PGFB_DICDI
ID PGFB_DICDI Reviewed; 769 AA.
AC Q54QG0; Q9NAX6;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 83.
DE RecName: Full=Bifunctional glycosyltransferase pgtA;
DE AltName: Full=FT85;
DE Includes:
DE RecName: Full=N-acetylglucosamine 3-beta-galactosyltransferase;
DE EC=2.4.1.- {ECO:0000269|PubMed:11423539, ECO:0000269|PubMed:12244067};
DE Includes:
DE RecName: Full=Alpha-1,2-fucosyltransferase;
DE EC=2.4.1.69 {ECO:0000269|PubMed:11423539};
GN Name=pgtA; Synonyms=fucB; ORFNames=DDB_G0283761;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, PROTEIN SEQUENCE OF
RP 146-184; 238-263; 288-302 AND 343-352, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=11423539; DOI=10.1074/jbc.m102555200;
RA van Der Wel H., Morris H.R., Panico M., Paxton T., North S.J., Dell A.,
RA Thomson J.M., West C.M.;
RT "A non-Golgi alpha 1,2-fucosyltransferase that modifies Skp1 in the
RT cytoplasm of Dictyostelium.";
RL J. Biol. Chem. 276:33952-33963(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [3]
RP CATALYTIC ACTIVITY, FUNCTION, AND MUTAGENESIS OF ASP-53; ASP-226; ASP-497;
RP ASP-509 AND ASP-654.
RX PubMed=12244067; DOI=10.1074/jbc.m208824200;
RA Van Der Wel H., Fisher S.Z., West C.M.;
RT "A bifunctional diglycosyltransferase forms the Fucalpha1,2Galbeta1,3-
RT disaccharide on Skp1 in the cytoplasm of dictyostelium.";
RL J. Biol. Chem. 277:46527-46534(2002).
CC -!- FUNCTION: Bifunctional protein composed of 2 glycosyltransferase
CC domains involved in glycosylating skp1. The N-terminal part catalyzes
CC the transfer of a galactose residue to GlcNAc-skp1 in a beta 1-3
CC linkage. The C-terminal part catalyzes the transfer of a fucose residue
CC to Gal-GlcNAc-skp1 in an alpha 1-2 linkage.
CC {ECO:0000269|PubMed:12244067}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N-acetyl-beta-D-glucosaminyl derivative + UDP-alpha-D-
CC galactose = a beta-D-galactosyl-(1->3)-N-acetyl-beta-D-glucosaminyl
CC derivative + H(+) + UDP; Xref=Rhea:RHEA:53432, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:61631, ChEBI:CHEBI:66914,
CC ChEBI:CHEBI:133506; Evidence={ECO:0000269|PubMed:12244067};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a beta-D-galactosyl-(1->3)-N-acetyl-beta-D-glucosaminyl
CC derivative + GDP-beta-L-fucose = an alpha-L-Fuc-(1->2)-beta-D-Gal-
CC (1->3)-beta-D-GlcNAc derivative + GDP + H(+); Xref=Rhea:RHEA:50664,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189,
CC ChEBI:CHEBI:133506, ChEBI:CHEBI:133509; EC=2.4.1.69;
CC Evidence={ECO:0000269|PubMed:11423539};
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. {ECO:0000305}.
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DR EMBL; AF279134; AAF82378.1; -; Genomic_DNA.
DR EMBL; AAFI02000057; EAL65495.1; -; Genomic_DNA.
DR RefSeq; XP_638911.1; XM_633819.1.
DR AlphaFoldDB; Q54QG0; -.
DR SMR; Q54QG0; -.
DR STRING; 44689.DDB0191458; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR CAZy; GT74; Glycosyltransferase Family 74.
DR PaxDb; Q54QG0; -.
DR EnsemblProtists; EAL65495; EAL65495; DDB_G0283761.
DR GeneID; 8624308; -.
DR KEGG; ddi:DDB_G0283761; -.
DR dictyBase; DDB_G0283761; pgtA.
DR eggNOG; ENOG502S9FF; Eukaryota.
DR HOGENOM; CLU_363472_0_0_1; -.
DR InParanoid; Q54QG0; -.
DR OMA; WSMFFNC; -.
DR PRO; PR:Q54QG0; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0005737; C:cytoplasm; IDA:dictyBase.
DR GO; GO:0031127; F:alpha-(1,2)-fucosyltransferase activity; IMP:dictyBase.
DR GO; GO:0008417; F:fucosyltransferase activity; IDA:dictyBase.
DR GO; GO:0008107; F:galactoside 2-alpha-L-fucosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0016263; F:glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase activity; IDA:dictyBase.
DR GO; GO:0006486; P:protein glycosylation; IDA:dictyBase.
DR GO; GO:0010265; P:SCF complex assembly; IDA:dictyBase.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR001173; Glyco_trans_2-like.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR Pfam; PF00535; Glycos_transf_2; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Glycosyltransferase; Reference proteome;
KW Transferase.
FT CHAIN 1..769
FT /note="Bifunctional glycosyltransferase pgtA"
FT /id="PRO_0000328252"
FT REGION 25..210
FT /note="N-acetylgalactosamine 3-beta-galactosyltransferase"
FT REGION 410..442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 442..769
FT /note="Alpha-1,2-fucosyltransferase"
FT SITE 53
FT /note="Important for Gal-transferase activity"
FT SITE 226
FT /note="Important for Gal-transferase activity"
FT SITE 509
FT /note="Important for Gal- and Fuc-transferase activities"
FT SITE 654
FT /note="Important for Fuc-transferase activity"
FT MUTAGEN 53
FT /note="D->N: Loss of Gal-transferase activity."
FT /evidence="ECO:0000269|PubMed:12244067"
FT MUTAGEN 226
FT /note="D->N: Loss of Gal-transferase activity."
FT /evidence="ECO:0000269|PubMed:12244067"
FT MUTAGEN 497
FT /note="D->N: Slight decrease in Gal-transferase activity."
FT /evidence="ECO:0000269|PubMed:12244067"
FT MUTAGEN 509
FT /note="D->N: 39-60% decrease in both Gal- and Fuc-
FT transferase activities."
FT /evidence="ECO:0000269|PubMed:12244067"
FT MUTAGEN 654
FT /note="D->N: Loss of Fuc-transferase activity and 80%
FT decrease in Gal-transferase activity."
FT /evidence="ECO:0000269|PubMed:12244067"
FT CONFLICT 413
FT /note="Missing (in Ref. 1; AAF82378)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 769 AA; 89838 MW; 8BB93A4F528C0D84 CRC64;
MNDSPIISVV LPFLIKDNDD KSLNYQGINN LIISIDSIIE QTFKEWELIL VDDGSNNEIL
EQLLSKRYST DNRIKFIINK ENKGIVKSLN DAILNHCSPT SKYIARMDSD DISHPTRLQS
QLKYLQSNET IDILGCPIKM FNNNKLIEIL NNNNNNNNIN NNVKELINII NNEESFKFIQ
HPDKDILMWS MFFNCCIVHP SVIFKRSIFT IEHCYEENNQ FPFIEDYLFW LKSLIMKGLN
ISNIQSSTPL LYLRKHNNSI SFKNIEKQKD STANASCYYL NILFKRFNID SEIIQNSSLS
MKEIIQFFQL SPSSLSKINN ISIELFEFAF KYLELIEKSC TKQQPNYSNS IKDAANEKMG
ELVSLCLSNY PNNQKSSLLW EKWLSRNPTS QLLSLLSNLN VKSSTTIINN NINNNNNNNN
NNNNNNNNNN NNNNNNNNNN NSILNFISGI NSNKINTPKS NNNKFKENGI RIICFSKDRA
FQLKEYLRTF FKYLKNDDNG NDKFEIIVDV LFTYSNEKFK NSYQLVIESF PQVNFIKEEN
FTDQLINLVQ KTNKLEYVMF SVDDILYYNE FNLKEYCLSL NSEPLALGFY MKLNKNITYC
HTCNQDITIP LNSNTISRTE NNFKYLKWNR NDNDCKKDWN YPWDLCSTIY RCNDIDSIIN
GIVKYYGIRN GINHPNRFEF NGNRPIIQKQ IYQNKPYCLC LSDHYSPMSV VTINRVQDVY
DNPIYDQTLS LDDLDQLLYS NKSLNDEKYK ENSLSLNFKS VHIGELFIS
