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ALG13_ASHGO
ID   ALG13_ASHGO             Reviewed;         203 AA.
AC   Q750J3;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 100.
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=AGL042W;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
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; AE016820; AAS54448.1; -; Genomic_DNA.
DR   RefSeq; NP_986624.1; NM_211686.1.
DR   AlphaFoldDB; Q750J3; -.
DR   SMR; Q750J3; -.
DR   STRING; 33169.AAS54448; -.
DR   EnsemblFungi; AAS54448; AAS54448; AGOS_AGL042W.
DR   GeneID; 4622923; -.
DR   KEGG; ago:AGOS_AGL042W; -.
DR   eggNOG; KOG3349; Eukaryota.
DR   HOGENOM; CLU_085408_2_0_1; -.
DR   InParanoid; Q750J3; -.
DR   OMA; ENKTRWP; -.
DR   Proteomes; UP000000591; Chromosome VII.
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..203
FT                   /note="UDP-N-acetylglucosamine transferase subunit ALG13"
FT                   /id="PRO_0000215596"
SQ   SEQUENCE   203 AA;  21794 MW;  B1BE7EC684D78168 CRC64;
     MSTTTKSKME GPKTVVVTCG ATVPFPGLVN AVLDRRVLAE LAQCGFSRVM VQYGRGFAAE
     FERQVGAAGA VRAACDAEGL EGCDAHAWRW QGLEIIGFAF HAQMESLIGT SAALVVSHAG
     TGSILDALRQ QKPLIVCVNE ALLDNHQEQI ARRFEALGHL WAIRADVDEL AGALARSTRE
     TLAPLPPAYK QGFAELLQDV AHR
 
 
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