CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-024450
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Methionine synthase 
Protein Synonyms/Alias
 5-methyltetrahydrofolate--homocysteine methyltransferase; Vitamin-B12 dependent methionine synthase; MS 
Gene Name
 Mtr 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
723MFLPQVIKSARVMKKubiquitination[1]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023
Functional Description
 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). 
Sequence Annotation
 DOMAIN 6 326 Hcy-binding.
 DOMAIN 359 620 Pterin-binding.
 DOMAIN 650 747 B12-binding N-terminal.
 DOMAIN 760 895 B12-binding.
 DOMAIN 911 1253 AdoMet activation.
 REGION 848 849 Cobalamin-binding (By similarity).
 REGION 1215 1216 S-adenosyl-L-methionine binding (By
 METAL 248 248 Zinc (By similarity).
 METAL 311 311 Zinc (By similarity).
 METAL 312 312 Zinc (By similarity).
 METAL 773 773 Cobalt (cobalamin axial ligand) (By
 BINDING 818 818 Cobalamin (By similarity).
 BINDING 962 962 S-adenosyl-L-methionine (By similarity).
 BINDING 1160 1160 S-adenosyl-L-methionine; via carbonyl
 BINDING 1164 1164 Cobalamin; via carbonyl oxygen (By  
Keyword
 Amino-acid biosynthesis; Cobalamin; Cobalt; Complete proteome; Cytoplasm; Metal-binding; Methionine biosynthesis; Methyltransferase; Reference proteome; Repeat; S-adenosyl-L-methionine; Transferase; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1253 AA 
Protein Sequence
MKKTLQDEIE AILRKRIMVL DGGMGTMIQR YKLSEEHFQG QEFKDHSRPL KGNNDILSIT 60
QPDIIYQIHK EYLLAGADII ETNTFSSTSI AQADYGLEHL AYRMNKCSAD VARKAAEEIT 120
LQTGVKRFVA GALGPTNKTL SVSPSVERPD YRNITFDELV DAYQEQAKGL LDGRVDILLI 180
ETIFDTANAK AALFAIQNLF EENYAPPRPI FISGTIVDKS GRTLSGQTGE AFVTSVSHSD 240
PLCIGLNCSL GAAEMRPFIE TIGKCTTAYV LCYPNAGLPN TFGDYDETPS TMATHLKDFA 300
VDGLVNIVGG CCGSTPDHIR EIAEAVKKCK PRVPPASVFE GHMLLSGLEP FRIGPYTNFV 360
NIGERCNVAG SRKFAKLIMA GNYEEALSIA KAQVEMGAQV LDINMDDGML DGPSAMTRFC 420
NSIASEPDIA KVPLCIDSSN FAVIEAGLKC CQGKCIVNSI SLKEGEGDFL EKARKIKKFG 480
AAVVVMAFDE EGQATETDVK VNVCTRAYHL LVDKVGFNPN DIIFDPNILT IGTGMEEHNL 540
YAINFIHATR VIKETLPGVR ISGGLSNLSF SFRGMEAIRE AMHGVFLYHA IKFGMDMGIV 600
NAGNLPVYDA IHKDLLQLCE DLIWNKDSEA TEKLLRYAQT HGTGGKKVIQ TDEWRNGSIE 660
ERLEYALVKG IEKHIVEDTE EARLNGEKYP RPLNIIEGPL MNGMKVVGDL FGAGKMFLPQ 720
VIKSARVMKK AVGHLIPFME KEREEARLIN GSVEEEDPYQ GTIVLATVKG DVHDIGKNIV 780
GVVLACNNFR VIDLGVMTPC DKILQAALDH KADIIGLSGL ITPSLDEMIF VAKEMERLAI 840
KIPLLIGGAT TSRTHTAVKI APRYSAPVIH VLDASKSVVV CSQLLDENLR DDYFEEILEE 900
YEDIRQDHYE SLKERKYVPL SQARKHGFHI DWLSEPHPVK PTFIGTQVFE DYNLQKLVDY 960
IDWKPFFDVW QLRGKYPNRG FPKIFNDKAV GEEARKVYND AQNMLNILIS QKKLQARGVV 1020
GFWPAQSVQD DIHLYAEGVV PQAAEPIATF YGLRQQAEKD SSSTDPYHCL SDFIAPLHSG 1080
VCDYLGLFAV ACFGVEELSK TYEDDGDDYS SIMVKALGDR LAEAFAEELH ERVRRELWAY 1140
SRSEQLGVPD LRRLRYEGIR PAPGYPSQPD HTEKLTMWRL ASIEQATGIR LTESLAMAPA 1200
SAVSGLYFSN VKAKYFAVGK ISKDQTEDYA LRKNMPVAEV EKWLGPILGY DTD 1253 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
 GO:0008898; F:homocysteine S-methyltransferase activity; IEA:InterPro.
 GO:0008705; F:methionine synthase activity; IMP:MGI.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. 
Interpro
 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. 
Pfam
 PF02310; B12-binding
 PF02607; B12-binding_2
 PF02965; Met_synt_B12
 PF00809; Pterin_bind
 PF02574; S-methyl_trans 
SMART
 SM01018; B12-binding_2 
PROSITE
 PS50974; ADOMET_ACTIVATION
 PS51332; B12_BINDING
 PS51337; B12_BINDING_NTER
 PS50970; HCY
 PS50972; PTERIN_BINDING 
PRINTS