CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004078
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Methionine synthase 
Protein Synonyms/Alias
 5-methyltetrahydrofolate--homocysteine methyltransferase; Methionine synthase, vitamin-B12-dependent; MS 
Gene Name
 metH 
Gene Synonyms/Alias
 b4019; JW3979 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
293LDADTMAKQIREWAQacetylation[1]
370TNVTGSAKFKRLIKEacetylation[1]
379KRLIKEEKYSEALDVacetylation[1]
437PIMIDSSKWDVIEKGacetylation[1]
443SKWDVIEKGLKCIQGacetylation[1]
446DVIEKGLKCIQGKGIacetylation[1]
471DAFIHHAKLLRRYGAacetylation[1]
637RLLELAEKYRGSKTDacetylation[1]
740EPFIEASKEQGKTNGacetylation[1]
978VEAQRLFKDANDMLDacetylation[1]
986DANDMLDKLSAEKTLacetylation[1]
991LDKLSAEKTLNPRGVacetylation[1]
1035HLRQQTEKTGFANYCacetylation[1]
1159WELLEVEKHTGMKLTacetylation[1]
Reference
 [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli.
 Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C.
 Mol Cell. 2013 Jul 25;51(2):265-72. [PMID: 23830618
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. 
Sequence Annotation
 DOMAIN 2 325 Hcy-binding.
 DOMAIN 356 617 Pterin-binding.
 DOMAIN 650 744 B12-binding N-terminal.
 DOMAIN 746 881 B12-binding.
 DOMAIN 897 1227 AdoMet activation.
 REGION 834 835 Cobalamin-binding.
 REGION 1189 1190 S-adenosyl-L-methionine binding.
 METAL 247 247 Zinc.
 METAL 310 310 Zinc.
 METAL 311 311 Zinc.
 METAL 759 759 Cobalt (cobalamin axial ligand).
 BINDING 804 804 Cobalamin.
 BINDING 946 946 S-adenosyl-L-methionine.
 BINDING 1134 1134 S-adenosyl-L-methionine; via carbonyl
 BINDING 1138 1138 Cobalamin; via carbonyl oxygen.  
Keyword
 3D-structure; Amino-acid biosynthesis; Cobalamin; Cobalt; Complete proteome; Direct protein sequencing; Metal-binding; Methionine biosynthesis; Methyltransferase; Reference proteome; Repeat; S-adenosyl-L-methionine; Transferase; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1227 AA 
Protein Sequence
MSSKVEQLRA QLNERILVLD GGMGTMIQSY RLNEADFRGE RFADWPCDLK GNNDLLVLSK 60
PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYQMESLS AEINFAAAKL ARACADEWTA 120
RTPEKPRYVA GVLGPTNRTA SISPDVNDPA FRNITFDGLV AAYRESTKAL VEGGADLILI 180
ETVFDTLNAK AAVFAVKTEF EALGVELPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA 240
LTFGLNCALG PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAQ 300
AGFLNIVGGC CGTTPQHIAA MSRAVEGLAP RKLPEIPVAC RLSGLEPLNI GEDSLFVNVG 360
ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VENGAQIIDI NMDEGMLDAE AAMVRFLNLI 420
AGEPDIARVP IMIDSSKWDV IEKGLKCIQG KGIVNSISMK EGVDAFIHHA KLLRRYGAAV 480
VVMAFDEQGQ ADTRARKIEI CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ 540
DFIGACEDIK RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG 600
QLAIYDDLPA ELRDAVEDVI LNRRDDGTER LLELAEKYRG SKTDDTANAQ QAEWRSWEVN 660
KRLEYSLVKG ITEFIEQDTE EARQQATRPI EVIEGPLMDG MNVVGDLFGE GKMFLPQVVK 720
SARVMKQAVA YLEPFIEASK EQGKTNGKMV IATVKGDVHD IGKNIVGVVL QCNNYEIVDL 780
GVMVPAEKIL RTAKEVNADL IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA 840
HTAVKIEQNY SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHGRKKPR 900
TPPVTLEAAR DNDFAFDWQA YTPPVAHRLG VQEVEASIET LRNYIDWTPF FMTWSLAGKY 960
PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KTLNPRGVVG LFPANRVGDD IEIYRDETRT 1020
HVINVSHHLR QQTEKTGFAN YCLADFVAPK LSGKADYIGA FAVTGGLEED ALADAFEAQH 1080
DDYNKIMVKA LADRLAEAFA EYLHERVRKV YWGYAPNENL SNEELIRENY QGIRPAPGYP 1140
ACPEHTEKAT IWELLEVEKH TGMKLTESFA MWPGASVSGW YFSHPDSKYY AVAQIQRDQV 1200
EDYARRKGMS VTEVERWLAP NLGYDAD 1227 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:EcoliWiki.
 GO:0031419; F:cobalamin binding; IDA:EcoCyc.
 GO:0008898; F:homocysteine S-methyltransferase activity; IDA:EcoCyc.
 GO:0008705; F:methionine synthase activity; IDA:EcoCyc.
 GO:0008270; F:zinc ion binding; IMP:EcoCyc.
 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