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UniProt functional annotation for P9WPQ5 | ||
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| UniProt code: P9WPQ5. |
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| Organism: | |
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv). |
| Taxonomy: | |
Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium tuberculosis complex. |
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| Function: | |
Catalyzes a mechanistically unusual reaction, the ATP- dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8- diaminopelargonic acid (DAPA, also called 7,8-diammoniononanoate) to form a ureido ring (PubMed:20565114). Can use a range of NTPs; has highest affinity for CTP (KD is measured as 17.2 uM or 0.160 uM in 2 different papers) while KD for ATP is 331 uM or 75 uM in the same papers. Gly-169 plays a role in NTP discrimination (PubMed:25801336, Ref.5). {ECO:0000269|PubMed:20565114, ECO:0000269|PubMed:25801336, ECO:0000269|Ref.5}. |
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| Catalytic activity: | |
Reaction=(7R,8S)-7,8-diammoniononanoate + ATP + CO2 = (4R,5S)- dethiobiotin + ADP + 3 H(+) + phosphate; Xref=Rhea:RHEA:15805, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:149469, ChEBI:CHEBI:149473, ChEBI:CHEBI:456216; EC=6.3.3.3; Evidence={ECO:0000255|HAMAP- Rule:MF_00336}; |
| Cofactor: | |
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_00336, ECO:0000269|PubMed:20565114, ECO:0000269|PubMed:30289406, ECO:0000269|Ref.5}; Note=Binds 1 Mg(2+) per subunit. {ECO:0000269|PubMed:20565114, ECO:0000269|PubMed:30289406, ECO:0000269|Ref.5}; |
| Activity regulation: | |
Inhibited by ADP. {ECO:0000269|PubMed:30289406}. |
| Biophysicochemical properties: | |
Kinetic parameters: KM=2 uM for DAPA (at pH 8.5 and at 20 degrees Celsius) {ECO:0000269|PubMed:20565114}; KM=29 uM for ATP (at pH 8.5 and at 20 degrees Celsius) {ECO:0000269|PubMed:20565114}; KM=30.2 uM for DAPA (at pH 7.5, 37 degrees Celsius) {ECO:0000269|PubMed:25801336}; KM=3.074 mM for NaHCO(3) (at pH 7.5, 37 degrees Celsius) {ECO:0000269|PubMed:25801336}; KM=30.2 uM for ATP (at pH 7.5, 37 degrees Celsius) {ECO:0000269|PubMed:25801336}; KM=25.2 uM for CTP (at pH 7.5, 37 degrees Celsius) {ECO:0000269|PubMed:25801336}; KM=26.3 uM for GTP (at pH 7.5, 37 degrees Celsius) {ECO:0000269|PubMed:25801336}; KM=17.7 uM for ITP (at pH 7.5, 37 degrees Celsius) {ECO:0000269|PubMed:25801336}; KM=23.2 uM for TTP (at pH 7.5, 37 degrees Celsius) {ECO:0000269|PubMed:25801336}; KM=26.1 uM for UTP (at pH 7.5, 37 degrees Celsius) {ECO:0000269|PubMed:25801336}; Vmax=3.5 umol/min/mg enzyme toward ATP (at pH 8.5 and at 20 degrees Celsius) {ECO:0000269|PubMed:20565114}; Vmax=6 umol/min/mg enzyme toward DAPA (at pH 8.5 and at 20 degrees Celsius) {ECO:0000269|PubMed:20565114}; |
| Pathway: | |
Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8- diaminononanoate: step 1/2. {ECO:0000255|HAMAP-Rule:MF_00336}. |
| Subunit: | |
Homodimer. {ECO:0000255|HAMAP-Rule:MF_00336, ECO:0000269|PubMed:20565114, ECO:0000269|PubMed:25801336, ECO:0000269|PubMed:30289406, ECO:0000269|Ref.5}. |
| Subcellular location: | |
Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00336}. |
| Domain: | |
While ADP, ATP, ITP, TTP and UTP can be crystallized in the enzyme in approximately the same place as CTP, it is their phosphate tails that anchor them to the enzyme, their nucleoside moieties do not bind in the same way CTP does. {ECO:0000269|PubMed:30289406, ECO:0000269|Ref.5}. |
| Similarity: | |
Belongs to the dethiobiotin synthetase family. {ECO:0000255|HAMAP-Rule:MF_00336}. |
Annotations taken from UniProtKB at the EBI.