Definition Bacillus licheniformis ATCC 14580, complete genome.
Accession NC_006322
Length 4,222,645

Click here to switch to the map view.

The map label for this gene is yqhM [H]

Identifier: 52786362

GI number: 52786362

Start: 2538228

End: 2539064

Strand: Reverse

Name: yqhM [H]

Synonym: BLi02624

Alternate gene names: 52786362

Gene position: 2539064-2538228 (Counterclockwise)

Preceding gene: 52786364

Following gene: 52786361

Centisome position: 60.13

GC content: 47.91

Gene sequence:

>837_bases
ATGGAAAAAGAAACATGGCGTTTTATCGATTCGGGACGACGGGATCCCGCTTTTAATATGGCGCTCGACGAGGCGCTCCT
TTTTTGGCACAGCGAAAATAAGATTCCGCCGACCATCCGCTTTTACGGCTGGAATCCGCCAACGCTTTCAGTCGGCTATT
TCCAAAATATCGAAAAGGAAATCAATCTGGATGCCGTCAAAAAACACGGTTTGGGCTTTGTGAGAAGGCCGACCGGAGGA
AGAGGCGTGCTTCATGACCAAGAGCTGACCTACAGCGTCATTGTGTCTGAAGAACACCCGGAAATGCCGAAGACGGTGAC
GGAAGCGTACCGCGTCATCTCTGAAGGTATTCTTGAAGGCTTCAGAGAGCTGGAGCTTGATGCGTATTTCGCCATACCGA
GAACGGAAAAAGAGAAACAGAGTCTGAAAAACCCGAGATCTTCCGTCTGCTTTGACGCCCCGTCGTGGTACGAGCTCGTT
GTCGAAGGCAGAAAGGTCGCAGGAAGCGCCCAGACAAGGCAGAAAGGAGTCATTCTTCAGCACGGTTCGATCCTTCTTGA
TCTGGATGAGGACAAGCTCTTTGATTTGTTTATTTACAAAAATGACCGCCTCAGAGAGCGCATGCAGAGAAACTTCAAAC
AAAAAGCGGTCGCCATCAATGAGCTGACGAAAGAAAAAGTCACGATTGAAGAAGCGAGCGAAGCTTTTAAAAAAGGGTTT
GAAAAAGGGCTTAACATTCATTTGGAGCCTTATGAACTGACGGAAGAGGAAACGGAATTTGTCGAAGATCTCGCCAGGAC
GAAGTATGCGACAGATGAATGGAATTATAGAAGGTAA

Upstream 100 bases:

>100_bases
GTAAAGCCTCAGAAATCTGTCATCTGATTCGCCGAATTTATTTTCAATTTTAAGAGGGAATGGTAGACTTATTTTATACC
AAAGAAAAAGAGGGTAGGTT

Downstream 100 bases:

>100_bases
TCGGGTGAAAACGTTATCCTGTTGCTTGTTTTTTGCATGCACATAGTGTAAACTTGTTATGATTTGAATAGGTGTAATTT
GGAGGGATTCGATGACAACA

Product: YqhM

Products: lipoyl-AMP; pyrophosphate; N6-lipoyl-lysine [C]

Alternate protein names: NA

Number of amino acids: Translated: 278; Mature: 278

Protein sequence:

>278_residues
MEKETWRFIDSGRRDPAFNMALDEALLFWHSENKIPPTIRFYGWNPPTLSVGYFQNIEKEINLDAVKKHGLGFVRRPTGG
RGVLHDQELTYSVIVSEEHPEMPKTVTEAYRVISEGILEGFRELELDAYFAIPRTEKEKQSLKNPRSSVCFDAPSWYELV
VEGRKVAGSAQTRQKGVILQHGSILLDLDEDKLFDLFIYKNDRLRERMQRNFKQKAVAINELTKEKVTIEEASEAFKKGF
EKGLNIHLEPYELTEEETEFVEDLARTKYATDEWNYRR

Sequences:

>Translated_278_residues
MEKETWRFIDSGRRDPAFNMALDEALLFWHSENKIPPTIRFYGWNPPTLSVGYFQNIEKEINLDAVKKHGLGFVRRPTGG
RGVLHDQELTYSVIVSEEHPEMPKTVTEAYRVISEGILEGFRELELDAYFAIPRTEKEKQSLKNPRSSVCFDAPSWYELV
VEGRKVAGSAQTRQKGVILQHGSILLDLDEDKLFDLFIYKNDRLRERMQRNFKQKAVAINELTKEKVTIEEASEAFKKGF
EKGLNIHLEPYELTEEETEFVEDLARTKYATDEWNYRR
>Mature_278_residues
MEKETWRFIDSGRRDPAFNMALDEALLFWHSENKIPPTIRFYGWNPPTLSVGYFQNIEKEINLDAVKKHGLGFVRRPTGG
RGVLHDQELTYSVIVSEEHPEMPKTVTEAYRVISEGILEGFRELELDAYFAIPRTEKEKQSLKNPRSSVCFDAPSWYELV
VEGRKVAGSAQTRQKGVILQHGSILLDLDEDKLFDLFIYKNDRLRERMQRNFKQKAVAINELTKEKVTIEEASEAFKKGF
EKGLNIHLEPYELTEEETEFVEDLARTKYATDEWNYRR

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: 32442; Mature: 32442

Theoretical pI: Translated: 5.34; Mature: 5.34

Prosite motif: NA

Important sites: NA

Signals:

None

Transmembrane regions:

None

Cys/Met content:

0.4 %Cys     (Translated Protein)
1.4 %Met     (Translated Protein)
1.8 %Cys+Met (Translated Protein)
0.4 %Cys     (Mature Protein)
1.4 %Met     (Mature Protein)
1.8 %Cys+Met (Mature Protein)

Secondary structure:

>Translated Secondary Structure
MEKETWRFIDSGRRDPAFNMALDEALLFWHSENKIPPTIRFYGWNPPTLSVGYFQNIEKE
CCCCHHHHHHCCCCCCCHHHHHHHHHEEEECCCCCCCEEEEECCCCCEEEHHHHHHHHHH
INLDAVKKHGLGFVRRPTGGRGVLHDQELTYSVIVSEEHPEMPKTVTEAYRVISEGILEG
CCHHHHHHCCCCEEECCCCCCCCEECCCCEEEEEEECCCCCCCHHHHHHHHHHHHHHHHH
FRELELDAYFAIPRTEKEKQSLKNPRSSVCFDAPSWYELVVEGRKVAGSAQTRQKGVILQ
HHHHCCEEEEECCCCCHHHHHHCCCCCCEEECCCCHHHHHCCCHHHCCCCHHHHCCEEEE
HGSILLDLDEDKLFDLFIYKNDRLRERMQRNFKQKAVAINELTKEKVTIEEASEAFKKGF
CCCEEEEECCCCEEEEEEECCHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHH
EKGLNIHLEPYELTEEETEFVEDLARTKYATDEWNYRR
HCCCCEEECCHHCCHHHHHHHHHHHHHCCCCCCCCCCC
>Mature Secondary Structure
MEKETWRFIDSGRRDPAFNMALDEALLFWHSENKIPPTIRFYGWNPPTLSVGYFQNIEKE
CCCCHHHHHHCCCCCCCHHHHHHHHHEEEECCCCCCCEEEEECCCCCEEEHHHHHHHHHH
INLDAVKKHGLGFVRRPTGGRGVLHDQELTYSVIVSEEHPEMPKTVTEAYRVISEGILEG
CCHHHHHHCCCCEEECCCCCCCCEECCCCEEEEEEECCCCCCCHHHHHHHHHHHHHHHHH
FRELELDAYFAIPRTEKEKQSLKNPRSSVCFDAPSWYELVVEGRKVAGSAQTRQKGVILQ
HHHHCCEEEEECCCCCHHHHHHCCCCCCEEECCCCHHHHHCCCHHHCCCCHHHHCCEEEE
HGSILLDLDEDKLFDLFIYKNDRLRERMQRNFKQKAVAINELTKEKVTIEEASEAFKKGF
CCCEEEEECCCCEEEEEEECCHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHH
EKGLNIHLEPYELTEEETEFVEDLARTKYATDEWNYRR
HCCCCEEECCHHCCHHHHHHHHHHHHHCCCCCCCCCCC

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]