The gene/protein map for NC_010682 is currently unavailable.
Definition Campylobacter jejuni subsp. doylei 269.97, complete genome.
Accession NC_009707
Length 1,845,106

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The map label for this gene is hisH [H]

Identifier: 153952021

GI number: 153952021

Start: 354786

End: 355403

Strand: Direct

Name: hisH [H]

Synonym: JJD26997_0399

Alternate gene names: 153952021

Gene position: 354786-355403 (Clockwise)

Preceding gene: 153951966

Following gene: 153952216

Centisome position: 19.23

GC content: 33.5

Gene sequence:

>618_bases
GTGTGTTTTAAAATGATAGCGCTCATTGATTACAAGGCGGGAAATTTAAACTCCGTTGCTAAGGCTTTTGAAAAAATAGG
AGCTACAAATTTCATAGCCCAAAATCCAAAAGATTTGCAAAAAGCAGATAAATTGCTTTTACCTGGAGTGGGATCTTTTA
AAGAAGCGATGAAAAATTTAAAAGAACTTGGTTTTATAGAAGCTTTAAAAGAGCAAGTTTTAGTGCAAAAAAAACCTATT
TTAGGCATTTGTTTAGGAATGCAGCTTTTTTTAGAAAAGGGCTATGAAGGTGGAGTTTGCGAAGGACTTGGCTTTGTTGA
AGGTGAGGTGGTGAAATTTGAAGAGGATTTGAATTTAAAAATCCCACACATGGGTTGGAATGAACTTGAAATTTTAAAAC
AAGAGCCTTTGTATCAAGGCATGGAAGATAAGAGTGATTTTTATTTTGTGCACTCTTTTTATGTGAGATGTAAAGATGAG
TTTGTCAGTGCTAAAGCACAATACGGGCATAAATTTGTCGCATCTTTGCAAAAAGATCATATTTTTGCGACGCAGTTTCA
TCCTGAAAAAAGTCAAAATTTAGGCTTAAAACTTTTAGAAAATTTTGTAAGGCTTTAA

Upstream 100 bases:

>100_bases
AAAAAATCGTAGATTCTTTTACCAATAAAAAAATCTTTAAACGCGATGAAAATGGCAAATTTATAAGAGATTATGATGGT
TCTTTGGTAAGAAAAGATGA

Downstream 100 bases:

>100_bases
ATGTTAAAAACTAGAATTATCCCCTGTGTGTTATTAAAAAATTCTCAACTTGTTAAAAGTATAGAATTTAAAGATTTTCG
CACTATAGGGCACTTAACTT

Product: imidazole glycerol phosphate synthase subunit HisH

Products: D-erythro-imidazole-glycerol-phosphate; AICAR; L-glutamate [C]

Alternate protein names: IGP synthase glutamine amidotransferase subunit 1; IGP synthase subunit hisH 1; ImGP synthase subunit hisH 1; IGPS subunit hisH 1 [H]

Number of amino acids: Translated: 205; Mature: 205

Protein sequence:

>205_residues
MCFKMIALIDYKAGNLNSVAKAFEKIGATNFIAQNPKDLQKADKLLLPGVGSFKEAMKNLKELGFIEALKEQVLVQKKPI
LGICLGMQLFLEKGYEGGVCEGLGFVEGEVVKFEEDLNLKIPHMGWNELEILKQEPLYQGMEDKSDFYFVHSFYVRCKDE
FVSAKAQYGHKFVASLQKDHIFATQFHPEKSQNLGLKLLENFVRL

Sequences:

>Translated_205_residues
MCFKMIALIDYKAGNLNSVAKAFEKIGATNFIAQNPKDLQKADKLLLPGVGSFKEAMKNLKELGFIEALKEQVLVQKKPI
LGICLGMQLFLEKGYEGGVCEGLGFVEGEVVKFEEDLNLKIPHMGWNELEILKQEPLYQGMEDKSDFYFVHSFYVRCKDE
FVSAKAQYGHKFVASLQKDHIFATQFHPEKSQNLGLKLLENFVRL
>Mature_205_residues
MCFKMIALIDYKAGNLNSVAKAFEKIGATNFIAQNPKDLQKADKLLLPGVGSFKEAMKNLKELGFIEALKEQVLVQKKPI
LGICLGMQLFLEKGYEGGVCEGLGFVEGEVVKFEEDLNLKIPHMGWNELEILKQEPLYQGMEDKSDFYFVHSFYVRCKDE
FVSAKAQYGHKFVASLQKDHIFATQFHPEKSQNLGLKLLENFVRL

Specific function: IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The hisH subunit provides the glutamine amidotransferase activity that produces the ammonia necessary to hisF for the synthesis of IGP and AICAR [H]

COG id: COG0118

COG function: function code E; Glutamine amidotransferase

Gene ontology:

Cell location: Cytoplasm [H]

Metaboloic importance: Non_Essential [C]

Operon status: Not Known

Operon components: None

Similarity: Contains 1 glutamine amidotransferase type-1 domain [H]

Homologues:

Organism=Escherichia coli, GI1788334, Length=200, Percent_Identity=38.5, Blast_Score=145, Evalue=1e-36,
Organism=Saccharomyces cerevisiae, GI6319725, Length=212, Percent_Identity=34.9056603773585, Blast_Score=129, Evalue=3e-31,

Paralogues:

None

Copy number: NA

Swissprot (AC and ID): NA

Other databases:

- InterPro:   IPR017926
- InterPro:   IPR000991
- InterPro:   IPR010139
- InterPro:   IPR016226 [H]

Pfam domain/function: PF00117 GATase [H]

EC number: 2.4.2.- [C]

Molecular weight: Translated: 23273; Mature: 23273

Theoretical pI: Translated: 7.03; Mature: 7.03

Prosite motif: PS00442 GATASE_TYPE_I

Important sites: NA

Signals:

None

Transmembrane regions:

None

Cys/Met content:

2.0 %Cys     (Translated Protein)
2.9 %Met     (Translated Protein)
4.9 %Cys+Met (Translated Protein)
2.0 %Cys     (Mature Protein)
2.9 %Met     (Mature Protein)
4.9 %Cys+Met (Mature Protein)

Secondary structure:

>Translated Secondary Structure
MCFKMIALIDYKAGNLNSVAKAFEKIGATNFIAQNPKDLQKADKLLLPGVGSFKEAMKNL
CHHHHEEHHCCCCCCHHHHHHHHHHHCCHHHHHCCHHHHHHHHHHHCCCCCHHHHHHHHH
KELGFIEALKEQVLVQKKPILGICLGMQLFLEKGYEGGVCEGLGFVEGEVVKFEEDLNLK
HHHHHHHHHHHHHHHHCCCHHHHHHHHHHHHHCCCCCCCCCCCCCCCCEEEEEECCCCEE
IPHMGWNELEILKQEPLYQGMEDKSDFYFVHSFYVRCKDEFVSAKAQYGHKFVASLQKDH
CCCCCCHHHHHHHHCHHHCCCCCCCCEEEEHHHHHHHHHHHHHHHHHHHHHHHHHHHHCC
IFATQFHPEKSQNLGLKLLENFVRL
EEEEECCCCCCCCCCHHHHHHHHCC
>Mature Secondary Structure
MCFKMIALIDYKAGNLNSVAKAFEKIGATNFIAQNPKDLQKADKLLLPGVGSFKEAMKNL
CHHHHEEHHCCCCCCHHHHHHHHHHHCCHHHHHCCHHHHHHHHHHHCCCCCHHHHHHHHH
KELGFIEALKEQVLVQKKPILGICLGMQLFLEKGYEGGVCEGLGFVEGEVVKFEEDLNLK
HHHHHHHHHHHHHHHHCCCHHHHHHHHHHHHHCCCCCCCCCCCCCCCCEEEEEECCCCEE
IPHMGWNELEILKQEPLYQGMEDKSDFYFVHSFYVRCKDEFVSAKAQYGHKFVASLQKDH
CCCCCCHHHHHHHHCHHHCCCCCCCCEEEEHHHHHHHHHHHHHHHHHHHHHHHHHHHHCC
IFATQFHPEKSQNLGLKLLENFVRL
EEEEECCCCCCCCCCHHHHHHHHCC

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: phosphoribulosylformimino-AICAR-P; L-glutamine [C]

Specific reaction: phosphoribulosylformimino-AICAR-P + L-glutamine = D-erythro-imidazole-glycerol-phosphate + AICAR + L-glutamate [C]

General reaction: Transferases; Glycosyltransferases; Pentosyltransferases [C]

Inhibitor: NA

Structure determination priority: 10.0

TargetDB status: NA

Availability: NA

References: 10688204 [H]