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Database: UniProt
Entry: A0A2T6ZMD7_TUBBO
LinkDB: A0A2T6ZMD7_TUBBO
Original site: A0A2T6ZMD7_TUBBO 
ID   A0A2T6ZMD7_TUBBO        Unreviewed;       456 AA.
AC   A0A2T6ZMD7;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 17.
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=B9Z19DRAFT_1028480 {ECO:0000313|EMBL:PUU76643.1};
OS   Tuber borchii (White truffle).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC   Pezizales; Tuberaceae; Tuber.
OX   NCBI_TaxID=42251 {ECO:0000313|EMBL:PUU76643.1, ECO:0000313|Proteomes:UP000244722};
RN   [1] {ECO:0000313|EMBL:PUU76643.1, ECO:0000313|Proteomes:UP000244722}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tbo3840 {ECO:0000313|EMBL:PUU76643.1,
RC   ECO:0000313|Proteomes:UP000244722};
RG   DOE Joint Genome Institute;
RA   Murat C., Kuo A., Barry K.W., Clum A., Dockter R.B., Fauchery L., Iotti M.,
RA   Kohler A., Labutti K., Lindquist E.A., Lipzen A., Ohm R.A., Wang M.,
RA   Grigoriev I.V., Zambonelli A., Martin F.M.;
RT   "Draft genome sequence of Tuber borchii Vittad., a whitish edible
RT   truffle.";
RL   Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
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:PUU76643.1}.
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DR   EMBL; NESQ01000181; PUU76643.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T6ZMD7; -.
DR   STRING; 42251.A0A2T6ZMD7; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000244722; Unassembled WGS sequence.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
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:0006488; P:dolichol-linked oligosaccharide biosynthetic process; IEA:InterPro.
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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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:UP000244722};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:PUU76643.1};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        7..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        35..57
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        78..102
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        137..156
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        168..192
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        212..231
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        238..257
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        269..287
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        299..317
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   456 AA;  50894 MW;  C1B61308B0906657 CRC64;
     MTQKITTGWF ISLFTLVGAC LGLIWTVFVG DGEPLIASLG FSGIAFSASY CLIVWLGDSF
     KRVGLKGKDI SKADRRELPE TMGAVCAVVY LMCMIVFLPF AFYEYFVTST SGGGNRDATV
     EGVETGRLLH KFPHNKLGEY LSAILSLQSM VILGVADDLF DIRWRHKLFL PVIAAIPMLM
     VYYVDFGVTN IVVPTSLQEY LGTALLDLSW GYYLYMAAIA IFCPNSINIL AGINGIEVSQ
     SIVIGSFIAI NDLLYISVEG HPATDSHLFS LYFLLPFIGV SLALWWHNWY PSKVFVGDTY
     CYFAGMTFAV VGILGHFSKT LLLLFIPQIF NFIYSAPQLF RLVPCPRHRL PRFNARSGLM
     EPSRAPFTKP PKWYIALALT ILEKLRLVQV WRNKEGVIME CSNLTLINLW IVTFGPMRED
     KATMGLMGLQ IACSIIGLLV RHKAALLVFP HDNLSI
//
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