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Q91X83

- METK1_MOUSE

UniProt

Q91X83 - METK1_MOUSE

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Protein

S-adenosylmethionine synthase isoform type-1

Gene

Mat1a

Organism
Mus musculus (Mouse)
Status
Reviewed - 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

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

  1. ATP binding Source: UniProtKB-KW
  2. metal ion binding Source: UniProtKB-KW
  3. methionine adenosyltransferase activity Source: MGI

GO - Biological processi

  1. one-carbon metabolic process Source: UniProtKB-KW
  2. S-adenosylmethionine biosynthetic process Source: UniProtKB-UniPathway
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_202492. Sulfur amino acid metabolism.
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: Chromosome 14

Organism-specific databases

MGIiMGI:88017. Mat1a.

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.
OMAiITSHAIV.
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:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
AK149542 mRNA. Translation: BAE28947.1 .
AK153832 mRNA. Translation: BAE32202.1 .
BC011211 mRNA. Translation: AAH11211.1 .
CCDSi CCDS26959.1.
PIRi A47151.
RefSeqi NP_598414.1. NM_133653.3.
XP_006518513.1. XM_006518450.1.
UniGenei Mm.14064.
Mm.486779.

3D structure databases

ProteinModelPortali Q91X83.
SMRi Q91X83. Positions 17-396.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-45874N.
IntActi Q91X83. 3 interactions.
MINTi MINT-1855350.
STRINGi 10090.ENSMUSP00000044288.

PTM databases

PhosphoSitei Q91X83.

2D gel databases

REPRODUCTION-2DPAGE Q91X83.

Proteomic databases

MaxQBi Q91X83.
PaxDbi Q91X83.
PRIDEi Q91X83.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000047286 ; ENSMUSP00000044288 ; ENSMUSG00000037798 .
GeneIDi 11720.
KEGGi mmu:11720.
UCSCi uc007tcm.1. mouse.

Organism-specific databases

CTDi 4143.
MGIi MGI:88017. Mat1a.

Phylogenomic databases

eggNOGi COG0192.
GeneTreei ENSGT00500000044811.
HOGENOMi HOG000245710.
HOVERGENi HBG001562.
InParanoidi Q91X83.
KOi K00789.
OMAi ITSHAIV.
OrthoDBi EOG7TF79H.
PhylomeDBi Q91X83.
TreeFami TF300511.

Enzyme and pathway databases

UniPathwayi UPA00315 ; UER00080 .
Reactomei REACT_202492. Sulfur amino acid metabolism.

Miscellaneous databases

NextBioi 279397.
PROi Q91X83.
SOURCEi Search...

Gene expression databases

Bgeei Q91X83.
CleanExi MM_MAT1A.
Genevestigatori Q91X83.

Family and domain databases

HAMAPi MF_00086. S_AdoMet_synth1.
InterProi IPR022631. 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 ]
PANTHERi PTHR11964. PTHR11964. 1 hit.
Pfami PF02773. S-AdoMet_synt_C. 1 hit.
PF02772. S-AdoMet_synt_M. 1 hit.
PF00438. S-AdoMet_synt_N. 1 hit.
[Graphical view ]
PIRSFi PIRSF000497. MAT. 1 hit.
SUPFAMi SSF55973. SSF55973. 3 hits.
TIGRFAMsi TIGR01034. metK. 1 hit.
PROSITEi PS00376. ADOMET_SYNTHASE_1. 1 hit.
PS00377. ADOMET_SYNTHASE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: October 1, 2014
This is version 109 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