Identification |
Name: |
Lipoyl synthase |
Synonyms: |
- Lip-syn
- LS
- Lipoate synthase
- Lipoic acid synthase
- Sulfur insertion protein lipA
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Gene Name: |
lipA |
Enzyme Class: |
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Biological Properties |
General Function: |
Involved in catalytic activity |
Specific Function: |
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives. Free octanoate is not a substrate for lipA |
Cellular Location: |
Cytoplasm |
KEGG Pathways: |
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KEGG Reactions: |
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Protein N6-(octanoyl)lysine | + | 2 Sulfur donor | + | 2 | + | Protein N6-(octanoyl)lysine | ↔ | Protein N6-(lipoyl)lysine | + | 2 | + | 2 | + | Protein N6-(lipoyl)lysine |
| | |
Octanoyl-[acp] | + | 2 Sulfur donor | + | 2 | ↔ | Lipoyl-[acp] | + | 2 | + | 2 |
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SMPDB Reactions: |
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PseudoCyc/BioCyc Reactions: |
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[4Fe-4S] iron-sulfur cluster | + | 2 | + | | + | | + | octanoate (protein bound) | → | [2Fe-2S] iron-sulfur cluster | + | 2 | + | 2 | + | lipoate (protein bound) | + | 2 | + | |
| | |
Protein N6-(octanoyl)lysine | + | 2 Sulfur donor | + | 2 | + | Protein N6-(octanoyl)lysine | ↔ | Protein N6-(lipoyl)lysine | + | 2 | + | 2 | + | Protein N6-(lipoyl)lysine |
| | |
Octanoyl-[acp] | + | 2 Sulfur donor | + | 2 | ↔ | Lipoyl-[acp] | + | 2 | + | 2 |
| | |
Octanoyl-[acyl-carrier protein] | + | 2 a sulfur donor | + | 2 S-adenosyl-L-methionine | → | Lipoyl-ACP | + | 2 | + | |
| | |
Protein N6-(octanoyl)lysine | + | 2 a sulfur donor | + | 2 S-adenosyl-L-methionine | → | Protein N6-(lipoyl)lysine | + | 2 | + | 2 |
| |
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Complex Reactions: |
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[4Fe-4S] iron-sulfur cluster | + | 2 | + | | + | | + | octanoate (protein bound) | → | [2Fe-2S] iron-sulfur cluster | + | 2 | + | 2 | + | lipoate (protein bound) | + | 2 | + | |
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Transports: |
Not Available |
Metabolites: |
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GO Classification: |
Function |
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4 iron, 4 sulfur cluster binding | binding | catalytic activity | iron-sulfur cluster binding | lipoate synthase activity | metal cluster binding | sulfurtransferase activity | transferase activity | transferase activity, transferring sulfur-containing groups | Process |
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cellular metabolic process | coenzyme metabolic process | cofactor metabolic process | lipoate biosynthetic process | lipoic acid biosynthetic process | lipoic acid metabolic process | metabolic process |
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Gene Properties |
Locus tag: |
PA2862 |
Strand: |
+ |
Entrez Gene ID: |
882662 |
Accession: |
NP_251552.1 |
GI: |
15598058 |
Sequence start: |
3214282 |
Sequence End: |
3215217 |
Sequence Length: |
935 |
Gene Sequence: |
>PA2862
ATGAAGAAGAAGTCTCTGCTCCCCCTCGGCCTGGCCATCGGTCTCGCCTCTCTCGCTGCCAGCCCTCTGATCCAGGCCAGCACCTACACCCAGACCAAATACCCCATCGTGCTGGCCCACGGCATGCTCGGCTTCGACAACATCCTCGGGGTCGACTACTGGTTCGGCATTCCCAGCGCCTTGCGCCGTGACGGTGCCCAGGTCTACGTCACCGAAGTCAGCCAGTTGGACACCTCGGAAGTCCGCGGCGAGCAGTTGCTGCAACAGGTGGAGGAAATCGTCGCCCTCAGCGGCCAGCCCAAGGTCAACCTGATCGGCCACAGCCACGGCGGGCCGACCATCCGCTACGTCGCCGCCGTACGTCCCGACCTGATCGCTTCCGCCACCAGCGTCGGCGCCCCGCACAAGGGTTCGGACACCGCCGACTTCCTGCGCCAGATCCCACCGGGTTCGGCCGGCGAGGCAGTCCTCTCCGGGCTGGTCAACAGCCTCGGCGCGCTGATCAGCTTCCTTTCCAGCGGCAGCACCGGTACGCAGAATTCACTGGGCTCGCTGGAGTCGCTGAACAGCGAGGGTGCCGCGCGCTTCAACGCCAAGTACCCGCAGGGCATCCCCACCTCGGCCTGCGGCGAAGGCGCCTACAAGGTCAACGGCGTGAGCTATTACTCCTGGAGCGGTTCCTCGCCGCTGACCAACTTCCTCGATCCGAGCGACGCCTTCCTCGGCGCCTCGTCGCTGACCTTCAAGAACGGCACCGCCAACGACGGCCTGGTCGGCACCTGCAGTTCGCACCTGGGCATGGTGATCCGCGACAACTACCGGATGAACCACCTGGACGAGGTGAACCAGGTCTTCGGCCTCACCAGCCTGTTCGAGACCAGCCCGGTCAGCGTCTACCGCCAGCACGCCAACCGCCTGAAGAACGCCAGCCTGTAG |
Protein Properties |
Protein Residues: |
311 |
Protein Molecular Weight: |
32.7 kDa |
Protein Theoretical pI: |
6.88 |
Hydropathicity (GRAVY score): |
-0.008 |
Charge at pH 7 (predicted): |
-0.39 |
Protein Sequence: |
>PA2862
MKKKSLLPLGLAIGLASLAASPLIQASTYTQTKYPIVLAHGMLGFDNILGVDYWFGIPSALRRDGAQVYVTEVSQLDTSEVRGEQLLQQVEEIVALSGQPKVNLIGHSHGGPTIRYVAAVRPDLIASATSVGAPHKGSDTADFLRQIPPGSAGEAVLSGLVNSLGALISFLSSGSTGTQNSLGSLESLNSEGAARFNAKYPQGIPTSACGEGAYKVNGVSYYSWSGSSPLTNFLDPSDAFLGASSLTFKNGTANDGLVGTCSSHLGMVIRDNYRMNHLDEVNQVFGLTSLFETSPVSVYRQHANRLKNASL |
References |
External Links: |
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General Reference: |
PaperBLAST - Find papers about PA2862 and its homologs
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