Top Level Name

  ⌊ Superfamily (core) Radical SAM

    ⌊ Subgroup PLP-dependent

     ⌊ Family L-lysine 2,3-aminomutase (yjeK like)

  ⌊ FunctionalDomain L-lysine 2,3-aminomutase (epmB) (ID 280350)

Superfamily Assignment Evidence Code(s) ISS PubMed:17042480
Family Assignment Evidence Code CFM PubMed:17042480 PubMed:20070887 PubMed:20729861 PubMed:22128152
This entry was last updated onJune 10, 2017

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Escherichia coli str. K-12 substr. MG1655 Taxon ID: 511145 16131971 NP_418570.1 (RefSeq) URP
Taxon ID: 543 446863293 WP_000940549.1 (RefSeq)
Escherichia coli Taxon ID: 562 857138824 AKO55291.1 (Genbank) URP
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Uniprot

Protein NameAccessionEC Number Identifier
L-lysine 2,3-aminomutase P39280 5.4.3.- EPMB_ECOLI (Swiss-Prot)

Sequence

Length of Enzyme (full-length): 342 | Length of Functional Domain: 335

1       10        20        30        40        50        60

MAHIVTLNTPSREDWLTQLADVVTDPDELLRLLNIDAEEKLLAGRSAKKLFALRVPRSFI
DRMEKGNPDDPLLRQVLTSQDEFVIAPGFSTDPLEEQHSVVPGLLHKYHNRALLLVKGGC
AVNCRYCFRRHFPYAENQGNKRNWQTALEYVAAHPELDEMIFSGGDPLMAKDHELDWLLT
QLEAIPHIKRLRIHSRLPIVIPARITEALVECFARSTLQILLVNHINHANEVDETFRQAM
AKLRRVGVTLLNQSVLLRDVNDNAQTLANLSNALFDAGVMPYYLHVLDKVQGAAHFMVSD
DEARQIMRELLTLVSGYLVPKLAREIGGEPSKTPLDLQLRQQ
This shows the full-length sequence of the enzyme. The region of the functional domain is highlighted in black letters, while the residual residues are shown in grey. The Superfamily domain, when present, is shown using underlining. In many cases the functional domain is the full-length sequence.
Conserved catalytic residues (as determined by automated alignment to family, subgroup, or superfamily HMMs) are shown with teal highlighting . Conserved catalytic residues which do not matched the Conserved Alignment Residue are shown with maroon highlighting . Information regarding their function can be found in the Conserved Residues section below.
FASTA formatted full-length sequence.
BLAST this sequence against SFLD.
Scan SFLD-HMMs with this sequence.

Conserved Residues
Superfamily CAR This EFD conserves 3/3 Superfamily-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
120 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
124 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
127 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
Subgroup CAR This EFD conserves 5/5 Subgroup-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
108 Tyr (Y) side chain PLP binding cofactor binding -- binding IEA
120 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
124 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
127 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
332 Lys (K) side chain PLP binding, reaction nucleophile cofactor binding -- binding,
covalent catalysis -- reactant 		ISS
Family CAR This EFD conserves 7/7 Family-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
108 Tyr (Y) side chain PLP binding cofactor binding -- binding IEA
111 Arg (R) side chain PLP binding cofactor binding -- binding IEA
120 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding IEA
124 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding IEA
127 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding IEA
129 Arg (R) side chain Binds substrate
Notes: This is the arginine that is responsible for Lysine and Glutamate substrate binding, thus it is reasonable to assume that it is also responsible for binding in the unknown family. 		substrate binding -- binding IEA
332 Lys (K) side chain PLP binding, reaction nucleophile cofactor binding -- binding,
covalent catalysis -- reactant 		IEA

Catalyzed Reaction

lysine 2,3-aminomutase

L-lysinium(1+)
32551		 (3S)-3,6-diammoniohexanoate
57434

EC: 5.4.3.2 | IntEnz: 5.4.3.2 | Kegg: 5.4.3.2 | BioCyc: 5.4.3.2 | BRENDA: 5.4.3.2

Curation History
Time Change Annotation Old Value New Value
May 14, 2014, 3:01 a.m. update curation agent holliday setDomainBoundaries.py
update domain end position 342 337
June 14, 2014, 2:53 a.m. update curation agent setDomainBoundaries.py holliday
update family assignment evidence code IEA CFM
update name Uncharacterised Radical SAM sequence L-lysine 2,3-aminomutase
Oct. 16, 2014, 3:54 a.m. update curation agent holliday setDomainBoundaries.py
May 11, 2015, 8:45 a.m. update curation agent setDomainBoundaries.py holliday
update curation agent holliday setDomainBoundaries.py
update name L-lysine 2,3-aminomutase L-lysine 2,3-aminomutase (epmB)
Oct. 15, 2016, 3:52 a.m. update domain end position 337 338
update domain start position 1 4
EC number assigned by UniProtKB accession ID.