ID   GNT1B_KLULA             Reviewed;         453 AA.
AC   Q6CT96;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 90.
DE   RecName: Full=Glucose N-acetyltransferase 1-B;
DE            EC=2.4.1.-;
DE   AltName: Full=N-acetylglucosaminyltransferase B;
GN   Name=GNT1-B; OrderedLocusNames=KLLA0C14366g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: N-acetylglucosaminyltransferase involved in the Golgi-
CC       specific modification of N-linked glycans. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-
CC       pass type II membrane protein {ECO:0000250}. Vacuole membrane
CC       {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the GNT1 family. {ECO:0000305}.
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DR   EMBL; CR382123; CAH01694.1; -; Genomic_DNA.
DR   RefSeq; XP_452843.1; XM_452843.1.
DR   AlphaFoldDB; Q6CT96; -.
DR   STRING; 28985.XP_452843.1; -.
DR   CAZy; GT8; Glycosyltransferase Family 8.
DR   EnsemblFungi; CAH01694; CAH01694; KLLA0_C14366g.
DR   GeneID; 2892336; -.
DR   KEGG; kla:KLLA0_C14366g; -.
DR   eggNOG; KOG1950; Eukaryota.
DR   HOGENOM; CLU_034860_1_0_1; -.
DR   InParanoid; Q6CT96; -.
DR   OMA; ILPHRVY; -.
DR   Proteomes; UP000000598; Chromosome C.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008375; F:acetylglucosaminyltransferase activity; IEA:InterPro.
DR   GO; GO:0006487; P:protein N-linked glycosylation; IEA:InterPro.
DR   Gene3D; 3.90.550.10; -; 1.
DR   InterPro; IPR030518; GNT1.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   PANTHER; PTHR11183:SF121; PTHR11183:SF121; 1.
DR   SUPFAM; SSF53448; SSF53448; 1.
PE   3: Inferred from homology;
KW   Glycoprotein; Golgi apparatus; Membrane; Reference proteome; Signal-anchor;
KW   Transferase; Transmembrane; Transmembrane helix; Vacuole.
FT   CHAIN           1..453
FT                   /note="Glucose N-acetyltransferase 1-B"
FT                   /id="PRO_0000087530"
FT   TOPO_DOM        1..8
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        9..29
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        30..453
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   MOTIF           187..189
FT                   /note="DXD"
FT   CARBOHYD        108
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        126
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        176
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   453 AA;  53508 MW;  C203F0D204122C28 CRC64;
     MLKRKVRYLL LIVVVFTGII LSVEAIMRFQ LNKNVDYYLK FFDKHKDNIE NMYDPLNIKQ
     IPYSTIDQLY TKRQSEAEPI DWDKFAYVNY ITDFEYLCNT LIQFRKLNDS GSKAKLLALV
     TDTLVNKSKE NKEVEALLNK IKSVSDRVAV TEVGSVIQPN DHTPWSKSLT KLAIFNLTDY
     ERIIYMDNDA IIHDKMDELF FLPSYVKFAA PISYWFVTAD DLRTVSTDTK KLFKTNKLDP
     IEKKLASRVK NSLEIYNHLP NLPQHFYSKS MNFIIDIDGF QKSDNKVNFA THLMVIKPDV
     TMANDIRDNI LPRYLKAKEE YDTDLINEEL YNFKELIYYQ FKIFRKIQYL FKPSVLILPY
     TKYGLLTKSI DDKRQKDLLK NAILGYERKE KDDLIQDAKF IHFSDYPLSK PWFYSNADDI
     QCSKKYSISD ENCQLWKSLY KEYLESRAIC QVN