AGLG_HALVD
ID AGLG_HALVD Reviewed; 313 AA.
AC D4GYH3; B2G4W7;
DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 03-AUG-2022, entry version 49.
DE RecName: Full=Glucosyl-dolichyl phosphate glucuronosyltransferase {ECO:0000305|PubMed:28809486};
DE EC=2.4.1.356 {ECO:0000305|PubMed:28809486};
DE AltName: Full=Archaeal glycosylation protein G;
DE AltName: Full=Glycosyltransferase AglG;
GN Name=aglG {ECO:0000303|PubMed:18631242}; OrderedLocusNames=HVO_1529;
OS Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 /
OS NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloferax.
OX NCBI_TaxID=309800;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION IN PROTEIN GLYCOSYLATION,
RP PATHWAY, AND GENE NAME.
RC STRAIN=DS2 / DS70;
RX PubMed=18631242; DOI=10.1111/j.1365-2958.2008.06352.x;
RA Yurist-Doutsch S., Abu-Qarn M., Battaglia F., Morris H.R., Hitchen P.G.,
RA Dell A., Eichler J.;
RT "AglF, aglG and aglI, novel members of a gene island involved in the N-
RT glycosylation of the Haloferax volcanii S-layer glycoprotein.";
RL Mol. Microbiol. 69:1234-1245(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC B-1768 / DS2;
RX PubMed=20333302; DOI=10.1371/journal.pone.0009605;
RA Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S., Madupu R.,
RA Robinson J., Khouri H., Ren Q., Lowe T.M., Maupin-Furlow J.,
RA Pohlschroder M., Daniels C., Pfeiffer F., Allers T., Eisen J.A.;
RT "The complete genome sequence of Haloferax volcanii DS2, a model
RT archaeon.";
RL PLoS ONE 5:E9605-E9605(2010).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=H53;
RX PubMed=21091511; DOI=10.1111/j.1365-2958.2010.07405.x;
RA Guan Z., Naparstek S., Kaminski L., Konrad Z., Eichler J.;
RT "Distinct glycan-charged phosphodolichol carriers are required for the
RT assembly of the pentasaccharide N-linked to the Haloferax volcanii S-layer
RT glycoprotein.";
RL Mol. Microbiol. 78:1294-1303(2010).
RN [4]
RP FUNCTION IN GLYCOSYLATION OF FLAGELLINS, AND DISRUPTION PHENOTYPE.
RC STRAIN=H53;
RX PubMed=22730124; DOI=10.1128/jb.00731-12;
RA Tripepi M., You J., Temel S., Onder O., Brisson D., Pohlschroder M.;
RT "N-glycosylation of Haloferax volcanii flagellins requires known Agl
RT proteins and is essential for biosynthesis of stable flagella.";
RL J. Bacteriol. 194:4876-4887(2012).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=28809486; DOI=10.1021/acs.bioconjchem.7b00436;
RA Elharar Y., Podilapu A.R., Guan Z., Kulkarni S.S., Eichler J.;
RT "Assembling Glycan-Charged Dolichol Phosphates: Chemoenzymatic Synthesis of
RT a Haloferax volcanii N-Glycosylation Pathway Intermediate.";
RL Bioconj. Chem. 28:2461-2470(2017).
CC -!- FUNCTION: Involved in the protein N-glycosylation pathway responsible
CC for the assembly and attachment of an N-linked pentasaccharide that
CC decorates the S-layer glycoprotein and flagellins (PubMed:18631242,
CC PubMed:21091511, PubMed:22730124). Catalyzes the transfer of a
CC glucuronate residue (GlcA) to a glucose residue already bound to a
CC dolichol phosphate (DolP), a compound that serves as a glycan lipid
CC carrier in Archaea. In vitro, is able to add GlcA to DolP-Glc in which
CC the omega-position isoprene is not saturated. However, the likely
CC physiological lipid substrate is alpha,omega-saturated
CC (PubMed:28809486). {ECO:0000269|PubMed:18631242,
CC ECO:0000269|PubMed:21091511, ECO:0000269|PubMed:22730124,
CC ECO:0000269|PubMed:28809486}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an archaeal dolichyl alpha-D-glucosyl phosphate + UDP-alpha-D-
CC glucuronate = an archaeal dolichyl beta-D-glucuronosyl-(1->4)-alpha-
CC D-glucosyl phosphate + H(+) + UDP; Xref=Rhea:RHEA:56160, Rhea:RHEA-
CC COMP:14396, Rhea:RHEA-COMP:14397, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58052, ChEBI:CHEBI:58223, ChEBI:CHEBI:139561,
CC ChEBI:CHEBI:139562; EC=2.4.1.356;
CC Evidence={ECO:0000305|PubMed:28809486};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56161;
CC Evidence={ECO:0000305|PubMed:28809486};
CC -!- PATHWAY: Cell surface structure biogenesis; S-layer biogenesis.
CC {ECO:0000269|PubMed:18631242}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:28809486};
CC Single-pass membrane protein {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Mutants contain only hexose-modified
CC phosphodolichols and exhibit defective or limited motility.
CC {ECO:0000269|PubMed:21091511, ECO:0000269|PubMed:22730124}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. {ECO:0000305}.
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DR EMBL; AM991130; CAQ51231.1; -; Genomic_DNA.
DR EMBL; CP001956; ADE02287.1; -; Genomic_DNA.
DR RefSeq; WP_004041407.1; NC_013967.1.
DR AlphaFoldDB; D4GYH3; -.
DR SMR; D4GYH3; -.
DR STRING; 309800.C498_03000; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR EnsemblBacteria; ADE02287; ADE02287; HVO_1529.
DR GeneID; 8926215; -.
DR KEGG; hvo:HVO_1529; -.
DR eggNOG; arCOG01387; Archaea.
DR HOGENOM; CLU_025996_19_2_2; -.
DR OMA; FPEEFDW; -.
DR OrthoDB; 107665at2157; -.
DR BioCyc; MetaCyc:MON-19284; -.
DR BRENDA; 2.4.1.356; 2561.
DR UniPathway; UPA00977; -.
DR Proteomes; UP000008243; 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:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
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; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..313
FT /note="Glucosyl-dolichyl phosphate glucuronosyltransferase"
FT /id="PRO_0000415421"
FT TRANSMEM 284..304
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 313 AA; 35802 MW; 318704140B04FDF8 CRC64;
MKVSVVVCTY SMERYESFSE TVESVLAQTY EPLELVIVVD GNEEEFDRVQ DDFGDIDDVV
LHCNDENRGI SYSRTKGAEL GTGDVVAMID DDATAEPDWI ETLVDTYENN PDAVAVGGTV
VPDWVARKPE FFPEEFYWLV GCDERGFGEH MEEVRNTYGS NISFKRDVFL EVGGYDTNTG
RKGDKHVQAH EAPVCIRIYE QTGERVIYNK QARVNHKLFE YRTEFDWLVF RSFWQGYSKR
VMDLLYPQAS DDKNAYLKDL MLVYVVDRLK NLVEDPSLAQ VQQLIAIFVF TAAVGFGYVY
GLLTPNLVEK TNN
