Top Level Name

  ⌊ Superfamily (core) Radical SAM

    ⌊ Subgroup PLP-dependent

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

  ⌊ FunctionalDomain L-lysine 2,3-aminomutase (ID 381080)

Superfamily Assignment Evidence Code(s) ISS
Family Assignment Evidence Code CFM IES PubMed:16166264
This entry was last updated onJune 10, 2017

References to Other Databases

Genbank

SpeciesGIAccessionProteome
n/a 217256570 ACK24655.1 (Genbank)
n/a 183004943 ACC34953.1 (Genbank)
Clostridium subterminale Taxon ID: 1550 5410603 AAD43134.1 (Genbank)
Show All

Uniprot

Protein NameAccessionEC Number Identifier
L-lysine 2,3-aminomutase Q9XBQ8 5.4.3.2 KAMA_CLOSU (Swiss-Prot)

Sequence

Length of Enzyme (full-length): 416 | Length of Functional Domain: 413

1       10        20        30        40        50        60

MINRRYELFKDVSDADWNDWRWQVRNRIETVEELKKYIPLTKEEEEGVAQCVKSLRMAIT
PYYLSLIDPNDPNDPVRKQAIPTALELNKAAADLEDPLHEDTDSPVPGLTHRYPDRVLLL
ITDMCSMYCRHCTRRRFAGQSDDSMPMERIDKAIDYIRNTPQVRDVLLSGGDALLVSDET
LEYIIAKLREIPHVEIVRIGSRTPVVLPQRITPELVNMLKKYHPVWLNTHFNHPNEITEE
STRACQLLADAGVPLGNQSVLLRGVNDCVHVMKELVNKLVKIRVRPYYIYQCDLSLGLEH
FRTPVSKGIEIIEGLRGHTSGYCVPTFVVDAPGGGGKTPVMPNYVISQSHDKVILRNFEG
VITTYSEPINYTPGCNCDVCTGKKKVHKVGVAGLLNGEGMALEPVGLERNKRHVQE
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
125 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
129 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
132 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
113 Tyr (Y) side chain PLP binding cofactor binding -- binding IEA
125 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
129 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
132 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
337 Lys (K) side chain PLP binding, reaction nucleophile cofactor binding -- binding,
covalent catalysis -- reactant 		ISS
Family CAR This EFD conserves 10/10 Family-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
113 Tyr (Y) side chain PLP binding
Notes: Tyr cited in MACiE. Also, PLP enzymes require a bulky aromatic or aliphatic residue that prevents the cofactor from moving in the active site once it has been released from the covalent attachment to the enzyme during the course of the reaction. 		cofactor binding -- binding IEA
116 Arg (R) side chain PLP binding cofactor binding -- binding IEA
125 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding IDA PubMed:16166264
129 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding IDA PubMed:16166264
132 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding IEA PubMed:16166264
134 Arg (R) side chain Binds lysine substrate substrate binding -- binding IEA
198 Arg (R) side chain PLP binding cofactor binding -- binding IEA
293 Asp (D) side chain Binds lysine substrate substrate binding -- binding ISS PubMed:17222594
330 Asp (D) side chain Binds lysine substrate substrate binding -- binding ISS PubMed:17222594
337 Lys (K) side chain PLP binding, reaction nucleophile cofactor binding -- binding,
covalent catalysis -- reactant 		IDA PubMed:16166264

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

Structures

PDB ID Title Molecule Name Number of
EFDs		 Resolution (Å) Mutant? Het group Links
2A5H 2.1 Angstrom X-Ray Crystal Structure Of Lysine-2,3-Aminomutase From Clostridium Subterminale Sb4, With Michaelis Analog (L-Alpha-Lysine External Aldimine Form Of Pyridoxal-5'-Phosphate). L-Lysine 2,3-Aminomutase 2 2.1 Selenomethionine
(6 more ⇓) 		CSA • PDB • PDBSum
Percent identity and alignment length from the BLAST match of the Functional Domain sequence to the PDB sequence.
"Yes" indicates that a GI associated with this Functional Domain was mapped to the PDB ID via UniProtKB.

Curation History
Time Change Annotation Old Value New Value
May 14, 2014, 3:30 a.m. update curation agent holliday setDomainBoundaries.py
update domain start position 1 2
Oct. 15, 2016, 5:10 a.m. update domain end position 416 414
EC number assigned by UniProtKB accession ID.