ALG13_CANAL
ID ALG13_CANAL Reviewed; 293 AA.
AC Q5ABE5; A0A1D8PCC1;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 2.
DT 03-AUG-2022, entry version 76.
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=CAALFM_C100810WA;
GN ORFNames=CaO19.13446, CaO19.6025;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(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; CP017623; AOW25778.1; -; Genomic_DNA.
DR RefSeq; XP_718987.2; XM_713894.2.
DR AlphaFoldDB; Q5ABE5; -.
DR SMR; Q5ABE5; -.
DR STRING; 237561.Q5ABE5; -.
DR GeneID; 3639346; -.
DR KEGG; cal:CAALFM_C100810WA; -.
DR CGD; CAL0000194250; orf19.13446.
DR VEuPathDB; FungiDB:C1_00810W_A; -.
DR eggNOG; KOG3349; Eukaryota.
DR HOGENOM; CLU_085408_2_0_1; -.
DR InParanoid; Q5ABE5; -.
DR OrthoDB; 1575485at2759; -.
DR PRO; PR:Q5ABE5; -.
DR Proteomes; UP000000559; Chromosome 1.
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..293
FT /note="UDP-N-acetylglucosamine transferase subunit ALG13"
FT /id="PRO_0000215598"
SQ SEQUENCE 293 AA; 34283 MW; B1758989887C46A8 CRC64;
MFDWRRLKPL RPHQIFFFYT TIQNYSDNGY QYSYKSNQIK SNQIKLNQQQ QTSRQLIRIN
NQLPPSVVLH NIIMKSILIT TGATITFKSL IQIILSPQFL NNLIRLKINK LIIQYGHEIK
NSINLSESFF NETINKYDLI NLFNLEIEET PIGDDDDDEG IRLFKNSDIE ILAFSYSSNI
NKYIENVDLI ISHAGTGSII DCLHLNKPLI VIVNDKLMDN HQLEIAQQFT KLNYCIYYSI
KELEQYVNNN DNNKDSRFWN QLNQLINGEL QLNKLPQTDG SIIETIICEE LEK