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Protein

UDP-glucose 4-epimerase uge1

Gene

uge1

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

Major UDP-glucose/-galactose 4-epimerase under glucose-rich conditions involved in protein galactosylation.1 Publication

Catalytic activityi

UDP-alpha-D-glucose = UDP-alpha-D-galactose.1 Publication

Cofactori

NAD+By similarity

Pathwayi: galactose metabolism

This protein is involved in the pathway galactose metabolism, which is part of Carbohydrate metabolism.
View all proteins of this organism that are known to be involved in the pathway galactose metabolism and in Carbohydrate metabolism.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi8 – 3932NADBy similarityAdd
BLAST

GO - Molecular functioni

  • UDP-glucose 4-epimerase activity Source: PomBase

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Carbohydrate metabolism, Galactose metabolism

Keywords - Ligandi

NAD

Enzyme and pathway databases

BRENDAi5.1.3.2. 5613.
ReactomeiR-SPO-70370. Galactose catabolism.
UniPathwayiUPA00214.

Names & Taxonomyi

Protein namesi
Recommended name:
UDP-glucose 4-epimerase uge1 (EC:5.1.3.2)
Alternative name(s):
Galactowaldenase
Gene namesi
Name:uge1
ORF Names:SPBC365.14c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBC365.14c.
PomBaseiSPBC365.14c. uge1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Disruption phenotypei

Leads to sensitivity to thiabendazole and microtubule-depolymerizing drugs.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 355355UDP-glucose 4-epimerase uge1PRO_0000318143Add
BLAST

Proteomic databases

MaxQBiQ9Y7X5.

Interactioni

Protein-protein interaction databases

BioGridi277454. 21 interactions.

Structurei

3D structure databases

ProteinModelPortaliQ9Y7X5.
SMRiQ9Y7X5. Positions 7-351.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

HOGENOMiHOG000168001.
InParanoidiQ9Y7X5.
KOiK01784.
OMAiSDPSWNI.
OrthoDBiEOG77T1F2.
PhylomeDBiQ9Y7X5.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR005886. GalE.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF16363. GDP_Man_Dehyd. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR01179. galE. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9Y7X5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTGVHEGTVL VTGGAGYIGS HTCVVLLEKG YDVVIVDNLC NSRVEAVHRI
60 70 80 90 100
EKLTGKKVIF HQVDLLDEPA LDKVFANQNI SAVIHFAGLK AVGESVQVPL
110 120 130 140 150
SYYKNNISGT INLIECMKKY NVRDFVFSSS ATVYGDPTRP GGTIPIPESC
160 170 180 190 200
PREGTSPYGR TKLFIENIIE DETKVNKSLN AALLRYFNPG GAHPSGELGE
210 220 230 240 250
DPLGIPNNLL PYIAQVAVGR LDHLNVFGDD YPTSDGTPIR DYIHVCDLAE
260 270 280 290 300
AHVAALDYLR QHFVSCRPWN LGSGTGSTVF QVLNAFSKAV GRDLPYKVTP
310 320 330 340 350
RRAGDVVNLT ANPTRANEEL KWKTSRSIYE ICVDTWRWQQ KYPYGFDLTH

TKTYK
Length:355
Mass (Da):39,234
Last modified:November 1, 1999 - v1
Checksum:iF8B24D00CD7AF7E3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAB44766.1.
PIRiT40321.
RefSeqiNP_596043.1. NM_001021953.2.

Genome annotation databases

EnsemblFungiiSPBC365.14c.1; SPBC365.14c.1:pep; SPBC365.14c.
GeneIDi2540938.
KEGGispo:SPBC365.14c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAB44766.1.
PIRiT40321.
RefSeqiNP_596043.1. NM_001021953.2.

3D structure databases

ProteinModelPortaliQ9Y7X5.
SMRiQ9Y7X5. Positions 7-351.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi277454. 21 interactions.

Proteomic databases

MaxQBiQ9Y7X5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBC365.14c.1; SPBC365.14c.1:pep; SPBC365.14c.
GeneIDi2540938.
KEGGispo:SPBC365.14c.

Organism-specific databases

EuPathDBiFungiDB:SPBC365.14c.
PomBaseiSPBC365.14c. uge1.

Phylogenomic databases

HOGENOMiHOG000168001.
InParanoidiQ9Y7X5.
KOiK01784.
OMAiSDPSWNI.
OrthoDBiEOG77T1F2.
PhylomeDBiQ9Y7X5.

Enzyme and pathway databases

UniPathwayiUPA00214.
BRENDAi5.1.3.2. 5613.
ReactomeiR-SPO-70370. Galactose catabolism.

Miscellaneous databases

PROiQ9Y7X5.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR005886. GalE.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF16363. GDP_Man_Dehyd. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR01179. galE. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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.
  2. "Global fitness profiling of fission yeast deletion strains by barcode sequencing."
    Han T.X., Xu X.Y., Zhang M.J., Peng X., Du L.L.
    Genome Biol. 11:R60.1-R60.13(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  3. "Characterization of two different types of UDP-glucose/-galactose 4-epimerase involved in galactosylation in fission yeast."
    Suzuki S., Matsuzawa T., Nukigi Y., Takegawa K., Tanaka N.
    Microbiology 156:708-718(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY.

Entry informationi

Entry nameiUGE1_SCHPO
AccessioniPrimary (citable) accession number: Q9Y7X5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: November 1, 1999
Last modified: June 8, 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.