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P33734 (HIS5_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 119. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
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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 hisHF
Short name=IGP synthase
Short name=IGPS
Short name=ImGP synthase

Including the following 2 domains:

  1. Glutamine amidotransferase
    EC=2.4.2.-
  2. Cyclase
    EC=4.1.3.-
Gene names
Name:HIS7
Ordered Locus Names:YBR248C
ORF Names:YBR1640
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length552 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The glutamine amidotransferase domain provides the ammonia necessary to the cyclase domain to produce IGP and AICAR from PRFAR.

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.

Pathway

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

Subunit structure

Monomer. Ref.7

Induction

By amino acid starvation. It has a GCN4-dependent and a GCN4-independent (basal) expression.

Miscellaneous

Present with 11800 molecules/cell in log phase SD medium. Ref.5

Sequence similarities

In the C-terminal section; belongs to the HisA/HisF family.

Contains 1 glutamine amidotransferase type-1 domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 552552Imidazole glycerol phosphate synthase hisHF
PRO_0000152476

Regions

Domain3 – 218216Glutamine amidotransferase type-1
Region236 – 552317Cyclase
Region364 – 3652PRFAR binding
Region402 – 4043PRFAR binding
Region474 – 4752PRFAR binding
Region500 – 5012PRFAR binding
Region523 – 5242PRFAR binding

Sites

Active site831For GATase activity By similarity
Active site1931For GATase activity By similarity
Active site1951For GATase activity By similarity
Active site2451 Potential
Active site4041 Potential
Binding site831Glutamine (covalent)
Binding site3321Substrate; via amide nitrogen
Binding site4691Substrate

Amino acid modifications

Modified residue431Phosphoserine Ref.6
Modified residue1751Phosphoserine Ref.6

Experimental info

Mutagenesis2391R → A, H or K: 1000-fold decrease in catalytic efficiency. Uncoupling of glutaminase activity from the cyclase activity. Ref.4
Mutagenesis2581K → A: No activity. Uncoupling of glutaminase activity from the cyclase activity. Ref.4
Mutagenesis2581K → R: Small reduction of activity. Ref.4
Mutagenesis3601K → A or R: Almost no effect on activity. Ref.4
Sequence conflict541G → A in CAA49469. Ref.1

Secondary structure

1 ............................................................................................ 552
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P33734 [UniParc].

Last modified October 1, 1994. Version 2.
Checksum: 046E11EA5F83ABA3

FASTA55261,068
        10         20         30         40         50         60 
MPVVHVIDVE SGNLQSLTNA IEHLGYEVQL VKSPKDFNIS GTSRLILPGV GNYGHFVDNL 

        70         80         90        100        110        120 
FNRGFEKPIR EYIESGKPIM GICVGLQALF AGSVESPKST GLNYIDFKLS RFDDSEKPVP 

       130        140        150        160        170        180 
EIGWNSCIPS ENLFFGLDPY KRYYFVHSFA AILNSEKKKN LENDGWKIAK AKYGSEEFIA 

       190        200        210        220        230        240 
AVNKNNIFAT QFHPEKSGKA GLNVIENFLK QQSPPIPNYS AEEKELLMND YSNYGLTRRI 

       250        260        270        280        290        300 
IACLDVRTND QGDLVVTKGD QYDVREKSDG KGVRNLGKPV QLAQKYYQQG ADEVTFLNIT 

       310        320        330        340        350        360 
SFRDCPLKDT PMLEVLKQAA KTVFVPLTVG GGIKDIVDVD GTKIPALEVA SLYFRSGADK 

       370        380        390        400        410        420 
VSIGTDAVYA AEKYYELGNR GDGTSPIETI SKAYGAQAVV ISVDPKRVYV NSQADTKNKV 

       430        440        450        460        470        480 
FETEYPGPNG EKYCWYQCTI KGGRESRDLG VWELTRACEA LGAGEILLNC IDKDGSNSGY 

       490        500        510        520        530        540 
DLELIEHVKD AVKIPVIASS GAGVPEHFEE AFLKTRADAC LGAGMFHRGE FTVNDVKEYL 

       550 
LEHGLKVRMD EE

« Hide

References

« Hide 'large scale' references
[1]"Cloning, primary structure, and regulation of the HIS7 gene encoding a bifunctional glutamine amidotransferase: cyclase from Saccharomyces cerevisiae."
Kuenzler M., Balmelli T., Egli C.M., Paravicini G., Braus G.H.
J. Bacteriol. 175:5548-5558(1993) [PubMed: 8366040] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[2]"Complete DNA sequence of yeast chromosome II."
Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C. expand/collapse author list , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.
EMBO J. 13:5795-5809(1994) [PubMed: 7813418] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"Substrate-induced changes in the ammonia channel for imidazole glycerol phosphate synthase."
Myers R.S., Jensen J.R., Deras I.L., Smith J.L., Davisson V.J.
Biochemistry 42:7013-7022(2003) [PubMed: 12795596] [Abstract]
Cited for: MUTAGENESIS OF ARG-239; LYS-258 AND LYS-360, BIOPHYSICOCHEMICAL PROPERTIES.
[5]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed: 14562106] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[6]"A multidimensional chromatography technology for in-depth phosphoproteome analysis."
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43 AND SER-175, MASS SPECTROMETRY.
[7]"Crystal structure of imidazole glycerol phosphate synthase: a tunnel through a (beta/alpha)8 barrel joins two active sites."
Chaudhuri B.N., Lange S.C., Myers R.S., Chittur S.V., Davisson V.J., Smith J.L.
Structure 9:987-997(2001) [PubMed: 11591353] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG, SUBUNIT.
[8]"Toward understanding the mechanism of the complex cyclization reaction catalyzed by imidazole glycerolphosphate synthase: crystal structures of a ternary complex and the free enzyme."
Chaudhuri B.N., Lange S.C., Myers R.S., Davisson V.J., Smith J.L.
Biochemistry 42:7003-7012(2003) [PubMed: 12795595] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF APOENZYME; IN COMPLEX WITH SUBSTRATE AND SUBSTRATE ANALOG AND IN COMPLEX WITH INHIBITOR.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X69815 Genomic DNA. Translation: CAA49469.1.
Z36117 Genomic DNA. Translation: CAA85211.1.
BK006936 Genomic DNA. Translation: DAA07364.1.
PIRS46125.
RefSeqNP_009807.1. NM_001178596.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1JVNX-ray2.10A/B1-552[»]
1OX4X-ray2.50A/B1-552[»]
1OX5X-ray2.50A/B1-552[»]
1OX6X-ray2.40A/B1-552[»]
ProteinModelPortalP33734.
SMRP33734. Positions 1-550.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-4222N.
MINTMINT-488633.
STRINGP33734.

Proteomic databases

PeptideAtlasP33734.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYBR248C; YBR248C; YBR248C.
GeneID852550.
KEGGsce:YBR248C.
NMPDRfig|4932.3.peg.522.

Organism-specific databases

CYGDYBR248c.
SGDS000000452. HIS7.

Phylogenomic databases

eggNOGfuNOG07470.
GeneTreeEFGT00050000003436.
HOGENOMHBG330620.
OMAACLDVRT.
OrthoDBEOG4TXG1N.

Gene expression databases

ArrayExpressP33734.
GenevestigatorP33734.
GermOnlineYBR248C. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR013785. Aldolase_TIM.
IPR017926. GATASE_1.
IPR006062. His_biosynth.
IPR004651. HisF.
IPR014640. IGPS_HisHF.
IPR010139. Imidazole-glycPsynth_HisH.
IPR011060. RibuloseP-bd_barrel.
[Graphical view]
Gene3DG3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
KOK01663.
PfamPF00117. GATase. 1 hit.
PF00977. His_biosynth. 1 hit.
[Graphical view]
PIRSFPIRSF036936. IGPS_HisHF. 1 hit.
SUPFAMSSF51366. RibP_bind_barrel. 1 hit.
TIGRFAMsTIGR00735. HisF. 1 hit.
TIGR01855. IMP_synth_hisH. 1 hit.
PROSITEPS51273. GATASE_TYPE_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio971637.

Entry information

Entry nameHIS5_YEAST
AccessionPrimary (citable) accession number: P33734
Secondary accession number(s): D6VQP4
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: October 1, 1994
Last modified: December 14, 2011
This is version 119 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome II

Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents