ID Q2UEQ3_ASPOR Unreviewed; 465 AA.
AC Q2UEQ3;
DT 24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2006, sequence version 1.
DT 24-JAN-2024, entry version 81.
DE RecName: Full=UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase {ECO:0000256|ARBA:ARBA00017659};
DE EC=2.7.8.15 {ECO:0000256|ARBA:ARBA00013225};
DE AltName: Full=GlcNAc-1-P transferase {ECO:0000256|ARBA:ARBA00029567};
DE AltName: Full=N-acetylglucosamine-1-phosphate transferase {ECO:0000256|ARBA:ARBA00033238};
GN ORFNames=AO090026000526 {ECO:0000313|EMBL:BAE59962.1};
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516 {ECO:0000313|EMBL:BAE59962.1, ECO:0000313|Proteomes:UP000006564};
RN [1] {ECO:0000313|EMBL:BAE59962.1, ECO:0000313|Proteomes:UP000006564}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40 {ECO:0000313|Proteomes:UP000006564};
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a dolichyl phosphate + UDP-N-acetyl-alpha-D-glucosamine = N-
CC acetyl-alpha-D-glucosaminyl-diphosphodolichol + UMP;
CC Xref=Rhea:RHEA:13289, Rhea:RHEA-COMP:9517, Rhea:RHEA-COMP:9519,
CC ChEBI:CHEBI:57683, ChEBI:CHEBI:57705, ChEBI:CHEBI:57865,
CC ChEBI:CHEBI:58427; EC=2.7.8.15;
CC Evidence={ECO:0000256|ARBA:ARBA00034004};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000256|ARBA:ARBA00004922}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004477}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 4 family.
CC {ECO:0000256|ARBA:ARBA00009317}.
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DR EMBL; AP007159; BAE59962.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2UEQ3; -.
DR STRING; 510516.Q2UEQ3; -.
DR EnsemblFungi; BAE59962; BAE59962; AO090026000526.
DR HOGENOM; CLU_029942_1_0_1; -.
DR OMA; LPHFNAR; -.
DR OrthoDB; 5481729at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000006564; Chromosome 3.
DR GO; GO:0043541; C:UDP-N-acetylglucosamine transferase complex; IEA:EnsemblFungi.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0003975; F:UDP-N-acetylglucosamine-dolichyl-phosphate N-acetylglucosaminephosphotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0009060; P:aerobic respiration; IEA:EnsemblFungi.
DR GO; GO:0006488; P:dolichol-linked oligosaccharide biosynthetic process; IEA:EnsemblFungi.
DR CDD; cd06855; GT_GPT_euk; 1.
DR InterPro; IPR000715; Glycosyl_transferase_4.
DR InterPro; IPR033895; GPT.
DR PANTHER; PTHR10571; UDP-N-ACETYLGLUCOSAMINE--DOLICHYL-PHOSPHATE N-ACETYLGLUCOSAMINEPHOSPHOTRANSFERASE; 1.
DR PANTHER; PTHR10571:SF0; UDP-N-ACETYLGLUCOSAMINE--DOLICHYL-PHOSPHATE N-ACETYLGLUCOSAMINEPHOSPHOTRANSFERASE; 1.
DR Pfam; PF00953; Glycos_transf_4; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000006564};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 36..62
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 83..104
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 140..159
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 171..192
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 212..232
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 274..295
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 307..331
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 427..445
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 465 AA; 51732 MW; 3C50B98389198B82 CRC64;
MNSSSLSRKE TWRLLMLVGI CAGILLNTFQ DEGAPLVASI AFTGIVFAVA YSLIKWLGPV
FMKAGLKGRD MAKPKRPEIP ETMGAVCAVV YLLALIFFIP FAFYKDIVAA TSGGGNRDVV
LEVHHVETGR MLHRFPHGRL ASYLSGLLSL QCIVILGLGD DLLDIRWRHK VLIPAFGAIP
MLIVYFVDFG VTQVVVPVPL QPYLGAFVDL GWLYYVYMAA VAIFCPNSIN MLAGINGVEV
AQSLVIAILL IANDALYLAP ITPYPHPATD SHLFSLYFLL PFVGVSLALL LHNWYPSKVF
VGDTYCYFAG MVFAVVGILG HFSKTLLLLF IPQIFNFLYS TPQLFKLIPC PRHRLPKFNA
LTGQLDASVT EWTVPPSPLI AAGLELLHQL RLVRVTKNDH GQIVESTNLT ILNLWLVWMG
PMKENRLAWN MVAVQVVCGL FGLFVRHRLA LLVFREDNRA SWYQL
//
