ALG13_KLULA
ID ALG13_KLULA Reviewed; 197 AA.
AC Q6CXY0;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 25-MAY-2022, entry version 89.
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=KLLA0A04774g;
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: 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}.
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DR EMBL; CR382121; CAH02797.1; -; Genomic_DNA.
DR RefSeq; XP_451209.1; XM_451209.1.
DR AlphaFoldDB; Q6CXY0; -.
DR SMR; Q6CXY0; -.
DR STRING; 28985.XP_451209.1; -.
DR EnsemblFungi; CAH02797; CAH02797; KLLA0_A04774g.
DR GeneID; 2896531; -.
DR KEGG; kla:KLLA0_A04774g; -.
DR eggNOG; KOG3349; Eukaryota.
DR HOGENOM; CLU_085408_2_0_1; -.
DR InParanoid; Q6CXY0; -.
DR OMA; ENKTRWP; -.
DR Proteomes; UP000000598; Chromosome A.
DR GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR GO; GO:0042406; C:extrinsic component of endoplasmic reticulum membrane; IEA:EnsemblFungi.
DR GO; GO:0043541; C:UDP-N-acetylglucosamine transferase complex; IEA:EnsemblFungi.
DR GO; GO:0042802; F:identical protein binding; IEA:EnsemblFungi.
DR GO; GO:0004577; F:N-acetylglucosaminyldiphosphodolichol N-acetylglucosaminyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006488; P:dolichol-linked oligosaccharide biosynthetic process; IEA:EnsemblFungi.
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..197
FT /note="UDP-N-acetylglucosamine transferase subunit ALG13"
FT /id="PRO_0000215602"
SQ SEQUENCE 197 AA; 22234 MW; 232E9C18DE06AE42 CRC64;
MNNTVLVTCG ATVSFPRLVE TVLDRSVTEK LKVLGYGRIV IQYGRGFSDT FLQLVEKHLG
LFTEKKSCGI KVLDKIENLK VISVDGIEIC GFEFSHDIEK LIANNIDLVI SHAGTGSILD
SLRVGKKLIV VVNDTLMDNH QQLIADKFEQ QKLLWSVHAN TEELLRALDR SENEELLKID
NTYNKQFEKL LYNVAID