ID A0A0V1LUT9_9BILA Unreviewed; 825 AA.
AC A0A0V1LUT9;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 34.
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 Name=cht-1 {ECO:0000313|EMBL:KRZ63269.1};
GN ORFNames=T02_5904 {ECO:0000313|EMBL:KRZ63269.1};
OS Trichinella nativa.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6335 {ECO:0000313|EMBL:KRZ63269.1, ECO:0000313|Proteomes:UP000054721};
RN [1] {ECO:0000313|EMBL:KRZ63269.1, ECO:0000313|Proteomes:UP000054721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS10 {ECO:0000313|EMBL:KRZ63269.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (MAY-2015) 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 glycosyl hydrolase 18 family. Chitinase
CC class II subfamily. {ECO:0000256|ARBA:ARBA00009121}.
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:KRZ63269.1}.
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DR EMBL; JYDW01000002; KRZ63269.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1LUT9; -.
DR STRING; 6335.A0A0V1LUT9; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000054721; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
DR GO; GO:0004568; F:chitinase activity; IEA:UniProt.
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:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0006032; P:chitin catabolic process; IEA:UniProt.
DR GO; GO:0006488; P:dolichol-linked oligosaccharide biosynthetic process; IEA:InterPro.
DR CDD; cd06855; GT_GPT_euk; 1.
DR Gene3D; 3.10.50.10; -; 1.
DR Gene3D; 2.170.140.10; Chitin binding domain; 2.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR002557; Chitin-bd_dom.
DR InterPro; IPR036508; Chitin-bd_dom_sf.
DR InterPro; IPR011583; Chitinase_II.
DR InterPro; IPR029070; Chitinase_insertion_sf.
DR InterPro; IPR001223; Glyco_hydro18_cat.
DR InterPro; IPR001579; Glyco_hydro_18_chit_AS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
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; PF01607; CBM_14; 2.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR Pfam; PF00953; Glycos_transf_4; 1.
DR SMART; SM00494; ChtBD2; 2.
DR SMART; SM00636; Glyco_18; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF54556; Chitinase insertion domain; 1.
DR SUPFAM; SSF57625; Invertebrate chitin-binding proteins; 2.
DR PROSITE; PS50940; CHIT_BIND_II; 2.
DR PROSITE; PS01095; GH18_1; 1.
DR PROSITE; PS51910; GH18_2; 1.
PE 3: Inferred from homology;
KW Chitin-binding {ECO:0000256|ARBA:ARBA00022669};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU000489};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000489};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000054721};
KW Signal {ECO:0000256|SAM:SignalP};
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 SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..825
FT /note="UDP-N-acetylglucosamine--dolichyl-phosphate N-
FT acetylglucosaminephosphotransferase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006882184"
FT TRANSMEM 601..620
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 632..653
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 673..693
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 705..722
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 728..749
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 761..779
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 785..805
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 52..426
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT DOMAIN 471..527
FT /note="Chitin-binding type-2"
FT /evidence="ECO:0000259|PROSITE:PS50940"
FT DOMAIN 558..612
FT /note="Chitin-binding type-2"
FT /evidence="ECO:0000259|PROSITE:PS50940"
SQ SEQUENCE 825 AA; 93826 MW; EB0981F57006B454 CRC64;
MFPTVEKNAL VLIIHTILLC TYEFNPSVST KALGNKYAVF SVGSKSAKTC QYIRGCYFTN
WAQYRTGDAS YMPEHYQPGL CTHIFFAFAK FTDNFIVATT EHNDIQSDNS GLYQRVNKLK
QQDPNLKTLL SVGGYGFGIQ KFQQLARNQY ARSKFVNSLK EFLRRFNFDG VDLDWEYPTS
ADYSHFIILV KDIADAFHYE SVTTGKPKLL LTAAVTGNEQ TAADGYNVQA MARYFDFVNV
MTYDFHGGWE MQTGINSPLY RYSAAVEWAK QWNVADAAEA WFKMGMPREK IVIGFATYGR
GWNLPIGNTD HGIRVGTRAV GPATATTLVQ QTGVAAFYEL CEMLENGARR FWDDESKTPY
LVHDGKWYSY DDPDSYSEKL TWLQNQGYGG AFVWSLDFDD FQGKCTLTNN EKYPLIKMFN
QLLCANAPQS NQTSTRRPLT TFPSTGNNDM LINGSDFDED TDEKLFENFT DKACYNKPPG
FWPDPKNCAE FFLCLDNGIY KMKCPANLHF DPLWRHCTLP ELSGCRRIPK TEPTPTTTTL
ADKRFTSRTT AQPSKGTLFV CDADGFFSNP TNCTQFYRCV GGVAFKFTCP QGLQFNQRHN
LVEFLSGILS ICCMVFLGFA DDVLDLRWRH KLLLPTVASL PLLMVYAATY NSTSIVIPLQ
LQPWFGKVLN IGVLYYVYIG MVAVFCTNAI NIYAGINGLE VGQSVIIAIS ILIFNIVQLV
RLEQECRYHM FSIYFLLPYI ATSLVLLRFN WYPASVFVGD TFCYFSGMLF AVVGILGHFS
KTLMLLFLPQ IFNFIFSLPQ LFRIIPCPRH RLPKYLTSFF VCKFQ
//
