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Protein

Guanosine-diphosphatase

Gene

gdp1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Protein inferred from homologyi

Functioni

After transfer of sugars to endogenous macromolecular acceptors, the enzyme converts nucleoside diphosphates to nucleoside monophosphates which in turn exit the Golgi lumen in a coupled antiporter reaction, allowing entry of additional nucleotide sugar from the cytosol.1 Publication

Catalytic activityi

GDP + H2O = GMP + phosphate.

Cofactori

Protein has several cofactor binding sites:

Pathwayi: protein glycosylation

This protein is involved in the pathway protein glycosylation, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein glycosylation and in Protein modification.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei256 – 2561Proton acceptorBy similarity

GO - Molecular functioni

  • guanosine-diphosphatase activity Source: PomBase
  • metal ion binding Source: UniProtKB-KW
  • uridine-diphosphatase activity Source: PomBase

GO - Biological processi

  • GDP catabolic process Source: PomBase
  • protein N-linked glycosylation Source: PomBase
  • UDP catabolic process Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Calcium, Manganese, Metal-binding

Enzyme and pathway databases

UniPathwayiUPA00378.

Names & Taxonomyi

Protein namesi
Recommended name:
Guanosine-diphosphatase (EC:3.6.1.42)
Short name:
GDPase
Gene namesi
Name:gdp1
ORF Names:SPAC824.08
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC824.08.
PomBaseiSPAC824.08.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1212CytoplasmicSequence analysisAdd
BLAST
Transmembranei13 – 3321Helical; Signal-anchor for type II membrane proteinSequence analysisAdd
BLAST
Topological domaini34 – 556523LumenalSequence analysisAdd
BLAST

GO - Cellular componenti

  • endoplasmic reticulum Source: PomBase
  • Golgi apparatus Source: PomBase
  • Golgi membrane Source: UniProtKB-SubCell
  • integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 556556Guanosine-diphosphatasePRO_0000209918Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi372 – 3721N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiQ9UT35.

Interactioni

Protein-protein interaction databases

BioGridi278325. 21 interactions.
MINTiMINT-4709480.

Family & Domainsi

Sequence similaritiesi

Belongs to the GDA1/CD39 NTPase family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

HOGENOMiHOG000206583.
InParanoidiQ9UT35.
KOiK01526.
OMAiHYEDIEL.
OrthoDBiEOG7QK0PD.
PhylomeDBiQ9UT35.

Family and domain databases

InterProiIPR000407. GDA1_CD39_NTPase.
[Graphical view]
PANTHERiPTHR11782. PTHR11782. 2 hits.
PfamiPF01150. GDA1_CD39. 1 hit.
[Graphical view]
PROSITEiPS01238. GDA1_CD39_NTPASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9UT35-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTPTMKSIAR RKALLIALSI FAVTFILWNG FPGSSNRPLP SSNDEFHYED
60 70 80 90 100
IELPSGYRSE GEVVDLLNPK DELEEPLFSE EPLFPVTTSI PTKTAVSKPK
110 120 130 140 150
IAPTSAAKDV TFSSSIDSDD CSVAYDNSKP VRQYVLMIDA GSTGSRVHVY
160 170 180 190 200
QFNNCNPSPK LEEEFFKMIE PGLSSFAGDP EGAAASLDPL LDYAMENVPE
210 220 230 240 250
EYRRCSPIAV KATAGLRLTG ESEAKAILKS VRQHLENDYP FPIVKDGVSI
260 270 280 290 300
LEGSMEGIYA WITINYLLGT LGGKATHSTV AVMDLGGAST QLVFEPRFAS
310 320 330 340 350
DGESLVDGDH KYVLDYNGEQ YELYQHSHLG YGLKEARKLI HKFVLNNAEA
360 370 380 390 400
LKESLELLGD STSIIHPCLH LNASLTHPDS KSEASEVVFV GPSLAHLSLQ
410 420 430 440 450
CRGIAEKALY KDKNCPVRPC SFNGVHQPKF TETFTDSPIY LISYFYDRMI
460 470 480 490 500
SLGMPSTFTI EDMKYLANSV CSGPTYWQDA FSLTDALKEL KEEPEWCLDL
510 520 530 540 550
NYMISLLSVG YEIPNNRQLH TAKKIDNKEL GWCLGASLSM LSEQNNGWNC

NVKEEI
Length:556
Mass (Da):61,589
Last modified:May 1, 2000 - v1
Checksum:i1D811E3D6A6BBB85
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF465240 Genomic DNA. Translation: AAL69974.1.
CU329670 Genomic DNA. Translation: CAB57338.1.
PIRiT39109.
RefSeqiNP_593447.1. NM_001018880.2.

Genome annotation databases

EnsemblFungiiSPAC824.08.1; SPAC824.08.1:pep; SPAC824.08.
GeneIDi2541834.
KEGGispo:SPAC824.08.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF465240 Genomic DNA. Translation: AAL69974.1.
CU329670 Genomic DNA. Translation: CAB57338.1.
PIRiT39109.
RefSeqiNP_593447.1. NM_001018880.2.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi278325. 21 interactions.
MINTiMINT-4709480.

Proteomic databases

MaxQBiQ9UT35.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC824.08.1; SPAC824.08.1:pep; SPAC824.08.
GeneIDi2541834.
KEGGispo:SPAC824.08.

Organism-specific databases

EuPathDBiFungiDB:SPAC824.08.
PomBaseiSPAC824.08.

Phylogenomic databases

HOGENOMiHOG000206583.
InParanoidiQ9UT35.
KOiK01526.
OMAiHYEDIEL.
OrthoDBiEOG7QK0PD.
PhylomeDBiQ9UT35.

Enzyme and pathway databases

UniPathwayiUPA00378.

Miscellaneous databases

NextBioi20802922.
PROiQ9UT35.

Family and domain databases

InterProiIPR000407. GDA1_CD39_NTPase.
[Graphical view]
PANTHERiPTHR11782. PTHR11782. 2 hits.
PfamiPF01150. GDA1_CD39. 1 hit.
[Graphical view]
PROSITEiPS01238. GDA1_CD39_NTPASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of gdp1+ as encoding a GDPase in the fission yeast Schizosaccharomyces pombe."
    Sanchez R., Franco A., Gacto M., Notario V., Cansado J.
    FEMS Microbiol. Lett. 228:33-38(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, COFACTOR, SUBCELLULAR LOCATION.
    Strain: 972 / ATCC 24843.
  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.
    , 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.

Entry informationi

Entry nameiGDA1_SCHPO
AccessioniPrimary (citable) accession number: Q9UT35
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: May 1, 2000
Last modified: November 11, 2015
This is version 99 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.