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The map label for this gene is yqhM [H]

Identifier: 218883389

GI number: 218883389

Start: 67247

End: 68023

Strand: Reverse

Name: yqhM [H]

Synonym: DKAM_0075

Alternate gene names: 218883389

Gene position: 68023-67247 (Counterclockwise)

Preceding gene: 218883401

Following gene: 218883388

Centisome position: 4.98

GC content: 44.79

Gene sequence:

>777_bases
ATGCCCGGGATAGCTGCCATGAGGCTTAGAGTAATAATCGATCTAGATGGCGGATCGGCATTTTTCAATATGGGAATGGA
TGAGGCATTGCTTAATCTTAGGATGTGGGAAGAGATACCTGATACGCTGAGGCTCTACGTCTTCGACCCCTCGGCTGTAA
CCATAGGGTATTTCCAGAAAATAGAGGAATCAGTGGATATGGATTATGCGTCATTACACGGGATAGATGTAACGAGGAGG
ATCAGTGGTGGGGGCTCGGTATACCATGATAGAAACGGTGAAGTAACATATAGTATTGTAACACCCGCTAGAGGAGTCTT
CAGCGATGTACGTGAAAGCTATGAAGTAATATGTAAGGGATTAATCGAGGCATTAAAGCTATTCGGGGTTGAAGCATCAT
TCATGCCCATCAACGATATCGTGGTTAATGGAAGAAAGATATCGGGCAGCGCCCAGGCAAGGAGAAAAGGATACCTGCTA
CAACATGGAACACTAATGTATGCAACAGACCTGGATACCGTGTCGAAGGTGTTGAAAGCTCCCCCAGTTAAACTGGTTTC
TAAGGGAGTGAAAAGCATTAGAGAAAGAGTCATCACGCTTCAAGAAGCATTATCTAGAAGGGTCAGCAAAGAGGAGGTTG
CCGAGGCATTGTTAAAAGGGTTCTCGAAGGCATTAAACGCCGAGATATACATAGATGAATACAGTGAAAACGAGTTGAGG
CTTACCGAGGAACTATCCCTTAAGTATAAGAGCAGGGAGTGGGTATTTAAGAGGTGA

Upstream 100 bases:

>100_bases
GCAAGCGTACCTATTGATGCCCTGACAAACATTACTATTTCACACCTTAAATTTAAAATTAAAATAACACTATAAATACC
GATAACCATGTTACAAAGTA

Downstream 100 bases:

>100_bases
TACCATATGAGGCTGACAAGAGTACTTAGAGGGGAGAAAACAGTAAGCATAGACATCGAGGTTGAAGAATGCGCAATAAG
GACGATCATGTTCTCGGGTG

Product: Lipoate-protein ligase a

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

Alternate protein names: NA

Number of amino acids: Translated: 258; Mature: 257

Protein sequence:

>258_residues
MPGIAAMRLRVIIDLDGGSAFFNMGMDEALLNLRMWEEIPDTLRLYVFDPSAVTIGYFQKIEESVDMDYASLHGIDVTRR
ISGGGSVYHDRNGEVTYSIVTPARGVFSDVRESYEVICKGLIEALKLFGVEASFMPINDIVVNGRKISGSAQARRKGYLL
QHGTLMYATDLDTVSKVLKAPPVKLVSKGVKSIRERVITLQEALSRRVSKEEVAEALLKGFSKALNAEIYIDEYSENELR
LTEELSLKYKSREWVFKR

Sequences:

>Translated_258_residues
MPGIAAMRLRVIIDLDGGSAFFNMGMDEALLNLRMWEEIPDTLRLYVFDPSAVTIGYFQKIEESVDMDYASLHGIDVTRR
ISGGGSVYHDRNGEVTYSIVTPARGVFSDVRESYEVICKGLIEALKLFGVEASFMPINDIVVNGRKISGSAQARRKGYLL
QHGTLMYATDLDTVSKVLKAPPVKLVSKGVKSIRERVITLQEALSRRVSKEEVAEALLKGFSKALNAEIYIDEYSENELR
LTEELSLKYKSREWVFKR
>Mature_257_residues
PGIAAMRLRVIIDLDGGSAFFNMGMDEALLNLRMWEEIPDTLRLYVFDPSAVTIGYFQKIEESVDMDYASLHGIDVTRRI
SGGGSVYHDRNGEVTYSIVTPARGVFSDVRESYEVICKGLIEALKLFGVEASFMPINDIVVNGRKISGSAQARRKGYLLQ
HGTLMYATDLDTVSKVLKAPPVKLVSKGVKSIRERVITLQEALSRRVSKEEVAEALLKGFSKALNAEIYIDEYSENELRL
TEELSLKYKSREWVFKR

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=258, Percent_Identity=29.0697674418605, Blast_Score=82, Evalue=2e-17,
Organism=Saccharomyces cerevisiae, GI6322415, Length=208, Percent_Identity=29.3269230769231, Blast_Score=67, Evalue=3e-12,

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: 28998; Mature: 28867

Theoretical pI: Translated: 6.81; Mature: 6.81

Prosite motif: NA

Important sites: NA

Signals:

None

Transmembrane regions:

None

Cys/Met content:

0.4 %Cys     (Translated Protein)
3.1 %Met     (Translated Protein)
3.5 %Cys+Met (Translated Protein)
0.4 %Cys     (Mature Protein)
2.7 %Met     (Mature Protein)
3.1 %Cys+Met (Mature Protein)

Secondary structure:

>Translated Secondary Structure
MPGIAAMRLRVIIDLDGGSAFFNMGMDEALLNLRMWEEIPDTLRLYVFDPSAVTIGYFQK
CCCHHEEEEEEEEEECCCCEEECCCHHHHHHHHHHHHHCCCEEEEEEECCCEEEHHHHHH
IEESVDMDYASLHGIDVTRRISGGGSVYHDRNGEVTYSIVTPARGVFSDVRESYEVICKG
HHHHHCCCHHHHCCCCEEEEECCCCCEEECCCCCEEEEEECCCHHHHHHHHHHHHHHHHH
LIEALKLFGVEASFMPINDIVVNGRKISGSAQARRKGYLLQHGTLMYATDLDTVSKVLKA
HHHHHHHHCCCCCCEEHHHEEECCEEECCCHHHHHCCEEEECCEEEEEECHHHHHHHHCC
PPVKLVSKGVKSIRERVITLQEALSRRVSKEEVAEALLKGFSKALNAEIYIDEYSENELR
CCHHHHHHHHHHHHHHHHHHHHHHHHCCCHHHHHHHHHHHHHHHCCCEEEEEECCCCCEE
LTEELSLKYKSREWVFKR
EHHHHHHEECCCCCCCCC
>Mature Secondary Structure 
PGIAAMRLRVIIDLDGGSAFFNMGMDEALLNLRMWEEIPDTLRLYVFDPSAVTIGYFQK
CCHHEEEEEEEEEECCCCEEECCCHHHHHHHHHHHHHCCCEEEEEEECCCEEEHHHHHH
IEESVDMDYASLHGIDVTRRISGGGSVYHDRNGEVTYSIVTPARGVFSDVRESYEVICKG
HHHHHCCCHHHHCCCCEEEEECCCCCEEECCCCCEEEEEECCCHHHHHHHHHHHHHHHHH
LIEALKLFGVEASFMPINDIVVNGRKISGSAQARRKGYLLQHGTLMYATDLDTVSKVLKA
HHHHHHHHCCCCCCEEHHHEEECCEEECCCHHHHHCCEEEECCEEEEEECHHHHHHHHCC
PPVKLVSKGVKSIRERVITLQEALSRRVSKEEVAEALLKGFSKALNAEIYIDEYSENELR
CCHHHHHHHHHHHHHHHHHHHHHHHHCCCHHHHHHHHHHHHHHHCCCEEEEEECCCCCEE
LTEELSLKYKSREWVFKR
EHHHHHHEECCCCCCCCC

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]