S-AdoMet_synt_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000497. MAT. 1 hit.
SUPFAMiSSF55973. SSF55973. 3 hits.
TIGRFAMsiTIGR01034. metK. 1 hit.
PROSITEiPS00376. ADOMET_SYNTHASE_1. 1 hit.
PS00377. ADOMET_SYNTHASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q3THS6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNGQLNGFHE AFIEEGTFLF TSESVGEGHP DKICDQISDA VLDAHLQQDP
60 70 80 90 100
DAKVACETVA KTGMILLAGE ITSRAAIDYQ KVVREAIKHI GYDDSSKGFD
110 120 130 140 150
YKTCNVLVAL EQQSPDIAQG VHLDRNEEDI GAGDQGLMFG YATDETEECM
160 170 180 190 200
PLTIVLAHKL NAKLAELRRN GTLPWLRPDS KTQVTVQYMQ DRGAVLPIRV
210 220 230 240 250
HTIVISVQHD EEVCLDEMRD ALKEKVIKAV VPAKYLDEDT IYHLQPSGRF
260 270 280 290 300
VIGGPQGDAG LTGRKIIVDT YGGWGAHGGG AFSGKDYTKV DRSAAYAARW
310 320 330 340 350
VAKSLVKGGL CRRVLVQVSY AIGVSHPLSI SIFHYGTSQK SERELLEIVK
360 370 380 390
KNFDLRPGVI VRDLDLKKPI YQRTAAYGHF GRDSFPWEVP KKLKY
Length:395
Mass (Da):43,689
Last modified:January 24, 2006 - v2
Checksum:iBB977989B75CB8F9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti24 – 241S → T in BAE40120 (PubMed:16141072).Curated
Sequence conflicti128 – 1281E → G in BAD06937 (Ref. 1) Curated
Sequence conflicti283 – 2831S → L in BAE38932 (PubMed:16141072).Curated
Sequence conflicti302 – 3021A → S in BAE40120 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB070266 mRNA. Translation: BAD06937.1.
AK166671 mRNA. Translation: BAE38932.1.
AK168155 mRNA. Translation: BAE40120.1.
CCDSiCCDS39515.1.
RefSeqiNP_663544.1. NM_145569.4.
UniGeneiMm.29815.
Mm.440743.
Mm.485037.

Genome annotation databases

EnsembliENSMUST00000059472; ENSMUSP00000087118; ENSMUSG00000053907.
ENSMUST00000193334; ENSMUSP00000142136; ENSMUSG00000104463.
GeneIDi232087.
KEGGimmu:232087.
UCSCiuc009cip.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB070266 mRNA. Translation: BAD06937.1.
AK166671 mRNA. Translation: BAE38932.1.
AK168155 mRNA. Translation: BAE40120.1.
CCDSiCCDS39515.1.
RefSeqiNP_663544.1. NM_145569.4.
UniGeneiMm.29815.
Mm.440743.
Mm.485037.

3D structure databases

ProteinModelPortaliQ3THS6.
SMRiQ3THS6. Positions 13-395.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-59526N.
IntActiQ3THS6. 1 interaction.
STRINGi10090.ENSMUSP00000087118.

PTM databases

iPTMnetiQ3THS6.
PhosphoSiteiQ3THS6.

Proteomic databases

EPDiQ3THS6.
PaxDbiQ3THS6.
PRIDEiQ3THS6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000059472; ENSMUSP00000087118; ENSMUSG00000053907.
ENSMUST00000193334; ENSMUSP00000142136; ENSMUSG00000104463.
GeneIDi232087.
KEGGimmu:232087.
UCSCiuc009cip.1. mouse.

Organism-specific databases

CTDi4144.
MGIiMGI:2443731. Mat2a.

Phylogenomic databases

eggNOGiKOG1506. Eukaryota.
COG0192. LUCA.
HOGENOMiHOG000245710.
HOVERGENiHBG001562.
InParanoidiQ3THS6.
KOiK00789.
OMAiGQMNGFH.
OrthoDBiEOG7TF79H.
PhylomeDBiQ3THS6.
TreeFamiTF300511.

Enzyme and pathway databases

UniPathwayiUPA00315; UER00080.
ReactomeiR-MMU-156581. Methylation.

Miscellaneous databases

ChiTaRSiMat2a. mouse.
PROiQ3THS6.
SOURCEiSearch...

Gene expression databases

BgeeiQ3THS6.
CleanExiMM_MAT2A.
ExpressionAtlasiQ3THS6. baseline and differential.
GenevisibleiQ3THS6. MM.

Family and domain databases

HAMAPiMF_00086. S_AdoMet_synth1.
InterProiIPR022631. ADOMET_SYNTHASE_CS.
IPR022630. S-AdoMet_synt_C.
IPR022629. S-AdoMet_synt_central.
IPR022628. S-AdoMet_synt_N.
IPR002133. S-AdoMet_synthetase.
IPR022636. S-AdoMet_synthetase_sfam.
[Graphical view]
PANTHERiPTHR11964. PTHR11964. 1 hit.
PfamiPF02773. S-AdoMet_synt_C. 1 hit.
PF02772. S-AdoMet_synt_M. 1 hit.
PF00438. S-AdoMet_synt_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000497. MAT. 1 hit.
SUPFAMiSSF55973. SSF55973. 3 hits.
TIGRFAMsiTIGR01034. metK. 1 hit.
PROSITEiPS00376. ADOMET_SYNTHASE_1. 1 hit.
PS00377. ADOMET_SYNTHASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "cDNA for mouse kidney methionine adenosyltransferase II alpha."
    Sakata S., Okumura S.
    Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: ddY.
    Tissue: Kidney.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and DBA/2.
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiMETK2_MOUSE
AccessioniPrimary (citable) accession number: Q3THS6
Secondary accession number(s): Q3TL60, Q76LX3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2006
Last sequence update: January 24, 2006
Last modified: June 8, 2016
This is version 111 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.