ID A0A061HKB4_BLUGR Unreviewed; 477 AA.
AC A0A061HKB4;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 24-JAN-2024, entry version 30.
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=BGT96224_1147 {ECO:0000313|EMBL:EPQ67196.1},
GN BGT96224V2_LOCUS30 {ECO:0000313|EMBL:SUZ07605.1};
OS Blumeria graminis f. sp. tritici 96224.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Erysiphales; Erysiphaceae; Blumeria.
OX NCBI_TaxID=1268274 {ECO:0000313|EMBL:SUZ07605.1};
RN [1] {ECO:0000313|Proteomes:UP000053110}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=96224 {ECO:0000313|Proteomes:UP000053110};
RX PubMed=23852167; DOI=10.1038/ng.2704;
RA Wicker T., Oberhaensli S., Parlange F., Buchmann J.P., Shatalina M.,
RA Roffler S., Ben-David R., Dolezel J., Simkova H., Schulze-Lefert P.,
RA Spanu P.D., Bruggmann R., Amselem J., Quesneville H.,
RA Ver Loren van Themaat E., Paape T., Shimizu K.K., Keller B.;
RT "The wheat powdery mildew genome shows the unique evolution of an obligate
RT biotroph.";
RL Nat. Genet. 45:1092-1096(2013).
RN [2] {ECO:0000313|EMBL:EPQ67196.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=96224 {ECO:0000313|EMBL:EPQ67196.1};
RA Oberhaensli S., Wicker T., Keller B.;
RT "The wheat powdery mildew genome reveals unique evolution of an obligate
RT biotroph.";
RL Submitted (JAN-2013) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:SUZ07605.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=96224 {ECO:0000313|EMBL:SUZ07605.1};
RA Quirk P.G., Krulwich T.A.;
RL Submitted (JUL-2018) 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}.
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DR EMBL; KE373804; EPQ67196.1; -; Genomic_DNA.
DR EMBL; UIGY01000001; SUZ07605.1; -; Genomic_DNA.
DR HOGENOM; CLU_029942_1_0_1; -.
DR OrthoDB; 5481729at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000053110; Unassembled WGS sequence.
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:UP000053110};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EPQ67196.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 28..46
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 52..74
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 95..115
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 189..218
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 230..250
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 262..278
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 290..308
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 320..338
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 344..364
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 447..470
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 477 AA; 53154 MW; E55103813C5573AC CRC64;
MPASLPTGKS EYPHKFAVAS ELSINESACL ASLSVACLAI IANAFCSDGK PLVASLAFSG
LAFSMSFSMI RWLGPTFVQA GLKGKDMSKL RPKELPETMG AVCAVVYLLV VIVFIPLPFY
KDIVAATSGG GNRDIVVELD LESVHTGRLL HKFPHSKLAS YLSAILSLQS VSILGFCDDL
FNIRWRHKFF IPGIASIPML IVYFVDFGVT QIVVPIPFRP YLGGLYDLGV FYYIYMFAVA
IFCPNSINIL AGINGIEVSQ SLVIALLLVL NDCLYLLVPY QHPATDSHLF SLYIILPFVG
VSLALWWHNR YPSRVFVGDT YCYFAGMVFV VVGVLGHFSK TLLLLFIPQI FNFIYSVPQL
FHIVPCPRHR LPRFNALTGL MEFSVVKWER APSAPITIMV KLLHNFHLVH INTDSNGVIT
QSSNFTLLNL WLFWFGPKRE DKLTREIILL QCLIGLMGLF VRHNCALLIF ESDNLGV
//
