ID   AGLK_METVO              Reviewed;         251 AA.
AC   B3VA58;
DT   17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 28.
DE   RecName: Full=UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminyltransferase {ECO:0000303|PubMed:23624439};
DE            EC=2.4.1.153 {ECO:0000269|PubMed:23624439};
DE   AltName: Full=Dol-P-GlcNAc synthase {ECO:0000303|PubMed:23624439};
GN   Name=aglK {ECO:0000303|PubMed:18978056};
OS   Methanococcus voltae.
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=2188;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 33273 / DSM 1537 / NBRC 100457 / OCM 70 / PS;
RX   PubMed=18978056; DOI=10.1128/jb.00885-08;
RA   Chaban B., Logan S.M., Kelly J.F., Jarrell K.F.;
RT   "AglC and AglK are involved in biosynthesis and attachment of diacetylated
RT   glucuronic acid to the N-glycan in Methanococcus voltae.";
RL   J. Bacteriol. 191:187-195(2009).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND SUBSTRATE SPECIFICITY.
RC   STRAIN=ATCC 33273 / DSM 1537 / NBRC 100457 / OCM 70 / PS;
RX   PubMed=23624439; DOI=10.1038/nchembio.1249;
RA   Larkin A., Chang M.M., Whitworth G.E., Imperiali B.;
RT   "Biochemical evidence for an alternate pathway in N-linked glycoprotein
RT   biosynthesis.";
RL   Nat. Chem. Biol. 9:367-373(2013).
CC   -!- FUNCTION: Involved in the assembly of an N-linked disaccharide that
CC       decorates the S-layer glycoprotein and flagellins (PubMed:18978056).
CC       AglK initiates N-linked glycosylation through the formation of alpha-
CC       linked dolichyl monophosphate N-acetylglucosamine. It catalyzes the
CC       transfer of GlcNAc from the donor substrate UDP-GlcNAc to dolichyl
CC       phosphate C55 (Dol-P) to yield Dol-P-GlcNAc (PubMed:23624439). AglK
CC       reaction proceeds with retention of stereochemistry (PubMed:23624439).
CC       The reaction is specific for UDP-GlcNAc. AglK shows a stronger
CC       preference for short dolichol (C55-60 Dol-P) substrates compared with
CC       the longer (C85-105 Dol-P) (PubMed:23624439).
CC       {ECO:0000269|PubMed:18978056, ECO:0000269|PubMed:23624439}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a dolichyl phosphate + UDP-N-acetyl-alpha-D-glucosamine = a
CC         dolichyl N-acetyl-alpha-D-glucosaminyl phosphate + UDP;
CC         Xref=Rhea:RHEA:14693, Rhea:RHEA-COMP:9517, Rhea:RHEA-COMP:9518,
CC         ChEBI:CHEBI:57683, ChEBI:CHEBI:57705, ChEBI:CHEBI:58050,
CC         ChEBI:CHEBI:58223; EC=2.4.1.153;
CC         Evidence={ECO:0000269|PubMed:23624439};
CC   -!- PATHWAY: Cell surface structure biogenesis; S-layer biogenesis.
CC       {ECO:0000305|PubMed:18978056}.
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000305|PubMed:18978056}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:23624439};
CC       Single-pass membrane protein {ECO:0000305|PubMed:23624439}.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene result in flagellins and
CC       S-layer proteins with significantly reduced apparent molecular masses,
CC       loss of flagellar assembly and absence of glycan attachment.
CC       {ECO:0000269|PubMed:18978056}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. {ECO:0000305}.
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DR   EMBL; EU726230; ACE74694.1; -; Genomic_DNA.
DR   AlphaFoldDB; B3VA58; -.
DR   SMR; B3VA58; -.
DR   CAZy; GT2; Glycosyltransferase Family 2.
DR   KEGG; ag:ACE74694; -.
DR   BioCyc; MetaCyc:MON-19263; -.
DR   BRENDA; 2.4.1.153; 3268.
DR   UniPathway; UPA00378; -.
DR   UniPathway; UPA00977; -.
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:0004166; F:dolichyl-phosphate alpha-N-acetylglucosaminyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0006491; P:N-glycan processing; IDA:UniProtKB.
DR   GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR   GO; GO:0045232; P:S-layer organization; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.90.550.10; -; 1.
DR   InterPro; IPR001173; Glyco_trans_2-like.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   Pfam; PF00535; Glycos_transf_2; 1.
DR   SUPFAM; SSF53448; SSF53448; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Glycosyltransferase; Membrane; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..251
FT                   /note="UDP-N-acetylglucosamine--dolichyl-phosphate N-
FT                   acetylglucosaminyltransferase"
FT                   /id="PRO_0000435655"
FT   TRANSMEM        150..167
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   251 AA;  28175 MW;  4DF5CAFA7858020E CRC64;
     MADKLIYLII PAYNEEKMIK NVVNNLQNHN YDNIIIVDDG SKDNTYKIMK ELEEESKQNN
     NNNNNNNNNK VIAIKHEQNK GVGGATITGL KKAYELGADI AVTFDADGQH APDDIAKVIQ
     PIINDSKEYV VGSRIKNPKE FKNMPLTKKV GNLGLSFITF LLGGYYVTDS QSGLRAFSKS
     ALKVLSEQLR AKRYETCSEA LIIAKKNKLN IGEVPIKTIY TEYSMARGTN VMIGFKIFYR
     LLMLKMGKVL D