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Q91X83 (METK1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
S-adenosylmethionine synthase isoform type-1

Short name=AdoMet synthase 1
EC=2.5.1.6
Alternative name(s):
Methionine adenosyltransferase 1
Short name=MAT 1
Gene names
Name:Mat1a
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length396 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Catalyzes the formation of S-adenosylmethionine from methionine and ATP By similarity. HAMAP-Rule MF_00086

Catalytic activity

ATP + L-methionine + H2O = phosphate + diphosphate + S-adenosyl-L-methionine. HAMAP-Rule MF_00086

Cofactor

Binds 2 divalent ions per subunit. Magnesium or cobalt By similarity.

Binds 1 potassium ion per subunit By similarity. HAMAP-Rule MF_00086

Pathway

Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1. HAMAP-Rule MF_00086

Subunit structure

Homotetramer or homodimer By similarity. HAMAP-Rule MF_00086

Post-translational modification

S-nitrosylation of Cys-121 inactivates the enzyme By similarity. HAMAP-Rule MF_00086

Sequence similarities

Belongs to the AdoMet synthase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 396396S-adenosylmethionine synthase isoform type-1 HAMAP-Rule MF_00086
PRO_0000174433

Regions

Nucleotide binding132 – 1376ATP Potential

Sites

Metal binding321Magnesium By similarity
Metal binding581Potassium By similarity
Metal binding2841Potassium By similarity
Metal binding2921Magnesium By similarity
Binding site301Substrate By similarity
Binding site1601ATP Potential
Binding site1801Substrate By similarity
Binding site2481Substrate By similarity
Binding site2501Substrate; via carbonyl oxygen By similarity
Binding site2591Substrate By similarity

Amino acid modifications

Modified residue1211S-nitrosocysteine By similarity
Disulfide bond35 ↔ 61 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q91X83 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: AAA593A669551EB8

FASTA39643,509
        10         20         30         40         50         60 
MNGPVDGLCD HSLSEEGAFM FTSESVGEGH PDKICDQISD AVLDAHLKQD PNAKVACETV 

        70         80         90        100        110        120 
CKTGMVLLCG EITSVAMVDY QRVVRDTIKH IGYDDSAKGF DFKTCNVLVA LEQQSPDIAQ 

       130        140        150        160        170        180 
CVHLDRNEED VGAGDQGLMF GYATDETEEC MPLTIVLAHK LNTRIADLRR SGVLPWLRPD 

       190        200        210        220        230        240 
SKTQVTVQYM QDNGAVIPVR IHTIVISVQH NEDITLEAMQ EALKEQVIKA VVPAKYLDED 

       250        260        270        280        290        300 
TVYHLQPSGR FVIGGPQGDA GVTGRKIIVD TYGGWGAHGG GAFSGKDYTK VDRSAAYAAR 

       310        320        330        340        350        360 
WVAKSLVKAG LCRRVLVQVS YAIGVAEPLS ISIFTYGTSN KTERELLEVV NKNFDLRPGV 

       370        380        390 
IVRDLDLKKP IYQKTACYGH FGRSEFPWEV PKKLVF 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK149542 mRNA. Translation: BAE28947.1.
AK153832 mRNA. Translation: BAE32202.1.
BC011211 mRNA. Translation: AAH11211.1.
PIRA47151.
RefSeqNP_598414.1. NM_133653.3.
XP_006518513.1. XM_006518450.1.
UniGeneMm.14064.
Mm.486779.

3D structure databases

ProteinModelPortalQ91X83.
SMRQ91X83. Positions 17-396.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-45874N.
IntActQ91X83. 3 interactions.
MINTMINT-1855350.
STRING10090.ENSMUSP00000044288.

PTM databases

PhosphoSiteQ91X83.

2D gel databases

REPRODUCTION-2DPAGEQ91X83.

Proteomic databases

PaxDbQ91X83.
PRIDEQ91X83.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000047286; ENSMUSP00000044288; ENSMUSG00000037798.
GeneID11720.
KEGGmmu:11720.
UCSCuc007tcm.1. mouse.

Organism-specific databases

CTD4143.
MGIMGI:88017. Mat1a.

Phylogenomic databases

eggNOGCOG0192.
GeneTreeENSGT00500000044811.
HOGENOMHOG000245710.
HOVERGENHBG001562.
InParanoidQ91X83.
KOK00789.
OMAINPTGRY.
OrthoDBEOG7TF79H.
PhylomeDBQ91X83.
TreeFamTF300511.

Enzyme and pathway databases

UniPathwayUPA00315; UER00080.

Gene expression databases

BgeeQ91X83.
CleanExMM_MAT1A.
GenevestigatorQ91X83.

Family and domain databases

HAMAPMF_00086. S_AdoMet_synth1.
InterProIPR022631. 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]
PANTHERPTHR11964. PTHR11964. 1 hit.
PfamPF02773. S-AdoMet_synt_C. 1 hit.
PF02772. S-AdoMet_synt_M. 1 hit.
PF00438. S-AdoMet_synt_N. 1 hit.
[Graphical view]
PIRSFPIRSF000497. MAT. 1 hit.
SUPFAMSSF55973. SSF55973. 3 hits.
TIGRFAMsTIGR01034. metK. 1 hit.
PROSITEPS00376. ADOMET_SYNTHASE_1. 1 hit.
PS00377. ADOMET_SYNTHASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio279397.
PROQ91X83.
SOURCESearch...

Entry information

Entry nameMETK1_MOUSE
AccessionPrimary (citable) accession number: Q91X83
Entry history
Integrated into UniProtKB/Swiss-Prot: January 24, 2006
Last sequence update: December 1, 2001
Last modified: April 16, 2014
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot