| Definition | Bacillus thuringiensis str. Al Hakam chromosome, complete genome. |
|---|---|
| Accession | NC_008600 |
| Length | 5,257,091 |
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The map label for this gene is lplA [H]
Identifier: 118479396
GI number: 118479396
Start: 4026060
End: 4026908
Strand: Reverse
Name: lplA [H]
Synonym: BALH_3813
Alternate gene names: 118479396
Gene position: 4026908-4026060 (Counterclockwise)
Preceding gene: 118479401
Following gene: 118479393
Centisome position: 76.6
GC content: 35.1
Gene sequence:
>849_bases ATGAGGTGCAGGATGGGAAAAGAAAAATGGTGTTATATTAACTCTGGTCAATGTTCACCGGCATTTAATATGGCGTTAGA TGAATGTTTATTAAATTGGCAAAGTGAAAAGAAAATGCCACCAACTATTCGTTTTTACGAATGGGAAGTACCAACATTAA CAGTCGGATATTTCCAGCGTGTTGAAAAAGATATTAATATGGATGTAGTTAACGAAAAGAAATATGGATTCGTTCGTCGT CAAACAGGCGGCAGGGGTGTATTACATGATAAAGAATTAACGTATAGTGTTATTGTGTCTGAAGATCATCCGAATATGCC AAAAACAGTTACAGAAGCGTATCGTGTTATTTCGCAAGGTTTACTAGATGGTTTTAAAGCATTAGGGTTAGAAGCGTATT ATGCAGTTCCAAAAACAGAAGCAGATCGTGAAAATTTAAAAAATCCACGCTCAGGCGTATGTTTTGATGCACCGTCTTGG TATGAAATTGTAGTAGAAGGAAGAAAAATCGCAGGTAGTGCGCAAACACGTCAAAAAGGTGTTATTTTGCAGCATGGATC GATTCCGTTAGAAATAGATTTAGATGAGTTATATGATCTGTTTTTATTCCCGAATGAGCGTGTAAAAGAACGTATGAAGA GTATGTTCTCTTCTAAAGCGGTAGCAATTAATGAATTAACAGACCGTACGTTTACAATCGAACAGTTAATTAAAGCGTTT GAGGTTGGGTTTGAAAAAGGATTAGATGTAGAGCTTGTTCCATATGAATTAACAGAAGAACAATTACATGAAGTGCAAAC ATTAGCAAAAGAAAAGTATGAAAGTAAAGAATGGAATTATAAAAAATAA
Upstream 100 bases:
>100_bases TTATGCAACAGATTCATTTGTATATAAGAAGAAATTTCGTATTCTTTCACAAATTTTGTCGAATTTGGTAGACTAGAGAA TGTGAAAAATAATTGGTTAT
Downstream 100 bases:
>100_bases GAGGTGGCAATTGCCGCCTCTTATTTTTTTATAGTAAATTAAGTACTTTTTCTACTTTGATTCCTTTATCTTGTAAAGAA CGAAGGCGATTGACAACGTC
Product: lipoate-protein ligase A
Products: lipoyl-AMP; pyrophosphate; N6-lipoyl-lysine [C]
Alternate protein names: NA
Number of amino acids: Translated: 282; Mature: 282
Protein sequence:
>282_residues MRCRMGKEKWCYINSGQCSPAFNMALDECLLNWQSEKKMPPTIRFYEWEVPTLTVGYFQRVEKDINMDVVNEKKYGFVRR QTGGRGVLHDKELTYSVIVSEDHPNMPKTVTEAYRVISQGLLDGFKALGLEAYYAVPKTEADRENLKNPRSGVCFDAPSW YEIVVEGRKIAGSAQTRQKGVILQHGSIPLEIDLDELYDLFLFPNERVKERMKSMFSSKAVAINELTDRTFTIEQLIKAF EVGFEKGLDVELVPYELTEEQLHEVQTLAKEKYESKEWNYKK
Sequences:
>Translated_282_residues MRCRMGKEKWCYINSGQCSPAFNMALDECLLNWQSEKKMPPTIRFYEWEVPTLTVGYFQRVEKDINMDVVNEKKYGFVRR QTGGRGVLHDKELTYSVIVSEDHPNMPKTVTEAYRVISQGLLDGFKALGLEAYYAVPKTEADRENLKNPRSGVCFDAPSW YEIVVEGRKIAGSAQTRQKGVILQHGSIPLEIDLDELYDLFLFPNERVKERMKSMFSSKAVAINELTDRTFTIEQLIKAF EVGFEKGLDVELVPYELTEEQLHEVQTLAKEKYESKEWNYKK >Mature_282_residues MRCRMGKEKWCYINSGQCSPAFNMALDECLLNWQSEKKMPPTIRFYEWEVPTLTVGYFQRVEKDINMDVVNEKKYGFVRR QTGGRGVLHDKELTYSVIVSEDHPNMPKTVTEAYRVISQGLLDGFKALGLEAYYAVPKTEADRENLKNPRSGVCFDAPSW YEIVVEGRKIAGSAQTRQKGVILQHGSIPLEIDLDELYDLFLFPNERVKERMKSMFSSKAVAINELTDRTFTIEQLIKAF EVGFEKGLDVELVPYELTEEQLHEVQTLAKEKYESKEWNYKK
Specific function: Catalyzes Both The ATP-Dependent Activation Of Exogenously Supplied Lipoate To Lipoyl-Amp And The Transfer Of The Activated Lipoyl On The Lipoate-Dependent Enzymes. Creates An Amide Linkage That Joins The Free Carboxyl Group Of Lipoic Acid To The Epsilon-
COG id: COG0095
COG function: function code H; Lipoate-protein ligase A
Gene ontology:
Cell location: Cytoplasm [C]
Metaboloic importance: Unknown [C]
Operon status: Not Known
Operon components: None
Similarity: NA
Homologues:
None
Paralogues:
None
Copy number: NA
Swissprot (AC and ID): NA
Other databases:
- InterPro: IPR004143 [H]
Pfam domain/function: PF03099 BPL_LipA_LipB [H]
EC number: 6.3.2.- [C]
Molecular weight: Translated: 32666; Mature: 32666
Theoretical pI: Translated: 5.54; Mature: 5.54
Prosite motif: NA
Important sites: NA
Signals:
None
Transmembrane regions:
None
Cys/Met content:
1.8 %Cys (Translated Protein) 2.8 %Met (Translated Protein) 4.6 %Cys+Met (Translated Protein) 1.8 %Cys (Mature Protein) 2.8 %Met (Mature Protein) 4.6 %Cys+Met (Mature Protein)
Secondary structure:
>Translated Secondary Structure MRCRMGKEKWCYINSGQCSPAFNMALDECLLNWQSEKKMPPTIRFYEWEVPTLTVGYFQR CCCCCCCCCEEEEECCCCCHHHHHHHHHHHHCCCCCCCCCCEEEEEEECCCEEEHHHHHH VEKDINMDVVNEKKYGFVRRQTGGRGVLHDKELTYSVIVSEDHPNMPKTVTEAYRVISQG HHHCCCCEEECCCCCCEEEECCCCCCCEECCCCEEEEEEECCCCCCCHHHHHHHHHHHHH LLDGFKALGLEAYYAVPKTEADRENLKNPRSGVCFDAPSWYEIVVEGRKIAGSAQTRQKG HHHHHHHHCCCEEEECCCCCCCHHHCCCCCCCCEECCCCCEEEEEECCHHCCCCHHHHCC VILQHGSIPLEIDLDELYDLFLFPNERVKERMKSMFSSKAVAINELTDRTFTIEQLIKAF EEEECCCEEEEEEHHHHHHHHCCCCHHHHHHHHHHHHCCCEEEHHHCCCEEHHHHHHHHH EVGFEKGLDVELVPYELTEEQLHEVQTLAKEKYESKEWNYKK HHHHHCCCCEEEECHHCCHHHHHHHHHHHHHHHCCCCCCCCC >Mature Secondary Structure MRCRMGKEKWCYINSGQCSPAFNMALDECLLNWQSEKKMPPTIRFYEWEVPTLTVGYFQR CCCCCCCCCEEEEECCCCCHHHHHHHHHHHHCCCCCCCCCCEEEEEEECCCEEEHHHHHH VEKDINMDVVNEKKYGFVRRQTGGRGVLHDKELTYSVIVSEDHPNMPKTVTEAYRVISQG HHHCCCCEEECCCCCCEEEECCCCCCCEECCCCEEEEEEECCCCCCCHHHHHHHHHHHHH LLDGFKALGLEAYYAVPKTEADRENLKNPRSGVCFDAPSWYEIVVEGRKIAGSAQTRQKG HHHHHHHHCCCEEEECCCCCCCHHHCCCCCCCCEECCCCCEEEEEECCHHCCCCHHHHCC VILQHGSIPLEIDLDELYDLFLFPNERVKERMKSMFSSKAVAINELTDRTFTIEQLIKAF EEEECCCEEEEEEHHHHHHHHCCCCHHHHHHHHHHHHCCCEEEHHHCCCEEHHHHHHHHH EVGFEKGLDVELVPYELTEEQLHEVQTLAKEKYESKEWNYKK HHHHHCCCCEEEECHHCCHHHHHHHHHHHHHHHCCCCCCCCC
PDB accession: NA
Resolution: NA
Structure class: Alpha Beta
Cofactors: NA
Metal ions: NA
Kcat value (1/min): NA
Specific activity: NA
Km value (mM): NA
Substrates: lipoic acid; ATP [C]
Specific reaction: Catalyzes first the reaction of lipoic acid and ATP to form lipoyl-AMP and pyrophosphate, then the formation N6-lipoyl-lysine from a specific lysine residue in lipoate-dependent enzymes [C]
General reaction: Ligases; Forming Carbon-Nitrogen Bonds; Other Carbon-Nitrogen Ligases [C]
Inhibitor: NA
Structure determination priority: 10.0
TargetDB status: NA
Availability: NA
References: 8969508; 9384377 [H]