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

Imidazoleglycerol-phosphate dehydratase

Gene

his5

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

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. ATP phosphoribosyltransferase (his1)
  2. Histidine biosynthesis bifunctional protein his7 (his7)
  3. Histidine biosynthesis bifunctional protein his7 (his7)
  4. 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase (SPAC3F10.09)
  5. Imidazole glycerol phosphate synthase hisHF (his4)
  6. Imidazoleglycerol-phosphate dehydratase (his5)
  7. Histidinol-phosphate aminotransferase (his3)
  8. Probable histidinol-phosphatase (SPCC1672.01)
  9. Histidinol dehydrogenase (his2)
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

UniPathwayiUPA00031; UER00011.

Names & Taxonomyi

Protein namesi
Recommended name:
Imidazoleglycerol-phosphate dehydratase (EC:4.2.1.19)
Short name:
IGPD
Gene namesi
Name:his5
ORF Names:SPBC21H7.07c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBC21H7.07c.
PomBaseiSPBC21H7.07c. his5.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: PomBase
  • nucleus Source: PomBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 216216Imidazoleglycerol-phosphate dehydratasePRO_0000158247Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei211 – 2111Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP40374.

PTM databases

iPTMnetiP40374.

Interactioni

Protein-protein interaction databases

BioGridi277200. 7 interactions.
MINTiMINT-4689594.

Structurei

3D structure databases

ProteinModelPortaliP40374.
SMRiP40374. Positions 1-202.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

HOGENOMiHOG000228064.
InParanoidiP40374.
KOiK01693.
OMAiHHIAESC.
OrthoDBiEOG712V6Z.
PhylomeDBiP40374.

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. 2 hits.
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.

P40374-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRRAFVERNT NETKISVAIA LDKAPLPEES NFIDELITSK HANQKGEQVI
60 70 80 90 100
QVDTGIGFLD HMYHALAKHA GWSLRLYSRG DLIIDDHHTA EDTAIALGIA
110 120 130 140 150
FKQAMGNFAG VKRFGHAYCP LDEALSRSVV DLSGRPYAVI DLGLKREKVG
160 170 180 190 200
ELSCEMIPHL LYSFSVAAGI TLHVTCLYGS NDHHRAESAF KSLAVAMRAA
210
TSLTGSSEVP STKGVL
Length:216
Mass (Da):23,520
Last modified:February 1, 1995 - v1
Checksum:i2A30A1126FB1ED32
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U07831 mRNA. Translation: AAA92791.1.
CU329671 Genomic DNA. Translation: CAA18867.1.
PIRiS55077.
RefSeqiNP_595932.1. NM_001021840.2.

Genome annotation databases

EnsemblFungiiSPBC21H7.07c.1; SPBC21H7.07c.1:pep; SPBC21H7.07c.
GeneIDi2540675.
KEGGispo:SPBC21H7.07c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U07831 mRNA. Translation: AAA92791.1.
CU329671 Genomic DNA. Translation: CAA18867.1.
PIRiS55077.
RefSeqiNP_595932.1. NM_001021840.2.

3D structure databases

ProteinModelPortaliP40374.
SMRiP40374. Positions 1-202.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi277200. 7 interactions.
MINTiMINT-4689594.

PTM databases

iPTMnetiP40374.

Proteomic databases

MaxQBiP40374.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBC21H7.07c.1; SPBC21H7.07c.1:pep; SPBC21H7.07c.
GeneIDi2540675.
KEGGispo:SPBC21H7.07c.

Organism-specific databases

EuPathDBiFungiDB:SPBC21H7.07c.
PomBaseiSPBC21H7.07c. his5.

Phylogenomic databases

HOGENOMiHOG000228064.
InParanoidiP40374.
KOiK01693.
OMAiHHIAESC.
OrthoDBiEOG712V6Z.
PhylomeDBiP40374.

Enzyme and pathway databases

UniPathwayiUPA00031; UER00011.

Miscellaneous databases

NextBioi20801799.
PROiP40374.

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. 2 hits.
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. "Characterization of Schizosaccharomyces pombe his1 and his5 cDNAs."
    Erickson F.L., Hannig E.M.
    Yeast 11:157-167(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "DNA sequencing and analysis of a 67.4 kb region from the right arm of Schizosaccharomyces pombe chromosome II reveals 28 open reading frames including the genes his5, pol5, ppa2, rip1, rpb8 and skb1."
    Xiang Z., Lyne M.H., Wood V., Rajandream M.A., Barrell B.G., Aves S.J.
    Yeast 15:893-901(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-211, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiHIS7_SCHPO
AccessioniPrimary (citable) accession number: P40374
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: January 20, 2016
This is version 111 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

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  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.