ID A0A074VJS9_9PEZI Unreviewed; 204 AA.
AC A0A074VJS9;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=M437DRAFT_77131 {ECO:0000313|EMBL:KEQ60773.1};
OS Aureobasidium melanogenum CBS 110374.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX NCBI_TaxID=1043003 {ECO:0000313|EMBL:KEQ60773.1, ECO:0000313|Proteomes:UP000030672};
RN [1] {ECO:0000313|EMBL:KEQ60773.1, ECO:0000313|Proteomes:UP000030672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 110374 {ECO:0000313|EMBL:KEQ60773.1,
RC ECO:0000313|Proteomes:UP000030672};
RX PubMed=24984952;
RA Gostin Ar C., Ohm R.A., Kogej T., Sonjak S., Turk M., Zajc J., Zalar P.,
RA Grube M., Sun H., Han J., Sharma A., Chiniquy J., Ngan C.Y., Lipzen A.,
RA Barry K., Grigoriev I.V., Gunde-Cimerman N.;
RT "Genome sequencing of four Aureobasidium pullulans varieties:
RT biotechnological potential, stress tolerance, and description of new
RT species.";
RL BMC Genomics 15:549-549(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}.
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DR EMBL; KL584841; KEQ60773.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A074VJS9; -.
DR STRING; 1043003.A0A074VJS9; -.
DR HOGENOM; CLU_085408_2_1_1; -.
DR OrthoDB; 167601at2759; -.
DR Proteomes; UP000030672; 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 Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 1.
DR InterPro; IPR007235; Glyco_trans_28_C.
DR PANTHER; PTHR47043; UDP-N-ACETYLGLUCOSAMINE TRANSFERASE SUBUNIT ALG13; 1.
DR PANTHER; PTHR47043:SF1; UDP-N-ACETYLGLUCOSAMINE TRANSFERASE SUBUNIT ALG13; 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|ARBA:ARBA00022824,
KW ECO:0000256|RuleBase:RU362128};
KW Glycosyltransferase {ECO:0000256|RuleBase:RU362128};
KW Reference proteome {ECO:0000313|Proteomes:UP000030672};
KW Transferase {ECO:0000256|RuleBase:RU362128}.
FT DOMAIN 106..174
FT /note="Glycosyl transferase family 28 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF04101"
SQ SEQUENCE 204 AA; 21772 MW; F42FAE55BCB003C7 CRC64;
MSDAPSSRPR KVCFVTIGAT ASFSALIRAT LSSSFCHALE QNHYTDLIVQ YGADGDSLFQ
SLVHDLDADK QHAAVNVSGF GLDTSGLGQY MKLAKTGGDD GGVEGLVVSH AGSGTILHAL
RVDVPLVVVP NSELLDNHQV ELADALADQE YVVHGKLEDL PQALLDAEKL RLRKKAWPPI
NSGTHRQTKG LAAVVDEEMG FLVD
//
