AGLB1_ARCFU
ID AGLB1_ARCFU Reviewed; 591 AA.
AC O29918;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Dolichyl-phosphooligosaccharide-protein glycotransferase 1;
DE EC=2.4.99.21 {ECO:0000269|PubMed:22559858};
DE AltName: Full=Archaeal glycosylation protein B;
DE Short=AglB-S1;
DE Short=AglB-Short 1;
DE AltName: Full=Oligosaccharyl transferase;
DE Short=OST;
DE Short=OTase;
GN Name=aglB1; OrderedLocusNames=AF_0329;
OS Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS 100126 / VC-16).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=224325;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=9389475; DOI=10.1038/37052;
RA Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA Smith H.O., Woese C.R., Venter J.C.;
RT "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT archaeon Archaeoglobus fulgidus.";
RL Nature 390:364-370(1997).
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:3VGP}
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 430-591, CATALYTIC ACTIVITY,
RP DOMAIN, AND MUTAGENESIS OF GLU-521 AND LYS-531.
RX PubMed=22559858; DOI=10.1021/bi300076u;
RA Matsumoto S., Igura M., Nyirenda J., Matsumoto M., Yuzawa S., Noda N.,
RA Inagaki F., Kohda D.;
RT "Crystal structure of the C-terminal globular domain of
RT oligosaccharyltransferase from Archaeoglobus fulgidus at 1.75 A
RT resolution.";
RL Biochemistry 51:4157-4166(2012).
CC -!- FUNCTION: Oligosaccharyl transferase (OST) that catalyzes the initial
CC transfer of a defined glycan (a GalNAc-linked heptasaccharide composed
CC of 4 Hex, 3 dHex and a sulfate for A.fulgidus AglB-S) from the lipid
CC carrier dolichol-monophosphate to an asparagine residue within an Asn-
CC X-Ser/Thr consensus motif in nascent polypeptide chains, the first step
CC in protein N-glycosylation. {ECO:0000269|PubMed:27015803}.
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:22559858};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:O29867};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:O29867};
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:O29867};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000305|PubMed:27015803}.
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:0000305|PubMed:22559858}.
CC -!- SIMILARITY: Belongs to the STT3 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE000782; AAB90907.1; -; Genomic_DNA.
DR PIR; A69291; A69291.
DR RefSeq; WP_010877836.1; NC_000917.1.
DR PDB; 3VGP; X-ray; 1.75 A; A=430-591.
DR PDBsum; 3VGP; -.
DR AlphaFoldDB; O29918; -.
DR SMR; O29918; -.
DR STRING; 224325.AF_0329; -.
DR CAZy; GT66; Glycosyltransferase Family 66.
DR DNASU; 1483543; -.
DR EnsemblBacteria; AAB90907; AAB90907; AF_0329.
DR GeneID; 24793868; -.
DR KEGG; afu:AF_0329; -.
DR eggNOG; arCOG02043; Archaea.
DR HOGENOM; CLU_008803_0_0_2; -.
DR OMA; AVSNNFQ; -.
DR OrthoDB; 5183at2157; -.
DR PhylomeDB; O29918; -.
DR BRENDA; 2.4.99.18; 414.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000002199; 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 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..591
FT /note="Dolichyl-phosphooligosaccharide-protein
FT glycotransferase 1"
FT /id="PRO_0000445594"
FT TOPO_DOM 1..5
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 27..67
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 68..88
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 89..91
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 92..112
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 113..121
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 122..142
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 143..147
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 148..168
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 169
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 170..190
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 191..219
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 220..240
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 241..252
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 253..273
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 274..275
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 276..296
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 297..303
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 304..324
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 325..327
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 328..344
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 345..347
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 348..368
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 369..408
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 409..429
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 430..591
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT REGION 465..467
FT /note="Interacts with target acceptor peptide in protein
FT substrate"
FT /evidence="ECO:0000250|UniProtKB:O29867"
FT MOTIF 34..36
FT /note="DXD motif 1"
FT /evidence="ECO:0000250|UniProtKB:O29867"
FT MOTIF 146..148
FT /note="DXD motif 2"
FT /evidence="ECO:0000250|UniProtKB:O29867"
FT MOTIF 295..298
FT /note="TIXE motif"
FT /evidence="ECO:0000250|UniProtKB:O29867"
FT MOTIF 465..469
FT /note="WWDYG motif"
FT /evidence="ECO:0000305|PubMed:22559858"
FT MOTIF 521..535
FT /note="DKi motif"
FT /evidence="ECO:0000305|PubMed:22559858"
FT BINDING 36
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 147
FT /ligand="a glycophospholipid"
FT /ligand_id="ChEBI:CHEBI:24397"
FT /ligand_note="archaeal dolichyl phosphooligosaccharide"
FT /evidence="ECO:0000250|UniProtKB:O29867"
FT BINDING 148
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:O29867"
FT BINDING 347
FT /ligand="a glycophospholipid"
FT /ligand_id="ChEBI:CHEBI:24397"
FT /ligand_note="archaeal dolichyl phosphooligosaccharide"
FT /evidence="ECO:0000250|UniProtKB:O29867"
FT SITE 36
FT /note="Interacts with target acceptor peptide in protein
FT substrate"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT SITE 139
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT SITE 298
FT /note="Interacts with target acceptor peptide in protein
FT substrate"
FT /evidence="ECO:0000250|UniProtKB:O29867"
FT SITE 531
FT /note="Interacts with target acceptor peptide in protein
FT substrate"
FT /evidence="ECO:0000250|UniProtKB:O29867"
FT MUTAGEN 521
FT /note="E->Q: Reduces catalytic activity."
FT /evidence="ECO:0000269|PubMed:22559858"
FT MUTAGEN 531
FT /note="K->A: Slightly reduces catalytic activity."
FT /evidence="ECO:0000269|PubMed:22559858"
FT MUTAGEN 531
FT /note="K->R,E,D: Significantly reduces catalytic activity."
FT /evidence="ECO:0000269|PubMed:22559858"
FT HELIX 433..447
FT /evidence="ECO:0007829|PDB:3VGP"
FT STRAND 461..463
FT /evidence="ECO:0007829|PDB:3VGP"
FT HELIX 468..471
FT /evidence="ECO:0007829|PDB:3VGP"
FT TURN 472..474
FT /evidence="ECO:0007829|PDB:3VGP"
FT HELIX 485..496
FT /evidence="ECO:0007829|PDB:3VGP"
FT HELIX 501..511
FT /evidence="ECO:0007829|PDB:3VGP"
FT STRAND 515..518
FT /evidence="ECO:0007829|PDB:3VGP"
FT HELIX 520..522
FT /evidence="ECO:0007829|PDB:3VGP"
FT HELIX 532..538
FT /evidence="ECO:0007829|PDB:3VGP"
FT HELIX 543..545
FT /evidence="ECO:0007829|PDB:3VGP"
FT HELIX 548..556
FT /evidence="ECO:0007829|PDB:3VGP"
FT HELIX 559..564
FT /evidence="ECO:0007829|PDB:3VGP"
FT TURN 565..570
FT /evidence="ECO:0007829|PDB:3VGP"
FT STRAND 572..580
FT /evidence="ECO:0007829|PDB:3VGP"
FT STRAND 583..588
FT /evidence="ECO:0007829|PDB:3VGP"
SQ SEQUENCE 591 AA; 67539 MW; ED5178587BAED4AB CRC64;
MDRKVLMLAV ILFALAVRFQ NFGEIFDSGI YYTGYDSYYH MRLVEVMVKE SFRPDYDYYI
NYPFGLKITW PPLFDYILAF PGMLFGFHSS EIFAVFLPVI LGVLSVVLIC LTALQIVNNQ
TFALISAFIY AAAPVAVWKT VLGQADHHAL VIFLFLLSAY LLLKDGVWKI LAGLPMLFMA
LAWLGSPIYG ALLAFSALVH FDRKALRLVA ASYLIPAISF VLYPPVGISF FGLAAFLFVG
SVVKGYEDRF RNATIYYIAL SLATVLIIYF IPLPHFEFVK GGINYIFGAN IYLPTISEAR
SLQIFEIISA SGYIYFIFAL ISVLFFRNRF VLSMFFLSFI LALMQLRFTE VLVVPSALLS
AYLVSLVLER LEYPVFEKAD EEEKSRRRKR KDRKVKQKNA EVEWKDHAVV AAFLVILAIP
CIVVAVVPFD LTEDWKEALE WMRTSLEEQN YLNPYEKPEY SVMSWWDYGN WILYVSKKAV
VCNNFQAGAV DAAKFFTAKS EDEAIKIAKK RGVRYVVTAD EITMKDANNT KFPAIMRIAG
YNVDLMTEGE ILNFFNHTVL YRLHMENAEN LTHFRLVKEF GDVKIFEVVG S
