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Protein

Imidazoleglycerol-phosphate dehydratase

Gene

HIS3

Organism
Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC MYA-565) (Filobasidiella neoformans)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Imidazole glycerol-phosphate dehydratase required for histidine biosynthesis.1 Publication

Catalytic activityi

D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O.1 Publication

Pathwayi: L-histidine biosynthesis

This protein is involved in step 6 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. no protein annotated in this organism
  2. no protein annotated in this organism
  3. no protein annotated in this organism
  4. no protein annotated in this organism
  5. no protein annotated in this organism
  6. Imidazoleglycerol-phosphate dehydratase (HIS3)
  7. no protein annotated in this organism
  8. no protein annotated in this organism
  9. no protein annotated in this organism
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.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Amino-acid biosynthesis, Histidine biosynthesis

Enzyme and pathway databases

BRENDAi4.2.1.19. 1723.
UniPathwayiUPA00031; UER00011.

Names & Taxonomyi

Protein namesi
Recommended name:
Imidazoleglycerol-phosphate dehydratase (EC:4.2.1.19)
Short name:
IGPD
Gene namesi
Name:HIS3
Ordered Locus Names:CNH01620
OrganismiCryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC MYA-565) (Filobasidiella neoformans)
Taxonomic identifieri214684 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaTremellomycetesTremellalesTremellaceaeFilobasidiellaFilobasidiella/Cryptococcus neoformans species complex
Proteomesi
  • UP000002149 Componenti: Chromosome 8

Organism-specific databases

EuPathDBiFungiDB:CNH01620.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 202202Imidazoleglycerol-phosphate dehydratasePRO_0000158236Add
BLAST

Proteomic databases

PaxDbiP0CO22.

Interactioni

Subunit structurei

Homotrimer.

Protein-protein interaction databases

STRINGi214684.XP_572341.1.

Structurei

Secondary structure

1
202
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 117Combined sources
Beta strandi16 – 238Combined sources
Turni27 – 293Combined sources
Beta strandi34 – 374Combined sources
Helixi41 – 5313Combined sources
Beta strandi57 – 648Combined sources
Helixi75 – 8915Combined sources
Beta strandi98 – 1058Combined sources
Beta strandi108 – 1158Combined sources
Beta strandi121 – 1255Combined sources
Beta strandi130 – 1334Combined sources
Helixi139 – 15214Combined sources
Beta strandi155 – 1628Combined sources
Helixi166 – 18520Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RHYX-ray2.30A/B1-202[»]
ProteinModelPortaliP0CO22.
SMRiP0CO22. Positions 2-187.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0CO22.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG3143. Eukaryota.
COG0131. LUCA.
InParanoidiP0CO22.
KOiK01693.
OMAiHHIAESC.
OrthoDBiEOG712V6Z.

Family and domain databases

HAMAPiMF_00076. HisB.
InterProiIPR000807. ImidazoleglycerolP_deHydtase.
IPR020565. ImidazoleglycerP_deHydtase_CS.
IPR020568. Ribosomal_S5_D2-typ_fold.
[Graphical view]
PANTHERiPTHR23133:SF2. PTHR23133:SF2. 1 hit.
PfamiPF00475. IGPD. 1 hit.
[Graphical view]
SUPFAMiSSF54211. SSF54211. 2 hits.
PROSITEiPS00954. IGP_DEHYDRATASE_1. 1 hit.
PS00955. IGP_DEHYDRATASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0CO22-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSERIASVER TTSETHISCT IDLDHIPGVT EQKINVSTGI GFLDHMFTAL
60 70 80 90 100
AKHGGMSLQL QCKGDLHIDD HHTAEDCALA LGEAFKKALG ERKGIKRYGY
110 120 130 140 150
AYAPLDESLS RAVIDISSRP YFMCHLPFTR EKVGDLSTEM VSHLLQSFAF
160 170 180 190 200
AAGVTLHIDS IRGENNHHIA ESAFKALALA IRMAISRTGG DDVPSTKGVL

AL
Length:202
Mass (Da):21,976
Last modified:June 28, 2011 - v1
Checksum:i619E1E6051C116CC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U04329 Genomic DNA. Translation: AAA50951.1.
AE017348 Genomic DNA. Translation: AAW45034.1.
RefSeqiXP_572341.1. XM_572341.1.

Genome annotation databases

EnsemblFungiiAAW45034; AAW45034; CNH01620.
GeneIDi3259352.
KEGGicne:CNH01620.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U04329 Genomic DNA. Translation: AAA50951.1.
AE017348 Genomic DNA. Translation: AAW45034.1.
RefSeqiXP_572341.1. XM_572341.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RHYX-ray2.30A/B1-202[»]
ProteinModelPortaliP0CO22.
SMRiP0CO22. Positions 2-187.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi214684.XP_572341.1.

Proteomic databases

PaxDbiP0CO22.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiAAW45034; AAW45034; CNH01620.
GeneIDi3259352.
KEGGicne:CNH01620.

Organism-specific databases

EuPathDBiFungiDB:CNH01620.

Phylogenomic databases

eggNOGiKOG3143. Eukaryota.
COG0131. LUCA.
InParanoidiP0CO22.
KOiK01693.
OMAiHHIAESC.
OrthoDBiEOG712V6Z.

Enzyme and pathway databases

UniPathwayiUPA00031; UER00011.
BRENDAi4.2.1.19. 1723.

Miscellaneous databases

EvolutionaryTraceiP0CO22.

Family and domain databases

HAMAPiMF_00076. HisB.
InterProiIPR000807. ImidazoleglycerolP_deHydtase.
IPR020565. ImidazoleglycerP_deHydtase_CS.
IPR020568. Ribosomal_S5_D2-typ_fold.
[Graphical view]
PANTHERiPTHR23133:SF2. PTHR23133:SF2. 1 hit.
PfamiPF00475. IGPD. 1 hit.
[Graphical view]
SUPFAMiSSF54211. SSF54211. 2 hits.
PROSITEiPS00954. IGP_DEHYDRATASE_1. 1 hit.
PS00955. IGP_DEHYDRATASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning, sequence analysis and expression of the gene encoding imidazole glycerol phosphate dehydratase in Cryptococcus neoformans."
    Parker A.R., Moore T.D., Edman J.C., Schwab J.M., Davisson V.J.
    Gene 145:135-138(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-26, FUNCTION, CATALYTIC ACTIVITY.
  2. "The genome of the basidiomycetous yeast and human pathogen Cryptococcus neoformans."
    Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D., Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E., Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A., Fox D.S.
    , Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C., Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J., Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A., Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E., Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A., Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W., Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.
    Science 307:1321-1324(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: JEC21 / ATCC MYA-565.
  3. "Crystal structure of imidazole glycerol-phosphate dehydratase: duplication of an unusual fold."
    Sinha S.C., Chaudhuri B.N., Burgner J.W., Yakovleva G., Davisson V.J., Smith J.L.
    J. Biol. Chem. 279:15491-15498(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).

Entry informationi

Entry nameiHIS7_CRYNJ
AccessioniPrimary (citable) accession number: P0CO22
Secondary accession number(s): P40919, Q55J26, Q5KCM8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 28, 2011
Last sequence update: June 28, 2011
Last modified: June 8, 2016
This is version 30 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, 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

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.