The new UniProt website is here!
Take me to UniProt BETA
UniProtKB - O74088 (AGLB1_PYRHO)
Protein
Dolichyl-phosphooligosaccharide-protein glycotransferase 1
Gene
aglB1
Organism
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Status
Functioni
Oligosaccharyl transferase (OST) that catalyzes the initial transfer of a defined glycan (ManNAcXyl2GlcAMan2GalNAc in Pyrococcus) from the lipid carrier dolichol-monophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation.
By similarityCatalytic activityi
- An archaeal dolichyl phosphooligosaccharide + [protein]-L-asparagine = an archaeal dolichyl phosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine.By similarity EC:2.4.99.21
Cofactori
: protein glycosylation Pathwayi
This protein is involved in the pathway protein glycosylation, which is part of Protein modification.By similarityView all proteins of this organism that are known to be involved in the pathway protein glycosylation and in Protein modification.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 57 | ManganeseBy similarity | 1 | |
Sitei | 57 | Interacts with target acceptor peptide in protein substrateBy similarity | 1 | |
Sitei | 160 | Important for catalytic activityBy similarity | 1 | |
Metal bindingi | 167 | ManganeseBy similarity | 1 | |
Metal bindingi | 169 | ManganeseBy similarity | 1 | |
Sitei | 350 | Interacts with target acceptor peptide in protein substrateBy similarity | 1 | |
Binding sitei | 420 | Glycophospholipid; archaeal dolichyl phosphooligosaccharideBy similarity | 1 | |
Binding sitei | 518 | Glycophospholipid; archaeal dolichyl phosphooligosaccharideBy similarity | 1 | |
Sitei | 576 | Interacts with target acceptor peptide in protein substrateBy similarity | 1 |
GO - Molecular functioni
- metal ion binding Source: UniProtKB-KW
- oligosaccharyl transferase activity Source: InterPro
GO - Biological processi
- protein glycosylation Source: UniProtKB-UniPathway
Keywordsi
Molecular function | Glycosyltransferase, Transferase |
Ligand | Magnesium, Manganese, Metal-binding |
Enzyme and pathway databases
BRENDAi | 2.4.99.18, 5244 |
UniPathwayi | UPA00378 |
Protein family/group databases
CAZyi | GT66, Glycosyltransferase Family 66 |
Names & Taxonomyi
Protein namesi | Recommended name: Dolichyl-phosphooligosaccharide-protein glycotransferase 1 (EC:2.4.99.21)Alternative name(s): Archaeal glycosylation protein B Short name: AglB-L Short name: AglB-Long Oligosaccharyl transferase Short name: OST Short name: OTase |
Gene namesi | Name:aglB1 Ordered Locus Names:PH0242 |
Organismi | Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3) |
Taxonomic identifieri | 70601 [NCBI] |
Taxonomic lineagei | Archaea › Euryarchaeota › Thermococci › Thermococcales › Thermococcaceae › Pyrococcus › |
Proteomesi |
|
Subcellular locationi
Plasma membrane
- Cell membrane By similarity; Multi-pass membrane protein By similarity
Plasma Membrane
- plasma membrane Source: UniProtKB-SubCell
Other locations
- integral component of membrane Source: UniProtKB-KW
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Topological domaini | 1 – 21 | CytoplasmicCuratedAdd BLAST | 21 | |
Transmembranei | 22 – 42 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 43 – 112 | ExtracellularCuratedAdd BLAST | 70 | |
Transmembranei | 113 – 133 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 134 – 135 | CytoplasmicCurated | 2 | |
Transmembranei | 136 – 156 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 157 – 165 | ExtracellularCurated | 9 | |
Transmembranei | 166 – 186 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 187 – 193 | CytoplasmicCurated | 7 | |
Transmembranei | 194 – 214 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 215 | ExtracellularCurated | 1 | |
Transmembranei | 216 – 236 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 237 – 247 | CytoplasmicCuratedAdd BLAST | 11 | |
Transmembranei | 248 – 268 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 269 | ExtracellularCurated | 1 | |
Transmembranei | 270 – 290 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 291 – 306 | CytoplasmicCuratedAdd BLAST | 16 | |
Transmembranei | 307 – 327 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 328 – 360 | ExtracellularCuratedAdd BLAST | 33 | |
Transmembranei | 361 – 381 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 382 – 396 | CytoplasmicCuratedAdd BLAST | 15 | |
Transmembranei | 397 – 417 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 418 | ExtracellularCurated | 1 | |
Transmembranei | 419 – 439 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 440 – 453 | CytoplasmicCuratedAdd BLAST | 14 | |
Transmembranei | 454 – 474 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 475 – 976 | ExtracellularCuratedAdd BLAST | 502 |
Keywords - Cellular componenti
Cell membrane, MembranePTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000445592 | 1 – 976 | Dolichyl-phosphooligosaccharide-protein glycotransferase 1Add BLAST | 976 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
AlphaFoldDBi | O74088 |
SMRi | O74088 |
ModBasei | Search... |
PDBe-KBi | Search... |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 513 – 515 | Interacts with target acceptor peptide in protein substrateBy similarity | 3 |
Motif
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Motifi | 55 – 57 | DXD motif 1By similarity | 3 | |
Motifi | 167 – 169 | DXD motif 2By similarity | 3 | |
Motifi | 347 – 350 | TIXE motifBy similarity | 4 | |
Motifi | 513 – 517 | WWDYG motifBy similarity | 5 | |
Motifi | 573 – 580 | DK motifBy similarity | 8 |
Domaini
Despite low primary sequence conservation between eukaryotic catalytic subunits and bacterial and archaeal single subunit OSTs (ssOST), structural comparison revealed several common motifs at spatially equivalent positions, like the DXD motif 1 on the external loop 1 and the DXD motif 2 on the external loop 2 involved in binding of the metal ion cofactor and the carboxamide group of the acceptor asparagine, the conserved Glu residue of the TIXE/SVSE motif on the external loop 5 involved in catalysis, as well as the WWDYG and the DK/MI motifs in the globular domain that define the binding pocket for the +2 Ser/Thr of the acceptor sequon. In bacterial ssOSTs, an Arg residue was found to interact with a negatively charged side chain at the -2 position of the sequon. This Arg is conserved in bacterial enzymes and correlates with an extended sequon requirement (Asp-X-Asn-X-Ser/Thr) for bacterial N-glycosylation.By similarity
Sequence similaritiesi
Belongs to the STT3 family.Curated
Keywords - Domaini
Transmembrane, Transmembrane helixPhylogenomic databases
eggNOGi | arCOG02044, Archaea |
OMAi | YGYWIES |
Family and domain databases
InterProi | View protein in InterPro IPR003674, Oligo_trans_STT3 IPR041530, OST_IS IPR041152, OST_P2 |
PANTHERi | PTHR13872, PTHR13872, 1 hit |
Pfami | View protein in Pfam PF18246, OST_IS, 1 hit PF18235, OST_P2, 1 hit PF02516, STT3, 1 hit |
i Sequence
Sequence statusi: Complete.
O74088-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MVKSKVKKVE KGKEGEEKRS TYVLLKKVLI PILVFGFAIY AFYLRHLTAG
60 70 80 90 100
KYFPDPDTFY HFEIYKLVLK EGLPRYYPMS DAPFGSLIGE PLGLYLLPAA
110 120 130 140 150
FYKVVSLFGY NELQAFLLWP PFVGFLGVIA VYLLGRKVLN EWTGLWGAVV
160 170 180 190 200
LTVSTANFSR TFSGNARGDG PFMALFIFAS VAMLYYLKES NKTRKIIYGT
210 220 230 240 250
LFVLLTVISL GAWNGSPFGL MVLLGFASLQ TIILFIFGKL EELKKFVKEF
260 270 280 290 300
YPAYLAILAF GYALTFPGIV KIGGFIRFAF EVFLGLIFLL VIMLYGGRYL
310 320 330 340 350
NYSDKKHRFL VVTIIVLLGF GGAYAYVGPK LFRLMGGAYQ STQVYETVQE
360 370 380 390 400
LAKTTIGDVK AYYGVESGNG LIFFLSIPGL LILLTKYLYD LFKKAKSDNE
410 420 430 440 450
TLFALVFYTM SLYLLYLAVR FLFLASYAVA LFFGIFIGFS MDVIEKMKEN
460 470 480 490 500
IGIKAALGIV LSLMILVIPF VHAPVLARSA RALKNTEIEV TGWEQALKWL
510 520 530 540 550
RSNTSKYATA TSWWDYGYWI ESSLLGNRRA SADGGHARDR DHILALFLAR
560 570 580 590 600
DGNISEVDFE SWELNYFIIY LNDWAKFNAI SYLGGAITRK EYNGDENGRG
610 620 630 640 650
RVTTILLTQA AGNVYVNPYA RIVIKVIQQN KTRRIAVNIG QLECSPILSV
660 670 680 690 700
AFPGNIKIKG SGRCSDGSPF PYVVYLTPSL GVLAYYKVAT SNFVKLAFGI
710 720 730 740 750
PTSSYSEFAE KLFSNFIPVY QYGSVIVYEF RPFAIYKIED FINGTWREVG
760 770 780 790 800
KLSPGKHTLR LYISAFGRDI KNATLYVYAL NGTKIIKRIK VGEIKYMNHL
810 820 830 840 850
EEYPIIVNVT LPTAQKYRFI LAQKGPVGVL TGPVRVNGKI TNPAYIMREG
860 870 880 890 900
ESGRLELKVG VDKEYTADLY LRATFIYLVR KGGKSNEDYD ASFEPHMDTF
910 920 930 940 950
FITKLKEGIK LRPGENEIVV NAEMPKNAIS SYKEKLEKEH GDKLIIRGIR
960 970
VEPVFIVEKE YTMIEVSASA PHHSSE
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | BA000001 Genomic DNA Translation: BAA29314.1 |
PIRi | C71248 |
Genome annotation databases
EnsemblBacteriai | BAA29314; BAA29314; BAA29314 |
KEGGi | pho:PH0242 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | BA000001 Genomic DNA Translation: BAA29314.1 |
PIRi | C71248 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
3VU1 | X-ray | 2.70 | A/B | 482-976 | [»] | |
AlphaFoldDBi | O74088 | |||||
SMRi | O74088 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
STRINGi | 70601.3256631 |
Protein family/group databases
CAZyi | GT66, Glycosyltransferase Family 66 |
Genome annotation databases
EnsemblBacteriai | BAA29314; BAA29314; BAA29314 |
KEGGi | pho:PH0242 |
Phylogenomic databases
eggNOGi | arCOG02044, Archaea |
OMAi | YGYWIES |
Enzyme and pathway databases
UniPathwayi | UPA00378 |
BRENDAi | 2.4.99.18, 5244 |
Family and domain databases
InterProi | View protein in InterPro IPR003674, Oligo_trans_STT3 IPR041530, OST_IS IPR041152, OST_P2 |
PANTHERi | PTHR13872, PTHR13872, 1 hit |
Pfami | View protein in Pfam PF18246, OST_IS, 1 hit PF18235, OST_P2, 1 hit PF02516, STT3, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | AGLB1_PYRHO | |
Accessioni | O74088Primary (citable) accession number: O74088 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | October 10, 2018 |
Last sequence update: | November 1, 1998 | |
Last modified: | May 25, 2022 | |
This is version 107 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structureDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families