ID A0A0J0XFI0_9TREE Unreviewed; 185 AA.
AC A0A0J0XFI0;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=UDP-N-acetylglucosamine transferase subunit ALG13 {ECO:0000256|ARBA:ARBA00017468, ECO:0000256|RuleBase:RU362128};
DE EC=2.4.1.141 {ECO:0000256|ARBA:ARBA00012614, ECO:0000256|RuleBase:RU362128};
DE AltName: Full=Asparagine-linked glycosylation protein 13 {ECO:0000256|ARBA:ARBA00032061, ECO:0000256|RuleBase:RU362128};
GN Name=ALG13 {ECO:0000256|RuleBase:RU362128};
GN ORFNames=CC85DRAFT_288149 {ECO:0000313|EMBL:KLT39808.1};
OS Cutaneotrichosporon oleaginosum.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Trichosporonales; Trichosporonaceae; Cutaneotrichosporon.
OX NCBI_TaxID=879819 {ECO:0000313|EMBL:KLT39808.1, ECO:0000313|Proteomes:UP000053611};
RN [1] {ECO:0000313|EMBL:KLT39808.1, ECO:0000313|Proteomes:UP000053611}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBC0246 {ECO:0000313|EMBL:KLT39808.1,
RC ECO:0000313|Proteomes:UP000053611};
RG DOE Joint Genome Institute;
RA Kourist R., Kracht O., Bracharz F., Lipzen A., Nolan M., Ohm R.,
RA Grigoriev I., Sun S., Heitman J., Bruck T., Nowrousian M.;
RT "Genomics and transcriptomics of the oil-accumulating basidiomycete yeast
RT T. oleaginosus allow insights into substrate utilization and the diverse
RT evolutionary trajectories of mating systems in fungi.";
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in protein N-glycosylation. Essential for the second
CC step of the dolichol-linked oligosaccharide pathway.
CC {ECO:0000256|ARBA:ARBA00024804, ECO:0000256|RuleBase:RU362128}.
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; Evidence={ECO:0000256|ARBA:ARBA00000601};
CC -!- SUBUNIT: Heterodimer with ALG14 to form a functional enzyme.
CC {ECO:0000256|ARBA:ARBA00011198, ECO:0000256|RuleBase:RU362128}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000256|ARBA:ARBA00004240, ECO:0000256|RuleBase:RU362128}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 28 family.
CC {ECO:0000256|ARBA:ARBA00006962, ECO:0000256|RuleBase:RU362128}.
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DR EMBL; KQ087248; KLT39808.1; -; Genomic_DNA.
DR RefSeq; XP_018276299.1; XM_018424148.1.
DR AlphaFoldDB; A0A0J0XFI0; -.
DR STRING; 879819.A0A0J0XFI0; -.
DR GeneID; 28984751; -.
DR OrthoDB; 167601at2759; -.
DR Proteomes; UP000053611; Unassembled WGS sequence.
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 Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 1.
DR InterPro; IPR039042; Alg13-like.
DR InterPro; IPR007235; Glyco_trans_28_C.
DR PANTHER; PTHR12867; GLYCOSYL TRANSFERASE-RELATED; 1.
DR PANTHER; PTHR12867:SF6; N-ACETYLGLUCOSAMINYLDIPHOSPHODOLICHOL N-ACETYLGLUCOSAMINYLTRANSFERASE; 1.
DR Pfam; PF04101; Glyco_tran_28_C; 1.
DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|RuleBase:RU362128};
KW Glycosyltransferase {ECO:0000256|RuleBase:RU362128};
KW Reference proteome {ECO:0000313|Proteomes:UP000053611};
KW Transferase {ECO:0000256|RuleBase:RU362128, ECO:0000313|EMBL:KLT39808.1}.
FT DOMAIN 11..173
FT /note="Glycosyl transferase family 28 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF04101"
SQ SEQUENCE 185 AA; 19211 MW; 57DFA33335B76672 CRC64;
MSTQTQTKGK TLLVTVGSTQ FAELSDAVLA ESTIAALRAA GVSTLIVQLG FAPIPAHVAA
VVGREGGKGE VGGLRVEVMR YTGSPGEMDA LMRSADGVVS HAGSGSILAA LRMPRPLLVV
PNDALMDDHQ QELAEALKEG GYLSVSDVDQ LAAGVQEMFG TQHKPFPPAK PERFAAILDE
TAGFV
//
