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O59852 (INV1_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 87. 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:
Invertase

EC=3.2.1.26
Alternative name(s):
Beta-fructofuranosidase
Saccharase
Gene names
Name:inv1
ORF Names:SPCC191.11
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length581 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Hydrolysis of terminal non-reducing beta-D-fructofuranoside residues in beta-D-fructofuranosides.

Post-translational modification

Glycosylated; contains 67% carbohydrates. This is composed of equimolar amounts of mannose and galactose. There is also a small amount of glucosamine present. Ref.4

Sequence similarities

Belongs to the glycosyl hydrolase 32 family.

Ontologies

Keywords
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processraffinose catabolic process

Inferred by curator. Source: GeneDB_Spombe

sucrose catabolic process

Inferred from mutant phenotype. Source: GeneDB_Spombe

   Cellular componentextracellular region

Inferred from sequence or structural similarity. Source: GeneDB_Spombe

fungal-type vacuole

Inferred from direct assay. Source: GeneDB_Spombe

   Molecular functionsucrose alpha-glucosidase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Potential
Chain23 – 581559Invertase
PRO_0000033397

Regions

Region94 – 974Substrate binding By similarity
Region158 – 1592Substrate binding By similarity
Region227 – 2282Substrate binding By similarity

Sites

Active site971 By similarity
Binding site1131Substrate By similarity
Binding site2801Substrate By similarity
Binding site3661Substrate By similarity

Amino acid modifications

Glycosylation371N-linked (GlcNAc...) Probable
Glycosylation401N-linked (GlcNAc...) Probable
Glycosylation461N-linked (GlcNAc...) Probable
Glycosylation571N-linked (GlcNAc...) Probable
Glycosylation621N-linked (GlcNAc...) Probable
Glycosylation791N-linked (GlcNAc...) Probable
Glycosylation1681N-linked (GlcNAc...) Probable
Glycosylation1751N-linked (GlcNAc...) Probable
Glycosylation3221N-linked (GlcNAc...) Probable
Glycosylation3991N-linked (GlcNAc...) Probable
Glycosylation4091N-linked (GlcNAc...) Probable
Glycosylation4251N-linked (GlcNAc...) Probable
Glycosylation4461N-linked (GlcNAc...) Probable
Glycosylation4521N-linked (GlcNAc...) Probable
Glycosylation5191N-linked (GlcNAc...) Probable
Glycosylation5691N-linked (GlcNAc...) Probable

Experimental info

Sequence conflict186 – 1894Missing Ref.3
Sequence conflict1901H → Y Ref.3
Sequence conflict1951A → P in BAA13903. Ref.3
Sequence conflict1981Q → L in BAA13903. Ref.3
Sequence conflict2051D → N in BAA13903. Ref.3
Sequence conflict2431I → M in BAA13903. Ref.3
Sequence conflict2461M → L in BAA13903. Ref.3
Sequence conflict2561S → P in BAA13903. Ref.3

Sequences

Sequence LengthMass (Da)Tools
O59852 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 70206A6CD1F27EC4

FASTA58164,407
        10         20         30         40         50         60 
MFLKYILASG ICLVSLLSST NAAPRHLYVK RYPVIYNASN ITEVSNSTTV PPPPFVNTTA 

        70         80         90        100        110        120 
PNGTCLGNYN EYLPSGYYNA TDRPKIHFTP SSGFMNDPNG LVYTGGVYHM FFQYSPKTLT 

       130        140        150        160        170        180 
AGEVHWGHTV SKDLIHWENY PIAIYPDEHE NGVLSLPFSG SAVVDVHNSS GLFSNDTIPE 

       190        200        210        220        230        240 
ERIVLIYTDH WTGVAERQAI AYTTDGGYTF KKYSGNPVLD INSLQFRDPK VIWDFDANRW 

       250        260        270        280        290        300 
VMIVAMSQNY GIAFYSSYDL IHWTELSVFS TSGYLGLQYE CPGMARVPVE GTDEYKWVLF 

       310        320        330        340        350        360 
ISINPGAPLG GSVVQYFVGD WNGTNFVPDD GQTRFVDLGK DFYASALYHS SSANADVIGV 

       370        380        390        400        410        420 
GWASNWQYTN QAPTQVFRSA MTVARKFTLR DVPQNPMTNL TSLIQTPLNV SLLRDETLFT 

       430        440        450        460        470        480 
APVINSSSSL SGSPITLPSN TAFEFNVTLS INYTEGCTTG YCLGRIIIDS DDPYRLQSIS 

       490        500        510        520        530        540 
VDVDFAASTL VINRAKAQMG WFNSLFTPSF ANDIYIYGNV TLYGIVDNGL LELYVNNGEK 

       550        560        570        580 
TYTNDFFFLQ GATPGQISFA AFQGVSFNNV TVTPLKTIWN C 

« Hide

References

« Hide 'large scale' references
[1]"Isolation and characterization of an invertase and its repressor genes from Schizosaccharomyces pombe."
Tanaka N., Ohuchi N., Mukai Y., Osaka Y., Ohtani Y., Tabuchi M., Bhuiyan M.S.A., Fukui H., Harashima S., Takegawa K.
Biochem. Biophys. Res. Commun. 245:246-253(1998) [PubMed: 9535817] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[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: 11859360] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 972 / ATCC 24843.
[3]"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: 9501991] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 88-581.
Strain: PR745.
[4]"Purification and characterization of the invertase from Schizosaccharomyces pombe."
Moreno S., Sanchez Y., Rodriguez L.
Biochem. J. 267:697-702(1990) [PubMed: 2187435] [Abstract]
Cited for: GLYCOSYLATION AT ASN-37; ASN-40; ASN-46; ASN-57; ASN-62; ASN-79; ASN-168; ASN-175; ASN-322; ASN-399; ASN-409; ASN-425; ASN-446; ASN-452; ASN-519 AND ASN-569.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB011433 Genomic DNA. Translation: BAA25684.1.
CU329672 Genomic DNA. Translation: CAB41057.1.
D89242 mRNA. Translation: BAA13903.1.
PIRJE0102.
RefSeqNP_588300.1. NM_001023290.1.

3D structure databases

ProteinModelPortalO59852.
ModBaseSearch...

Protein-protein interaction databases

STRINGO59852.

Protein family/group databases

CAZyGH32. Glycoside Hydrolase Family 32.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPCC191.11.1; SPCC191.11.1:pep; SPCC191.11.
GeneID2539227.
GenomeReviewsGene locus inv1 in contig CU329672_GR.
KEGGspo:SPCC191.11.
NMPDRfig|4896.1.peg.638.

Organism-specific databases

GeneDB_SpombeSPCC191.11.

Phylogenomic databases

eggNOGfuNOG06317.
GeneTreeEFGT00050000003072.
HOGENOMHBG693902.
OMANWQYTNQ.
OrthoDBEOG4V1B86.

Enzyme and pathway databases

BioCycSPOM-XXX-01:SPOM-XXX-01-000226-MONOMER.

Gene expression databases

ArrayExpressO59852.

Family and domain databases

InterProIPR008985. ConA-like_lec_gl.
IPR001362. Glyco_hydro_32.
IPR018053. Glyco_hydro_32_AS.
IPR013148. Glyco_hydro_32_N.
IPR023296. Glyco_hydro_43_beta-prop.
[Graphical view]
Gene3DG3DSA:2.115.10.20. Glyco_hydro_43_beta-prop. 1 hit.
KOK01193.
PfamPF00251. Glyco_hydro_32N. 1 hit.
[Graphical view]
SMARTSM00640. Glyco_32. 1 hit.
[Graphical view]
SUPFAMSSF49899. ConA_like_lec_gl. 1 hit.
SSF75005. Glyco_hydro_43_beta-prop. 1 hit.
PROSITEPS00609. GLYCOSYL_HYDROL_F32. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameINV1_SCHPO
AccessionPrimary (citable) accession number: O59852
Secondary accession number(s): P78891
Entry history
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: August 1, 1998
Last modified: December 14, 2011
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

SIMILARITY comments

Index of protein domains and families