AGLB1_PYRFU
ID AGLB1_PYRFU Reviewed; 967 AA.
AC Q8U4D2;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Dolichyl-phosphooligosaccharide-protein glycotransferase 1;
DE EC=2.4.99.21 {ECO:0000269|PubMed:18046457};
DE AltName: Full=Archaeal glycosylation protein B;
DE Short=AglB-L;
DE Short=AglB-Long;
DE AltName: Full=Oligosaccharyl transferase;
DE Short=OST;
DE Short=OTase;
GN Name=aglB1; OrderedLocusNames=PF0156;
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(1999).
RN [2]
RP COMPOSITION OF LIPID-LINKED OLIGOSACCHARIDE.
RX PubMed=27015803; DOI=10.1074/jbc.m115.713156;
RA Taguchi Y., Fujinami D., Kohda D.;
RT "Comparative analysis of archaeal lipid-linked oligosaccharides that serve
RT as oligosaccharide donors for Asn glycosylation.";
RL J. Biol. Chem. 291:11042-11054(2016).
RN [3] {ECO:0007744|PDB:2ZAG, ECO:0007744|PDB:2ZAI}
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 471-967, FUNCTION, CATALYTIC
RP ACTIVITY, AND COFACTOR.
RX PubMed=18046457; DOI=10.1038/sj.emboj.7601940;
RA Igura M., Maita N., Kamishikiryo J., Yamada M., Obita T., Maenaka K.,
RA Kohda D.;
RT "Structure-guided identification of a new catalytic motif of
RT oligosaccharyltransferase.";
RL EMBO J. 27:234-243(2008).
CC -!- FUNCTION: Oligosaccharyl transferase (OST) that catalyzes the initial
CC transfer of a defined glycan (ManNAcXyl(2)GlcAMan(2)GalNAc in
CC P.furiosus) from the lipid carrier dolichol-monophosphate to an
CC asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent
CC polypeptide chains, the first step in protein N-glycosylation.
CC {ECO:0000269|PubMed:18046457}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an archaeal dolichyl phosphooligosaccharide + [protein]-L-
CC asparagine = an archaeal dolichyl phosphate + a glycoprotein with the
CC oligosaccharide chain attached by N-beta-D-glycosyl linkage to a
CC protein L-asparagine.; EC=2.4.99.21;
CC Evidence={ECO:0000269|PubMed:18046457};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:18046457};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:18046457};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000305|PubMed:18046457}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q2EMT4};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:Q2EMT4}.
CC -!- DOMAIN: Despite low primary sequence conservation between eukaryotic
CC catalytic subunits and bacterial and archaeal single subunit OSTs
CC (ssOST), structural comparison revealed several common motifs at
CC spatially equivalent positions, like the DXD motif 1 on the external
CC loop 1 and the DXD motif 2 on the external loop 2 involved in binding
CC of the metal ion cofactor and the carboxamide group of the acceptor
CC asparagine, the conserved Glu residue of the TIXE/SVSE motif on the
CC external loop 5 involved in catalysis, as well as the WWDYG and the
CC DK/MI motifs in the globular domain that define the binding pocket for
CC the +2 Ser/Thr of the acceptor sequon. In bacterial ssOSTs, an Arg
CC residue was found to interact with a negatively charged side chain at
CC the -2 position of the sequon. This Arg is conserved in bacterial
CC enzymes and correlates with an extended sequon requirement (Asp-X-Asn-
CC X-Ser/Thr) for bacterial N-glycosylation.
CC {ECO:0000250|UniProtKB:O29867}.
CC -!- SIMILARITY: Belongs to the STT3 family. {ECO:0000305}.
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DR EMBL; AE009950; AAL80280.1; -; Genomic_DNA.
DR PDB; 2ZAG; X-ray; 3.00 A; A/B/C/D=471-967.
DR PDB; 2ZAI; X-ray; 2.70 A; A/B/C/D=471-967.
DR PDBsum; 2ZAG; -.
DR PDBsum; 2ZAI; -.
DR AlphaFoldDB; Q8U4D2; -.
DR SMR; Q8U4D2; -.
DR STRING; 186497.PF0156; -.
DR CAZy; GT66; Glycosyltransferase Family 66.
DR PRIDE; Q8U4D2; -.
DR EnsemblBacteria; AAL80280; AAL80280; PF0156.
DR KEGG; pfu:PF0156; -.
DR PATRIC; fig|186497.12.peg.162; -.
DR eggNOG; arCOG02044; Archaea.
DR HOGENOM; CLU_304340_0_0_2; -.
DR OMA; YGYWIES; -.
DR PhylomeDB; Q8U4D2; -.
DR BRENDA; 2.4.99.18; 5243.
DR UniPathway; UPA00378; -.
DR EvolutionaryTrace; Q8U4D2; -.
DR Proteomes; UP000001013; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004576; F:oligosaccharyl transferase activity; IEA:InterPro.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR InterPro; IPR003674; Oligo_trans_STT3.
DR InterPro; IPR041530; OST_IS.
DR InterPro; IPR041152; OST_P2.
DR PANTHER; PTHR13872; PTHR13872; 1.
DR Pfam; PF18246; OST_IS; 1.
DR Pfam; PF18235; OST_P2; 1.
DR Pfam; PF02516; STT3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Glycosyltransferase; Magnesium; Manganese;
KW Membrane; Metal-binding; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..967
FT /note="Dolichyl-phosphooligosaccharide-protein
FT glycotransferase 1"
FT /id="PRO_0000445590"
FT TOPO_DOM 1..21
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 22..42
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 43..112
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 113..133
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 134..135
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 136..156
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 157..165
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 166..186
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 187..193
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 194..214
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 215
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 216..236
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 237..247
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 248..268
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 269
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 270..290
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 291..306
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 307..327
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 328..360
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 361..381
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 382..396
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 397..417
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 418
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 419..439
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 440..453
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 454..474
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 475..967
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT REGION 511..513
FT /note="Interacts with target acceptor peptide in protein
FT substrate"
FT /evidence="ECO:0000250|UniProtKB:O29867"
FT MOTIF 53..55
FT /note="DXD motif 1"
FT /evidence="ECO:0000250|UniProtKB:O29867"
FT MOTIF 165..167
FT /note="DXD motif 2"
FT /evidence="ECO:0000250|UniProtKB:O29867"
FT MOTIF 345..348
FT /note="TIXE motif"
FT /evidence="ECO:0000250|UniProtKB:O29867"
FT MOTIF 511..515
FT /note="WWDYG motif"
FT /evidence="ECO:0000305|PubMed:18046457"
FT MOTIF 571..578
FT /note="DK motif"
FT /evidence="ECO:0000305|PubMed:18046457"
FT BINDING 55
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:O29867"
FT BINDING 165
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:O29867"
FT BINDING 167
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:O29867"
FT BINDING 418
FT /ligand="a glycophospholipid"
FT /ligand_id="ChEBI:CHEBI:24397"
FT /ligand_note="archaeal dolichyl phosphooligosaccharide"
FT /evidence="ECO:0000250|UniProtKB:O29867"
FT BINDING 516
FT /ligand="a glycophospholipid"
FT /ligand_id="ChEBI:CHEBI:24397"
FT /ligand_note="archaeal dolichyl phosphooligosaccharide"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT SITE 55
FT /note="Interacts with target acceptor peptide in protein
FT substrate"
FT /evidence="ECO:0000250|UniProtKB:O29867"
FT SITE 158
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT SITE 348
FT /note="Interacts with target acceptor peptide in protein
FT substrate"
FT /evidence="ECO:0000250|UniProtKB:O29867"
FT SITE 574
FT /note="Interacts with target acceptor peptide in protein
FT substrate"
FT /evidence="ECO:0000250|UniProtKB:O29867"
FT HELIX 491..501
FT /evidence="ECO:0007829|PDB:2ZAI"
FT STRAND 508..510
FT /evidence="ECO:0007829|PDB:2ZAI"
FT HELIX 511..513
FT /evidence="ECO:0007829|PDB:2ZAI"
FT HELIX 514..519
FT /evidence="ECO:0007829|PDB:2ZAI"
FT TURN 520..523
FT /evidence="ECO:0007829|PDB:2ZAI"
FT STRAND 527..529
FT /evidence="ECO:0007829|PDB:2ZAG"
FT HELIX 537..547
FT /evidence="ECO:0007829|PDB:2ZAI"
FT HELIX 551..553
FT /evidence="ECO:0007829|PDB:2ZAI"
FT HELIX 557..560
FT /evidence="ECO:0007829|PDB:2ZAI"
FT STRAND 564..568
FT /evidence="ECO:0007829|PDB:2ZAI"
FT HELIX 569..574
FT /evidence="ECO:0007829|PDB:2ZAI"
FT HELIX 575..581
FT /evidence="ECO:0007829|PDB:2ZAI"
FT HELIX 587..591
FT /evidence="ECO:0007829|PDB:2ZAI"
FT STRAND 603..609
FT /evidence="ECO:0007829|PDB:2ZAI"
FT STRAND 612..615
FT /evidence="ECO:0007829|PDB:2ZAI"
FT TURN 616..619
FT /evidence="ECO:0007829|PDB:2ZAI"
FT STRAND 620..623
FT /evidence="ECO:0007829|PDB:2ZAI"
FT TURN 625..628
FT /evidence="ECO:0007829|PDB:2ZAI"
FT STRAND 630..633
FT /evidence="ECO:0007829|PDB:2ZAI"
FT STRAND 636..639
FT /evidence="ECO:0007829|PDB:2ZAI"
FT STRAND 641..648
FT /evidence="ECO:0007829|PDB:2ZAI"
FT STRAND 651..653
FT /evidence="ECO:0007829|PDB:2ZAI"
FT STRAND 666..670
FT /evidence="ECO:0007829|PDB:2ZAI"
FT STRAND 672..679
FT /evidence="ECO:0007829|PDB:2ZAI"
FT HELIX 680..682
FT /evidence="ECO:0007829|PDB:2ZAI"
FT HELIX 686..692
FT /evidence="ECO:0007829|PDB:2ZAI"
FT HELIX 702..709
FT /evidence="ECO:0007829|PDB:2ZAI"
FT STRAND 710..715
FT /evidence="ECO:0007829|PDB:2ZAI"
FT STRAND 717..724
FT /evidence="ECO:0007829|PDB:2ZAI"
FT STRAND 726..738
FT /evidence="ECO:0007829|PDB:2ZAI"
FT STRAND 740..744
FT /evidence="ECO:0007829|PDB:2ZAI"
FT STRAND 748..759
FT /evidence="ECO:0007829|PDB:2ZAI"
FT STRAND 764..777
FT /evidence="ECO:0007829|PDB:2ZAI"
FT STRAND 779..792
FT /evidence="ECO:0007829|PDB:2ZAI"
FT STRAND 799..805
FT /evidence="ECO:0007829|PDB:2ZAI"
FT STRAND 809..821
FT /evidence="ECO:0007829|PDB:2ZAI"
FT STRAND 846..857
FT /evidence="ECO:0007829|PDB:2ZAI"
FT STRAND 859..874
FT /evidence="ECO:0007829|PDB:2ZAI"
FT STRAND 876..879
FT /evidence="ECO:0007829|PDB:2ZAI"
FT STRAND 887..905
FT /evidence="ECO:0007829|PDB:2ZAI"
FT STRAND 907..917
FT /evidence="ECO:0007829|PDB:2ZAI"
FT HELIX 922..934
FT /evidence="ECO:0007829|PDB:2ZAI"
FT HELIX 935..937
FT /evidence="ECO:0007829|PDB:2ZAI"
FT STRAND 938..962
FT /evidence="ECO:0007829|PDB:2ZAI"
SQ SEQUENCE 967 AA; 108585 MW; 413F6559AF8699ED CRC64;
MVKTQIKEKK KDEKVTIPLP GKIKTVLAFL VVLAFAAYGF YIRHLTAGKY FSDPDTFYHF
EIYKLVLKEG LPRYYPMADA PFGSLIGEPL GLYILPAIFY KIISIFGYNE LEAFLLWPPF
VGFLSVIGVY LLGRKVLNEW AGMWGAIILS VLTANFSRTF SGNARGDGPF MMLFTFSAVL
MLYYLTEENK NKKIIWGTLF VLLAGISTAA WNGSPFGLMV LLGFASFQTI ILFIFGKINE
LREFIKEYYP AYLGILAISY LLTIPGIGKI GGFVRFAFEV FLGLVFLAIV MLYGGKYLNY
SDKKHRFAVV AVIVIAGFAG AYIYVGPKLF TLMGGAYQST QVYETVQELA KTDWGDVKVY
YGVEKPNGIV FFLGLVGAMI VTARYLYKLF KDGRRPHEEL FAITFYVMSI YLLWTAARFL
FLASYAIALM SGVFAGYVLE TVEKMKESIP IKAALGGVIA IMLLLIPLTH GPLLAQSAKS
MRTTEIETSG WEDALKWLRE NTPEYSTATS WWDYGYWIES SLLGQRRASA DGGHARDRDH
ILALFLARDG NISEVDFESW ELNYFLVYLN DWAKFNAISY LGGAITRREY NGDESGRGAV
TTLLPLPRYG EKYVNLYAKV IVDVSNSSVK VTVGDRECDP LMVTFTPSGK TIKGTGTCSD
GNAFPYVLHL TPTIGVLAYY KVATANFIKL AFGVPASTIP GFSDKLFSNF EPVYESGNVI
VYRFTPFGIY KIEENINGTW KQVYNLTPGK HELKLYISAF GRDIENATLY IYAINNEKII
EKIKIAEISH MDYLNEYPIA VNVTLPNATS YRFVLVQKGP IGVLLDAPKV NGEIRSPTNI
LREGESGEIE LKVGVDKDYT ADLYLRATFI YLVRKSGKDN EDYDAAFEPQ MDVFFITKIG
ENIQLKEGEN TVKVRAELPE GVISSYKDEL QRKYGDKLII RGIRVEPVFI AEKEYLMLEV
SASAPHH
