Definition Legionella pneumophila subsp. pneumophila str. Philadelphia 1 chromosome, complete genome.
Accession NC_002942
Length 3,397,754

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The map label for this gene is hisH

Identifier: 52841429

GI number: 52841429

Start: 1324284

End: 1324883

Strand: Reverse

Name: hisH

Synonym: lpg1196

Alternate gene names: 52841429

Gene position: 1324883-1324284 (Counterclockwise)

Preceding gene: 52841430

Following gene: 52841428

Centisome position: 38.99

GC content: 37.33

Gene sequence:

>600_bases
ATGATTGCTGTGATTGATGTCAGTGGGAATAATTTAACTTCTCTGACAAATGCCTTGATTCGATTGGGAGGGCATTTTGC
ACTGACCCATGATGCTGAAGAAATACAAAAAGCAAGCCATGTCATTTTGCCAGGGGTTGGAACAGCACGTTCTGGTATGA
CAGCTTTGCAGCAAAATGGGCTAATAGACGTTTTAAGAACCTTAACCCAACCACTTCTTGGCATCTGTCTTGGAATGCAA
TTATTGCTTGAATACAGCGAAGAAGACGACATACCCTGCCTGGGTTTGATTCCTGGAGTTGCAGAGTTATTAAAAGCTGA
AAGAAATCATCCTGTTCCTCATATGGGATGGAACAATCTTCATTGGCAAAAAACATCATCATTACAACAAGGATTAAATA
ATAGTGATTATGTTTATTTTGTTCATAGCTATGCTCTAAAAGCAGATAATTATGCATTAGCTCGATGTCAGTATCATGAA
GAGTTCACTGCAGTTGTAAAAAAAGGTAATTTTTATGGTATGCAATTTCATCCAGAAAAATCAGCCAATGTTGGCATGGT
ATTACTAAATAACTTTTTATCTTTGGAGTCTACATGTTAG

Upstream 100 bases:

>100_bases
ATCACCACATGATCGAAGCATGCTTCAAAGTTTTAGGTAGAGCCTTGCGACAGGCATGCTCAAGAACGAATAATTATCTA
CCTTCAACCAAGGGTGTATT

Downstream 100 bases:

>100_bases
TTATTCCAGCTATTGATTTGCAATCTGGACGATGTGTGCGCTTAAAACAAGGACGGTTTGATCAAGTAACGCAATTTAGC
GTTTTTCCCATAGAAAGGGC

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: 199; Mature: 199

Protein sequence:

>199_residues
MIAVIDVSGNNLTSLTNALIRLGGHFALTHDAEEIQKASHVILPGVGTARSGMTALQQNGLIDVLRTLTQPLLGICLGMQ
LLLEYSEEDDIPCLGLIPGVAELLKAERNHPVPHMGWNNLHWQKTSSLQQGLNNSDYVYFVHSYALKADNYALARCQYHE
EFTAVVKKGNFYGMQFHPEKSANVGMVLLNNFLSLESTC

Sequences:

>Translated_199_residues
MIAVIDVSGNNLTSLTNALIRLGGHFALTHDAEEIQKASHVILPGVGTARSGMTALQQNGLIDVLRTLTQPLLGICLGMQ
LLLEYSEEDDIPCLGLIPGVAELLKAERNHPVPHMGWNNLHWQKTSSLQQGLNNSDYVYFVHSYALKADNYALARCQYHE
EFTAVVKKGNFYGMQFHPEKSANVGMVLLNNFLSLESTC
>Mature_199_residues
MIAVIDVSGNNLTSLTNALIRLGGHFALTHDAEEIQKASHVILPGVGTARSGMTALQQNGLIDVLRTLTQPLLGICLGMQ
LLLEYSEEDDIPCLGLIPGVAELLKAERNHPVPHMGWNNLHWQKTSSLQQGLNNSDYVYFVHSYALKADNYALARCQYHE
EFTAVVKKGNFYGMQFHPEKSANVGMVLLNNFLSLESTC

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=195, Percent_Identity=42.0512820512821, Blast_Score=166, Evalue=1e-42,
Organism=Saccharomyces cerevisiae, GI6319725, Length=214, Percent_Identity=35.0467289719626, Blast_Score=103, Evalue=1e-23,

Paralogues:

None

Copy number: NA

Swissprot (AC and ID): NA

Other databases:

- InterPro:   IPR006220
- InterPro:   IPR017926
- InterPro:   IPR000991
- InterPro:   IPR010139
- InterPro:   IPR016226 [H]

Pfam domain/function: PF00117 GATase [H]

EC number: 2.4.2.- [C]

Molecular weight: Translated: 21936; Mature: 21936

Theoretical pI: Translated: 6.22; Mature: 6.22

Prosite motif: PS00442 GATASE_TYPE_I

Important sites: NA

Signals:

None

Transmembrane regions:

None

Cys/Met content:

2.0 %Cys     (Translated Protein)
3.0 %Met     (Translated Protein)
5.0 %Cys+Met (Translated Protein)
2.0 %Cys     (Mature Protein)
3.0 %Met     (Mature Protein)
5.0 %Cys+Met (Mature Protein)

Secondary structure:

>Translated Secondary Structure
MIAVIDVSGNNLTSLTNALIRLGGHFALTHDAEEIQKASHVILPGVGTARSGMTALQQNG
CEEEEEECCCCHHHHHHHHHHHCCCEEEECCHHHHHHHCEEEECCCCCCHHHHHHHHHCC
LIDVLRTLTQPLLGICLGMQLLLEYSEEDDIPCLGLIPGVAELLKAERNHPVPHMGWNNL
HHHHHHHHHHHHHHHHHHHHHHHHCCCCCCCCEEHHHHHHHHHHHHHCCCCCCCCCCCCC
HWQKTSSLQQGLNNSDYVYFVHSYALKADNYALARCQYHEEFTAVVKKGNFYGMQFHPEK
CCCCHHHHHCCCCCCCEEEEEEEEEECCCCEEEEHHHHHHHHHHHHHCCCEEEEEECCCC
SANVGMVLLNNFLSLESTC
CCCCHHHHHHHHHHHCCCC
>Mature Secondary Structure
MIAVIDVSGNNLTSLTNALIRLGGHFALTHDAEEIQKASHVILPGVGTARSGMTALQQNG
CEEEEEECCCCHHHHHHHHHHHCCCEEEECCHHHHHHHCEEEECCCCCCHHHHHHHHHCC
LIDVLRTLTQPLLGICLGMQLLLEYSEEDDIPCLGLIPGVAELLKAERNHPVPHMGWNNL
HHHHHHHHHHHHHHHHHHHHHHHHCCCCCCCCEEHHHHHHHHHHHHHCCCCCCCCCCCCC
HWQKTSSLQQGLNNSDYVYFVHSYALKADNYALARCQYHEEFTAVVKKGNFYGMQFHPEK
CCCCHHHHHCCCCCCCEEEEEEEEEECCCCEEEEHHHHHHHHHHHHHCCCEEEEEECCCC
SANVGMVLLNNFLSLESTC
CCCCHHHHHHHHHHHCCCC

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: 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: NA