Click here to switch to the map view.

The map label for this gene is yqhM [H]

Identifier: 218905344

GI number: 218905344

Start: 4030955

End: 4031791

Strand: Reverse

Name: yqhM [H]

Synonym: BCAH820_4228

Alternate gene names: 218905344

Gene position: 4031791-4030955 (Counterclockwise)

Preceding gene: 218905351

Following gene: 218905342

Centisome position: 76.03

GC content: 35.13

Gene sequence:

>837_bases
ATGGGAAAAGAAAAATGGTGTTATATTAACTCTGGTCAATGTTCACCGGCATTTAATATGGCGTTAGATGAATGTTTATT
AAATTGGCAAAGTGAAAAGAAAATGCCACCAACTATTCGTTTTTACGAATGGGAAGTACCAACATTAACAGTCGGGTATT
TCCAGCGTGTTGAAAAAGATATTAATATGGATGTAGTTAACGAAAAGAAATATGGATTCGTTCGTCGTCAAACAGGCGGC
AGGGGTGTATTACATGATAAAGAATTAACGTATAGTGTTATTGTGTCTGAAGATCATCCGAATATGCCAAAAACAGTTAC
AGAAGCGTATCGTGTTATTTCGCAAGGTTTACTAGATGGTTTTAAAGCATTAGGGTTAGAAGCGTATTATGCAGTTCCAA
AAACAGAAGCAGATCGTGAAAATTTAAAAAATCCACGCTCAGGCGTATGTTTTGATGCACCGTCTTGGTATGAAATTGTA
GTAGAAGGAAGAAAAATCGCAGGTAGTGCGCAAACACGTCAAAAAGGTGTTATTTTGCAGCATGGATCGATTCCGTTAGA
AATAGATTTAGATGAGTTATATGATCTGTTTTTATTCCCGAATGAGCGTGTAAAAGAACGTATGAAGAGTATGTTCTCTT
CTAAAGCGGTAGCAATTAATGAATTAACAGACCGTACGTTTACAATCGAGCAGTTAATTAAAGCGTTTGAGGTTGGGTTT
GAAAAAGGATTAGATGTAGAGCTTGTTCCGTATGAATTAACAGAAGAACAATTACATGAAGTGCAAACATTAGCAAAAGA
AAAGTATGAAAGTAAAGAATGGAATTATAAAAAATAA

Upstream 100 bases:

>100_bases
TTCATTTGTATATAAGAAGAAATTTCGTATTCTTTCACAAATTTTGTCGAATTTGGTAGACTAGAGAATGTGAAAAATAA
TTGGTTATATGAGGTGCAGG

Downstream 100 bases:

>100_bases
GAGGTGGCAATTGCCGCCTCTTATTTTTTTATAGTAAATTAAGTACTTTTTCTACTTTGATTCCTTTATCTTGTAAAGAA
CGAAGGCGATTGACAACGTC

Product: putative lipoate-protein ligase A

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

Alternate protein names: NA

Number of amino acids: Translated: 278; Mature: 277

Protein sequence:

>278_residues
MGKEKWCYINSGQCSPAFNMALDECLLNWQSEKKMPPTIRFYEWEVPTLTVGYFQRVEKDINMDVVNEKKYGFVRRQTGG
RGVLHDKELTYSVIVSEDHPNMPKTVTEAYRVISQGLLDGFKALGLEAYYAVPKTEADRENLKNPRSGVCFDAPSWYEIV
VEGRKIAGSAQTRQKGVILQHGSIPLEIDLDELYDLFLFPNERVKERMKSMFSSKAVAINELTDRTFTIEQLIKAFEVGF
EKGLDVELVPYELTEEQLHEVQTLAKEKYESKEWNYKK

Sequences:

>Translated_278_residues
MGKEKWCYINSGQCSPAFNMALDECLLNWQSEKKMPPTIRFYEWEVPTLTVGYFQRVEKDINMDVVNEKKYGFVRRQTGG
RGVLHDKELTYSVIVSEDHPNMPKTVTEAYRVISQGLLDGFKALGLEAYYAVPKTEADRENLKNPRSGVCFDAPSWYEIV
VEGRKIAGSAQTRQKGVILQHGSIPLEIDLDELYDLFLFPNERVKERMKSMFSSKAVAINELTDRTFTIEQLIKAFEVGF
EKGLDVELVPYELTEEQLHEVQTLAKEKYESKEWNYKK
>Mature_277_residues
GKEKWCYINSGQCSPAFNMALDECLLNWQSEKKMPPTIRFYEWEVPTLTVGYFQRVEKDINMDVVNEKKYGFVRRQTGGR
GVLHDKELTYSVIVSEDHPNMPKTVTEAYRVISQGLLDGFKALGLEAYYAVPKTEADRENLKNPRSGVCFDAPSWYEIVV
EGRKIAGSAQTRQKGVILQHGSIPLEIDLDELYDLFLFPNERVKERMKSMFSSKAVAINELTDRTFTIEQLIKAFEVGFE
KGLDVELVPYELTEEQLHEVQTLAKEKYESKEWNYKK

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: 32119; Mature: 31988

Theoretical pI: Translated: 5.16; Mature: 5.16

Prosite motif: NA

Important sites: NA

Signals:

None

Transmembrane regions:

None

Cys/Met content:

1.4 %Cys     (Translated Protein)
2.5 %Met     (Translated Protein)
4.0 %Cys+Met (Translated Protein)
1.4 %Cys     (Mature Protein)
2.2 %Met     (Mature Protein)
3.6 %Cys+Met (Mature Protein)

Secondary structure:

>Translated Secondary Structure
MGKEKWCYINSGQCSPAFNMALDECLLNWQSEKKMPPTIRFYEWEVPTLTVGYFQRVEKD
CCCCCEEEEECCCCCHHHHHHHHHHHHCCCCCCCCCCEEEEEEECCCEEEHHHHHHHHHC
INMDVVNEKKYGFVRRQTGGRGVLHDKELTYSVIVSEDHPNMPKTVTEAYRVISQGLLDG
CCCEEECCCCCCEEEECCCCCCCEECCCCEEEEEEECCCCCCCHHHHHHHHHHHHHHHHH
FKALGLEAYYAVPKTEADRENLKNPRSGVCFDAPSWYEIVVEGRKIAGSAQTRQKGVILQ
HHHHCCCEEEECCCCCCCHHHCCCCCCCCEECCCCCEEEEEECCHHCCCCHHHHCCEEEE
HGSIPLEIDLDELYDLFLFPNERVKERMKSMFSSKAVAINELTDRTFTIEQLIKAFEVGF
CCCEEEEEEHHHHHHHHCCCCHHHHHHHHHHHHCCCEEEHHHCCCEEHHHHHHHHHHHHH
EKGLDVELVPYELTEEQLHEVQTLAKEKYESKEWNYKK
HCCCCEEEECHHCCHHHHHHHHHHHHHHHCCCCCCCCC
>Mature Secondary Structure 
GKEKWCYINSGQCSPAFNMALDECLLNWQSEKKMPPTIRFYEWEVPTLTVGYFQRVEKD
CCCCEEEEECCCCCHHHHHHHHHHHHCCCCCCCCCCEEEEEEECCCEEEHHHHHHHHHC
INMDVVNEKKYGFVRRQTGGRGVLHDKELTYSVIVSEDHPNMPKTVTEAYRVISQGLLDG
CCCEEECCCCCCEEEECCCCCCCEECCCCEEEEEEECCCCCCCHHHHHHHHHHHHHHHHH
FKALGLEAYYAVPKTEADRENLKNPRSGVCFDAPSWYEIVVEGRKIAGSAQTRQKGVILQ
HHHHCCCEEEECCCCCCCHHHCCCCCCCCEECCCCCEEEEEECCHHCCCCHHHHCCEEEE
HGSIPLEIDLDELYDLFLFPNERVKERMKSMFSSKAVAINELTDRTFTIEQLIKAFEVGF
CCCEEEEEEHHHHHHHHCCCCHHHHHHHHHHHHCCCEEEHHHCCCEEHHHHHHHHHHHHH
EKGLDVELVPYELTEEQLHEVQTLAKEKYESKEWNYKK
HCCCCEEEECHHCCHHHHHHHHHHHHHHHCCCCCCCCC

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]