Q54QG0 (PGFB_DICDI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Dictyostelium discoideum (Slime mold) [Reference proteome]

Taxonomic identifier

44689 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Amoebozoa › Mycetozoa › Dictyosteliida › Dictyostelium

Protein attributes

Sequence length	769 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Molecular function	Glycosyltransferase Transferase
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	protein glycosylation Inferred from direct assay Ref.1Ref.3. Source: dictyBase
Cellular_component	cytoplasm Inferred from direct assay PubMed 8662604. Source: dictyBase
Molecular_function	alpha-(1,2)-fucosyltransferase activity Inferred from mutant phenotype Ref.1. Source: dictyBase galactoside 2-alpha-L-fucosyltransferase activity Inferred from electronic annotation. Source: EC glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase activity Inferred from direct assay Ref.3. Source: dictyBase
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 769	769	Bifunctional glycosyltransferase pgtA		PRO_0000328252
Regions
	Region	25 – 210	186	N-acetylgalactosamine 3-beta-galactosyltransferase
	Region	442 – 769	328	Alpha-1,2-fucosyltransferase
	Compositional bias	151 – 162	12	Poly-Asn
	Compositional bias	409 – 441	33	Poly-Asn
Sites
	Site	53	1	Important for Gal-transferase activity
	Site	226	1	Important for Gal-transferase activity
	Site	509	1	Important for Gal- and Fuc-transferase activities
	Site	654	1	Important for Fuc-transferase activity
Experimental info
	Mutagenesis	53	1	D → N: Loss of Gal-transferase activity. Ref.3
	Mutagenesis	226	1	D → N: Loss of Gal-transferase activity. Ref.3
	Mutagenesis	497	1	D → N: Slight decrease in Gal-transferase activity. Ref.3
	Mutagenesis	509	1	D → N: 39-60% decrease in both Gal- and Fuc-transferase activities. Ref.3
	Mutagenesis	654	1	D → N: Loss of Fuc-transferase activity and 80% decrease in Gal-transferase activity. Ref.3
	Sequence conflict	413	1	Missing in AAF82378. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q54QG0 [UniParc]. Last modified May 24, 2005. Version 1. Checksum: 8BB93A4F528C0D84	FASTA	769	89,838
	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

References

	« Hide 'large scale' referencesShow '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, 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. , 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.
RefSeq	XP_638911.1. XM_633819.1.
3D structure databases
ProteinModelPortal	Q54QG0.
ModBase	Search...
Protein-protein interaction databases
STRING	44689.DDB_0191458.
Protein family/group databases
CAZy	GT2. Glycosyltransferase Family 2. GT74. Glycosyltransferase Family 74.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblProtists	DDB0191458; DDB0191458; DDB_G0283761.
GeneID	8624308.
KEGG	ddi:DDB_G0283761.
Organism-specific databases
dictyBase	DDB_G0283761. pgtA.
Phylogenomic databases
eggNOG	COG0463.
KO	K12245.
OMA	NITYCHT.
Family and domain databases
InterPro	IPR001173. Glyco_trans_2. [Graphical view]
Pfam	PF00535. Glycos_transf_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PGFB_DICDI

Accession

Primary (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:	May 29, 2013
This is version 48 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)