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UniProt functional annotation for P12995 | ||
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| UniProt code: P12995. |
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| Organism: | |
Escherichia coli (strain K12). |
| Taxonomy: | |
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia. |
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| Function: | |
Catalyzes the transfer of the alpha-amino group from S- adenosyl-L-methionine (SAM) to 7-keto-8-aminopelargonic acid (KAPA) to form 7,8-diaminopelargonic acid (DAPA). It is the only animotransferase known to utilize SAM as an amino donor (PubMed:1092681). Complements a bioU deletion in Synechocystis PCC 6803 (PubMed:32042199). {ECO:0000269|PubMed:1092681, ECO:0000269|PubMed:32042199}. |
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| Catalytic activity: | |
Reaction=(S)-8-amino-7-oxononanoate + S-adenosyl-L-methionine = (7R,8S)-7,8-diammoniononanoate + S-adenosyl-4-methylsulfanyl-2- oxobutanoate; Xref=Rhea:RHEA:16861, ChEBI:CHEBI:16490, ChEBI:CHEBI:59789, ChEBI:CHEBI:149468, ChEBI:CHEBI:149469; EC=2.6.1.62; |
| Cofactor: | |
Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:1092681}; |
| Activity regulation: | |
Inhibited by amiclenomycin. S-adenosyl-L-(2- hydroxy-4-methylthio)butyric acid and adenosine are competitive inhibitors with SAM and uncompetitive inhibitors with KAPA as substrates. S-adenosyl-L-ethionine, adenine and 8-keto-7- aminopelargonic acid are non-competitive inhibitors with both substrates. {ECO:0000269|PubMed:1092682, ECO:0000269|PubMed:12218056, ECO:0000269|PubMed:16042602}. |
| Biophysicochemical properties: | |
Kinetic parameters: KM=1.2 uM for KAPA {ECO:0000269|PubMed:1092682, ECO:0000269|PubMed:12379100}; KM=150 uM for SAM {ECO:0000269|PubMed:1092682, ECO:0000269|PubMed:12379100}; KM=21 uM for pyridoxamine phosphate (PMP) {ECO:0000269|PubMed:1092682, ECO:0000269|PubMed:12379100}; KM=32 uM for pyridoxal phosphate (PLP) {ECO:0000269|PubMed:1092682, ECO:0000269|PubMed:12379100}; KM=1000 uM for 8-keto-7-aminopelargonic acid {ECO:0000269|PubMed:1092682, ECO:0000269|PubMed:12379100}; Vmax=0.16 umol/min/mg enzyme with KAPA as substrate {ECO:0000269|PubMed:1092682, ECO:0000269|PubMed:12379100}; Vmax=0.027 umol/min/mg enzyme with 8-keto-7-aminopelargonic acid as substrate {ECO:0000269|PubMed:1092682, ECO:0000269|PubMed:12379100}; |
| Pathway: | |
Cofactor biosynthesis; biotin biosynthesis; 7,8- diaminononanoate from 8-amino-7-oxononanoate (SAM route): step 1/1. |
| Subunit: | |
Homodimer. {ECO:0000269|PubMed:10452893, ECO:0000269|PubMed:1092681, ECO:0000269|PubMed:12218056, ECO:0000269|PubMed:12379100, ECO:0000269|PubMed:14756557}. |
| Subcellular location: | |
Cytoplasm {ECO:0000250}. |
| Induction: | |
Repressed by BirA. {ECO:0000269|PubMed:6456358}. |
| Disruption phenotype: | |
Loss of biotin synthesis. {ECO:0000269|PubMed:32042199}. |
| Miscellaneous: | |
Catalysis proceeds by a classical ping-pong bi-bi reaction mechanism. |
| Similarity: | |
Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. BioA subfamily. {ECO:0000305}. |
Annotations taken from UniProtKB at the EBI.