ID   ALG13_DEBHA             Reviewed;         212 AA.
AC   Q6BST1;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=UDP-N-acetylglucosamine transferase subunit ALG13;
DE            EC=2.4.1.141;
DE   AltName: Full=Asparagine-linked glycosylation protein 13;
GN   Name=ALG13; OrderedLocusNames=DEHA2D06468g;
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS   / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
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: Involved in protein N-glycosylation. Essential for the second
CC       step of the dolichol-linked oligosaccharide pathway (By similarity).
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N-acetyl-alpha-D-glucosaminyl-diphosphodolichol + UDP-N-
CC         acetyl-alpha-D-glucosamine = H(+) + N,N'-diacetylchitobiosyl
CC         diphosphodolichol + UDP; Xref=Rhea:RHEA:23380, Rhea:RHEA-COMP:9519,
CC         Rhea:RHEA-COMP:9520, ChEBI:CHEBI:15378, ChEBI:CHEBI:57269,
CC         ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:58427;
CC         EC=2.4.1.141;
CC   -!- SUBUNIT: Heterodimer with ALG14 to form a functional enzyme.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 28 family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CR382136; CAG86883.2; -; Genomic_DNA.
DR   RefSeq; XP_458739.2; XM_458739.1.
DR   AlphaFoldDB; Q6BST1; -.
DR   SMR; Q6BST1; -.
DR   STRING; 4959.XP_458739.2; -.
DR   CAZy; GT1; Glycosyltransferase Family 1.
DR   PRIDE; Q6BST1; -.
DR   EnsemblFungi; CAG86883; CAG86883; DEHA2D06468g.
DR   GeneID; 2900986; -.
DR   KEGG; dha:DEHA2D06468g; -.
DR   VEuPathDB; FungiDB:DEHA2D06468g; -.
DR   eggNOG; KOG3349; Eukaryota.
DR   HOGENOM; CLU_085408_2_0_1; -.
DR   InParanoid; Q6BST1; -.
DR   OMA; QYGNEIK; -.
DR   OrthoDB; 1575485at2759; -.
DR   Proteomes; UP000000599; Chromosome D.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0004577; F:N-acetylglucosaminyldiphosphodolichol N-acetylglucosaminyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006488; P:dolichol-linked oligosaccharide biosynthetic process; IEA:InterPro.
DR   InterPro; IPR039042; Alg13-like.
DR   InterPro; IPR007235; Glyco_trans_28_C.
DR   PANTHER; PTHR12867; PTHR12867; 1.
DR   Pfam; PF04101; Glyco_tran_28_C; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum; Glycosyltransferase; Reference proteome;
KW   Transferase.
FT   CHAIN           1..212
FT                   /note="UDP-N-acetylglucosamine transferase subunit ALG13"
FT                   /id="PRO_0000215601"
SQ   SEQUENCE   212 AA;  23838 MW;  1A1E46A9AB4CA7B0 CRC64;
     MTSVLFTSGA TVTFRELIEV ITSYDFIVET IIGNGITRMI VQYGNEIETG TQKHVSEEFY
     RQCVEDKELK QSLQLEVVSG SQNDSNVVTY RSNKYRGFEM VVFPFSNDIG SFISESDVVI
     SHAGTGSIID TLRLEKPLIV VTNDKLMNKH QEEVADELVK LGCCRKMTIE DMKSSQLKDC
     ISEILSGPET FNKLPECSTT EVEGIIYHEL VK