Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P78917 (G6PI_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glucose-6-phosphate isomerase

Short name=GPI
EC=5.3.1.9
Alternative name(s):
Phosphoglucose isomerase
Short name=PGI
Phosphohexose isomerase
Short name=PHI
Gene names
Name:pgi1
ORF Names:SPBC1604.05
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length550 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

D-glucose 6-phosphate = D-fructose 6-phosphate. HAMAP-Rule MF_00473

Pathway

Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 2/4. HAMAP-Rule MF_00473

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00473.

Sequence similarities

Belongs to the GPI family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 550550Glucose-6-phosphate isomerase HAMAP-Rule MF_00473
PRO_0000180577

Sites

Active site3631Proton donor By similarity
Active site3941 By similarity
Active site5161 By similarity

Amino acid modifications

Modified residue4551Phosphothreonine Ref.3

Experimental info

Sequence conflict41S → C in BAA13929. Ref.1
Sequence conflict13 – 142QA → EV in BAA13929. Ref.1
Sequence conflict1681G → A in BAA13929. Ref.1
Sequence conflict1981A → S in BAA13929. Ref.1
Sequence conflict5191A → V in BAA13929. Ref.1
Sequence conflict5361D → Y in BAA13929. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P78917 [UniParc].

Last modified May 30, 2000. Version 2.
Checksum: D882FC8D6C64B793

FASTA55060,884
        10         20         30         40         50         60 
MSFSLASTLP AWQAVQTHYE SVGKHLVLKE LFAKDSSRFE KFSFTFNGLK EEDGPILFDF 

        70         80         90        100        110        120 
SKNLITEETV ELLVKLAKEA NVEGLRDALF AGEHINFTED RAVFHPALRN VSEKPMKVNG 

       130        140        150        160        170        180 
QDVMPGVRKV LRHMKEFSDA VRSGAWKGYT GKPIKSIVNV GIGGSDLGPV MVTEALKPYG 

       190        200        210        220        230        240 
QENLELHFVS NIDGTHLAEA LKKCDPETTL FLIASKTFTT AETCTNAKSA KDWFLASAKD 

       250        260        270        280        290        300 
PSHVAKHFVA LSTNEKEVTA FGISAQNMFE FSDWVGGRYS VWSAIGLSVA LYIGYENFEA 

       310        320        330        340        350        360 
FLSGAHAMDE YFCSTPLEKN IPALAALISI WYSDFFGAQT HLVAPYDQYL HRFPAYLQQL 

       370        380        390        400        410        420 
SMESNGKAIT RSGDMVNYTT GKILWGEPGT NSQHSFFQLI HQGTKLIPAD FLIPIESHNP 

       430        440        450        460        470        480 
IDNNKHHRML FSNFAAQTEA LMLGKTPAEV KAEGTPDEIV PHKTFVGNRP SNSIIAKKIT 

       490        500        510        520        530        540 
PASLGALIAF YEWVTFTEGA VWNINSFDQF GVELGKKLAK NVLAQLETKG DVENHDSSTN 

       550 
GLINLFKNGF 

« Hide

References

[1]"Identification of open reading frames in Schizosaccharomyces pombe cDNAs."
Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.
DNA Res. 4:363-369(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: PR745.
[2]"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. expand/collapse author list , 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.
[3]"Phosphoproteome analysis of fission yeast."
Wilson-Grady J.T., Villen J., Gygi S.P.
J. Proteome Res. 7:1088-1097(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-455, IDENTIFICATION BY MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D89268 mRNA. Translation: BAA13929.1.
CU329671 Genomic DNA. Translation: CAA22338.1.
PIRT39509.
T43196.
RefSeqNP_596635.1. NM_001022556.2.

3D structure databases

ProteinModelPortalP78917.
SMRP78917. Positions 7-548.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid276182. 4 interactions.
MINTMINT-4691541.
STRING4896.SPBC1604.05-1.

Proteomic databases

PaxDbP78917.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPBC1604.05.1; SPBC1604.05.1:pep; SPBC1604.05.
GeneID2539625.
KEGGspo:SPBC1604.05.

Organism-specific databases

PomBaseSPBC1604.05.

Phylogenomic databases

eggNOGCOG0166.
HOGENOMHOG000261371.
KOK01810.
OMALKMHFVS.
OrthoDBEOG7N0CDV.
PhylomeDBP78917.

Enzyme and pathway databases

UniPathwayUPA00109; UER00181.

Family and domain databases

Gene3D1.10.1390.10. 1 hit.
HAMAPMF_00473. G6P_isomerase.
InterProIPR001672. G6P_Isomerase.
IPR023096. G6P_Isomerase_C.
IPR018189. Phosphoglucose_isomerase_CS.
[Graphical view]
PANTHERPTHR11469. PTHR11469. 1 hit.
PfamPF00342. PGI. 1 hit.
[Graphical view]
PRINTSPR00662. G6PISOMERASE.
PROSITEPS00765. P_GLUCOSE_ISOMERASE_1. 1 hit.
PS00174. P_GLUCOSE_ISOMERASE_2. 1 hit.
PS51463. P_GLUCOSE_ISOMERASE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20800781.
PROP78917.

Entry information

Entry nameG6PI_SCHPO
AccessionPrimary (citable) accession number: P78917
Secondary accession number(s): O94371
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: May 30, 2000
Last modified: April 16, 2014
This is version 92 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways