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UniProt functional annotation for Q1LCS4 | ||
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| UniProt code: Q1LCS4. |
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| Organism: | |
Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 / CH34) (Ralstonia metallidurans). |
| Taxonomy: | |
Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; Burkholderiaceae; Cupriavidus. |
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| Function: | |
Catalyzes the oxidative ring opening of 3-hydroxyanthranilate to 2-amino-3-carboxymuconate semialdehyde, which spontaneously cyclizes to quinolinate. {ECO:0000255|HAMAP-Rule:MF_00825, ECO:0000269|PubMed:15909977}. |
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| Catalytic activity: | |
Reaction=3-hydroxyanthranilate + O2 = (2Z,4Z)-2-amino-3-carboxymuconate 6-semialdehyde; Xref=Rhea:RHEA:17953, ChEBI:CHEBI:15379, ChEBI:CHEBI:36559, ChEBI:CHEBI:77612; EC=1.13.11.6; Evidence={ECO:0000255|HAMAP-Rule:MF_00825}; |
| Cofactor: | |
Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000255|HAMAP-Rule:MF_00825, ECO:0000269|PubMed:15909978}; Note=Binds 2 Fe(2+) ions per subunit. {ECO:0000255|HAMAP-Rule:MF_00825, ECO:0000269|PubMed:15909978}; |
| Activity regulation: | |
Inhibited by 4-chloro-3-hydroxyanthranilate. Mechanism of inactivation involves the oxidation of the catalytic active site Fe(2+) to the catalytically inactive Fe(3+) oxidation state, superoxide production, and formation of two disulfide bonds between Cys-125 and Cys-128, and Cys-162 and Cys-165. Enzyme can be reactivated under reducing conditions. {ECO:0000269|PubMed:15909977}. |
| Biophysicochemical properties: | |
Kinetic parameters: KM=22.4 uM for 3-hydroxyanthranilate {ECO:0000269|PubMed:15909978}; |
| Pathway: | |
Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from L-kynurenine: step 3/3. {ECO:0000255|HAMAP-Rule:MF_00825}. |
| Subunit: | |
Homodimer. {ECO:0000255|HAMAP-Rule:MF_00825, ECO:0000269|PubMed:15909978}. |
| Similarity: | |
Belongs to the 3-HAO family. {ECO:0000255|HAMAP- Rule:MF_00825}. |
Annotations taken from UniProtKB at the EBI.