ID   AGLC_METVO              Reviewed;         321 AA.
AC   B3VA59;
DT   17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 32.
DE   RecName: Full=Dolichyl N-acetyl-alpha-D-glucosaminyl phosphate 3-beta-D-2,3-diacetamido-2,3-dideoxy-beta-D-glucuronosyltransferase {ECO:0000303|PubMed:23624439};
DE            EC=2.4.1.335 {ECO:0000269|PubMed:23624439};
DE   AltName: Full=Glc-2,3-diNAcA glycosyltransferase {ECO:0000303|PubMed:23624439};
DE   AltName: Full=UDP-Glc-2,3-diNAcA glycosyltransferase {ECO:0000303|PubMed:23624439};
GN   Name=aglC {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       AglC catalyzes the transfer of 2,3-diacetamido-2,3-dideoxy-alpha-D-
CC       glucuronic acid (Glc-2,3-diNAcA) from uridine 5'-diphospho 2,3-
CC       diacetamido-2,3-dideoxy-alpha-D-glucuronic acid (UDP-Glc-2,3-diNAcA) to
CC       the AglK product Dol-P-GlcNAc to yield Dol-P-GlcNAc-Glc-2,3-diNAcA
CC       (PubMed:23624439). AglC is specific for the monophosphate-linked Dol-P-
CC       GlcNAc (PubMed:23624439). {ECO:0000269|PubMed:18978056,
CC       ECO:0000269|PubMed:23624439}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an archaeal dolichyl N-acetyl-alpha-D-glucosaminyl phosphate +
CC         UDP-2,3-diacetamido-2,3-dideoxy-alpha-D-glucuronate = an archaeal
CC         dolichyl 3-O-(2,3-diacetamido-2,3-dideoxy- beta-D-glucuronosyl)-N-
CC         acetyl- alpha-D-glucosaminyl phosphate + H(+) + UDP;
CC         Xref=Rhea:RHEA:47596, Rhea:RHEA-COMP:11931, Rhea:RHEA-COMP:12047,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:58745,
CC         ChEBI:CHEBI:88021, ChEBI:CHEBI:88026; EC=2.4.1.335;
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       Multi-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; EU726231; ACE74695.1; -; Genomic_DNA.
DR   AlphaFoldDB; B3VA59; -.
DR   SMR; B3VA59; -.
DR   CAZy; GT2; Glycosyltransferase Family 2.
DR   KEGG; ag:ACE74695; -.
DR   BioCyc; MetaCyc:MON-19264; -.
DR   BRENDA; 2.4.1.335; 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:0016758; F:hexosyltransferase 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..321
FT                   /note="Dolichyl N-acetyl-alpha-D-glucosaminyl phosphate 3-
FT                   beta-D-2,3-diacetamido-2,3-dideoxy-beta-D-
FT                   glucuronosyltransferase"
FT                   /id="PRO_0000435654"
FT   TRANSMEM        252..272
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        290..310
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   321 AA;  37328 MW;  4225C4DC1DB03D5A CRC64;
     MNFISIIIPT FNEEKYITKC LENWFNQDYP KENYEILIFD GKSTDKTLDV IKELQKKHNF
     ENIKIYTNEK RKQVYAFNEG IKNANGDFFI IFGAHAYPEQ DFLKNNIETY QRIKKEEPKL
     AGVGGIINKI SENMSAEIAK VIYSTPLSGG SSFWYAKEGF FSNTVVYGMY DTKMIKESEI
     LFDTDFITGQ DFEFNLHLIK EGFKLYTNPN IVSSYYTRSS VKKFIKQTIS YGAAKGLMIR
     KGYFNILWLF PFGFLFMLLS IIITGLLIFI YIMAILIDTI RLLIKTREPL YIALPILLFL
     FHCLISYGFF KGLIKGNSTF K