lipoate-protein ligase A [Chlamydia psittaci 02DC15]
lipoate--protein ligase family protein( domain architecture ID 46944)
lipoate--protein ligase family protein, similar to Staphylococcus aureus lipoate--protein ligase 1 and Saccharomyces cerevisiae octanoyltransferase
List of domain hits
Name | Accession | Description | Interval | E-value | ||||
BPL_LplA_LipB super family | cl14057 | biotin-lipoate ligase family; This family includes biotin protein ligase (BPL), ... |
1-217 | 2.22e-30 | ||||
biotin-lipoate ligase family; This family includes biotin protein ligase (BPL), lipoate-protein ligase A (LplA) and octanoyl-[acyl carrier protein]-protein acyltransferase (LipB). Biotin is covalently attached at the active site of certain enzymes that transfer carbon dioxide from bicarbonate to organic acids to form cellular metabolites. Biotin protein ligase (BPL) is the enzyme responsible for attaching biotin to a specific lysine at the active site of biotin enzymes. Biotin attachment is a two step reaction that results in the formation of an amide linkage between the carboxyl group of biotin and the epsilon-amino group of the modified lysine. Lipoate-protein ligase A (LplA) catalyses the formation of an amide linkage between lipoic acid and a specific lysine residue in lipoate dependent enzymes. The actual alignment was detected with superfamily member cd16443: Pssm-ID: 449326 Cd Length: 209 Bit Score: 111.19 E-value: 2.22e-30
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Name | Accession | Description | Interval | E-value | ||||
LplA | cd16443 | lipoate-protein ligase; Lipoate-protein ligase A (LplA) catalyzes the formation of an amide ... |
1-217 | 2.22e-30 | ||||
lipoate-protein ligase; Lipoate-protein ligase A (LplA) catalyzes the formation of an amide linkage between free lipoic acid and a specific lysine residue of the lipoyl domain in lipoate dependent enzymes, similar to the biotinylation reaction mediated by biotinyl protein ligase (BPL). The two step reaction includes activation of exogenously supplied lipoic acid at the expense of ATP to lipoyl-AMP and then transfer to the epsilon-amino group of a specific lysine residue of the lipoyl domain of the target protein. Pssm-ID: 319742 Cd Length: 209 Bit Score: 111.19 E-value: 2.22e-30
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BPL_LplA_LipB | pfam03099 | Biotin/lipoate A/B protein ligase family; This family includes biotin protein ligase, ... |
38-164 | 3.68e-16 | ||||
Biotin/lipoate A/B protein ligase family; This family includes biotin protein ligase, lipoate-protein ligase A and B. Biotin is covalently attached at the active site of certain enzymes that transfer carbon dioxide from bicarbonate to organic acids to form cellular metabolites. Biotin protein ligase (BPL) is the enzyme responsible for attaching biotin to a specific lysine at the active site of biotin enzymes. Each organizm probably has only one BPL. Biotin attachment is a two step reaction that results in the formation of an amide linkage between the carboxyl group of biotin and the epsilon-amino group of the modified lysine. Lipoate-protein ligase A (LPLA) catalyzes the formation of an amide linkage between lipoic acid and a specific lysine residue in lipoate dependent enzymes. The unusual biosynthesis pathway of lipoic acid is mechanistically intertwined with attachment of the cofactor. Pssm-ID: 427135 Cd Length: 132 Bit Score: 72.09 E-value: 3.68e-16
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LplA | COG0095 | Lipoate-protein ligase A [Coenzyme transport and metabolism]; Lipoate-protein ligase A is part ... |
1-159 | 1.38e-15 | ||||
Lipoate-protein ligase A [Coenzyme transport and metabolism]; Lipoate-protein ligase A is part of the Pathway/BioSystem: Lipoate biosynthesis Pssm-ID: 439865 Cd Length: 246 Bit Score: 72.96 E-value: 1.38e-15
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lipoyltrans | TIGR00545 | lipoyltransferase and lipoate-protein ligase; One member of this group of proteins is bovine ... |
1-161 | 9.95e-04 | ||||
lipoyltransferase and lipoate-protein ligase; One member of this group of proteins is bovine lipoyltransferase, which transfers the lipoyl group from lipoyl-AMP to the specific Lys of lipoate-dependent enzymes. However, it does not first activate lipoic acid with ATP to create lipoyl-AMP and pyrophosphate. Another member of this group, lipoate-protein ligase A from E. coli, catalyzes both the activation and the transfer of lipoate. Homology between the two is full-length, except for the bovine mitochondrial targeting signal, but is strongest toward the N-terminus. [Protein fate, Protein modification and repair] Pssm-ID: 161920 [Multi-domain] Cd Length: 324 Bit Score: 39.42 E-value: 9.95e-04
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Name | Accession | Description | Interval | E-value | ||||
LplA | cd16443 | lipoate-protein ligase; Lipoate-protein ligase A (LplA) catalyzes the formation of an amide ... |
1-217 | 2.22e-30 | ||||
lipoate-protein ligase; Lipoate-protein ligase A (LplA) catalyzes the formation of an amide linkage between free lipoic acid and a specific lysine residue of the lipoyl domain in lipoate dependent enzymes, similar to the biotinylation reaction mediated by biotinyl protein ligase (BPL). The two step reaction includes activation of exogenously supplied lipoic acid at the expense of ATP to lipoyl-AMP and then transfer to the epsilon-amino group of a specific lysine residue of the lipoyl domain of the target protein. Pssm-ID: 319742 Cd Length: 209 Bit Score: 111.19 E-value: 2.22e-30
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BPL_LplA_LipB | pfam03099 | Biotin/lipoate A/B protein ligase family; This family includes biotin protein ligase, ... |
38-164 | 3.68e-16 | ||||
Biotin/lipoate A/B protein ligase family; This family includes biotin protein ligase, lipoate-protein ligase A and B. Biotin is covalently attached at the active site of certain enzymes that transfer carbon dioxide from bicarbonate to organic acids to form cellular metabolites. Biotin protein ligase (BPL) is the enzyme responsible for attaching biotin to a specific lysine at the active site of biotin enzymes. Each organizm probably has only one BPL. Biotin attachment is a two step reaction that results in the formation of an amide linkage between the carboxyl group of biotin and the epsilon-amino group of the modified lysine. Lipoate-protein ligase A (LPLA) catalyzes the formation of an amide linkage between lipoic acid and a specific lysine residue in lipoate dependent enzymes. The unusual biosynthesis pathway of lipoic acid is mechanistically intertwined with attachment of the cofactor. Pssm-ID: 427135 Cd Length: 132 Bit Score: 72.09 E-value: 3.68e-16
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LplA | COG0095 | Lipoate-protein ligase A [Coenzyme transport and metabolism]; Lipoate-protein ligase A is part ... |
1-159 | 1.38e-15 | ||||
Lipoate-protein ligase A [Coenzyme transport and metabolism]; Lipoate-protein ligase A is part of the Pathway/BioSystem: Lipoate biosynthesis Pssm-ID: 439865 Cd Length: 246 Bit Score: 72.96 E-value: 1.38e-15
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lipoyltrans | TIGR00545 | lipoyltransferase and lipoate-protein ligase; One member of this group of proteins is bovine ... |
1-161 | 9.95e-04 | ||||
lipoyltransferase and lipoate-protein ligase; One member of this group of proteins is bovine lipoyltransferase, which transfers the lipoyl group from lipoyl-AMP to the specific Lys of lipoate-dependent enzymes. However, it does not first activate lipoic acid with ATP to create lipoyl-AMP and pyrophosphate. Another member of this group, lipoate-protein ligase A from E. coli, catalyzes both the activation and the transfer of lipoate. Homology between the two is full-length, except for the bovine mitochondrial targeting signal, but is strongest toward the N-terminus. [Protein fate, Protein modification and repair] Pssm-ID: 161920 [Multi-domain] Cd Length: 324 Bit Score: 39.42 E-value: 9.95e-04
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Blast search parameters | ||||
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