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Q9Z2Q4

- METH_RAT

UniProt

Q9Z2Q4 - METH_RAT

Protein

Methionine synthase

Gene

Mtr

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 97 (01 Oct 2014)
      Sequence version 1 (01 May 1999)
      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. amino acid binding Source: RGD
    2. cobalamin binding Source: RGD
    3. folic acid binding Source: RGD
    4. methionine synthase activity Source: RGD
    5. methyltransferase activity Source: RGD
    6. S-adenosylmethionine-homocysteine S-methyltransferase activity Source: InterPro
    7. zinc ion binding Source: InterPro

    GO - Biological processi

    1. homocysteine metabolic process Source: RGD
    2. methionine biosynthetic process Source: RGD
    3. methionine metabolic process Source: RGD
    4. protein methylation Source: RGD
    5. tetrahydrofolate metabolic process Source: RGD

    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

    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
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi621283. 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_0000312902Add
    BLAST

    Proteomic databases

    PaxDbiQ9Z2Q4.
    PRIDEiQ9Z2Q4.

    PTM databases

    PhosphoSiteiQ9Z2Q4.

    Expressioni

    Gene expression databases

    GenevestigatoriQ9Z2Q4.

    Interactioni

    Protein-protein interaction databases

    BioGridi249519. 1 interaction.
    IntActiQ9Z2Q4. 1 interaction.
    STRINGi10116.ENSRNOP00000023973.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9Z2Q4.
    SMRiQ9Z2Q4. Positions 652-908, 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.
    HOGENOMiHOG000251409.
    HOVERGENiHBG006347.
    InParanoidiQ9Z2Q4.
    KOiK00548.
    PhylomeDBiQ9Z2Q4.

    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.

    Q9Z2Q4-1 [UniParc]FASTAAdd to Basket

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    MKKTLQDEIE AILRKRIMVL DGGMGTMIQR YKLSEENFQG QEFKDHSRPL     50
    KGNNDILSIT QPDVIYQIHK EYLLAGADII ETNTFSSTSI AQADYGLEHL 100
    AYRMNKCSAD VARKAAEEIT LQTGVKRFVA GSLGPTNKTL SVSPSVERPD 150
    YRNITFDELV EAYQEQAKGL LDGGVDILLI ETIFDTANAK AALFALQKLF 200
    EENYASPRPI FISGTIVDKS GRTLSGQTGE AFVTSVSHSD PLCIGLNCAL 250
    GAAEMRPFIE TIGKCTTAYV LCYPNAGLPN TFGDYDETPA MMAMHLKDFA 300
    VDGLVNVVGG CCGSTPDHIR EIAEAVKNCK PRVPPDSVFE GHMLLSGLEP 350
    FRIGPYTNFV NIGERCNVAG SKKFAKLIMA GNYEEALSVA KVQVEMGAQV 400
    LDINMDDGML DGPSAMTKFC NFIASEPDIA KVPLCIDSSN FAVIEAGLKC 450
    CQGKCIVNSI SLKEGEEDFL EKARKIKKFG AAVVVMAFDE EGQATETDVK 500
    VSVCTRAYHL LVEKVGFNPN DIIFDPNILT IGTGMEEHNL YAINFIHATR 550
    VIKETLPGVR ISGGLSNLSF AFRGMDAIRE AMHGVFLYHA IKFGMDMGIV 600
    NAGSLPVYDD IHKDLLQLCE DLIWNRDAEA TEKLLRYAQT HGKGGKKVIQ 650
    TDEWRNGSIE ERLEYALVKG IEKHIVEDTE EARLNREKYP RPLNIIEGPL 700
    MNGMKVVGDL FGAGKMFLPQ VIKSARVMKK AVGHLIPFME KEREEARVLN 750
    GSVEEEDPYQ GTIVLATVKG DVHDIGKNIV GVVLGCNNFR VIDLGVMTPC 800
    DKILQAALDH KADIIGLSGL ITPSLDEMIF VAKEMERLAI KIPLLIGGAT 850
    TSRTHTAVKI APRYSAPVIH VLDASKSVVV CSQLLDENLK DDYFEEILEE 900
    YEDIRQDHYE SLKERKYLPL SQARKHSFHI DWLSEPHPVK PTFIGTQVFE 950
    DYNLQKLVDY IDWKPFFDVW QLRGKYPNRG FPKIFNDKAV GEEARKVYED 1000
    AQNMLSILIS RKKLRARGVV GFWPAQSVQD DIHLYAEGAV PQAAEPIATF 1050
    YGLRQQAEKD SSSTDPYHCL SDFVAPLHSG VRDYLGLFAV ACFGVEELSK 1100
    AYEDDGDDYS SIMVKALGDR LAEAFAEELH ERVRRELWAY CGSEQLGVTD 1150
    LRKLRYEGIR PAPGYPSQPD HTEKLTMWRL ANIEQATGIR LTESLAMAPA 1200
    SAVSGLYFSN VKSKYFAVGK ISKDQIEDYA LRKNMSVAEV EKWLGPILGY 1250
    DTD 1253
    Length:1,253
    Mass (Da):139,164
    Last modified:May 1, 1999 - v1
    Checksum:i96BD40B796EBD75B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF034214 mRNA. Translation: AAD05384.1.
    PIRiT42376.
    RefSeqiNP_110491.1. NM_030864.1.
    UniGeneiRn.205061.

    Genome annotation databases

    GeneIDi81522.
    KEGGirno:81522.
    UCSCiRGD:621283. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF034214 mRNA. Translation: AAD05384.1 .
    PIRi T42376.
    RefSeqi NP_110491.1. NM_030864.1.
    UniGenei Rn.205061.

    3D structure databases

    ProteinModelPortali Q9Z2Q4.
    SMRi Q9Z2Q4. Positions 652-908, 914-1252.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 249519. 1 interaction.
    IntActi Q9Z2Q4. 1 interaction.
    STRINGi 10116.ENSRNOP00000023973.

    PTM databases

    PhosphoSitei Q9Z2Q4.

    Proteomic databases

    PaxDbi Q9Z2Q4.
    PRIDEi Q9Z2Q4.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 81522.
    KEGGi rno:81522.
    UCSCi RGD:621283. rat.

    Organism-specific databases

    CTDi 4548.
    RGDi 621283. Mtr.

    Phylogenomic databases

    eggNOGi COG1410.
    HOGENOMi HOG000251409.
    HOVERGENi HBG006347.
    InParanoidi Q9Z2Q4.
    KOi K00548.
    PhylomeDBi Q9Z2Q4.

    Enzyme and pathway databases

    UniPathwayi UPA00051 ; UER00081 .

    Miscellaneous databases

    NextBioi 615041.
    PROi Q9Z2Q4.

    Gene expression databases

    Genevestigatori Q9Z2Q4.

    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. "Cloning, sequencing, and heterologous expression of rat methionine synthase cDNA."
      Yamada K., Tobimatsu T., Toraya T.
      Biosci. Biotechnol. Biochem. 62:2155-2160(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: Wistar.
      Tissue: Liver.

    Entry informationi

    Entry nameiMETH_RAT
    AccessioniPrimary (citable) accession number: Q9Z2Q4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 15, 2008
    Last sequence update: May 1, 1999
    Last modified: October 1, 2014
    This is version 97 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3