ID   ALG13_CRYNB             Reviewed;         200 AA.
AC   P0CN89; Q55YI6; Q5KLF2;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   25-MAY-2022, entry version 34.
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=CNBB0300;
OS   Cryptococcus neoformans var. neoformans serotype D (strain B-3501A)
OS   (Filobasidiella neoformans).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus neoformans species complex.
OX   NCBI_TaxID=283643;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B-3501A;
RX   PubMed=15653466; DOI=10.1126/science.1103773;
RA   Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA   Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA   Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA   Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA   Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA   Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA   Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA   Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA   Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA   Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT   "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT   neoformans.";
RL   Science 307:1321-1324(2005).
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; AAEY01000006; EAL22809.1; -; Genomic_DNA.
DR   RefSeq; XP_777456.1; XM_772363.1.
DR   AlphaFoldDB; P0CN89; -.
DR   SMR; P0CN89; -.
DR   EnsemblFungi; AAW41985; AAW41985; CNB05490.
DR   EnsemblFungi; EAL22809; EAL22809; CNBB0300.
DR   GeneID; 4934141; -.
DR   KEGG; cnb:CNBB0300; -.
DR   VEuPathDB; FungiDB:CNBB0300; -.
DR   HOGENOM; CLU_085408_2_2_1; -.
DR   Proteomes; UP000001435; Chromosome 2.
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; Transferase.
FT   CHAIN           1..200
FT                   /note="UDP-N-acetylglucosamine transferase subunit ALG13"
FT                   /id="PRO_0000410099"
SQ   SEQUENCE   200 AA;  22241 MW;  C24A865CF7DEA59B CRC64;
     MAHPFTLLVT VGSTLFPSLT SHVLLPTFLS LLQSLGVQRL VVQYGRAELK LQDDVKQTLN
     IDSQGDGIGV WSDNDGDRVR DEKQNGMVVE VMRFTNDFEG LVGKSDAVIS HAGSGSILTV
     LRRAPPIPLL VVPNRSLMDD HQSELADALY KDGYVMVASV EDLEEKVQPF LKIWPSQAKL
     FPETRKEVFR EVVDDLMGYD