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A6H5Y3

- METH_MOUSE

UniProt

A6H5Y3 - METH_MOUSE

Protein

Methionine synthase

Gene

Mtr

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 73 (01 Oct 2014)
      Sequence version 1 (24 Jul 2007)
      Previous versions | rss
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    Functioni

    Catalyzes the transfer of a methyl group from methyl-cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and methionine. Subsequently, remethylates the cofactor using methyltetrahydrofolate By similarity.By similarity

    Catalytic activityi

    5-methyltetrahydrofolate + L-homocysteine = tetrahydrofolate + L-methionine.

    Cofactori

    Methylcobalamin (MeCBL).By similarity
    Binds 1 zinc ion per subunit.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi248 – 2481ZincPROSITE-ProRule annotation
    Metal bindingi311 – 3111ZincPROSITE-ProRule annotation
    Metal bindingi312 – 3121ZincPROSITE-ProRule annotation
    Metal bindingi773 – 7731Cobalt (cobalamin axial ligand)By similarity
    Binding sitei818 – 8181CobalaminBy similarity
    Binding sitei962 – 9621S-adenosyl-L-methionineBy similarity
    Binding sitei1160 – 11601S-adenosyl-L-methionine; via carbonyl oxygenBy similarity
    Binding sitei1164 – 11641Cobalamin; via carbonyl oxygenBy similarity

    GO - Molecular functioni

    1. cobalamin binding Source: UniProtKB-KW
    2. methionine synthase activity Source: MGI
    3. S-adenosylmethionine-homocysteine S-methyltransferase activity Source: InterPro
    4. zinc ion binding Source: InterPro

    GO - Biological processi

    1. methionine biosynthetic process Source: MGI
    2. pteridine-containing compound metabolic process Source: InterPro

    Keywords - Molecular functioni

    Methyltransferase, Transferase

    Keywords - Biological processi

    Amino-acid biosynthesis, Methionine biosynthesis

    Keywords - Ligandi

    Cobalamin, Cobalt, Metal-binding, S-adenosyl-L-methionine, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_189091. Defective MTRR causes methylmalonic aciduria and homocystinuria type cblE.
    REACT_189092. Defective MTR causes methylmalonic aciduria and homocystinuria type cblG.
    REACT_189118. Cobalamin (Cbl, vitamin B12) transport and metabolism.
    REACT_202492. Sulfur amino acid metabolism.
    UniPathwayiUPA00051; UER00081.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Methionine synthase (EC:2.1.1.13)
    Alternative name(s):
    5-methyltetrahydrofolate--homocysteine methyltransferase
    Vitamin-B12 dependent methionine synthase
    Short name:
    MS
    Gene namesi
    Name:Mtr
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 13

    Organism-specific databases

    MGIiMGI:894292. Mtr.

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 12531253Methionine synthasePRO_0000312901Add
    BLAST

    Proteomic databases

    MaxQBiA6H5Y3.
    PaxDbiA6H5Y3.
    PRIDEiA6H5Y3.

    PTM databases

    PhosphoSiteiA6H5Y3.

    Expressioni

    Gene expression databases

    BgeeiA6H5Y3.
    GenevestigatoriA6H5Y3.

    Structurei

    3D structure databases

    ProteinModelPortaliA6H5Y3.
    SMRiA6H5Y3. Positions 4-639, 653-908, 914-1252.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini6 – 326321Hcy-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini359 – 620262Pterin-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini650 – 74798B12-binding N-terminalPROSITE-ProRule annotationAdd
    BLAST
    Domaini760 – 895136B12-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini911 – 1253343AdoMet activationPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni848 – 8492Cobalamin-bindingBy similarity
    Regioni1215 – 12162S-adenosyl-L-methionine bindingBy similarity

    Domaini

    Modular enzyme with four functionally distinct domains. The isolated Hcy-binding domain catalyzes methyl transfer from free methylcobalamin to homocysteine. The Hcy-binding domain in association with the pterin-binding domain catalyzes the methylation of cob(I)alamin by methyltetrahydrofolate and the methylation of homocysteine. The B12-binding domain binds the cofactor. The AdoMet activation domain binds S-adenosyl-L-methionine. Under aerobic conditions cob(I)alamin can be converted to inactive cob(II)alamin. Reductive methylation by S-adenosyl-L-methionine and flavodoxin regenerates methylcobalamin By similarity.By similarity

    Sequence similaritiesi

    Contains 1 AdoMet activation domain.PROSITE-ProRule annotation
    Contains 1 B12-binding domain.PROSITE-ProRule annotation
    Contains 1 Hcy-binding domain.PROSITE-ProRule annotation
    Contains 1 pterin-binding domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG1410.
    GeneTreeiENSGT00420000029824.
    HOGENOMiHOG000251409.
    HOVERGENiHBG006347.
    InParanoidiA6H5Y3.
    KOiK00548.
    OMAiLTEHYAM.
    OrthoDBiEOG7TF786.
    PhylomeDBiA6H5Y3.
    TreeFamiTF312829.

    Family and domain databases

    Gene3Di1.10.1240.10. 1 hit.
    3.10.196.10. 1 hit.
    3.20.20.20. 1 hit.
    3.20.20.330. 1 hit.
    3.40.50.280. 1 hit.
    InterProiIPR003759. Cbl-bd_cap.
    IPR006158. Cobalamin-bd.
    IPR011005. Dihydropteroate_synth-like.
    IPR011822. MetH.
    IPR000489. Pterin-binding.
    IPR003726. S_MeTrfase.
    IPR004223. VitB12-dep_Met_synth_activ_dom.
    [Graphical view]
    PfamiPF02310. B12-binding. 1 hit.
    PF02607. B12-binding_2. 1 hit.
    PF02965. Met_synt_B12. 1 hit.
    PF00809. Pterin_bind. 1 hit.
    PF02574. S-methyl_trans. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000381. MetH. 1 hit.
    SMARTiSM01018. B12-binding_2. 1 hit.
    [Graphical view]
    SUPFAMiSSF47644. SSF47644. 1 hit.
    SSF51717. SSF51717. 1 hit.
    SSF52242. SSF52242. 1 hit.
    SSF56507. SSF56507. 1 hit.
    SSF82282. SSF82282. 1 hit.
    TIGRFAMsiTIGR02082. metH. 1 hit.
    PROSITEiPS50974. ADOMET_ACTIVATION. 1 hit.
    PS51332. B12_BINDING. 1 hit.
    PS51337. B12_BINDING_NTER. 1 hit.
    PS50970. HCY. 1 hit.
    PS50972. PTERIN_BINDING. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    A6H5Y3-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKKTLQDEIE AILRKRIMVL DGGMGTMIQR YKLSEEHFQG QEFKDHSRPL     50
    KGNNDILSIT QPDIIYQIHK EYLLAGADII ETNTFSSTSI AQADYGLEHL 100
    AYRMNKCSAD VARKAAEEIT LQTGVKRFVA GALGPTNKTL SVSPSVERPD 150
    YRNITFDELV DAYQEQAKGL LDGRVDILLI ETIFDTANAK AALFAIQNLF 200
    EENYAPPRPI FISGTIVDKS GRTLSGQTGE AFVTSVSHSD PLCIGLNCSL 250
    GAAEMRPFIE TIGKCTTAYV LCYPNAGLPN TFGDYDETPS TMATHLKDFA 300
    VDGLVNIVGG CCGSTPDHIR EIAEAVKKCK PRVPPASVFE GHMLLSGLEP 350
    FRIGPYTNFV NIGERCNVAG SRKFAKLIMA GNYEEALSIA KAQVEMGAQV 400
    LDINMDDGML DGPSAMTRFC NSIASEPDIA KVPLCIDSSN FAVIEAGLKC 450
    CQGKCIVNSI SLKEGEGDFL EKARKIKKFG AAVVVMAFDE EGQATETDVK 500
    VNVCTRAYHL LVDKVGFNPN DIIFDPNILT IGTGMEEHNL YAINFIHATR 550
    VIKETLPGVR ISGGLSNLSF SFRGMEAIRE AMHGVFLYHA IKFGMDMGIV 600
    NAGNLPVYDA IHKDLLQLCE DLIWNKDSEA TEKLLRYAQT HGTGGKKVIQ 650
    TDEWRNGSIE ERLEYALVKG IEKHIVEDTE EARLNGEKYP RPLNIIEGPL 700
    MNGMKVVGDL FGAGKMFLPQ VIKSARVMKK AVGHLIPFME KEREEARLIN 750
    GSVEEEDPYQ GTIVLATVKG DVHDIGKNIV GVVLACNNFR VIDLGVMTPC 800
    DKILQAALDH KADIIGLSGL ITPSLDEMIF VAKEMERLAI KIPLLIGGAT 850
    TSRTHTAVKI APRYSAPVIH VLDASKSVVV CSQLLDENLR DDYFEEILEE 900
    YEDIRQDHYE SLKERKYVPL SQARKHGFHI DWLSEPHPVK PTFIGTQVFE 950
    DYNLQKLVDY IDWKPFFDVW QLRGKYPNRG FPKIFNDKAV GEEARKVYND 1000
    AQNMLNILIS QKKLQARGVV GFWPAQSVQD DIHLYAEGVV PQAAEPIATF 1050
    YGLRQQAEKD SSSTDPYHCL SDFIAPLHSG VCDYLGLFAV ACFGVEELSK 1100
    TYEDDGDDYS SIMVKALGDR LAEAFAEELH ERVRRELWAY SRSEQLGVPD 1150
    LRRLRYEGIR PAPGYPSQPD HTEKLTMWRL ASIEQATGIR LTESLAMAPA 1200
    SAVSGLYFSN VKAKYFAVGK ISKDQTEDYA LRKNMPVAEV EKWLGPILGY 1250
    DTD 1253
    Length:1,253
    Mass (Da):139,069
    Last modified:July 24, 2007 - v1
    Checksum:i5507CAD9F9522537
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti343 – 3431M → L in BAE24997. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC145683 mRNA. Translation: AAI45684.1.
    BC145685 mRNA. Translation: AAI45686.1.
    AK142258 mRNA. Translation: BAE24997.1.
    CCDSiCCDS36591.1.
    RefSeqiNP_001074597.1. NM_001081128.3.
    UniGeneiMm.40335.

    Genome annotation databases

    EnsembliENSMUST00000099856; ENSMUSP00000097442; ENSMUSG00000021311.
    GeneIDi238505.
    KEGGimmu:238505.
    UCSCiuc007plh.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC145683 mRNA. Translation: AAI45684.1 .
    BC145685 mRNA. Translation: AAI45686.1 .
    AK142258 mRNA. Translation: BAE24997.1 .
    CCDSi CCDS36591.1.
    RefSeqi NP_001074597.1. NM_001081128.3.
    UniGenei Mm.40335.

    3D structure databases

    ProteinModelPortali A6H5Y3.
    SMRi A6H5Y3. Positions 4-639, 653-908, 914-1252.
    ModBasei Search...
    MobiDBi Search...

    Chemistry

    ChEMBLi CHEMBL3188.

    PTM databases

    PhosphoSitei A6H5Y3.

    Proteomic databases

    MaxQBi A6H5Y3.
    PaxDbi A6H5Y3.
    PRIDEi A6H5Y3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000099856 ; ENSMUSP00000097442 ; ENSMUSG00000021311 .
    GeneIDi 238505.
    KEGGi mmu:238505.
    UCSCi uc007plh.2. mouse.

    Organism-specific databases

    CTDi 4548.
    MGIi MGI:894292. Mtr.

    Phylogenomic databases

    eggNOGi COG1410.
    GeneTreei ENSGT00420000029824.
    HOGENOMi HOG000251409.
    HOVERGENi HBG006347.
    InParanoidi A6H5Y3.
    KOi K00548.
    OMAi LTEHYAM.
    OrthoDBi EOG7TF786.
    PhylomeDBi A6H5Y3.
    TreeFami TF312829.

    Enzyme and pathway databases

    UniPathwayi UPA00051 ; UER00081 .
    Reactomei REACT_189091. Defective MTRR causes methylmalonic aciduria and homocystinuria type cblE.
    REACT_189092. Defective MTR causes methylmalonic aciduria and homocystinuria type cblG.
    REACT_189118. Cobalamin (Cbl, vitamin B12) transport and metabolism.
    REACT_202492. Sulfur amino acid metabolism.

    Miscellaneous databases

    NextBioi 383806.
    PROi A6H5Y3.
    SOURCEi Search...

    Gene expression databases

    Bgeei A6H5Y3.
    Genevestigatori A6H5Y3.

    Family and domain databases

    Gene3Di 1.10.1240.10. 1 hit.
    3.10.196.10. 1 hit.
    3.20.20.20. 1 hit.
    3.20.20.330. 1 hit.
    3.40.50.280. 1 hit.
    InterProi IPR003759. Cbl-bd_cap.
    IPR006158. Cobalamin-bd.
    IPR011005. Dihydropteroate_synth-like.
    IPR011822. MetH.
    IPR000489. Pterin-binding.
    IPR003726. S_MeTrfase.
    IPR004223. VitB12-dep_Met_synth_activ_dom.
    [Graphical view ]
    Pfami PF02310. B12-binding. 1 hit.
    PF02607. B12-binding_2. 1 hit.
    PF02965. Met_synt_B12. 1 hit.
    PF00809. Pterin_bind. 1 hit.
    PF02574. S-methyl_trans. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000381. MetH. 1 hit.
    SMARTi SM01018. B12-binding_2. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47644. SSF47644. 1 hit.
    SSF51717. SSF51717. 1 hit.
    SSF52242. SSF52242. 1 hit.
    SSF56507. SSF56507. 1 hit.
    SSF82282. SSF82282. 1 hit.
    TIGRFAMsi TIGR02082. metH. 1 hit.
    PROSITEi PS50974. ADOMET_ACTIVATION. 1 hit.
    PS51332. B12_BINDING. 1 hit.
    PS51337. B12_BINDING_NTER. 1 hit.
    PS50970. HCY. 1 hit.
    PS50972. PTERIN_BINDING. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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].
      Tissue: Brain.
    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] OF 1-738.
      Strain: C57BL/6J.
      Tissue: Heart.

    Entry informationi

    Entry nameiMETH_MOUSE
    AccessioniPrimary (citable) accession number: A6H5Y3
    Secondary accession number(s): Q3UQP2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 15, 2008
    Last sequence update: July 24, 2007
    Last modified: October 1, 2014
    This is version 73 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    L-homocysteine is bound via the zinc atom.By similarity

    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