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Lysine 5,6-aminomutase beta subunit (5,6-LAM) (EC 5.4.3.3) (D-lysine 5,6-aminomutase beta subunit) (L-beta-lysine 5,6-aminomutase beta subunit)

 KAME_ACESD              Reviewed;         262 AA.
E3PRJ4; Q9ZFE5;
18-APR-2012, integrated into UniProtKB/Swiss-Prot.
08-MAR-2011, sequence version 1.
12-SEP-2018, entry version 47.
RecName: Full=Lysine 5,6-aminomutase beta subunit {ECO:0000305};
Short=5,6-LAM {ECO:0000303|PubMed:11318641, ECO:0000303|PubMed:15514022};
EC=5.4.3.3 {ECO:0000269|PubMed:10617592, ECO:0000269|PubMed:11318641};
AltName: Full=D-lysine 5,6-aminomutase beta subunit {ECO:0000312|EMBL:CBH21498.1};
AltName: Full=L-beta-lysine 5,6-aminomutase beta subunit {ECO:0000305};
Name=kamE; OrderedLocusNames=CLOST_1378;
Acetoanaerobium sticklandii (strain ATCC 12662 / DSM 519 / JCM 1433 /
NCIMB 10654) (Clostridium sticklandii).
Bacteria; Firmicutes; Clostridia; Clostridiales;
Peptostreptococcaceae; Acetoanaerobium.
NCBI_TaxID=499177;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF N-TERMINUS,
FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION,
BIOPHYSICOCHEMICAL PROPERTIES, EPR SPECTROSCOPY, AND PATHWAY.
PubMed=10617592; DOI=10.1074/jbc.275.1.106;
Chang C.H., Frey P.A.;
"Cloning, sequencing, heterologous expression, purification, and
characterization of adenosylcobalamin-dependent D-lysine 5, 6-
aminomutase from Clostridium sticklandii.";
J. Biol. Chem. 275:106-114(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 12662 / DSM 519 / JCM 1433 / NCIMB 10654;
PubMed=20937090; DOI=10.1186/1471-2164-11-555;
Fonknechten N., Chaussonnerie S., Tricot S., Lajus A., Andreesen J.R.,
Perchat N., Pelletier E., Gouyvenoux M., Barbe V., Salanoubat M.,
Le Paslier D., Weissenbach J., Cohen G.N., Kreimeyer A.;
"Clostridium sticklandii, a specialist in amino acid
degradation:revisiting its metabolism through its genome sequence.";
BMC Genomics 11:555-555(2010).
[3]
FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND REACTION MECHANISM.
PubMed=11318641;
Tang K.H., Chang C.H., Frey P.A.;
"Electron transfer in the substrate-dependent suicide inactivation of
lysine 5,6-aminomutase.";
Biochemistry 40:5190-5199(2001).
[4]
X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) IN COMPLEX WITH B12 AND
PYRIDOXAL PHOSPHATE, COFACTOR, AND SUBUNIT.
PubMed=15514022; DOI=10.1073/pnas.0407074101;
Berkovitch F., Behshad E., Tang K.H., Enns E.A., Frey P.A.,
Drennan C.L.;
"A locking mechanism preventing radical damage in the absence of
substrate, as revealed by the x-ray structure of lysine 5,6-
aminomutase.";
Proc. Natl. Acad. Sci. U.S.A. 101:15870-15875(2004).
-!- FUNCTION: Catalyzes the migration of the L-beta-lysine and D-
lysine epsilon amino group to the delta carbon to produce 3,5-
diaminohexanoate and 2,5-diaminohexanoate, respectively.
{ECO:0000269|PubMed:10617592, ECO:0000269|PubMed:11318641}.
-!- CATALYTIC ACTIVITY: (3S)-3,6-diaminohexanoate = (3S,5S)-3,5-
diaminohexanoate. {ECO:0000269|PubMed:11318641}.
-!- CATALYTIC ACTIVITY: D-lysine = 2,5-diaminohexanoate.
{ECO:0000269|PubMed:10617592, ECO:0000269|PubMed:11318641}.
-!- COFACTOR:
Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408;
Evidence={ECO:0000269|PubMed:10617592,
ECO:0000269|PubMed:11318641};
-!- COFACTOR:
Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
Evidence={ECO:0000269|PubMed:11318641,
ECO:0000269|PubMed:15514022};
-!- ACTIVITY REGULATION: Rapidly inactivated in the presence of D-
lysine and to a lesser extent in the absence of adenosylcobalamin
(Adocbl). Activity is stable in the presence of Adocbl when D-
lysine is absent. Adocbl imparts thermal stability at 37 degrees
Celsius. {ECO:0000269|PubMed:10617592}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=6.6 uM for adenosylcobalamin (for recombinant alpha and beta
subunits expressed together in E.coli to overcome presence of
corrinoids in native system) {ECO:0000269|PubMed:10617592};
-!- PATHWAY: Amino-acid metabolism; lysine degradation.
{ECO:0000269|PubMed:10617592}.
-!- SUBUNIT: Heterotetramer of 2 alpha and 2 beta subunits.
{ECO:0000303|PubMed:15514022}.
-!- SIMILARITY: Belongs to the KamE family. {ECO:0000255}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; AF104259; AAC79718.1; -; Genomic_DNA.
EMBL; FP565809; CBH21498.1; -; Genomic_DNA.
RefSeq; WP_013361591.1; NC_014614.1.
PDB; 1XRS; X-ray; 2.80 A; B=1-262.
PDBsum; 1XRS; -.
ProteinModelPortal; E3PRJ4; -.
SMR; E3PRJ4; -.
IntAct; E3PRJ4; 1.
STRING; 499177.CLOST_1378; -.
EnsemblBacteria; CBH21498; CBH21498; CLOST_1378.
GeneID; 35557648; -.
KEGG; cst:CLOST_1378; -.
eggNOG; ENOG4107CHF; Bacteria.
eggNOG; COG5012; LUCA.
HOGENOM; HOG000223896; -.
KO; K18011; -.
OMA; AIMNMKG; -.
OrthoDB; POG091H10H2; -.
SABIO-RK; E3PRJ4; -.
UniPathway; UPA00225; -.
EvolutionaryTrace; E3PRJ4; -.
Proteomes; UP000007041; Chromosome.
GO; GO:0047702; F:beta-lysine 5,6-aminomutase activity; IEA:UniProtKB-EC.
GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
Gene3D; 3.30.30.60; -; 1.
InterPro; IPR006158; Cobalamin-bd.
InterPro; IPR036724; Cobalamin-bd_sf.
InterPro; IPR028991; KamE_N.
InterPro; IPR036843; KamE_N_sf.
Pfam; PF02310; B12-binding; 1.
Pfam; PF16554; OAM_dimer; 1.
SUPFAM; SSF117778; SSF117778; 1.
SUPFAM; SSF52242; SSF52242; 1.
PROSITE; PS51332; B12_BINDING; 1.
1: Evidence at protein level;
3D-structure; Cobalamin; Cobalt; Complete proteome;
Direct protein sequencing; Isomerase; Metal-binding;
Pyridoxal phosphate; Reference proteome.
CHAIN 1 262 Lysine 5,6-aminomutase beta subunit.
/FTId=PRO_0000416984.
DOMAIN 120 262 B12-binding. {ECO:0000255|PROSITE-
ProRule:PRU00666}.
REGION 130 136 Adenosylcobalamin binding.
{ECO:0000269|PubMed:15514022}.
REGION 185 192 Adenosylcobalamin binding.
{ECO:0000269|PubMed:15514022}.
REGION 219 223 Adenosylcobalamin binding.
{ECO:0000269|PubMed:15514022}.
REGION 239 244 Adenosylcobalamin binding.
{ECO:0000269|PubMed:15514022}.
METAL 133 133 Cobalt (adenosylcobalamin axial ligand);
via tele nitrogen.
{ECO:0000312|PDB:1XRS}.
MOD_RES 144 144 N6-(pyridoxal phosphate)lysine.
{ECO:0000269|PubMed:15514022}.
STRAND 34 42 {ECO:0000244|PDB:1XRS}.
HELIX 46 57 {ECO:0000244|PDB:1XRS}.
STRAND 65 73 {ECO:0000244|PDB:1XRS}.
STRAND 76 83 {ECO:0000244|PDB:1XRS}.
HELIX 106 116 {ECO:0000244|PDB:1XRS}.
STRAND 121 128 {ECO:0000244|PDB:1XRS}.
HELIX 135 141 {ECO:0000244|PDB:1XRS}.
HELIX 152 154 {ECO:0000244|PDB:1XRS}.
STRAND 158 162 {ECO:0000244|PDB:1XRS}.
STRAND 165 167 {ECO:0000244|PDB:1XRS}.
HELIX 169 178 {ECO:0000244|PDB:1XRS}.
STRAND 182 187 {ECO:0000244|PDB:1XRS}.
HELIX 195 209 {ECO:0000244|PDB:1XRS}.
HELIX 213 215 {ECO:0000244|PDB:1XRS}.
STRAND 216 221 {ECO:0000244|PDB:1XRS}.
HELIX 227 231 {ECO:0000244|PDB:1XRS}.
TURN 232 234 {ECO:0000244|PDB:1XRS}.
STRAND 236 239 {ECO:0000244|PDB:1XRS}.
HELIX 245 260 {ECO:0000244|PDB:1XRS}.
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


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