AGTA_DICDI
ID AGTA_DICDI Reviewed; 648 AA.
AC Q54RP0; Q2LAG6;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 105.
DE RecName: Full=UDP-galactose:fucoside alpha-3-galactosyltransferase;
DE EC=2.4.1.37;
DE AltName: Full=Alpha-GalT1;
DE AltName: Full=Fucosylgalactoside 3-alpha-galactosyltransferase;
DE AltName: Full=Skp1 alpha-3-galactosyltransferase;
GN Name=agtA; Synonyms=GT78; ORFNames=DDB_G0283005;
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], PROTEIN SEQUENCE OF 95-100; 246-251;
RP 336-343; 352-357; 390-397 AND 492-499, FUNCTION, DOMAIN, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=AX3;
RX PubMed=16495217; DOI=10.1074/jbc.m513664200;
RA Ercan A., Panico M., Sutton-Smith M., Dell A., Morris H.R., Matta K.L.,
RA Gay D.F., West C.M.;
RT "Molecular characterization of a novel UDP-galactose:fucoside alpha3-
RT galactosyltransferase that modifies Skp1 in the cytoplasm of
RT Dictyostelium.";
RL J. Biol. Chem. 281:12713-12721(2006).
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 FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, SUBSTRATE
RP SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBCELLULAR LOCATION.
RC STRAIN=AX3;
RX PubMed=15123660; DOI=10.1074/jbc.m313858200;
RA Ketcham C., Wang F., Fisher S.Z., Ercan A., van der Wel H., Locke R.D.,
RA Sirajud-Doulah K., Matta K.L., West C.M.;
RT "Specificity of a soluble UDP-galactose:fucoside alpha1,3-
RT galactosyltransferase that modifies the cytoplasmic glycoprotein Skp1 in
RT Dictyostelium.";
RL J. Biol. Chem. 279:29050-29059(2004).
CC -!- FUNCTION: Specifically catalyzes the transfer of a galactosyl residue
CC to the hydroxyproline-linked saccharide on Skp1 protein (fpaA/fpaB).
CC Catalyzes the formation of a Gal-alpha-1,3-Fuc linkage, leading to Gal-
CC Fuc-Gal-GlcNAc-HyPro143-Skp1. {ECO:0000269|PubMed:15123660,
CC ECO:0000269|PubMed:16495217}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an alpha-L-fucosyl-(1->2)-beta-D-galactosyl derivative + UDP-
CC alpha-D-galactose = an alpha-D-galactosyl-(1->3)-[alpha-L-fucosyl-
CC (1->2)]-beta-D-galactosyl derivative + H(+) + UDP;
CC Xref=Rhea:RHEA:14349, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:66914, ChEBI:CHEBI:140327, ChEBI:CHEBI:140328;
CC EC=2.4.1.37; Evidence={ECO:0000269|PubMed:15123660};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:15123660};
CC Note=Divalent metal cations. Mn(2+) is 4-fold better than Mg(2+).
CC {ECO:0000269|PubMed:15123660};
CC -!- ACTIVITY REGULATION: Stimulated by dithiothreitol (DTT) in vitro.
CC Totally inhibited by EDTA. {ECO:0000269|PubMed:15123660}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.5 uM for UDP-Gal {ECO:0000269|PubMed:15123660};
CC KM=3.8 mM for Fuc-alpha-1-Bn {ECO:0000269|PubMed:15123660};
CC KM=0.84 mM for Fuc-alpha-1,2-Gal-beta-1-Bn
CC {ECO:0000269|PubMed:15123660};
CC KM=0.82 mM for Fuc-alpha-1,2-Gal-beta-1-pNP
CC {ECO:0000269|PubMed:15123660};
CC KM=0.006 mM for Fuc-alpha-1,2-Gal-beta-1,3-GlcNAc-alpha-1-Skp1
CC {ECO:0000269|PubMed:15123660};
CC Note=The catalytic efficiency with the presumed natural substrate
CC Fuc-alpha-1,2-Gal-beta-1,3-GlcNAc-alpha-1-Skp1 is 21-fold and 21000-
CC fold higher than that of the synthetic substrates Fuc-alpha-1,2-Gal-
CC beta-1-pNP and Fuc-alpha-1-Bn, respectively.;
CC pH dependence:
CC Optimum pH is 6.4-7.4. {ECO:0000269|PubMed:15123660};
CC Temperature dependence:
CC Optimum temperature is 37 degrees Celsius.
CC {ECO:0000269|PubMed:15123660};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15123660}.
CC -!- DOMAIN: Consists of two domains: an N-terminal catalytic domain and a
CC C-terminal domain, not required for activity, that is predicted to form
CC a beta-propeller-like protein-protein interaction domain.
CC {ECO:0000269|PubMed:16495217}.
CC -!- DISRUPTION PHENOTYPE: Cells show an accumulation of the non-
CC galactosylated isoform of Skp1 in cells. {ECO:0000269|PubMed:16495217}.
CC -!- MISCELLANEOUS: Not required for growth.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 77 family.
CC {ECO:0000305}.
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DR EMBL; DQ340632; ABC67744.1; -; Genomic_DNA.
DR EMBL; AAFI02000049; EAL65946.1; -; Genomic_DNA.
DR RefSeq; XP_639311.1; XM_634219.1.
DR AlphaFoldDB; Q54RP0; -.
DR SMR; Q54RP0; -.
DR BioGRID; 1248885; 1.
DR STRING; 44689.DDB0231341; -.
DR CAZy; GT77; Glycosyltransferase Family 77.
DR PaxDb; Q54RP0; -.
DR EnsemblProtists; EAL65946; EAL65946; DDB_G0283005.
DR GeneID; 8623882; -.
DR KEGG; ddi:DDB_G0283005; -.
DR dictyBase; DDB_G0283005; agtA.
DR eggNOG; KOG0263; Eukaryota.
DR HOGENOM; CLU_423026_0_0_1; -.
DR InParanoid; Q54RP0; -.
DR OMA; AICNEKP; -.
DR PhylomeDB; Q54RP0; -.
DR Reactome; R-DDI-8951664; Neddylation.
DR Reactome; R-DDI-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SABIO-RK; Q54RP0; -.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q54RP0; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0005737; C:cytoplasm; IDA:dictyBase.
DR GO; GO:0004381; F:fucosylgalactoside 3-alpha-galactosyltransferase activity; IDA:dictyBase.
DR GO; GO:0031154; P:culmination involved in sorocarp development; IMP:dictyBase.
DR GO; GO:0043687; P:post-translational protein modification; IDA:dictyBase.
DR GO; GO:0006486; P:protein glycosylation; IDA:dictyBase.
DR GO; GO:0010265; P:SCF complex assembly; IDA:dictyBase.
DR Gene3D; 2.130.10.10; -; 3.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR005069; Nucl-diP-sugar_transferase.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF03407; Nucleotid_trans; 1.
DR Pfam; PF00400; WD40; 5.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 2.
DR PROSITE; PS50082; WD_REPEATS_2; 5.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Glycosyltransferase; Magnesium;
KW Manganese; Reference proteome; Repeat; Transferase; WD repeat.
FT CHAIN 1..648
FT /note="UDP-galactose:fucoside alpha-3-
FT galactosyltransferase"
FT /id="PRO_0000328554"
FT REPEAT 320..358
FT /note="WD 1"
FT REPEAT 372..420
FT /note="WD 2"
FT REPEAT 422..461
FT /note="WD 3"
FT REPEAT 464..505
FT /note="WD 4"
FT REPEAT 507..546
FT /note="WD 5"
FT REPEAT 556..595
FT /note="WD 6"
FT REPEAT 617..648
FT /note="WD 7"
SQ SEQUENCE 648 AA; 75244 MW; 1A92113B7C48E9D4 CRC64;
MEKKVEYIKE NDKIVLMCNY GFRDMTLNLL KCFEKLSIDK SRYILYCMDD KAYQFFAEFK
GIECQRFSRD DIINSSTSST QLFHDNNTND NKGIYSENAE SYGDIGFRAI CNEKPLVVLD
VLKKGYNVLW TDTDIVWKRD PFIHFYQDIN QENQFTNDDD IDLYVQQDDD DICAGFYFIR
SNQRTIKFIQ DSINFLNPCI DDQIAMRLFL KSQGINIKSK NILLSLSEND KKDKIRYRLL
DKKLFPNGTN YFNLKITQRD NITPFIIHNN CIIGHRSKKD RFIEYGLWYI NDDEIDINSN
INNDDENNKE IKLFKNVLKN HTDIITSINS SDDGKLFTTS IDKSIKIWKF ENTSGNDTDN
GIFKVLKSKY IHKRGGIWST FIFSSNNNNN NDYGFENLLT SSHDKTIQYW DNNLQVIQTF
IGHTGIINQL IVIPNSSYFF TCSDDNTIRQ FDLNNINFKR VFIGHNGWVS SIAINKNLNT
LYSCSNDGTI RFWDINSGRC LNIIKGNQGG WIRKIIYNDN LNQLISGGND GTIKIWSCDN
LNNFNDNQYL LKINTNENSS INDLQFDSDT NLIYCAFENG SLKSFKLTSN NNNNNNNNNN
NNNNTINYSL DKVYQGHLNS SINCIHISKS LNLLFSGGFD KQIKSWDL
