KAME_ACESD
ID KAME_ACESD Reviewed; 262 AA.
AC E3PRJ4; Q9ZFE5;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 08-MAR-2011, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Lysine 5,6-aminomutase beta subunit {ECO:0000305};
DE Short=5,6-LAM {ECO:0000303|PubMed:11318641, ECO:0000303|PubMed:15514022};
DE EC=5.4.3.3 {ECO:0000269|PubMed:10617592, ECO:0000269|PubMed:11318641};
DE AltName: Full=D-lysine 5,6-aminomutase beta subunit {ECO:0000312|EMBL:CBH21498.1};
DE AltName: Full=L-beta-lysine 5,6-aminomutase beta subunit {ECO:0000305};
GN Name=kamE; OrderedLocusNames=CLOST_1378;
OS Acetoanaerobium sticklandii (strain ATCC 12662 / DSM 519 / JCM 1433 / CCUG
OS 9281 / NCIMB 10654 / HF) (Clostridium sticklandii).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC Acetoanaerobium.
OX NCBI_TaxID=499177;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF N-TERMINUS,
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, EPR SPECTROSCOPY, AND PATHWAY.
RX PubMed=10617592; DOI=10.1074/jbc.275.1.106;
RA Chang C.H., Frey P.A.;
RT "Cloning, sequencing, heterologous expression, purification, and
RT characterization of adenosylcobalamin-dependent D-lysine 5, 6-aminomutase
RT from Clostridium sticklandii.";
RL J. Biol. Chem. 275:106-114(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12662 / DSM 519 / JCM 1433 / CCUG 9281 / NCIMB 10654 / HF;
RX PubMed=20937090; DOI=10.1186/1471-2164-11-555;
RA Fonknechten N., Chaussonnerie S., Tricot S., Lajus A., Andreesen J.R.,
RA Perchat N., Pelletier E., Gouyvenoux M., Barbe V., Salanoubat M.,
RA Le Paslier D., Weissenbach J., Cohen G.N., Kreimeyer A.;
RT "Clostridium sticklandii, a specialist in amino acid degradation:revisiting
RT its metabolism through its genome sequence.";
RL BMC Genomics 11:555-555(2010).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND REACTION MECHANISM.
RX PubMed=11318641; DOI=10.1021/bi010157j;
RA Tang K.H., Chang C.H., Frey P.A.;
RT "Electron transfer in the substrate-dependent suicide inactivation of
RT lysine 5,6-aminomutase.";
RL Biochemistry 40:5190-5199(2001).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) IN COMPLEX WITH B12 AND PYRIDOXAL
RP PHOSPHATE, COFACTOR, AND SUBUNIT.
RX PubMed=15514022; DOI=10.1073/pnas.0407074101;
RA Berkovitch F., Behshad E., Tang K.H., Enns E.A., Frey P.A., Drennan C.L.;
RT "A locking mechanism preventing radical damage in the absence of substrate,
RT as revealed by the x-ray structure of lysine 5,6-aminomutase.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15870-15875(2004).
CC -!- FUNCTION: Catalyzes the migration of the L-beta-lysine and D-lysine
CC epsilon amino group to the delta carbon to produce 3,5-diaminohexanoate
CC and 2,5-diaminohexanoate, respectively. {ECO:0000269|PubMed:10617592,
CC ECO:0000269|PubMed:11318641}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3S)-3,6-diaminohexanoate = (3S,5S)-3,5-diaminohexanoate;
CC Xref=Rhea:RHEA:21736, ChEBI:CHEBI:57434, ChEBI:CHEBI:57436;
CC EC=5.4.3.3; Evidence={ECO:0000269|PubMed:11318641};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-lysine = (2R,5S)-2,5-diaminohexanoate; Xref=Rhea:RHEA:18241,
CC ChEBI:CHEBI:32557, ChEBI:CHEBI:137487; EC=5.4.3.3;
CC Evidence={ECO:0000269|PubMed:10617592, ECO:0000269|PubMed:11318641};
CC -!- COFACTOR:
CC Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408;
CC Evidence={ECO:0000269|PubMed:10617592, ECO:0000269|PubMed:11318641};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:11318641, ECO:0000269|PubMed:15514022};
CC -!- ACTIVITY REGULATION: Rapidly inactivated in the presence of D-lysine
CC and to a lesser extent in the absence of adenosylcobalamin (Adocbl).
CC Activity is stable in the presence of Adocbl when D-lysine is absent.
CC Adocbl imparts thermal stability at 37 degrees Celsius.
CC {ECO:0000269|PubMed:10617592}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=6.6 uM for adenosylcobalamin (for recombinant alpha and beta
CC subunits expressed together in E.coli to overcome presence of
CC corrinoids in native system) {ECO:0000269|PubMed:10617592};
CC -!- PATHWAY: Amino-acid metabolism; lysine degradation.
CC {ECO:0000269|PubMed:10617592}.
CC -!- SUBUNIT: Heterotetramer of 2 alpha and 2 beta subunits.
CC {ECO:0000303|PubMed:15514022}.
CC -!- SIMILARITY: Belongs to the KamE family. {ECO:0000255}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF104259; AAC79718.1; -; Genomic_DNA.
DR EMBL; FP565809; CBH21498.1; -; Genomic_DNA.
DR PDB; 1XRS; X-ray; 2.80 A; B=1-262.
DR PDBsum; 1XRS; -.
DR AlphaFoldDB; E3PRJ4; -.
DR SMR; E3PRJ4; -.
DR IntAct; E3PRJ4; 1.
DR STRING; 1511.CLOST_1378; -.
DR EnsemblBacteria; CBH21498; CBH21498; CLOST_1378.
DR KEGG; cst:CLOST_1378; -.
DR eggNOG; COG2185; Bacteria.
DR HOGENOM; CLU_065773_0_0_9; -.
DR OMA; AIMNMKG; -.
DR BRENDA; 5.4.3.3; 1522.
DR SABIO-RK; E3PRJ4; -.
DR UniPathway; UPA00225; -.
DR EvolutionaryTrace; E3PRJ4; -.
DR Proteomes; UP000007041; Chromosome.
DR GO; GO:0047702; F:beta-lysine 5,6-aminomutase activity; IEA:UniProtKB-EC.
DR GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
DR GO; GO:0047826; F:D-lysine 5,6-aminomutase activity; IEA:RHEA.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR Gene3D; 3.30.30.60; -; 1.
DR InterPro; IPR006158; Cobalamin-bd.
DR InterPro; IPR036724; Cobalamin-bd_sf.
DR InterPro; IPR028991; KamE_N.
DR InterPro; IPR036843; KamE_N_sf.
DR Pfam; PF02310; B12-binding; 1.
DR Pfam; PF16554; OAM_dimer; 1.
DR SUPFAM; SSF117778; SSF117778; 1.
DR SUPFAM; SSF52242; SSF52242; 1.
DR PROSITE; PS51332; B12_BINDING; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cobalamin; Cobalt; Direct protein sequencing; Isomerase;
KW Metal-binding; Pyridoxal phosphate; Reference proteome.
FT CHAIN 1..262
FT /note="Lysine 5,6-aminomutase beta subunit"
FT /id="PRO_0000416984"
FT DOMAIN 120..262
FT /note="B12-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00666"
FT BINDING 130..136
FT /ligand="adenosylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:18408"
FT /evidence="ECO:0000269|PubMed:15514022"
FT BINDING 133
FT /ligand="adenosylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:18408"
FT /ligand_part="Co"
FT /ligand_part_id="ChEBI:CHEBI:27638"
FT /note="axial binding residue"
FT /evidence="ECO:0000312|PDB:1XRS"
FT BINDING 185..192
FT /ligand="adenosylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:18408"
FT /evidence="ECO:0000269|PubMed:15514022"
FT BINDING 219..223
FT /ligand="adenosylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:18408"
FT /evidence="ECO:0000269|PubMed:15514022"
FT BINDING 239..244
FT /ligand="adenosylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:18408"
FT /evidence="ECO:0000269|PubMed:15514022"
FT MOD_RES 144
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000269|PubMed:15514022"
FT STRAND 34..42
FT /evidence="ECO:0007829|PDB:1XRS"
FT HELIX 46..57
FT /evidence="ECO:0007829|PDB:1XRS"
FT STRAND 65..73
FT /evidence="ECO:0007829|PDB:1XRS"
FT STRAND 76..83
FT /evidence="ECO:0007829|PDB:1XRS"
FT HELIX 106..116
FT /evidence="ECO:0007829|PDB:1XRS"
FT STRAND 121..128
FT /evidence="ECO:0007829|PDB:1XRS"
FT HELIX 135..141
FT /evidence="ECO:0007829|PDB:1XRS"
FT HELIX 152..154
FT /evidence="ECO:0007829|PDB:1XRS"
FT STRAND 158..162
FT /evidence="ECO:0007829|PDB:1XRS"
FT STRAND 165..167
FT /evidence="ECO:0007829|PDB:1XRS"
FT HELIX 169..178
FT /evidence="ECO:0007829|PDB:1XRS"
FT STRAND 182..187
FT /evidence="ECO:0007829|PDB:1XRS"
FT HELIX 195..209
FT /evidence="ECO:0007829|PDB:1XRS"
FT HELIX 213..215
FT /evidence="ECO:0007829|PDB:1XRS"
FT STRAND 216..221
FT /evidence="ECO:0007829|PDB:1XRS"
FT HELIX 227..231
FT /evidence="ECO:0007829|PDB:1XRS"
FT TURN 232..234
FT /evidence="ECO:0007829|PDB:1XRS"
FT STRAND 236..239
FT /evidence="ECO:0007829|PDB:1XRS"
FT HELIX 245..260
FT /evidence="ECO:0007829|PDB:1XRS"
SQ SEQUENCE 262 AA; 29224 MW; 248765160F6EF46F CRC64;
MSSGLYSMEK KEFDKVLDLE RVKPYGDTMN DGKVQLSFTL PLKNNERSAE AAKQIALKMG
LEEPSVVMQQ SLDEEFTFFV VYGNFVQSVN YNEIHVEAVN SEILSMEETD EYIKENIGRK
IVVVGASTGT DAHTVGIDAI MNMKGYAGHY GLERYEMIDA YNLGSQVANE DFIKKAVELE
ADVLLVSQTV TQKNVHIQNM THLIELLEAE GLRDRFVLLC GGPRINNEIA KELGYDAGFG
PGRFADDVAT FAVKTLNDRM NS
