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Q57AH5 (HIS5_BRUAB) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Imidazole glycerol phosphate synthase subunit HisH

EC=2.4.2.-
Alternative name(s):
IGP synthase glutamine amidotransferase subunit
IGP synthase subunit HisH
ImGP synthase subunit HisH
Short name=IGPS subunit HisH
Gene names
Name:hisH
Ordered Locus Names:BruAb1_2058
OrganismBrucella abortus biovar 1 (strain 9-941) [Complete proteome] [HAMAP]
Taxonomic identifier262698 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella

Protein attributes

Sequence length216 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

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 By similarity. HAMAP-Rule MF_00278

Catalytic activity

5-[(5-phospho-1-deoxyribulos-1-ylamino)methylideneamino]-1-(5-phosphoribosyl)imidazole-4-carboxamide + L-glutamine = imidazole-glycerol phosphate + 5-aminoimidazol-4-carboxamide ribonucleotide + L-glutamate + H2O. HAMAP-Rule MF_00278

Pathway

Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 5/9. HAMAP-Rule MF_00278

Subunit structure

Heterodimer of HisH and HisF By similarity. HAMAP-Rule MF_00278

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00278.

Sequence similarities

Contains 1 glutamine amidotransferase type-1 domain.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Histidine biosynthesis
   Cellular componentCytoplasm
   DomainGlutamine amidotransferase
   Molecular functionTransferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processglutamine metabolic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

histidine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionimidazoleglycerol-phosphate synthase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 216216Imidazole glycerol phosphate synthase subunit HisH HAMAP-Rule MF_00278
PRO_0000231707

Regions

Domain2 – 216215Glutamine amidotransferase type-1

Sites

Active site881Nucleophile By similarity
Active site1961 By similarity
Active site1981 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q57AH5 [UniParc].

Last modified May 10, 2005. Version 1.
Checksum: E87CAEF18E2D1A09

FASTA21623,232
        10         20         30         40         50         60 
MRVAIIDYGS GNLRSATKAF ERAAHESGIS AEIDLTCDAQ RVASADRIVL PGVGAYADCR 

        70         80         90        100        110        120 
RGLDAAPGMV EALNDTVLKK ARPFLGICVG MQLMSERGLE KTVTNGLGWI AGDVREMVPS 

       130        140        150        160        170        180 
DASLKIPQIG WNRIHVKHSH PIFDGIPTGD DGLHAYFVHS YMLDAKNASD VLAVTDYGGD 

       190        200        210 
VTAAVGRDNM VGTQFHPEKS QLLGLSLIAN FLKWKP 

« Hide

References

[1]"Completion of the genome sequence of Brucella abortus and comparison to the highly similar genomes of Brucella melitensis and Brucella suis."
Halling S.M., Peterson-Burch B.D., Bricker B.J., Zuerner R.L., Qing Z., Li L.-L., Kapur V., Alt D.P., Olsen S.C.
J. Bacteriol. 187:2715-2726(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 9-941.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017223 Genomic DNA. Translation: AAX75359.1.
RefSeqYP_222720.1. NC_006932.1.

3D structure databases

ProteinModelPortalQ57AH5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING262698.BruAb1_2058.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAX75359; AAX75359; BruAb1_2058.
GeneID3339689.
KEGGbmb:BruAb1_2058.
PATRIC17825969. VBIBruAbo15061_2172.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0118.
HOGENOMHOG000025030.
KOK02501.
OMAMGWNDLV.
OrthoDBEOG69KV05.

Enzyme and pathway databases

BioCycBABO262698:GJC2-2108-MONOMER.
UniPathwayUPA00031; UER00010.

Family and domain databases

Gene3D3.40.50.880. 1 hit.
HAMAPMF_00278. HisH.
InterProIPR029062. Class_I_gatase-like.
IPR017926. GATASE.
IPR010139. Imidazole-glycPsynth_HisH.
[Graphical view]
PfamPF00117. GATase. 1 hit.
[Graphical view]
PIRSFPIRSF000495. Amidotransf_hisH. 1 hit.
SUPFAMSSF52317. SSF52317. 1 hit.
TIGRFAMsTIGR01855. IMP_synth_hisH. 1 hit.
PROSITEPS51273. GATASE_TYPE_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHIS5_BRUAB
AccessionPrimary (citable) accession number: Q57AH5
Entry history
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: May 10, 2005
Last modified: June 11, 2014
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Brucella abortus strain 9-941

Brucella abortus (strain 9-941): entries and gene names