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: 153951018

GI number: 153951018

Start: 1726286

End: 1726873

Strand: Direct

Name: hisH [H]

Synonym: JJD26997_1955

Alternate gene names: 153951018

Gene position: 1726286-1726873 (Clockwise)

Preceding gene: 153951969

Following gene: 153951118

Centisome position: 93.56

GC content: 32.48

Gene sequence:

>588_bases
ATGAAACTAGTTATCATCGATACAGCCTGTGCGAATTTGGCATCTTTGAAATTTTGTCTGGATAGATTAGGTTTTAATGC
AACTATCAGCAGGGATTTAAAAGAGCTTGAAAGTGCGGATAAGCTTTTTTTACCTGGAGTGGGTACCGCAAAAGAAGCAA
TGAAAAATTTAGAACAATTTAATCTTATTGATTTTATTCAAAATACCAAAAAACCTTTGCTTGGTATTTGTTTAGGTATG
CAAATTTTAGGAAATTTTTCTGAAGAATTAAATCAAGAAACCTTAAAACTCATAGATTTTACAACCCAAAAATTTAAAGC
TAAAGAAGGCTTTACTTTTCCACATACGGGATGGAATCAAGTTCATAGCTCTCATGCTTTATTTAAAGGTTTAGAAGGGG
CTTATTTTTATTTTGTGCATAGTTATTGCGTAGGACTTGGGGAATACACTATAGCAGATTGTGAGTATTCGCAAAAATTT
AGCGCAAGTGTAATGAAAGATAATTTTTACGGGGTGCAATTTCACCCTGAAAGAAGTAGTGAAGCGGGGGAAATTTTAAT
TTCAAATTTTATTAAGGATATAGGATGA

Upstream 100 bases:

>100_bases
TAGCTAGAAAGAAAGAATTAGAAAATAATTTTAACACCATTAAAAGCAAAATTAATGATTTGAAATTATTGGGTAAAAAT
AGTTTATTTCAAGGAGTGAT

Downstream 100 bases:

>100_bases
CTCAAATCATACCCGCACTTGATCTTATAGATGGCGAAGTAGTGCGTCTTGTAAAAGGGGATTATAAACAAAAAAAAGTA
TATAAATACAATCCCTTAAA

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 2; IGP synthase subunit hisH 2; ImGP synthase subunit hisH 2; IGPS subunit hisH 2 [H]

Number of amino acids: Translated: 195; Mature: 195

Protein sequence:

>195_residues
MKLVIIDTACANLASLKFCLDRLGFNATISRDLKELESADKLFLPGVGTAKEAMKNLEQFNLIDFIQNTKKPLLGICLGM
QILGNFSEELNQETLKLIDFTTQKFKAKEGFTFPHTGWNQVHSSHALFKGLEGAYFYFVHSYCVGLGEYTIADCEYSQKF
SASVMKDNFYGVQFHPERSSEAGEILISNFIKDIG

Sequences:

>Translated_195_residues
MKLVIIDTACANLASLKFCLDRLGFNATISRDLKELESADKLFLPGVGTAKEAMKNLEQFNLIDFIQNTKKPLLGICLGM
QILGNFSEELNQETLKLIDFTTQKFKAKEGFTFPHTGWNQVHSSHALFKGLEGAYFYFVHSYCVGLGEYTIADCEYSQKF
SASVMKDNFYGVQFHPERSSEAGEILISNFIKDIG
>Mature_195_residues
MKLVIIDTACANLASLKFCLDRLGFNATISRDLKELESADKLFLPGVGTAKEAMKNLEQFNLIDFIQNTKKPLLGICLGM
QILGNFSEELNQETLKLIDFTTQKFKAKEGFTFPHTGWNQVHSSHALFKGLEGAYFYFVHSYCVGLGEYTIADCEYSQKF
SASVMKDNFYGVQFHPERSSEAGEILISNFIKDIG

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=196, Percent_Identity=51.0204081632653, Blast_Score=197, Evalue=3e-52,
Organism=Saccharomyces cerevisiae, GI6319725, Length=209, Percent_Identity=34.9282296650718, Blast_Score=102, Evalue=3e-23,

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: 21906; Mature: 21906

Theoretical pI: Translated: 6.01; Mature: 6.01

Prosite motif: PS00442 GATASE_TYPE_I

Important sites: NA

Signals:

None

Transmembrane regions:

None

Cys/Met content:

2.6 %Cys     (Translated Protein)
2.1 %Met     (Translated Protein)
4.6 %Cys+Met (Translated Protein)
2.6 %Cys     (Mature Protein)
2.1 %Met     (Mature Protein)
4.6 %Cys+Met (Mature Protein)

Secondary structure:

>Translated Secondary Structure
MKLVIIDTACANLASLKFCLDRLGFNATISRDLKELESADKLFLPGVGTAKEAMKNLEQF
CEEEEEEHHHHHHHHHHHHHHHHCCCCHHHHHHHHHHCCCCEECCCCCCHHHHHHHHHHH
NLIDFIQNTKKPLLGICLGMQILGNFSEELNQETLKLIDFTTQKFKAKEGFTFPHTGWNQ
HHHHHHHHCCCHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCCCCCCCCHHH
VHSSHALFKGLEGAYFYFVHSYCVGLGEYTIADCEYSQKFSASVMKDNFYGVQFHPERSS
HHHHHHHHHCCCCHHHHHHHHHHHHCCCEEEECCCCHHHHHHHHHHCCCEEEEECCCCCC
EAGEILISNFIKDIG
CHHHHHHHHHHHHCC
>Mature Secondary Structure
MKLVIIDTACANLASLKFCLDRLGFNATISRDLKELESADKLFLPGVGTAKEAMKNLEQF
CEEEEEEHHHHHHHHHHHHHHHHCCCCHHHHHHHHHHCCCCEECCCCCCHHHHHHHHHHH
NLIDFIQNTKKPLLGICLGMQILGNFSEELNQETLKLIDFTTQKFKAKEGFTFPHTGWNQ
HHHHHHHHCCCHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCCCCCCCCHHH
VHSSHALFKGLEGAYFYFVHSYCVGLGEYTIADCEYSQKFSASVMKDNFYGVQFHPERSS
HHHHHHHHHCCCCHHHHHHHHHHHHCCCEEEECCCCHHHHHHHHHHCCCEEEEECCCCCC
EAGEILISNFIKDIG
CHHHHHHHHHHHHCC

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]