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Q54QG0 (PGFB_DICDI) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 52. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
Bifunctional glycosyltransferase pgtA
Alternative name(s):
FT85

Including the following 2 domains:

  1. N-acetylglucosamine 3-beta-galactosyltransferase
    EC=2.4.1.-
  2. Alpha-1,2-fucosyltransferase
    EC=2.4.1.69
Gene names
Name:pgtA
Synonyms:fucB
ORF Names:DDB_G0283761
OrganismDictyostelium discoideum (Slime mold) [Reference proteome]
Taxonomic identifier44689 [NCBI]
Taxonomic lineageEukaryotaAmoebozoaMycetozoaDictyosteliidaDictyostelium

Protein attributes

Sequence length769 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Bifunctional protein composed of 2 glycosyltransferase domains involved in glycosylating skp1. The N-terminal part catalyzes the transfer of a galactose residue to GlcNAc-skp1 in a beta 1-3 linkage. The C-terminal part catalyzes the transfer of a fucose residue to Gal-GlgNAc-skp1 in an alpha 1-2 linkage. Ref.3

Catalytic activity

UDP-alpha-D-galactose + alpha-N-acetylglucosamine-R = UDP + beta-D-galactosyl-1,3-alpha-N-acetylglucosamine-R. Ref.1 Ref.3

GDP-beta-L-fucose + beta-D-galactosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide = GDP + alpha-L-fucosyl-(1->2)-beta-D-galactosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide. Ref.1 Ref.3

Sequence similarities

Belongs to the glycosyltransferase 2 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 769769Bifunctional glycosyltransferase pgtA
PRO_0000328252

Regions

Region25 – 210186N-acetylgalactosamine 3-beta-galactosyltransferase
Region442 – 769328Alpha-1,2-fucosyltransferase
Compositional bias151 – 16212Poly-Asn
Compositional bias409 – 44133Poly-Asn

Sites

Site531Important for Gal-transferase activity
Site2261Important for Gal-transferase activity
Site5091Important for Gal- and Fuc-transferase activities
Site6541Important for Fuc-transferase activity

Experimental info

Mutagenesis531D → N: Loss of Gal-transferase activity. Ref.3
Mutagenesis2261D → N: Loss of Gal-transferase activity. Ref.3
Mutagenesis4971D → N: Slight decrease in Gal-transferase activity. Ref.3
Mutagenesis5091D → N: 39-60% decrease in both Gal- and Fuc-transferase activities. Ref.3
Mutagenesis6541D → N: Loss of Fuc-transferase activity and 80% decrease in Gal-transferase activity. Ref.3
Sequence conflict4131Missing in AAF82378. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q54QG0 [UniParc].

Last modified May 24, 2005. Version 1.
Checksum: 8BB93A4F528C0D84

FASTA76989,838
        10         20         30         40         50         60 
MNDSPIISVV LPFLIKDNDD KSLNYQGINN LIISIDSIIE QTFKEWELIL VDDGSNNEIL 

        70         80         90        100        110        120 
EQLLSKRYST DNRIKFIINK ENKGIVKSLN DAILNHCSPT SKYIARMDSD DISHPTRLQS 

       130        140        150        160        170        180 
QLKYLQSNET IDILGCPIKM FNNNKLIEIL NNNNNNNNIN NNVKELINII NNEESFKFIQ 

       190        200        210        220        230        240 
HPDKDILMWS MFFNCCIVHP SVIFKRSIFT IEHCYEENNQ FPFIEDYLFW LKSLIMKGLN 

       250        260        270        280        290        300 
ISNIQSSTPL LYLRKHNNSI SFKNIEKQKD STANASCYYL NILFKRFNID SEIIQNSSLS 

       310        320        330        340        350        360 
MKEIIQFFQL SPSSLSKINN ISIELFEFAF KYLELIEKSC TKQQPNYSNS IKDAANEKMG 

       370        380        390        400        410        420 
ELVSLCLSNY PNNQKSSLLW EKWLSRNPTS QLLSLLSNLN VKSSTTIINN NINNNNNNNN 

       430        440        450        460        470        480 
NNNNNNNNNN NNNNNNNNNN NSILNFISGI NSNKINTPKS NNNKFKENGI RIICFSKDRA 

       490        500        510        520        530        540 
FQLKEYLRTF FKYLKNDDNG NDKFEIIVDV LFTYSNEKFK NSYQLVIESF PQVNFIKEEN 

       550        560        570        580        590        600 
FTDQLINLVQ KTNKLEYVMF SVDDILYYNE FNLKEYCLSL NSEPLALGFY MKLNKNITYC 

       610        620        630        640        650        660 
HTCNQDITIP LNSNTISRTE NNFKYLKWNR NDNDCKKDWN YPWDLCSTIY RCNDIDSIIN 

       670        680        690        700        710        720 
GIVKYYGIRN GINHPNRFEF NGNRPIIQKQ IYQNKPYCLC LSDHYSPMSV VTINRVQDVY 

       730        740        750        760 
DNPIYDQTLS LDDLDQLLYS NKSLNDEKYK ENSLSLNFKS VHIGELFIS 

« Hide

References

« Hide 'large scale' references
[1]"A non-Golgi alpha 1,2-fucosyltransferase that modifies Skp1 in the cytoplasm of Dictyostelium."
van Der Wel H., Morris H.R., Panico M., Paxton T., North S.J., Dell A., Thomson J.M., West C.M.
J. Biol. Chem. 276:33952-33963(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, PROTEIN SEQUENCE OF 146-184; 238-263; 288-302 AND 343-352, IDENTIFICATION BY MASS SPECTROMETRY.
[2]"The genome of the social amoeba Dictyostelium discoideum."
Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N. expand/collapse author list , Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.
Nature 435:43-57(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: AX4.
[3]"A bifunctional diglycosyltransferase forms the Fucalpha1,2Galbeta1,3-disaccharide on Skp1 in the cytoplasm of dictyostelium."
Van Der Wel H., Fisher S.Z., West C.M.
J. Biol. Chem. 277:46527-46534(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY, FUNCTION, MUTAGENESIS OF ASP-53; ASP-226; ASP-497; ASP-509 AND ASP-654.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF279134 Genomic DNA. Translation: AAF82378.1.
AAFI02000057 Genomic DNA. Translation: EAL65495.1.
RefSeqXP_638911.1. XM_633819.1.

3D structure databases

ProteinModelPortalQ54QG0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING44689.DDB_0191458.

Protein family/group databases

CAZyGT2. Glycosyltransferase Family 2.
GT74. Glycosyltransferase Family 74.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblProtistsDDB0191458; DDB0191458; DDB_G0283761.
GeneID8624308.
KEGGddi:DDB_G0283761.

Organism-specific databases

dictyBaseDDB_G0283761. pgtA.

Phylogenomic databases

eggNOGCOG0463.
OMANITYCHT.

Family and domain databases

Gene3D3.90.550.10. 1 hit.
InterProIPR001173. Glyco_trans_2-like.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PfamPF00535. Glycos_transf_2. 1 hit.
[Graphical view]
SUPFAMSSF53448. SSF53448. 2 hits.
ProtoNetSearch...

Entry information

Entry namePGFB_DICDI
AccessionPrimary (citable) accession number: Q54QG0
Secondary accession number(s): Q9NAX6
Entry history
Integrated into UniProtKB/Swiss-Prot: April 8, 2008
Last sequence update: May 24, 2005
Last modified: June 11, 2014
This is version 52 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Dictyostelium discoideum

Dictyostelium discoideum: entries, gene names and cross-references to dictyBase