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Database: UniProt
Entry: Q2U8A9_ASPOR
LinkDB: Q2U8A9_ASPOR
Original site: Q2U8A9_ASPOR 
ID   Q2U8A9_ASPOR            Unreviewed;       477 AA.
AC   Q2U8A9;
DT   24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT   24-JAN-2006, sequence version 1.
DT   27-MAR-2024, entry version 66.
DE   RecName: Full=N-acetylgalactosaminide beta-1,3-galactosyltransferase {ECO:0000256|ARBA:ARBA00012557};
DE            EC=2.4.1.122 {ECO:0000256|ARBA:ARBA00012557};
GN   ORFNames=AO090701000504 {ECO:0000313|EMBL:BAE62206.1};
OS   Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=510516 {ECO:0000313|EMBL:BAE62206.1, ECO:0000313|Proteomes:UP000006564};
RN   [1] {ECO:0000313|EMBL:BAE62206.1, ECO:0000313|Proteomes:UP000006564}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42149 / RIB 40 {ECO:0000313|Proteomes:UP000006564};
RX   PubMed=16372010; DOI=10.1038/nature04300;
RA   Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA   Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA   Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA   Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA   Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA   Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA   Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA   Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA   Takahashi M., Takase K., Terabayashi Y., Wortman J., Yamada O.,
RA   Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA   Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA   Kikuchi H.;
RT   "Genome sequencing and analysis of Aspergillus oryzae.";
RL   Nature 438:1157-1161(2005).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an N-acetyl-alpha-D-galactosaminyl derivative + UDP-alpha-D-
CC         galactose = a beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-
CC         galactosaminyl derivative + H(+) + UDP; Xref=Rhea:RHEA:15621,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:28257, ChEBI:CHEBI:58223,
CC         ChEBI:CHEBI:66914, ChEBI:CHEBI:133470; EC=2.4.1.122;
CC         Evidence={ECO:0000256|ARBA:ARBA00000862};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000256|ARBA:ARBA00004922}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-
CC       pass type II membrane protein {ECO:0000256|ARBA:ARBA00004606}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 31 family. Beta3-Gal-T
CC       subfamily. {ECO:0000256|ARBA:ARBA00006462}.
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DR   EMBL; AP007164; BAE62206.1; -; Genomic_DNA.
DR   RefSeq; XP_001823339.1; XM_001823287.1.
DR   AlphaFoldDB; Q2U8A9; -.
DR   STRING; 510516.Q2U8A9; -.
DR   CAZy; GT31; Glycosyltransferase Family 31.
DR   EnsemblFungi; BAE62206; BAE62206; AO090701000504.
DR   GeneID; 5995396; -.
DR   KEGG; aor:AO090701000504; -.
DR   VEuPathDB; FungiDB:AO090701000504; -.
DR   HOGENOM; CLU_022549_0_0_1; -.
DR   OMA; CATFPKH; -.
DR   OrthoDB; 2949690at2759; -.
DR   Proteomes; UP000006564; Chromosome 5.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016757; F:glycosyltransferase activity; IEA:InterPro.
DR   Gene3D; 3.90.550.50; -; 1.
DR   InterPro; IPR026050; C1GALT1/C1GALT1_chp1.
DR   InterPro; IPR003378; Fringe-like_glycosylTrfase.
DR   InterPro; IPR003609; Pan_app.
DR   PANTHER; PTHR23033:SF43; -; 1.
DR   PANTHER; PTHR23033; BETA1,3-GALACTOSYLTRANSFERASE; 1.
DR   Pfam; PF02434; Fringe; 1.
DR   Pfam; PF00024; PAN_1; 1.
PE   3: Inferred from homology;
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006564};
KW   Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   DOMAIN          188..284
FT                   /note="Fringe-like glycosyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF02434"
FT   DOMAIN          392..428
FT                   /note="Apple"
FT                   /evidence="ECO:0000259|Pfam:PF00024"
SQ   SEQUENCE   477 AA;  54638 MW;  8196BFF887C6E91E CRC64;
     MARIILSRKT TNLLVFILFV VIVASVFKIS VPDTSLDPAT LYHHATGHDK NEPDYWEWET
     TTRFAPIKNQ FTASSSADDD HLCDSFPTYV LSRIQVVLKI GASEPADRVD AQISTVTRCI
     PNLLIVSDRE SELKGHRVHD ILATLPESFR FNVTDLEPYE ALRRGDEKAV GSNEGWYLDR
     FKFLPMVERA HETNPTAQWY VFLESDTYYV WDNLFRLLDQ YDPSEPLYFG SPSPGREISQ
     GKPMYFAYGG AGFVLSGGAM KKMVHRHHGS MGECIEPSLS LQYEDIVKGD CCGDSVLGWV
     LYQKGVKLSG LWPMFNPHPL HSIPFDNAYW CQPVISMHKT MLSDMKGLIE WENQRDRKKP
     LLYADLFEYT RMGTFESKPD WDNGDWGGFR EPDESPAHMS MEACRTACHE HAECLSYTYD
     HSGHCILVRT MRLGHSKPPT NEVRLSAGWD VSKMRNWRAS HQCEKPMWVK PSITRIF
//
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