Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Imidazole glycerol phosphate synthase hisHF

Gene

HIS7

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

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.

Pathwayi: L-histidine biosynthesis

This protein is involved in step 5 of the subpathway that synthesizes L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate.
Proteins known to be involved in the 9 steps of the subpathway in this organism are:
  1. ATP phosphoribosyltransferase (HIS1)
  2. Histidine biosynthesis trifunctional protein (HIS4)
  3. Histidine biosynthesis trifunctional protein (HIS4)
  4. 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase (HIS6)
  5. Imidazole glycerol phosphate synthase hisHF (HIS7)
  6. Imidazoleglycerol-phosphate dehydratase (HIS3)
  7. Histidinol-phosphate aminotransferase (HIS5)
  8. Histidinol-phosphatase (HIS2)
  9. Histidine biosynthesis trifunctional protein (HIS4)
This subpathway is part of the pathway L-histidine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate, the pathway L-histidine biosynthesis and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei83 – 831For GATase activityBy similarity
Binding sitei83 – 831Glutamine (covalent)
Active sitei193 – 1931For GATase activityBy similarity
Active sitei195 – 1951For GATase activityBy similarity
Active sitei245 – 2451Sequence analysis
Binding sitei332 – 3321Substrate; via amide nitrogen
Active sitei404 – 4041Sequence analysis
Binding sitei469 – 4691Substrate

GO - Molecular functioni

  • glutaminase activity Source: SGD
  • imidazoleglycerol-phosphate synthase activity Source: SGD
  • oxo-acid-lyase activity Source: InterPro

GO - Biological processi

  • glutamine metabolic process Source: UniProtKB-KW
  • histidine biosynthetic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Lyase, Transferase

Keywords - Biological processi

Amino-acid biosynthesis, Histidine biosynthesis, Stress response

Enzyme and pathway databases

BioCyciYEAST:YBR248C-MONOMER.
BRENDAi4.3.1.B2. 984.
SABIO-RKP33734.
UniPathwayiUPA00031; UER00010.

Names & Taxonomyi

Protein namesi
Recommended name:
Imidazole glycerol phosphate synthase hisHF
Short name:
IGP synthase
Short name:
IGPS
Short name:
ImGP synthase
Including the following 2 domains:
Glutamine amidotransferase (EC:2.4.2.-)
Cyclase (EC:4.1.3.-)
Gene namesi
Name:HIS7
Ordered Locus Names:YBR248C
ORF Names:YBR1640
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:YBR248C.
SGDiS000000452. HIS7.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: InterPro
  • intracellular Source: SGD
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi239 – 2391R → A, H or K: 1000-fold decrease in catalytic efficiency. Uncoupling of glutaminase activity from the cyclase activity. 1 Publication
Mutagenesisi258 – 2581K → A: No activity. Uncoupling of glutaminase activity from the cyclase activity. 1 Publication
Mutagenesisi258 – 2581K → R: Small reduction of activity. 1 Publication
Mutagenesisi360 – 3601K → A or R: Almost no effect on activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 552552Imidazole glycerol phosphate synthase hisHFPRO_0000152476Add
BLAST

Proteomic databases

MaxQBiP33734.
PeptideAtlasiP33734.

PTM databases

iPTMnetiP33734.

Expressioni

Inductioni

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

Interactioni

Subunit structurei

Monomer.2 Publications

Protein-protein interaction databases

BioGridi32943. 10 interactions.
DIPiDIP-4222N.
MINTiMINT-488633.

Structurei

Secondary structure

1
552
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 75Combined sources
Helixi15 – 239Combined sources
Beta strandi27 – 337Combined sources
Helixi34 – 363Combined sources
Helixi39 – 413Combined sources
Beta strandi45 – 495Combined sources
Helixi53 – 6210Combined sources
Helixi66 – 749Combined sources
Beta strandi79 – 835Combined sources
Helixi84 – 874Combined sources
Beta strandi90 – 934Combined sources
Beta strandi104 – 1118Combined sources
Turni114 – 1163Combined sources
Beta strandi119 – 1257Combined sources
Beta strandi143 – 1508Combined sources
Helixi155 – 1639Combined sources
Beta strandi167 – 1737Combined sources
Beta strandi176 – 1849Combined sources
Beta strandi187 – 1937Combined sources
Helixi194 – 1963Combined sources
Helixi198 – 20912Combined sources
Helixi221 – 2277Combined sources
Helixi232 – 2354Combined sources
Beta strandi240 – 2489Combined sources
Beta strandi250 – 2523Combined sources
Beta strandi254 – 2574Combined sources
Helixi277 – 28812Combined sources
Beta strandi292 – 2998Combined sources
Helixi307 – 3093Combined sources
Helixi311 – 3199Combined sources
Turni320 – 3223Combined sources
Beta strandi327 – 3326Combined sources
Helixi346 – 35611Combined sources
Beta strandi359 – 3635Combined sources
Helixi365 – 37612Combined sources
Helixi386 – 3949Combined sources
Helixi396 – 3983Combined sources
Beta strandi399 – 4035Combined sources
Beta strandi405 – 4128Combined sources
Helixi413 – 4153Combined sources
Beta strandi433 – 4408Combined sources
Turni441 – 4444Combined sources
Beta strandi445 – 4506Combined sources
Helixi451 – 46010Combined sources
Beta strandi465 – 4684Combined sources
Helixi471 – 4733Combined sources
Turni474 – 4763Combined sources
Helixi482 – 49110Combined sources
Beta strandi496 – 4983Combined sources
Helixi505 – 51410Combined sources
Beta strandi518 – 5236Combined sources
Helixi524 – 5274Combined sources
Helixi533 – 54210Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1JVNX-ray2.10A/B1-552[»]
1OX4X-ray2.50A/B1-552[»]
1OX5X-ray2.50A/B1-552[»]
1OX6X-ray2.40A/B1-552[»]
ProteinModelPortaliP33734.
SMRiP33734. Positions 1-550.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP33734.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini3 – 218216Glutamine amidotransferase type-1Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni236 – 552317CyclaseAdd
BLAST
Regioni364 – 3652PRFAR binding
Regioni402 – 4043PRFAR binding
Regioni474 – 4752PRFAR binding
Regioni500 – 5012PRFAR binding
Regioni523 – 5242PRFAR binding

Sequence similaritiesi

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

Keywords - Domaini

Glutamine amidotransferase

Phylogenomic databases

HOGENOMiHOG000162393.
InParanoidiP33734.
KOiK01663.
OMAiCIDKDGT.
OrthoDBiEOG79GTGF.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
3.40.50.880. 1 hit.
HAMAPiMF_00278. HisH.
InterProiIPR013785. Aldolase_TIM.
IPR029062. Class_I_gatase-like.
IPR017926. GATASE.
IPR006062. His_biosynth.
IPR004651. HisF.
IPR014640. IGPS_HisHF.
IPR010139. Imidazole-glycPsynth_HisH.
IPR011060. RibuloseP-bd_barrel.
[Graphical view]
PfamiPF00117. GATase. 1 hit.
PF00977. His_biosynth. 1 hit.
[Graphical view]
PIRSFiPIRSF036936. IGPS_HisHF. 1 hit.
SUPFAMiSSF51366. SSF51366. 1 hit.
SSF52317. SSF52317. 1 hit.
TIGRFAMsiTIGR00735. hisF. 1 hit.
TIGR01855. IMP_synth_hisH. 1 hit.
PROSITEiPS51273. GATASE_TYPE_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P33734-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPVVHVIDVE SGNLQSLTNA IEHLGYEVQL VKSPKDFNIS GTSRLILPGV
60 70 80 90 100
GNYGHFVDNL FNRGFEKPIR EYIESGKPIM GICVGLQALF AGSVESPKST
110 120 130 140 150
GLNYIDFKLS RFDDSEKPVP EIGWNSCIPS ENLFFGLDPY KRYYFVHSFA
160 170 180 190 200
AILNSEKKKN LENDGWKIAK AKYGSEEFIA AVNKNNIFAT QFHPEKSGKA
210 220 230 240 250
GLNVIENFLK QQSPPIPNYS AEEKELLMND YSNYGLTRRI IACLDVRTND
260 270 280 290 300
QGDLVVTKGD QYDVREKSDG KGVRNLGKPV QLAQKYYQQG ADEVTFLNIT
310 320 330 340 350
SFRDCPLKDT PMLEVLKQAA KTVFVPLTVG GGIKDIVDVD GTKIPALEVA
360 370 380 390 400
SLYFRSGADK VSIGTDAVYA AEKYYELGNR GDGTSPIETI SKAYGAQAVV
410 420 430 440 450
ISVDPKRVYV NSQADTKNKV FETEYPGPNG EKYCWYQCTI KGGRESRDLG
460 470 480 490 500
VWELTRACEA LGAGEILLNC IDKDGSNSGY DLELIEHVKD AVKIPVIASS
510 520 530 540 550
GAGVPEHFEE AFLKTRADAC LGAGMFHRGE FTVNDVKEYL LEHGLKVRMD

EE
Length:552
Mass (Da):61,068
Last modified:October 1, 1994 - v2
Checksum:i046E11EA5F83ABA3
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti54 – 541G → A in CAA49469 (PubMed:8366040).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X69815 Genomic DNA. Translation: CAA49469.1.
Z36117 Genomic DNA. Translation: CAA85211.1.
BK006936 Genomic DNA. Translation: DAA07364.1.
PIRiS46125.
RefSeqiNP_009807.3. NM_001178596.3.

Genome annotation databases

EnsemblFungiiYBR248C; YBR248C; YBR248C.
GeneIDi852550.
KEGGisce:YBR248C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X69815 Genomic DNA. Translation: CAA49469.1.
Z36117 Genomic DNA. Translation: CAA85211.1.
BK006936 Genomic DNA. Translation: DAA07364.1.
PIRiS46125.
RefSeqiNP_009807.3. NM_001178596.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1JVNX-ray2.10A/B1-552[»]
1OX4X-ray2.50A/B1-552[»]
1OX5X-ray2.50A/B1-552[»]
1OX6X-ray2.40A/B1-552[»]
ProteinModelPortaliP33734.
SMRiP33734. Positions 1-550.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32943. 10 interactions.
DIPiDIP-4222N.
MINTiMINT-488633.

PTM databases

iPTMnetiP33734.

Proteomic databases

MaxQBiP33734.
PeptideAtlasiP33734.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYBR248C; YBR248C; YBR248C.
GeneIDi852550.
KEGGisce:YBR248C.

Organism-specific databases

EuPathDBiFungiDB:YBR248C.
SGDiS000000452. HIS7.

Phylogenomic databases

HOGENOMiHOG000162393.
InParanoidiP33734.
KOiK01663.
OMAiCIDKDGT.
OrthoDBiEOG79GTGF.

Enzyme and pathway databases

UniPathwayiUPA00031; UER00010.
BioCyciYEAST:YBR248C-MONOMER.
BRENDAi4.3.1.B2. 984.
SABIO-RKP33734.

Miscellaneous databases

EvolutionaryTraceiP33734.
PROiP33734.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
3.40.50.880. 1 hit.
HAMAPiMF_00278. HisH.
InterProiIPR013785. Aldolase_TIM.
IPR029062. Class_I_gatase-like.
IPR017926. GATASE.
IPR006062. His_biosynth.
IPR004651. HisF.
IPR014640. IGPS_HisHF.
IPR010139. Imidazole-glycPsynth_HisH.
IPR011060. RibuloseP-bd_barrel.
[Graphical view]
PfamiPF00117. GATase. 1 hit.
PF00977. His_biosynth. 1 hit.
[Graphical view]
PIRSFiPIRSF036936. IGPS_HisHF. 1 hit.
SUPFAMiSSF51366. SSF51366. 1 hit.
SSF52317. SSF52317. 1 hit.
TIGRFAMsiTIGR00735. hisF. 1 hit.
TIGR01855. IMP_synth_hisH. 1 hit.
PROSITEiPS51273. GATASE_TYPE_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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.
    , 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. 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] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF ARG-239; LYS-258 AND LYS-360, BIOPHYSICOCHEMICAL PROPERTIES.
  5. 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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF APOENZYME; IN COMPLEX WITH SUBSTRATE AND SUBSTRATE ANALOG AND IN COMPLEX WITH INHIBITOR.

Entry informationi

Entry nameiHIS5_YEAST
AccessioniPrimary (citable) accession number: P33734
Secondary accession number(s): D6VQP4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: October 1, 1994
Last modified: June 8, 2016
This is version 152 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 11800 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  5. Yeast chromosome II
    Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.