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   27-MAR-2024, entry version 89.
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 (Social amoeba).
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.Q54QG0; -.
DR   CAZy; GT2; Glycosyltransferase Family 2.
DR   CAZy; GT74; Glycosyltransferase Family 74.
DR   PaxDb; 44689-DDB0191458; -.
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:0010265; P:SCF complex assembly; IDA:dictyBase.
DR   InterPro; IPR001173; Glyco_trans_2-like.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   PANTHER; PTHR22916:SF69; BIFUNCTIONAL GLYCOSYLTRANSFERASE PGTA; 1.
DR   PANTHER; PTHR22916; GLYCOSYLTRANSFERASE; 1.
DR   Pfam; PF00535; Glycos_transf_2; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 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
FT                   Fuc-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
//