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epmB

Gene
epmB
Protein
L-lysine 2,3-aminomutase
Organism
Escherichia coli (strain K12)
Length
342 amino acids
Function
With EpmA is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P) on 'Lys-34'. EpmB appears to act before EpmA. Displays lysine 2,3-aminomutase activity, producing (R)-beta-lysine from (S)-alpha-lysine (L-lysine). Cannot use (S)-ornithine or (R)-alpha-lysine as a substrate.
Similarity
Belongs to the radical SAM superfamily. KamA family.
Mass
38.75 kDa
Sequence
MAHIVTLNTPSREDWLTQLADVVTDPDELLRLLNIDAEEKLLAGRSAKKLFALRVPRSFIDRMEKGNPDDPLLRQVLTSQDEFVIAPGFSTDPLEEQHSVVPGLLHKYHNRALLLVKGGCAVNCRYCFRRHFPYAENQGNKRNWQTALEYVAAHPELDEMIFSGGDPLMAKDHELDWLLTQLEAIPHIKRLRIHSRLPIVIPARITEALVECFARSTLQILLVNHINHANEVDETFRQAMAKLRRVGVTLLNQSVLLRDVNDNAQTLANLSNALFDAGVMPYYLHVLDKVQGAAHFMVSDDEARQIMRELLTLVSGYLVPKLAREIGGEPSKTPLDLQLRQQ

Gene
epmB
Protein
L-lysine 2,3-aminomutase
Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Length
342 amino acids
Function
With EpmA is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P) on 'Lys-34'. EpmB appears to act before EpmA. Displays lysine 2,3-aminomutase activity, producing (R)-beta-lysine from (S)-alpha-lysine (L-lysine) (By similarity).
Similarity
Belongs to the radical SAM superfamily. KamA family.
Mass
38.777 kDa
Sequence
MAHIVTLNTPLREDWLAQLADVVTNPDELLHLLQIEADENLRAGQDARRLFALRVPRAFIARMEKGNPDDPLLRQVLTSRDEFIVAPGFSTDPLEEQHSVVPGLLHKYQNRALLLVKGGCAVNCRYCFRRHFPYAENQGNKRNWTVALEYIAAHPELDEIIFSGGDPLMAKDHELDWLLTQLEAIKHVKRLRIHSRLPIVIPARITDELVARFDQSRLQILLVNHINHANEVDEAFGLAMKKLRHVGVTLLNQSVLLRGVNDNARTLANLSNALFDAGVMPYYLHVLDKVQGAAHFMVTDDEARQIMRELLTLVSGYMVPRLAREIGGEPSKTPLDLQLRQC

Gene
epmB
Protein
L-lysine 2,3-aminomutase
Organism
Escherichia coli (strain K12)
Length
342 amino acids
Function
With EpmA is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P) on 'Lys-34'. EpmB appears to act before EpmA. Displays lysine 2,3-aminomutase activity, producing (R)-beta-lysine from (S)-alpha-lysine (L-lysine). Cannot use (S)-ornithine or (R)-alpha-lysine as a substrate.
Similarity
Belongs to the radical SAM superfamily. KamA family.
Mass
38.75 kDa
Sequence
MAHIVTLNTPSREDWLTQLADVVTDPDELLRLLNIDAEEKLLAGRSAKKLFALRVPRSFIDRMEKGNPDDPLLRQVLTSQDEFVIAPGFSTDPLEEQHSVVPGLLHKYHNRALLLVKGGCAVNCRYCFRRHFPYAENQGNKRNWQTALEYVAAHPELDEMIFSGGDPLMAKDHELDWLLTQLEAIPHIKRLRIHSRLPIVIPARITEALVECFARSTLQILLVNHINHANEVDETFRQAMAKLRRVGVTLLNQSVLLRDVNDNAQTLANLSNALFDAGVMPYYLHVLDKVQGAAHFMVSDDEARQIMRELLTLVSGYLVPKLAREIGGEPSKTPLDLQLRQQ

Gene
epmB
Protein
L-lysine 2,3-aminomutase
Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Length
342 amino acids
Function
With EpmA is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P) on 'Lys-34'. EpmB appears to act before EpmA. Displays lysine 2,3-aminomutase activity, producing (R)-beta-lysine from (S)-alpha-lysine (L-lysine) (By similarity).
Similarity
Belongs to the radical SAM superfamily. KamA family.
Mass
38.777 kDa
Sequence
MAHIVTLNTPLREDWLAQLADVVTNPDELLHLLQIEADENLRAGQDARRLFALRVPRAFIARMEKGNPDDPLLRQVLTSRDEFIVAPGFSTDPLEEQHSVVPGLLHKYQNRALLLVKGGCAVNCRYCFRRHFPYAENQGNKRNWTVALEYIAAHPELDEIIFSGGDPLMAKDHELDWLLTQLEAIKHVKRLRIHSRLPIVIPARITDELVARFDQSRLQILLVNHINHANEVDEAFGLAMKKLRHVGVTLLNQSVLLRGVNDNARTLANLSNALFDAGVMPYYLHVLDKVQGAAHFMVTDDEARQIMRELLTLVSGYMVPRLAREIGGEPSKTPLDLQLRQC

Gene
epmB
Protein
L-lysine 2,3-aminomutase
Organism
Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp)
Length
340 amino acids
Function
With EpmA is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P) on 'Lys-34'. EpmB appears to act before EpmA. Displays lysine 2,3-aminomutase activity, producing (R)-beta-lysine from (S)-alpha-lysine (L-lysine) (By similarity).
Similarity
Belongs to the radical SAM superfamily. KamA family.
Mass
39.661 kDa
Sequence
MLNKKIKKNHKEDWITELTNAITNPDELLRTLNLKSNTKYFKNIQVQKLFSLRVPKTFVSRMKKNDPFDPLLLQILPHTKELKNNHNFVQDPLEETKNVIIPGLIRKYNNRILLLLKTNCAINCRYCFRRYFPYSQHPGNKENLNLAIQYIKNQTDLNEVILSGGDPLMAKDHEIQWIVNTLSNIYHIKRLRIHTRLPIVIPSRITNNLCKILSTTRLKILIVTHINHAQEINHELQYNINKLHKLGITLLNQSVLLRGINDNAKILSQLSNKLFDINILPYYLHILDKVKSTTHFYVSEKQASIIVVELLSMISGFLVPKLVCEHPGKNSKIYINLNMK

Gene
epmB
Protein
L-lysine 2,3-aminomutase
Organism
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Length
338 amino acids
Function
With EpmA is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P) on 'Lys-34'. EpmB appears to act before EpmA. Displays lysine 2,3-aminomutase activity, producing (R)-beta-lysine from (S)-alpha-lysine (L-lysine) (By similarity).
Similarity
Belongs to the radical SAM superfamily. KamA family.
Mass
38.676 kDa
Sequence
MRILPQEPVIREEQNWLTILKNAISDPKLLLKALNLPEDDFEQSIAARKLFSLRVPQPFIDKIEKGNPQDPLFLQVMCSDLEFVQAEGFSTDPLEEKNANAVPNILHKYRNRLLFMAKGGCAVNCRYCFRRHFPYDENPGNKKSWQLALDYIAAHSEIEEVIFSGGDPLMAKDHELAWLIKHLENIPHLQRLRIHTRLPVVIPQRITDEFCTLLAETRLQTVMVTHINHPNEIDQIFAHAMQKLNAVNVTLLNQSVLLKGVNDDAQILKILSDKLFQTGILPYYLHLLDKVQGASHFLISDIEAMQIYKTLQSLTSGYLVPKLAREIAGEPNKTLYAE

Gene
epmB
Protein
L-lysine 2,3-aminomutase
Organism
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Length
338 amino acids
Function
With EpmA is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P) on 'Lys-34'. EpmB appears to act before EpmA. Displays lysine 2,3-aminomutase activity, producing (R)-beta-lysine from (S)-alpha-lysine (L-lysine) (By similarity).
Similarity
Belongs to the radical SAM superfamily. KamA family.
Mass
38.676 kDa
Sequence
MRILPQEPVIREEQNWLTILKNAISDPKLLLKALNLPEDDFEQSIAARKLFSLRVPQPFIDKIEKGNPQDPLFLQVMCSDLEFVQAEGFSTDPLEEKNANAVPNILHKYRNRLLFMAKGGCAVNCRYCFRRHFPYDENPGNKKSWQLALDYIAAHSEIEEVIFSGGDPLMAKDHELAWLIKHLENIPHLQRLRIHTRLPVVIPQRITDEFCTLLAETRLQTVMVTHINHPNEIDQIFAHAMQKLNAVNVTLLNQSVLLKGVNDDAQILKILSDKLFQTGILPYYLHLLDKVQGASHFLISDIEAMQIYKTLQSLTSGYLVPKLAREIAGEPNKTLYAE

Gene
epmB
Protein
L-lysine 2,3-aminomutase
Organism
Buchnera aphidicola subsp. Schizaphis graminum (strain Sg)
Length
337 amino acids
Function
With EpmA is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P) on 'Lys-34'. EpmB appears to act before EpmA. Displays lysine 2,3-aminomutase activity, producing (R)-beta-lysine from (S)-alpha-lysine (L-lysine) (By similarity).
Similarity
Belongs to the radical SAM superfamily. KamA family.
Mass
39.502 kDa
Sequence
MKHYNTKKLNREKDSWLYEISNSIVEPKKLLKFLHLEKYPKYYDSKPKKVFPFRVPYSFASRMKKNDPKDPLLLQVITKNQEFLNNLQFNEDPVKEKKDIVLPGLLHKYKDRVLWILKTNCAINCRYCFRKHFPYEKNKGNKKNWIQILHYISQNIELNEVILSGGDPLMAKDHELLWLITSLSKIKHIKRLRIHTRLPIVIPNRITSDLCQIFSNSVLKIIIVTHINHPQEINEQLSDSLLKLKKSNVILLNQSVLLKNINDNAIILAELSSRLCENNIIPYYLHILDKVKGTSHFLVSNKKAKSIISDLMKMISGFLVPRLVFDNGSKDNKLIII