AGLB2_PYRHO
ID AGLB2_PYRHO Reviewed; 758 AA.
AC O58981;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Dolichyl-phosphooligosaccharide-protein glycotransferase 2;
DE EC=2.4.99.21;
DE AltName: Full=Archaeal glycosylation protein B;
DE Short=AglB-S;
DE Short=AglB-Short;
DE AltName: Full=Oligosaccharyl transferase;
DE Short=OST;
DE Short=OTase;
GN Name=aglB2; OrderedLocusNames=PH1271;
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).
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; BAA30374.1; -; Genomic_DNA.
DR PIR; D71072; D71072.
DR RefSeq; WP_010885360.1; NC_000961.1.
DR AlphaFoldDB; O58981; -.
DR SMR; O58981; -.
DR STRING; 70601.3257691; -.
DR CAZy; GT66; Glycosyltransferase Family 66.
DR TCDB; 9.B.142.3.2; the integral membrane glycosyltransferase family 39 (gt39) family.
DR DNASU; 1443596; -.
DR EnsemblBacteria; BAA30374; BAA30374; BAA30374.
DR GeneID; 1443596; -.
DR KEGG; pho:PH1271; -.
DR eggNOG; arCOG02044; Archaea.
DR OMA; FWYSVAL; -.
DR OrthoDB; 5183at2157; -.
DR BRENDA; 2.4.99.18; 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 PANTHER; PTHR13872; PTHR13872; 1.
DR Pfam; PF02516; STT3; 1.
PE 3: Inferred from homology;
KW Cell membrane; Glycosyltransferase; Magnesium; Manganese; Membrane;
KW Metal-binding; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..758
FT /note="Dolichyl-phosphooligosaccharide-protein
FT glycotransferase 2"
FT /id="PRO_0000445593"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 28..92
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 93..113
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 114..120
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 121..141
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 142..145
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 146..166
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 167..175
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 176..196
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 197..217
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 218..226
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 227..247
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 248..281
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 282..302
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 303..310
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 311..331
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 332..352
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 353..373
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 374..379
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 380..400
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 401
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 402..422
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 423..433
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 434..454
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 455..758
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT REGION 488..490
FT /note="Interacts with target acceptor peptide in protein
FT substrate"
FT /evidence="ECO:0000250|UniProtKB:O29867"
FT MOTIF 29..31
FT /note="DXD motif 1"
FT /evidence="ECO:0000250|UniProtKB:O29867"
FT MOTIF 144..146
FT /note="DXD motif 2"
FT /evidence="ECO:0000250|UniProtKB:O29867"
FT MOTIF 340..343
FT /note="TIXE motif"
FT /evidence="ECO:0000250|UniProtKB:O29867"
FT MOTIF 488..492
FT /note="WWDYG motif"
FT /evidence="ECO:0000250|UniProtKB:Q8U4D2"
FT MOTIF 540..547
FT /note="DK motif"
FT /evidence="ECO:0000250|UniProtKB:Q8U4D2"
FT BINDING 31
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:O29867"
FT BINDING 144
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:O29867"
FT BINDING 146
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:O29867"
FT BINDING 401
FT /ligand="a glycophospholipid"
FT /ligand_id="ChEBI:CHEBI:24397"
FT /ligand_note="archaeal dolichyl phosphooligosaccharide"
FT /evidence="ECO:0000250|UniProtKB:O29867"
FT SITE 31
FT /note="Interacts with target acceptor peptide in protein
FT substrate"
FT /evidence="ECO:0000250|UniProtKB:O29867"
FT SITE 137
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT SITE 343
FT /note="Interacts with target acceptor peptide in protein
FT substrate"
FT /evidence="ECO:0000250|UniProtKB:O29867"
FT SITE 543
FT /note="Interacts with target acceptor peptide in protein
FT substrate"
FT /evidence="ECO:0000250|UniProtKB:O29867"
SQ SEQUENCE 758 AA; 86787 MW; BA1175519DB950F4 CRC64;
MKRRYSILII LLVAIFYRMI TFRFKYLLGY DPYFHLAYIE EVNKVGKWIN FLTFAGGPWG
YQVKLFHPLG LWMTPLYLYK LLKVFGVSLT TTFKITPVIF GVLTVIFLYL SLLKLYDEKR
AFFGGFFLAI SYGHVFRSMA NYYRGDNYML FWYSVALLGI SLALGIKKGK WKYKRLIFYT
LPVLASGFSA IFWQAYYPIF AFLLSNALLL AVGAFILKKD KYLLDSIILI LSTAFGVLLA
NYLGGIFGYG MLGYAKWLGK SVAKKLGLEF GYLKDVYLIL HLKYLVPISL SFVLVLILLG
FLTKDIRIRS LFLGIASFIG IIILFKRFEA LKELSTGFGI FKEAPILETQ PTSFKDLWAA
FSLSFFLTPL FFIRFKKPRV EDFLTLGLII PSVYMLKTWT RFLFIGSMAI AIMSGIGIVE
LYEAIKPRLN GKKALATGII TLVILPGVIA GLSFKEVCSL HPEMNEAWER ALKWLKNNSN
ENDVILAWWD WGHFITYYAR RSPIAQGGPS VGVALYLLGK LNENWAINLG VDYVIVSYYD
FLKFGAILST ANLSKRYNIR GYGLVVLPLR ASTGALIFEN RGYRAIVRHD KSWNAVIIYN
GQMIYPRKLY VEHKEGVQEI KPPESNSNTY LYVNLNYGYA IFMNGNAFNT TLVRLFITPE
KPYKLVYSDG GLIKIFKLEH PNVKVERRES NVILNFENGT SLGLYFFLDN GTMVLSKWYN
VKGKNEFIVP KVNASVARYV LKRGKKVVDR GVFRLSYN
