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Sequence of AGLB_METVO

EC Number:2.4.99.21

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
dolichyl-phosphooligosaccharide-protein glycotransferase
Q2EMT4
Methanococcus voltae
917
102424
Reaction
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
Other sequences found for EC No. 2.4.99.21

General information:

Sequence
show sequence in fasta format
  0 MTENNEKVKN SDSANNQSSK NSKFNFNFED KKVKCAKTIL IIIFLAFLSF QMRAQTADMG
 60 FTTNEQYLDV FSDDNGRMYL TALDPYYYLR MSENYLENGH TGDTLKNIDG QQVPWDSYKY
120 GPTGARATFN LLSVVTVWVY QVWHAMDSTV TLMNAAFWVP AILSMFLITP IFFTVRRITS
180 SDIGGAVAAI LASLSPSIFV KTVAGFSDTP ILEILPLLFI VWFIIEAIHY SKEKNYKSLI
240 YGLLATLMLA LYPFMWSAWW YGYYIVIAFL VIYAIYKGIS YNSIAKYTKS KNNNHKDKIE
300 SEKLEMLNIL KISGLFIIGG AVLITALYGV STTMNALQAP LNYLGLDEVS SQTGWPNVLT
360 TVSELDTASL DEIISSSLGS IHLFAIGLIG IFLSLFRKVL TPVKQISNGL AEKLDIKYAL
420 LLIIWFAVTF LAASKGVRFV ALMVPPLSIG VGIFVGFIEQ FIKNNLDKKY EYVAYPTIAI
480 IVLYALFTIY RADSADLVRM LLPSNYVPIA EGIMLASLAV LIIYKVAELI AESNKKLVMN
540 KIFMILLAIG LITPTIATIV PFYSVPTYND GWGESLEWIN TQTPNNSVVT CWWDNGHIYT
600 WKTDRMVTFD GSSQNTPRAY WVGRAFSTSN ESLANGIFRM LASSGDKAYT TDSVLIKKTG
660 SIKNTVDVLN EILPLTKSDA QKALKNSSYK FTDTEVSEIL DATHPKVTNP DYLITYNRMT
720 SIASVWSYFG NWDFNLPAGT SRSEREAGSF QGLQTYATNI NDTLIVRSLI QQTAEYNIYT
780 LIEVRNETLT GAMMAVTNDG QMQTQQLNMH KVKLMVNENG KSKMYNSLAD PDGQLSLLIK
840 VDKNSIIGTD GSNNPVYSSS SWMATANLED SVYSKLHFFD GEGLDTIKLE KESLDPTANG
900 VQPGFKVFSV DYGNYSK
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Sequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
1154982
Chaban B.,Voisin S.,Kelly J.,Logan S.M.,Jarrell K.F.
Identification of genes involved in the biosynthesis and attachment of Methanococcus voltae N-linked glycans: insight into N-linked glycosylation pathways in Archaea.
Mol. Microbiol.
61
259-268
2006
1154983
Larkin A.,Chang M.M.,Whitworth G.E.,Imperiali B.
Biochemical evidence for an alternate pathway in N-linked glycoprotein biosynthesis.
Nat. Chem. Biol.
9
367-373
2013
1154984
Cohen-Rosenzweig C.,Guan Z.,Shaanan B.,Eichler J.
Substrate promiscuity: AglB, the archaeal oligosaccharyltransferase, can process a variety of lipid-linked glycans.
Appl. Environ. Microbiol.
80
486-496
2014
1154985
Taguchi Y.,Fujinami D.,Kohda D.
Comparative analysis of archaeal lipid-linked oligosaccharides that serve as oligosaccharide donors for Asn glycosylation.
J. Biol. Chem.
291
11042-11054
2016