Click here to switch to the map view.

The map label for this gene is lipB

Identifier: 16120181

GI number: 16120181

Start: 197890

End: 198399

Strand: Direct

Name: lipB

Synonym: VNG6256G

Alternate gene names: 16120181

Gene position: 197890-198399 (Clockwise)

Preceding gene: 16120180

Following gene: 16120183

Centisome position: 54.15

GC content: 66.08

Gene sequence:

>510_bases
ATGTACGTCGAACCCGGTGCGGTGCTGACGTACTCGCTGTACCTCCCGCCCGAGGACGTTCCCGACGACGTTGCCGACAG
CTACGTGTACCTCGACCAGTGGGCCATCGACGCCCTGCAGGCTGTCGGCATCGACGCCAGCTACGAGCCGCTGAACGACA
TTGTGCACGCCGACGGCAAGCTCGGCGGGGCGGCGCAGCTGCGGACTGACGGGGCGGTGTTGCACCACACGACGATGAGC
TACGATCTGGACATCGAGCGGATGCTTCGCGTGCTCCGGATCGGGGAAGAGAAACTCTCGGATAAGGCCGTGGCGTCCGC
CGAAAAGCGGGTTGCAGTGATGACTGATCACACTGACGCGTCGCGTGCCACGATCGTCGATGCACTCGTTGCGGCGATCG
GGGACACGTTCGAAACGCGGCGGGGATCGCTGTCGGCGGCGACTCGGGAGGCGGCGCGCACGCTCGCAGCCGAACAGTTC
GACACGGCGGCGTGGACGCGGAAGCTGTAG

Upstream 100 bases:

>100_bases
CCCGATCGGGCGGTTCCAGTCCTACGAGGACGAGGTCGCCACCGACTACGTGGAGCGCCACGACATCGACGTGGTGCGGC
GCGCGACCGGTGGCGGGGCG

Downstream 100 bases:

>100_bases
GGTGCCCGGAATCGCTACGTGAGCACGCGCTTGACGTCGAGGCCGGTCGCGCGCCGCACGACCGCCTGCACGGGATCGAC
GGCGTTGCGGAGGTTGTGTG

Product: lipoate protein ligase

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

Alternate protein names: Biotin/Lipoate A/B Protein Ligase; Lipoate-Protein Ligase A; Lipoate Protein Ligase; Lipoate-Protein Ligase A N-Terminal Section; Biotin/Lipoate A/B Protein Ligase Family Protein; LplA-Like Lipoate-Protein Ligase A ; Lipoate-Protein Ligase A C-Terminal Fragment; Lipoate-Protein Ligase A

Number of amino acids: Translated: 169; Mature: 169

Protein sequence:

>169_residues
MYVEPGAVLTYSLYLPPEDVPDDVADSYVYLDQWAIDALQAVGIDASYEPLNDIVHADGKLGGAAQLRTDGAVLHHTTMS
YDLDIERMLRVLRIGEEKLSDKAVASAEKRVAVMTDHTDASRATIVDALVAAIGDTFETRRGSLSAATREAARTLAAEQF
DTAAWTRKL

Sequences:

>Translated_169_residues
MYVEPGAVLTYSLYLPPEDVPDDVADSYVYLDQWAIDALQAVGIDASYEPLNDIVHADGKLGGAAQLRTDGAVLHHTTMS
YDLDIERMLRVLRIGEEKLSDKAVASAEKRVAVMTDHTDASRATIVDALVAAIGDTFETRRGSLSAATREAARTLAAEQF
DTAAWTRKL
>Mature_169_residues
MYVEPGAVLTYSLYLPPEDVPDDVADSYVYLDQWAIDALQAVGIDASYEPLNDIVHADGKLGGAAQLRTDGAVLHHTTMS
YDLDIERMLRVLRIGEEKLSDKAVASAEKRVAVMTDHTDASRATIVDALVAAIGDTFETRRGSLSAATREAARTLAAEQF
DTAAWTRKL

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:

NA

Pfam domain/function: NA

EC number: 6.3.2.- [C]

Molecular weight: Translated: 18369; Mature: 18369

Theoretical pI: Translated: 4.38; Mature: 4.38

Prosite motif: NA

Important sites: NA

Signals:

None

Transmembrane regions:

None

Cys/Met content:

0.0 %Cys     (Translated Protein)
2.4 %Met     (Translated Protein)
2.4 %Cys+Met (Translated Protein)
0.0 %Cys     (Mature Protein)
2.4 %Met     (Mature Protein)
2.4 %Cys+Met (Mature Protein)

Secondary structure:

>Translated Secondary Structure
MYVEPGAVLTYSLYLPPEDVPDDVADSYVYLDQWAIDALQAVGIDASYEPLNDIVHADGK
CCCCCCCEEEEEEECCCCCCCHHHHHCEEHHHHHHHHHHHHHCCCCCCCHHHHHHHCCCC
LGGAAQLRTDGAVLHHTTMSYDLDIERMLRVLRIGEEKLSDKAVASAEKRVAVMTDHTDA
CCCCEEECCCCEEEEEECCCCCCCHHHHHHHHHHCHHHHHHHHHHHHHHEEEEEECCCCC
SRATIVDALVAAIGDTFETRRGSLSAATREAARTLAAEQFDTAAWTRKL
HHHHHHHHHHHHHCCHHHHCCCCHHHHHHHHHHHHHHHHHHHHHHHCCC
>Mature Secondary Structure
MYVEPGAVLTYSLYLPPEDVPDDVADSYVYLDQWAIDALQAVGIDASYEPLNDIVHADGK
CCCCCCCEEEEEEECCCCCCCHHHHHCEEHHHHHHHHHHHHHCCCCCCCHHHHHHHCCCC
LGGAAQLRTDGAVLHHTTMSYDLDIERMLRVLRIGEEKLSDKAVASAEKRVAVMTDHTDA
CCCCEEECCCCEEEEEECCCCCCCHHHHHHHHHHCHHHHHHHHHHHHHHEEEEEECCCCC
SRATIVDALVAAIGDTFETRRGSLSAATREAARTLAAEQFDTAAWTRKL
HHHHHHHHHHHHHCCHHHHCCCCHHHHHHHHHHHHHHHHHHHHHHHCCC

PDB accession: NA

Resolution: NA

Structure class: Unstructured

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: NA