ID G0SUI4_RHOT2 Unreviewed; 191 AA.
AC G0SUI4;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 22-FEB-2023, entry version 29.
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=RTG_00091 {ECO:0000313|EMBL:EGU13654.1};
OS Rhodosporidium toruloides (strain ATCC 204091 / IIP 30 / MTCC 1151) (Yeast)
OS (Rhodotorula glutinis (strain ATCC 204091)).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=1001064 {ECO:0000313|EMBL:EGU13654.1, ECO:0000313|Proteomes:UP000006141};
RN [1] {ECO:0000313|EMBL:EGU13654.1, ECO:0000313|Proteomes:UP000006141}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204091 / IIP 30 / MTCC 1151
RC {ECO:0000313|Proteomes:UP000006141};
RX PubMed=24526636; DOI=10.1128/genomeA.00046-14;
RA Paul D., Magbanua Z., Arick M.II., French T., Bridges S.M., Burgess S.C.,
RA Lawrence M.L.;
RT "Genome sequence of the oleaginous yeast Rhodotorula glutinis ATCC
RT 204091.";
RL Genome Announc. 2:E0004614-E0004614(2014).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EGU13654.1}.
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DR EMBL; AEVR02000026; EGU13654.1; -; Genomic_DNA.
DR AlphaFoldDB; G0SUI4; -.
DR HOGENOM; CLU_085408_2_2_1; -.
DR InParanoid; G0SUI4; -.
DR Proteomes; UP000006141; 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:UP000006141};
KW Transferase {ECO:0000256|RuleBase:RU362128, ECO:0000313|EMBL:EGU13654.1}.
FT DOMAIN 4..96
FT /note="Glycosyl transferase family 28 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF04101"
SQ SEQUENCE 191 AA; 20883 MW; 8D0C569FC2595BD9 CRC64;
MPSTCVLTVG STRFDPLVAS FLDPTSLSSL SSLGIQHVLA QVGNSSLPEG WKEGTRMTEQ
GLQVEVVRFL GDLEERVGRA DLVVSHAGAG SILSFLRPLN SSSPSSSAER TRRQLVLIPN
STLMDSHQSD LADEMEKKGW AVVCRRPEDL PATLKQLASR AEQQGEMPAP DYPELYKGRM
QRIIDETLGY V
//