Definition Pyrococcus furiosus DSM 3638, complete genome.
Accession NC_003413
Length 1,908,256

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The map label for this gene is yqhM [H]

Identifier: 18977746

GI number: 18977746

Start: 1289128

End: 1289907

Strand: Reverse

Name: yqhM [H]

Synonym: PF1374

Alternate gene names: 18977746

Gene position: 1289907-1289128 (Counterclockwise)

Preceding gene: 18977749

Following gene: 18977738

Centisome position: 67.6

GC content: 39.23

Gene sequence:

>780_bases
ATGTTAGCGGATTGTAATATGGTGGAGTTTATGAGGTTTATTCCTCTAATAGTTGCTAGACCTGAAGTGCAGATGGCGAT
TGATGAGGCGATTCTAATAGCTAGAAGTGAGGGAAAAGTTCCTGATACTGTAAGATTATATGTTTTCAAGCCGAGTTCAG
TGACTATTGGGAGGTTTCAGAGCGTTAGACACGATGTTAATGTGGAGAAAGCAGAAGAACTTGGAATACCTATAGTGAGG
AGAATTACTGGGGGAGGAAGTGTATTCCATGACGAATATGGGGAGATAACGTATTCAGTTATAATTGACGAGAACTATCA
TCCGAGCCTTAAGAATATCTACGAAAGTTACAGATTTTTGGCTGGCCCCTTGGTTGATGCTCTACAAGATCTTGGAGTTA
AAGCTGAGTTCTCTGGACTGAATGATATTGTAGTTAATGGCAAGAAGATAAGCGGGTCAGCTCAGACGAGAAAAAGGGGA
GTAATTCTTCAGCATGGAACATTTATGTATGCAACAAGACTTGAAGTTTTGGGAAGTGTATTGAAGGTCTCTAAAGAGAA
GCTTAAGGATAAGGGCATTAAAAGCATCTTTGAGAGAGTGACCACATTGGAAAAAGAAGGAATTGAAATGAGCAGAGAAG
AAGCTTATAATCTTTTGAAAAATTCCTTCTTTAGGGCTTTCCCGCTAGAAGAGGGGGAACTTACAAAGTATGAACTTGAA
CTAGCTGAAAAGCTTATAGAAGAGAAATATGGGAGAAAAGAATGGAACTTTCAGAGATAG

Upstream 100 bases:

>100_bases
TTTAAAAATTTAATGTCCTTATATACTTGGCTCGGCGGTGACCACTTTCATCATAAGCTCAGCTAAGACCGATTTCCTCA
TAGCCAAATTTTATTAAGCT

Downstream 100 bases:

>100_bases
ATCATTTAAGGGCTAAGTCAACGTGAATGAAGGCTTGTTCAACTTCAGGGAGTTCTTCAACTTTTCTTTTAACTTCTTCA
CTGATGTCGTGAGCTTTCTT

Product: lipoate-protein ligase a

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

Alternate protein names: NA

Number of amino acids: Translated: 259; Mature: 259

Protein sequence:

>259_residues
MLADCNMVEFMRFIPLIVARPEVQMAIDEAILIARSEGKVPDTVRLYVFKPSSVTIGRFQSVRHDVNVEKAEELGIPIVR
RITGGGSVFHDEYGEITYSVIIDENYHPSLKNIYESYRFLAGPLVDALQDLGVKAEFSGLNDIVVNGKKISGSAQTRKRG
VILQHGTFMYATRLEVLGSVLKVSKEKLKDKGIKSIFERVTTLEKEGIEMSREEAYNLLKNSFFRAFPLEEGELTKYELE
LAEKLIEEKYGRKEWNFQR

Sequences:

>Translated_259_residues
MLADCNMVEFMRFIPLIVARPEVQMAIDEAILIARSEGKVPDTVRLYVFKPSSVTIGRFQSVRHDVNVEKAEELGIPIVR
RITGGGSVFHDEYGEITYSVIIDENYHPSLKNIYESYRFLAGPLVDALQDLGVKAEFSGLNDIVVNGKKISGSAQTRKRG
VILQHGTFMYATRLEVLGSVLKVSKEKLKDKGIKSIFERVTTLEKEGIEMSREEAYNLLKNSFFRAFPLEEGELTKYELE
LAEKLIEEKYGRKEWNFQR
>Mature_259_residues
MLADCNMVEFMRFIPLIVARPEVQMAIDEAILIARSEGKVPDTVRLYVFKPSSVTIGRFQSVRHDVNVEKAEELGIPIVR
RITGGGSVFHDEYGEITYSVIIDENYHPSLKNIYESYRFLAGPLVDALQDLGVKAEFSGLNDIVVNGKKISGSAQTRKRG
VILQHGTFMYATRLEVLGSVLKVSKEKLKDKGIKSIFERVTTLEKEGIEMSREEAYNLLKNSFFRAFPLEEGELTKYELE
LAEKLIEEKYGRKEWNFQR

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:

Organism=Escherichia coli, GI1790846, Length=253, Percent_Identity=31.6205533596838, Blast_Score=96, Evalue=3e-21,

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: 29518; Mature: 29518

Theoretical pI: Translated: 6.54; Mature: 6.54

Prosite motif: NA

Important sites: NA

Signals:

None

Transmembrane regions:

None

Cys/Met content:

0.4 %Cys     (Translated Protein)
2.3 %Met     (Translated Protein)
2.7 %Cys+Met (Translated Protein)
0.4 %Cys     (Mature Protein)
2.3 %Met     (Mature Protein)
2.7 %Cys+Met (Mature Protein)

Secondary structure:

>Translated Secondary Structure
MLADCNMVEFMRFIPLIVARPEVQMAIDEAILIARSEGKVPDTVRLYVFKPSSVTIGRFQ
CCCCCCHHHHHHHHHHHHCCCHHHHHHHHHHEEECCCCCCCCEEEEEEECCCCEEHHHHH
SVRHDVNVEKAEELGIPIVRRITGGGSVFHDEYGEITYSVIIDENYHPSLKNIYESYRFL
HHHHCCCCHHHHHCCCCEEEEECCCCCEEECCCCCEEEEEEEECCCCCHHHHHHHHHHHH
AGPLVDALQDLGVKAEFSGLNDIVVNGKKISGSAQTRKRGVILQHGTFMYATRLEVLGSV
HHHHHHHHHHCCCEEECCCCCEEEECCEEECCCHHHHHCCEEEECCCCHHHHHHHHHHHH
LKVSKEKLKDKGIKSIFERVTTLEKEGIEMSREEAYNLLKNSFFRAFPLEEGELTKYELE
HHHHHHHHHHHHHHHHHHHHHHHHHHCCCCCHHHHHHHHHHHHHHCCCCCCCCCHHHHHH
LAEKLIEEKYGRKEWNFQR
HHHHHHHHHCCCCCCCCCC
>Mature Secondary Structure
MLADCNMVEFMRFIPLIVARPEVQMAIDEAILIARSEGKVPDTVRLYVFKPSSVTIGRFQ
CCCCCCHHHHHHHHHHHHCCCHHHHHHHHHHEEECCCCCCCCEEEEEEECCCCEEHHHHH
SVRHDVNVEKAEELGIPIVRRITGGGSVFHDEYGEITYSVIIDENYHPSLKNIYESYRFL
HHHHCCCCHHHHHCCCCEEEEECCCCCEEECCCCCEEEEEEEECCCCCHHHHHHHHHHHH
AGPLVDALQDLGVKAEFSGLNDIVVNGKKISGSAQTRKRGVILQHGTFMYATRLEVLGSV
HHHHHHHHHHCCCEEECCCCCEEEECCEEECCCHHHHHCCEEEECCCCHHHHHHHHHHHH
LKVSKEKLKDKGIKSIFERVTTLEKEGIEMSREEAYNLLKNSFFRAFPLEEGELTKYELE
HHHHHHHHHHHHHHHHHHHHHHHHHHCCCCCHHHHHHHHHHHHHHCCCCCCCCCHHHHHH
LAEKLIEEKYGRKEWNFQR
HHHHHHHHHCCCCCCCCCC

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]