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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)DescriptionActionsGraphical viewLength
Active sitei83For GATase activityBy similarity1
Binding sitei83Glutamine (covalent)1
Active sitei193For GATase activityBy similarity1
Active sitei195For GATase activityBy similarity1
Active sitei245Sequence analysis1
Binding sitei332Substrate; via amide nitrogen1
Active sitei404Sequence analysis1
Binding sitei469Substrate1

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)DescriptionActionsGraphical viewLength
Mutagenesisi239R → A, H or K: 1000-fold decrease in catalytic efficiency. Uncoupling of glutaminase activity from the cyclase activity. 1 Publication1
Mutagenesisi258K → A: No activity. Uncoupling of glutaminase activity from the cyclase activity. 1 Publication1
Mutagenesisi258K → R: Small reduction of activity. 1 Publication1
Mutagenesisi360K → A or R: Almost no effect on activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001524761 – 552Imidazole glycerol phosphate synthase hisHFAdd BLAST552

Proteomic databases

MaxQBiP33734.
PRIDEiP33734.

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 interactors.
DIPiDIP-4222N.
MINTiMINT-488633.

Structurei

Secondary structure

1552
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 7Combined sources5
Helixi15 – 23Combined sources9
Beta strandi27 – 33Combined sources7
Helixi34 – 36Combined sources3
Helixi39 – 41Combined sources3
Beta strandi45 – 49Combined sources5
Helixi53 – 62Combined sources10
Helixi66 – 74Combined sources9
Beta strandi79 – 83Combined sources5
Helixi84 – 87Combined sources4
Beta strandi90 – 93Combined sources4
Beta strandi104 – 111Combined sources8
Turni114 – 116Combined sources3
Beta strandi119 – 125Combined sources7
Beta strandi143 – 150Combined sources8
Helixi155 – 163Combined sources9
Beta strandi167 – 173Combined sources7
Beta strandi176 – 184Combined sources9
Beta strandi187 – 193Combined sources7
Helixi194 – 196Combined sources3
Helixi198 – 209Combined sources12
Helixi221 – 227Combined sources7
Helixi232 – 235Combined sources4
Beta strandi240 – 248Combined sources9
Beta strandi250 – 252Combined sources3
Beta strandi254 – 257Combined sources4
Helixi277 – 288Combined sources12
Beta strandi292 – 299Combined sources8
Helixi307 – 309Combined sources3
Helixi311 – 319Combined sources9
Turni320 – 322Combined sources3
Beta strandi327 – 332Combined sources6
Helixi346 – 356Combined sources11
Beta strandi359 – 363Combined sources5
Helixi365 – 376Combined sources12
Helixi386 – 394Combined sources9
Helixi396 – 398Combined sources3
Beta strandi399 – 403Combined sources5
Beta strandi405 – 412Combined sources8
Helixi413 – 415Combined sources3
Beta strandi433 – 440Combined sources8
Turni441 – 444Combined sources4
Beta strandi445 – 450Combined sources6
Helixi451 – 460Combined sources10
Beta strandi465 – 468Combined sources4
Helixi471 – 473Combined sources3
Turni474 – 476Combined sources3
Helixi482 – 491Combined sources10
Beta strandi496 – 498Combined sources3
Helixi505 – 514Combined sources10
Beta strandi518 – 523Combined sources6
Helixi524 – 527Combined sources4
Helixi533 – 542Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP33734.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini3 – 218Glutamine amidotransferase type-1Add BLAST216

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni236 – 552CyclaseAdd BLAST317
Regioni364 – 365PRFAR binding2
Regioni402 – 404PRFAR binding3
Regioni474 – 475PRFAR binding2
Regioni500 – 501PRFAR binding2
Regioni523 – 524PRFAR binding2

Sequence similaritiesi

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

Keywords - Domaini

Glutamine amidotransferase

Phylogenomic databases

HOGENOMiHOG000162393.
InParanoidiP33734.
KOiK01663.
OMAiCIDKDGT.
OrthoDBiEOG092C1DZ2.

Family and domain databases

CDDicd01748. GATase1_IGP_Synthase. 1 hit.
cd04731. HisF. 1 hit.
Gene3Di3.20.20.70. 1 hit.
3.40.50.880. 1 hit.
HAMAPiMF_00278. HisH. 1 hit.
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)DescriptionActionsGraphical viewLength
Sequence conflicti54G → A in CAA49469 (PubMed:8366040).Curated1

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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

PTM databases

iPTMnetiP33734.

Proteomic databases

MaxQBiP33734.
PRIDEiP33734.

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.
OrthoDBiEOG092C1DZ2.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiP33734.
PROiP33734.

Family and domain databases

CDDicd01748. GATase1_IGP_Synthase. 1 hit.
cd04731. HisF. 1 hit.
Gene3Di3.20.20.70. 1 hit.
3.40.50.880. 1 hit.
HAMAPiMF_00278. HisH. 1 hit.
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...

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: November 2, 2016
This is version 156 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.