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Database: UniProt
Entry: Q4X146_ASPFU
LinkDB: Q4X146_ASPFU
Original site: Q4X146_ASPFU 
ID   Q4X146_ASPFU            Unreviewed;       468 AA.
AC   Q4X146;
DT   05-JUL-2005, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2005, sequence version 1.
DT   24-JAN-2024, entry version 96.
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=AFUA_2G11240 {ECO:0000313|EMBL:EAL93419.1};
OS   Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 /
OS   Af293) (Neosartorya fumigata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=330879 {ECO:0000313|EMBL:EAL93419.1, ECO:0000313|Proteomes:UP000002530};
RN   [1] {ECO:0000313|EMBL:EAL93419.1, ECO:0000313|Proteomes:UP000002530}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100
RC   {ECO:0000313|Proteomes:UP000002530};
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.,
RA   Fedorova N., Fedorova N., Feldblyum T.V., Fischer R., Fosker N., Fraser A.,
RA   Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B., Haas H., Harris D., Horiuchi H.,
RA   Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K.,
RA   Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafon A., Latge J.P.,
RA   Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y.,
RA   Molina M., Monod M., Mouyna I., Mulligan S., Murphy L., O'Neil S.,
RA   Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A.,
RA   Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H.,
RA   Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M.,
RA   Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D.,
RA   Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G.,
RA   Vazquez de Aldana C.R., Weidman J., White O., Woodward J., Yu J.H.,
RA   Fraser C., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.,
RA   Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(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}.
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:EAL93419.1}.
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DR   EMBL; AAHF01000001; EAL93419.1; -; Genomic_DNA.
DR   RefSeq; XP_755457.1; XM_750364.1.
DR   AlphaFoldDB; Q4X146; -.
DR   STRING; 330879.Q4X146; -.
DR   EnsemblFungi; EAL93419; EAL93419; AFUA_2G11240.
DR   GeneID; 3512883; -.
DR   KEGG; afm:AFUA_2G11240; -.
DR   VEuPathDB; FungiDB:Afu2g11240; -.
DR   eggNOG; KOG2788; Eukaryota.
DR   HOGENOM; CLU_029942_1_0_1; -.
DR   InParanoid; Q4X146; -.
DR   OMA; LPHFNAR; -.
DR   OrthoDB; 5481729at2759; -.
DR   UniPathway; UPA00378; -.
DR   PHI-base; PHI:2515; -.
DR   Proteomes; UP000002530; Chromosome 2.
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; IBA:GO_Central.
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:UP000002530};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EAL93419.1};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        15..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        39..61
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        82..106
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        143..162
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        174..195
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        215..236
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        243..262
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        277..298
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        310..334
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   468 AA;  51878 MW;  AC5B25C9E171658B CRC64;
     MNSAYASSLS RRETWRLLVL AGAGIGIIVN SLQGDGAPLI ASIAFSAVAF ALTFSLIRWL
     GPVFMRAGLK GKDMAKPRRP EIPETMGAVC AVVYLLALIF FIPFAFYKDI VAATSGGGNR
     DVVLEIAHVE NGRFLHRFPH SKLASYLSGL LSLQCIVILG IGDDLLDIRW RHKVLIPAFG
     AIPMLIVYFV DFGVTHVVVP VPLQPYLGTF VDLGWLYYVY MAAIAIFCPN AINMLAGING
     VEVAQSLVIA VLLVANDLLY IAPTTPFPHP ATDSHLFSLY FLLPFIGVSV ALLCHNWYPS
     KVFVGDTYCY FAGMVFAVVG ILGHFSKTLL LLFIPQIFNF LYSTPQLFHI IPCPRHRLPK
     FNAMSGLLDA SVTEWTVPPG PLVATGLEIL HRMRLIRITK NEEGEIVEST NLTILNLWLI
     WMGPMREDRL AWHMVMVQTA CGALGLFVRH RLALLVFQQD NRAFRYGV
//
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