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The map label for this gene is hisH [H]

Identifier: 119945365

GI number: 119945365

Start: 2010222

End: 2010824

Strand: Reverse

Name: hisH [H]

Synonym: Ping_1653

Alternate gene names: 119945365

Gene position: 2010824-2010222 (Counterclockwise)

Preceding gene: 119945366

Following gene: 119945364

Centisome position: 44.1

GC content: 44.61

Gene sequence:

>603_bases
ATGAACATAGTCATTATTGATACGGGTTGCGCTAACCTCTCTTCGGTTAGGTTTGCCATCGAACGTTTAGGCTATAGTGT
CACCGTCAGTAAAGATCCGGCCATTTTACAGCAGGCAGATAAGCTCTTTTTACCCGGTGTCGGCACTGCTAAAGAGGCAA
TGGCTAATTTAATTGAGCGTAATTTAGTTGAACCAATTAAAAGCCTGACCCAACCTGTTTTAGGGATCTGTTTAGGCATG
CAGATGTTAGCGGATGCCTCGGAAGAAGGTTTTGGTGATCAACCTATTATTGAAACACTGGGAATAGTTGAAGGCCATAT
CGAAAAGATGGATGTTGCGCCGCTACGCTCTCCCCATATGGGCTGGAATCAAATCACCCCTAAACTTGATGAACCTTTAT
TTAAAGATATTCCTGCGGGCAGTTACTTCTACTTTGTGCACAGTTATGCCCTGCCAGTCAATGAAAATACCATCGCCAGT
TGCGAGTATGGTACGCCGTTTACTGCGGCCGTTAATAAAGATAATTTTTACGGGGTACAGTTTCACCCCGAACGCTCCGG
TAAAGCTGGCGCCCAACTGATTAAAAACTTCCTGGAGCTTTAA

Upstream 100 bases:

>100_bases
CTCACCATATGGTTGAAGGTTTATTCAAAACGTTTGGCCGTACCCTTCGCCAATGTATACAAGTTGTGGGAACCGACTTA
CCTTCAAGCAAAGGTGTTTT

Downstream 100 bases:

>100_bases
AATGATTATTCCAGCACTCGATCTTATCGATGGCAAAGTCGTGCGTTTATATCAAGGTGATTACGCACAAAAAACAGTTT
ACAGTGACTCCCCGCAAAGC

Product: imidazole glycerol phosphate synthase, glutamine amidotransferase subunit

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

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

Number of amino acids: Translated: 200; Mature: 200

Protein sequence:

>200_residues
MNIVIIDTGCANLSSVRFAIERLGYSVTVSKDPAILQQADKLFLPGVGTAKEAMANLIERNLVEPIKSLTQPVLGICLGM
QMLADASEEGFGDQPIIETLGIVEGHIEKMDVAPLRSPHMGWNQITPKLDEPLFKDIPAGSYFYFVHSYALPVNENTIAS
CEYGTPFTAAVNKDNFYGVQFHPERSGKAGAQLIKNFLEL

Sequences:

>Translated_200_residues
MNIVIIDTGCANLSSVRFAIERLGYSVTVSKDPAILQQADKLFLPGVGTAKEAMANLIERNLVEPIKSLTQPVLGICLGM
QMLADASEEGFGDQPIIETLGIVEGHIEKMDVAPLRSPHMGWNQITPKLDEPLFKDIPAGSYFYFVHSYALPVNENTIAS
CEYGTPFTAAVNKDNFYGVQFHPERSGKAGAQLIKNFLEL
>Mature_200_residues
MNIVIIDTGCANLSSVRFAIERLGYSVTVSKDPAILQQADKLFLPGVGTAKEAMANLIERNLVEPIKSLTQPVLGICLGM
QMLADASEEGFGDQPIIETLGIVEGHIEKMDVAPLRSPHMGWNQITPKLDEPLFKDIPAGSYFYFVHSYALPVNENTIAS
CEYGTPFTAAVNKDNFYGVQFHPERSGKAGAQLIKNFLEL

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=61.5, Blast_Score=249, Evalue=7e-68,
Organism=Saccharomyces cerevisiae, GI6319725, Length=213, Percent_Identity=37.0892018779343, Blast_Score=123, Evalue=2e-29,

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: 21873; Mature: 21873

Theoretical pI: Translated: 4.71; Mature: 4.71

Prosite motif: PS00442 GATASE_TYPE_I

Important sites: NA

Signals:

None

Transmembrane regions:

None

Cys/Met content:

1.5 %Cys     (Translated Protein)
3.0 %Met     (Translated Protein)
4.5 %Cys+Met (Translated Protein)
1.5 %Cys     (Mature Protein)
3.0 %Met     (Mature Protein)
4.5 %Cys+Met (Mature Protein)

Secondary structure:

>Translated Secondary Structure
MNIVIIDTGCANLSSVRFAIERLGYSVTVSKDPAILQQADKLFLPGVGTAKEAMANLIER
CEEEEEECCCCCHHHHHHHHHHCCCEEEECCCHHHHHHHHHHCCCCCCHHHHHHHHHHHH
NLVEPIKSLTQPVLGICLGMQMLADASEEGFGDQPIIETLGIVEGHIEKMDVAPLRSPHM
HHHHHHHHHHHHHHHHHHHHHHHHCCCCCCCCCCHHHHHHHHHHHHHHHHCCCCCCCCCC
GWNQITPKLDEPLFKDIPAGSYFYFVHSYALPVNENTIASCEYGTPFTAAVNKDNFYGVQ
CHHHCCCCCCCHHHHHCCCCCEEEEEEEEECCCCCCCEEEECCCCCEEEEECCCCEEEEE
FHPERSGKAGAQLIKNFLEL
ECCCCCCHHHHHHHHHHHCC
>Mature Secondary Structure
MNIVIIDTGCANLSSVRFAIERLGYSVTVSKDPAILQQADKLFLPGVGTAKEAMANLIER
CEEEEEECCCCCHHHHHHHHHHCCCEEEECCCHHHHHHHHHHCCCCCCHHHHHHHHHHHH
NLVEPIKSLTQPVLGICLGMQMLADASEEGFGDQPIIETLGIVEGHIEKMDVAPLRSPHM
HHHHHHHHHHHHHHHHHHHHHHHHCCCCCCCCCCHHHHHHHHHHHHHHHHCCCCCCCCCC
GWNQITPKLDEPLFKDIPAGSYFYFVHSYALPVNENTIASCEYGTPFTAAVNKDNFYGVQ
CHHHCCCCCCCHHHHHCCCCCEEEEEEEEECCCCCCCEEEECCCCCEEEEECCCCEEEEE
FHPERSGKAGAQLIKNFLEL
ECCCCCCHHHHHHHHHHHCC

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