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Protein

S-adenosylmethionine synthase isoform type-1

Gene

Mat1a

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei30 – 301SubstrateBy similarity
Metal bindingi32 – 321MagnesiumBy similarity
Metal bindingi58 – 581PotassiumBy similarity
Binding sitei160 – 1601ATPSequence Analysis
Binding sitei180 – 1801SubstrateBy similarity
Binding sitei248 – 2481SubstrateBy similarity
Binding sitei250 – 2501Substrate; via carbonyl oxygenBy similarity
Binding sitei259 – 2591SubstrateBy similarity
Metal bindingi284 – 2841PotassiumBy similarity
Metal bindingi292 – 2921MagnesiumBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi132 – 1376ATPSequence Analysis

GO - Molecular functioni

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

GO - Biological processi

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

ReactomeiREACT_277860. Sulfur amino acid metabolism.
REACT_283123. Methylation.
UniPathwayiUPA00315; UER00080.

Names & Taxonomyi

Protein namesi
Recommended name:
S-adenosylmethionine synthase isoform type-1 (EC:2.5.1.6)
Short name:
AdoMet synthase 1
Alternative name(s):
Methionine adenosyltransferase 1
Short name:
MAT 1
Gene namesi
Name:Mat1a
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 14

Organism-specific databases

MGIiMGI:88017. Mat1a.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 396396S-adenosylmethionine synthase isoform type-1PRO_0000174433Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi35 ↔ 61By similarity
Modified residuei121 – 1211S-nitrosocysteineBy similarity

Post-translational modificationi

S-nitrosylation of Cys-121 inactivates the enzyme.By similarity

Keywords - PTMi

Disulfide bond, S-nitrosylation

Proteomic databases

MaxQBiQ91X83.
PaxDbiQ91X83.
PRIDEiQ91X83.

2D gel databases

REPRODUCTION-2DPAGEQ91X83.

PTM databases

PhosphoSiteiQ91X83.

Expressioni

Gene expression databases

BgeeiQ91X83.
CleanExiMM_MAT1A.
GenevestigatoriQ91X83.

Interactioni

Subunit structurei

Homotetramer or homodimer.By similarity

Protein-protein interaction databases

DIPiDIP-45874N.
IntActiQ91X83. 3 interactions.
MINTiMINT-1855350.
STRINGi10090.ENSMUSP00000044288.

Structurei

3D structure databases

ProteinModelPortaliQ91X83.
SMRiQ91X83. Positions 17-396.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the AdoMet synthase family.Curated

Phylogenomic databases

eggNOGiCOG0192.
GeneTreeiENSGT00500000044811.
HOGENOMiHOG000245710.
HOVERGENiHBG001562.
InParanoidiQ91X83.
KOiK00789.
OMAiSEFPWEI.
OrthoDBiEOG7TF79H.
PhylomeDBiQ91X83.
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.

Q91X83-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNGPVDGLCD HSLSEEGAFM FTSESVGEGH PDKICDQISD AVLDAHLKQD
60 70 80 90 100
PNAKVACETV CKTGMVLLCG EITSVAMVDY QRVVRDTIKH IGYDDSAKGF
110 120 130 140 150
DFKTCNVLVA LEQQSPDIAQ CVHLDRNEED VGAGDQGLMF GYATDETEEC
160 170 180 190 200
MPLTIVLAHK LNTRIADLRR SGVLPWLRPD SKTQVTVQYM QDNGAVIPVR
210 220 230 240 250
IHTIVISVQH NEDITLEAMQ EALKEQVIKA VVPAKYLDED TVYHLQPSGR
260 270 280 290 300
FVIGGPQGDA GVTGRKIIVD TYGGWGAHGG GAFSGKDYTK VDRSAAYAAR
310 320 330 340 350
WVAKSLVKAG LCRRVLVQVS YAIGVAEPLS ISIFTYGTSN KTERELLEVV
360 370 380 390
NKNFDLRPGV IVRDLDLKKP IYQKTACYGH FGRSEFPWEV PKKLVF
Length:396
Mass (Da):43,509
Last modified:December 1, 2001 - v1
Checksum:iAAA593A669551EB8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK149542 mRNA. Translation: BAE28947.1.
AK153832 mRNA. Translation: BAE32202.1.
BC011211 mRNA. Translation: AAH11211.1.
CCDSiCCDS26959.1.
PIRiA47151.
RefSeqiNP_598414.1. NM_133653.3.
XP_006518513.1. XM_006518450.1.
UniGeneiMm.14064.
Mm.486779.

Genome annotation databases

EnsembliENSMUST00000047286; ENSMUSP00000044288; ENSMUSG00000037798.
GeneIDi11720.
KEGGimmu:11720.
UCSCiuc007tcm.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK149542 mRNA. Translation: BAE28947.1.
AK153832 mRNA. Translation: BAE32202.1.
BC011211 mRNA. Translation: AAH11211.1.
CCDSiCCDS26959.1.
PIRiA47151.
RefSeqiNP_598414.1. NM_133653.3.
XP_006518513.1. XM_006518450.1.
UniGeneiMm.14064.
Mm.486779.

3D structure databases

ProteinModelPortaliQ91X83.
SMRiQ91X83. Positions 17-396.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-45874N.
IntActiQ91X83. 3 interactions.
MINTiMINT-1855350.
STRINGi10090.ENSMUSP00000044288.

PTM databases

PhosphoSiteiQ91X83.

2D gel databases

REPRODUCTION-2DPAGEQ91X83.

Proteomic databases

MaxQBiQ91X83.
PaxDbiQ91X83.
PRIDEiQ91X83.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000047286; ENSMUSP00000044288; ENSMUSG00000037798.
GeneIDi11720.
KEGGimmu:11720.
UCSCiuc007tcm.1. mouse.

Organism-specific databases

CTDi4143.
MGIiMGI:88017. Mat1a.

Phylogenomic databases

eggNOGiCOG0192.
GeneTreeiENSGT00500000044811.
HOGENOMiHOG000245710.
HOVERGENiHBG001562.
InParanoidiQ91X83.
KOiK00789.
OMAiSEFPWEI.
OrthoDBiEOG7TF79H.
PhylomeDBiQ91X83.
TreeFamiTF300511.

Enzyme and pathway databases

UniPathwayiUPA00315; UER00080.
ReactomeiREACT_277860. Sulfur amino acid metabolism.
REACT_283123. Methylation.

Miscellaneous databases

NextBioi279397.
PROiQ91X83.
SOURCEiSearch...

Gene expression databases

BgeeiQ91X83.
CleanExiMM_MAT1A.
GenevestigatoriQ91X83.

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. "Cloning and expression of murine S-adenosylmethionine synthetase."
    Sakata S.F., Shelly L.L., Ruppert S., Schutz G., Chou J.Y.
    J. Biol. Chem. 268:13978-13986(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  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.
    Tissue: Liver and Thymus.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Liver.

Entry informationi

Entry nameiMETK1_MOUSE
AccessioniPrimary (citable) accession number: Q91X83
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2006
Last sequence update: December 1, 2001
Last modified: April 1, 2015
This is version 114 of the entry and version 1 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

External Data

Dasty 3

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 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.