Tag | Content |
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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 |
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293 | LDADTMAKQIREWAQ | acetylation | [1] | 370 | TNVTGSAKFKRLIKE | acetylation | [1] | 379 | KRLIKEEKYSEALDV | acetylation | [1] | 437 | PIMIDSSKWDVIEKG | acetylation | [1] | 443 | SKWDVIEKGLKCIQG | acetylation | [1] | 446 | DVIEKGLKCIQGKGI | acetylation | [1] | 471 | DAFIHHAKLLRRYGA | acetylation | [1] | 637 | RLLELAEKYRGSKTD | acetylation | [1] | 740 | EPFIEASKEQGKTNG | acetylation | [1] | 978 | VEAQRLFKDANDMLD | acetylation | [1] | 986 | DANDMLDKLSAEKTL | acetylation | [1] | 991 | LDKLSAEKTLNPRGV | acetylation | [1] | 1035 | HLRQQTEKTGFANYC | acetylation | [1] | 1159 | WELLEVEKHTGMKLT | acetylation | [1] |
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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. |
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SMART | |
PROSITE | |
PRINTS | |