|
|
||
|
|
|
|
|
UniProt functional annotation for Q9XBQ8 | ||
|
|
|
|
|
|
||
| UniProt code: Q9XBQ8. |
|
||
| Organism: | |
Clostridium subterminale. |
| Taxonomy: | |
Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae; Clostridium. |
|
||
|
||
| Function: | |
Catalyzes the interconversion of L-alpha-lysine and L-beta- lysine. {ECO:0000269|PubMed:1329954, ECO:0000269|PubMed:1850415, ECO:0000269|PubMed:5438361}. |
|
||
| Catalytic activity: | |
Reaction=L-lysine = (3S)-3,6-diaminohexanoate; Xref=Rhea:RHEA:19177, ChEBI:CHEBI:32551, ChEBI:CHEBI:57434; EC=5.4.3.2; Evidence={ECO:0000269|PubMed:5438361}; |
| Cofactor: | |
Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Note=Binds 1 [4Fe-4S] cluster per subunit. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.; |
| Cofactor: | |
Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; |
| Cofactor: | |
Name=Co(2+); Xref=ChEBI:CHEBI:48828; Note=Binds 1 Co(2+) ion per subunit.; |
| Cofactor: | |
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 1 zinc ion per subunit.; |
| Activity regulation: | |
The enzyme is activated by S-adenosyl-methionine. Activity is dependent on the levels of Fe(2+), S(2-) and Co(2+). Activity is stimulated by addition of EDTA. S-adenosylhomocysteine competitively inhibits the activity whereas 5'-methylthioadenosine is not inhibitory in the presence of S-adenosylmethionine. Competitively inhibited by 4-thialysine. Inhibited by sodium borohydride (1 mM) when added with 2 mM dithionate. Moderately inhibited by beta- mercaptoethanol (30 mM) along with dithionate. Higher concentrations of Fe(2+) partially inhibit the activity and Co(2+) at 1 mM is a strong inhibitor. Hydroxylamine, isonicotinic acid hydrazide inhibit effectively, in addition, hydrazine, D-penicillamine and D-cycloserine are also inhibitory at high concentrations. {ECO:0000269|PubMed:11370852, ECO:0000269|PubMed:1850415, ECO:0000269|PubMed:5438361}. |
| Biophysicochemical properties: | |
Kinetic parameters: KM=6.6 uM for L-lysine {ECO:0000269|PubMed:11370852, ECO:0000269|PubMed:1329954, ECO:0000269|PubMed:5438361}; KM=28 nM for adenosylmethionine {ECO:0000269|PubMed:11370852, ECO:0000269|PubMed:1329954, ECO:0000269|PubMed:5438361}; KM=1.4 mM for 4-thialysine {ECO:0000269|PubMed:11370852, ECO:0000269|PubMed:1329954, ECO:0000269|PubMed:5438361}; Vmax=0.19 umol/min/mg enzyme with 4-thialysine as substrate (at 37 degrees Celsius and pH 8) {ECO:0000269|PubMed:11370852, ECO:0000269|PubMed:1329954, ECO:0000269|PubMed:5438361}; pH dependence: Optimum pH is 8.0. Displays half maximal activity between pH 6.0 and 9.8. {ECO:0000269|PubMed:11370852, ECO:0000269|PubMed:1329954, ECO:0000269|PubMed:5438361}; Redox potential: E(0) is between -336 and -370 mV for 4Fe-4S cluster. {ECO:0000269|PubMed:11370852, ECO:0000269|PubMed:1329954, ECO:0000269|PubMed:5438361}; Temperature dependence: Optimum temperature is 37 degrees Celsius. It has strong activity at 37 degrees Celsius but is reversibly inactivated in temperatures between 37 and 65 degrees Celsius. Minimal loss of activity is observed in enzyme stored at -10 degrees Celsius in the presence of 15% glycerol. {ECO:0000269|PubMed:11370852, ECO:0000269|PubMed:1329954, ECO:0000269|PubMed:5438361}; |
| Pathway: | |
Amino-acid degradation; L-lysine degradation via acetate pathway. |
| Subunit: | |
Homohexamer; trimer of dimers. Forms a homotetramer in crystal. {ECO:0000269|PubMed:16166264, ECO:0000269|PubMed:2019591}. |
| Similarity: | |
Belongs to the radical SAM superfamily. KamA family. {ECO:0000305}. |
Annotations taken from UniProtKB at the EBI.