AGLB1_PYRHO
ID AGLB1_PYRHO Reviewed; 976 AA.
AC O74088;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Dolichyl-phosphooligosaccharide-protein glycotransferase 1;
DE EC=2.4.99.21;
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=PH0242;
OS Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS 100139 / OT-3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=70601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT "Complete sequence and gene organization of the genome of a hyper-
RT thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL DNA Res. 5:55-76(1998).
RN [2] {ECO:0007744|PDB:3VU1}
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 482-976.
RX PubMed=23177926; DOI=10.1016/j.str.2012.10.011;
RA Nyirenda J., Matsumoto S., Saitoh T., Maita N., Noda N.N., Inagaki F.,
RA Kohda D.;
RT "Crystallographic and NMR evidence for flexibility in
RT oligosaccharyltransferases and its catalytic significance.";
RL Structure 21:32-41(2013).
CC -!- FUNCTION: Oligosaccharyl transferase (OST) that catalyzes the initial
CC transfer of a defined glycan (ManNAcXyl(2)GlcAMan(2)GalNAc in
CC Pyrococcus) 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:0000250|UniProtKB:Q8U4D2}.
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:0000250|UniProtKB:Q8U4D2};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q8U4D2};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q8U4D2};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000250|UniProtKB:Q8U4D2}.
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; BA000001; BAA29314.1; -; Genomic_DNA.
DR PIR; C71248; C71248.
DR PDB; 3VU1; X-ray; 2.70 A; A/B=482-976.
DR PDBsum; 3VU1; -.
DR AlphaFoldDB; O74088; -.
DR SMR; O74088; -.
DR STRING; 70601.3256631; -.
DR CAZy; GT66; Glycosyltransferase Family 66.
DR EnsemblBacteria; BAA29314; BAA29314; BAA29314.
DR KEGG; pho:PH0242; -.
DR eggNOG; arCOG02044; Archaea.
DR OMA; YGYWIES; -.
DR BRENDA; 2.4.99.18; 5244.
DR BRENDA; 2.4.99.21; 5244.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000000752; 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; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..976
FT /note="Dolichyl-phosphooligosaccharide-protein
FT glycotransferase 1"
FT /id="PRO_0000445592"
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..976
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT REGION 513..515
FT /note="Interacts with target acceptor peptide in protein
FT substrate"
FT /evidence="ECO:0000250|UniProtKB:O29867"
FT MOTIF 55..57
FT /note="DXD motif 1"
FT /evidence="ECO:0000250|UniProtKB:O29867"
FT MOTIF 167..169
FT /note="DXD motif 2"
FT /evidence="ECO:0000250|UniProtKB:O29867"
FT MOTIF 347..350
FT /note="TIXE motif"
FT /evidence="ECO:0000250|UniProtKB:O29867"
FT MOTIF 513..517
FT /note="WWDYG motif"
FT /evidence="ECO:0000250|UniProtKB:Q8U4D2"
FT MOTIF 573..580
FT /note="DK motif"
FT /evidence="ECO:0000250|UniProtKB:Q8U4D2"
FT BINDING 57
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 169
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:O29867"
FT BINDING 420
FT /ligand="a glycophospholipid"
FT /ligand_id="ChEBI:CHEBI:24397"
FT /ligand_note="archaeal dolichyl phosphooligosaccharide"
FT /evidence="ECO:0000250|UniProtKB:O29867"
FT BINDING 518
FT /ligand="a glycophospholipid"
FT /ligand_id="ChEBI:CHEBI:24397"
FT /ligand_note="archaeal dolichyl phosphooligosaccharide"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT SITE 57
FT /note="Interacts with target acceptor peptide in protein
FT substrate"
FT /evidence="ECO:0000250|UniProtKB:O29867"
FT SITE 160
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT SITE 350
FT /note="Interacts with target acceptor peptide in protein
FT substrate"
FT /evidence="ECO:0000250|UniProtKB:O29867"
FT SITE 576
FT /note="Interacts with target acceptor peptide in protein
FT substrate"
FT /evidence="ECO:0000250|UniProtKB:O29867"
FT HELIX 493..503
FT /evidence="ECO:0007829|PDB:3VU1"
FT STRAND 510..514
FT /evidence="ECO:0007829|PDB:3VU1"
FT TURN 516..519
FT /evidence="ECO:0007829|PDB:3VU1"
FT STRAND 532..536
FT /evidence="ECO:0007829|PDB:3VU1"
FT HELIX 540..549
FT /evidence="ECO:0007829|PDB:3VU1"
FT HELIX 553..555
FT /evidence="ECO:0007829|PDB:3VU1"
FT HELIX 559..562
FT /evidence="ECO:0007829|PDB:3VU1"
FT STRAND 566..570
FT /evidence="ECO:0007829|PDB:3VU1"
FT HELIX 571..576
FT /evidence="ECO:0007829|PDB:3VU1"
FT HELIX 577..583
FT /evidence="ECO:0007829|PDB:3VU1"
FT HELIX 589..593
FT /evidence="ECO:0007829|PDB:3VU1"
FT STRAND 605..610
FT /evidence="ECO:0007829|PDB:3VU1"
FT STRAND 612..617
FT /evidence="ECO:0007829|PDB:3VU1"
FT TURN 618..621
FT /evidence="ECO:0007829|PDB:3VU1"
FT STRAND 622..628
FT /evidence="ECO:0007829|PDB:3VU1"
FT STRAND 630..639
FT /evidence="ECO:0007829|PDB:3VU1"
FT STRAND 642..645
FT /evidence="ECO:0007829|PDB:3VU1"
FT STRAND 647..651
FT /evidence="ECO:0007829|PDB:3VU1"
FT TURN 652..655
FT /evidence="ECO:0007829|PDB:3VU1"
FT STRAND 656..659
FT /evidence="ECO:0007829|PDB:3VU1"
FT STRAND 662..664
FT /evidence="ECO:0007829|PDB:3VU1"
FT STRAND 667..669
FT /evidence="ECO:0007829|PDB:3VU1"
FT STRAND 672..676
FT /evidence="ECO:0007829|PDB:3VU1"
FT STRAND 678..685
FT /evidence="ECO:0007829|PDB:3VU1"
FT HELIX 686..688
FT /evidence="ECO:0007829|PDB:3VU1"
FT HELIX 692..698
FT /evidence="ECO:0007829|PDB:3VU1"
FT HELIX 708..715
FT /evidence="ECO:0007829|PDB:3VU1"
FT STRAND 716..722
FT /evidence="ECO:0007829|PDB:3VU1"
FT STRAND 725..730
FT /evidence="ECO:0007829|PDB:3VU1"
FT STRAND 732..742
FT /evidence="ECO:0007829|PDB:3VU1"
FT STRAND 745..748
FT /evidence="ECO:0007829|PDB:3VU1"
FT STRAND 750..752
FT /evidence="ECO:0007829|PDB:3VU1"
FT STRAND 754..765
FT /evidence="ECO:0007829|PDB:3VU1"
FT STRAND 770..781
FT /evidence="ECO:0007829|PDB:3VU1"
FT STRAND 784..797
FT /evidence="ECO:0007829|PDB:3VU1"
FT STRAND 805..811
FT /evidence="ECO:0007829|PDB:3VU1"
FT STRAND 815..827
FT /evidence="ECO:0007829|PDB:3VU1"
FT STRAND 834..836
FT /evidence="ECO:0007829|PDB:3VU1"
FT STRAND 839..841
FT /evidence="ECO:0007829|PDB:3VU1"
FT STRAND 852..863
FT /evidence="ECO:0007829|PDB:3VU1"
FT STRAND 865..885
FT /evidence="ECO:0007829|PDB:3VU1"
FT STRAND 892..911
FT /evidence="ECO:0007829|PDB:3VU1"
FT STRAND 913..923
FT /evidence="ECO:0007829|PDB:3VU1"
FT HELIX 928..940
FT /evidence="ECO:0007829|PDB:3VU1"
FT HELIX 941..943
FT /evidence="ECO:0007829|PDB:3VU1"
FT STRAND 944..968
FT /evidence="ECO:0007829|PDB:3VU1"
SQ SEQUENCE 976 AA; 109970 MW; BF5FB82FBADC60A9 CRC64;
MVKSKVKKVE KGKEGEEKRS TYVLLKKVLI PILVFGFAIY AFYLRHLTAG KYFPDPDTFY
HFEIYKLVLK EGLPRYYPMS DAPFGSLIGE PLGLYLLPAA FYKVVSLFGY NELQAFLLWP
PFVGFLGVIA VYLLGRKVLN EWTGLWGAVV LTVSTANFSR TFSGNARGDG PFMALFIFAS
VAMLYYLKES NKTRKIIYGT LFVLLTVISL GAWNGSPFGL MVLLGFASLQ TIILFIFGKL
EELKKFVKEF YPAYLAILAF GYALTFPGIV KIGGFIRFAF EVFLGLIFLL VIMLYGGRYL
NYSDKKHRFL VVTIIVLLGF GGAYAYVGPK LFRLMGGAYQ STQVYETVQE LAKTTIGDVK
AYYGVESGNG LIFFLSIPGL LILLTKYLYD LFKKAKSDNE TLFALVFYTM SLYLLYLAVR
FLFLASYAVA LFFGIFIGFS MDVIEKMKEN IGIKAALGIV LSLMILVIPF VHAPVLARSA
RALKNTEIEV TGWEQALKWL RSNTSKYATA TSWWDYGYWI ESSLLGNRRA SADGGHARDR
DHILALFLAR DGNISEVDFE SWELNYFIIY LNDWAKFNAI SYLGGAITRK EYNGDENGRG
RVTTILLTQA AGNVYVNPYA RIVIKVIQQN KTRRIAVNIG QLECSPILSV AFPGNIKIKG
SGRCSDGSPF PYVVYLTPSL GVLAYYKVAT SNFVKLAFGI PTSSYSEFAE KLFSNFIPVY
QYGSVIVYEF RPFAIYKIED FINGTWREVG KLSPGKHTLR LYISAFGRDI KNATLYVYAL
NGTKIIKRIK VGEIKYMNHL EEYPIIVNVT LPTAQKYRFI LAQKGPVGVL TGPVRVNGKI
TNPAYIMREG ESGRLELKVG VDKEYTADLY LRATFIYLVR KGGKSNEDYD ASFEPHMDTF
FITKLKEGIK LRPGENEIVV NAEMPKNAIS SYKEKLEKEH GDKLIIRGIR VEPVFIVEKE
YTMIEVSASA PHHSSE
