AGLD_HALVD
ID AGLD_HALVD Reviewed; 624 AA.
AC D4GUA0; A4VB68;
DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 03-AUG-2022, entry version 52.
DE RecName: Full=Glycosyltransferase AglD;
DE EC=2.4.1.-;
DE AltName: Full=Archaeal glycosylation protein D;
GN Name=aglD; OrderedLocusNames=HVO_0798;
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, PATHWAY, AND GENE NAME.
RC STRAIN=DS2 / DS70;
RX PubMed=17996897; DOI=10.1016/j.jmb.2007.10.042;
RA Abu-Qarn M., Yurist-Doutsch S., Giordana A., Trauner A., Morris H.R.,
RA Hitchen P., Medalia O., Dell A., Eichler J.;
RT "Haloferax volcanii AglB and AglD are involved in N-glycosylation of the S-
RT layer glycoprotein and proper assembly of the surface layer.";
RL J. Mol. Biol. 374:1224-1236(2007).
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 MUTAGENESIS OF ASP-110; ASP-112; ASP-133; GLY-137; SER-138; ARG-139;
RP ASP-173; GLN-175; CYS-176; GLY-177; PHE-178; LYS-179; ASP-195 AND ASP-201.
RC STRAIN=DS2 / DS70;
RX PubMed=20585355; DOI=10.1155/2010/315108;
RA Kaminski L., Eichler J.;
RT "Identification of residues important for the activity of Haloferax
RT volcanii AglD, a component of the archaeal N-glycosylation pathway.";
RL Archaea 2010:315108-315108(2010).
RN [4]
RP FUNCTION.
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 [5]
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).
CC -!- FUNCTION: Involved in the assembly of a N-linked pentasaccharide that
CC decorates the S-layer glycoprotein and flagellins. Catalyzes the
CC addition of the mannose found at position 5 of the pentasaccharide to
CC its own distinct dolichol phosphate carrier.
CC {ECO:0000269|PubMed:17996897, ECO:0000269|PubMed:21091511,
CC ECO:0000269|PubMed:22730124}.
CC -!- PATHWAY: Cell surface structure biogenesis; S-layer biogenesis.
CC {ECO:0000269|PubMed:17996897}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Mutants exhibit defective or limited motility.
CC {ECO:0000269|PubMed:22730124}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. {ECO:0000305}.
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DR EMBL; AM698042; CAM91696.1; -; Genomic_DNA.
DR EMBL; CP001956; ADE04998.1; -; Genomic_DNA.
DR RefSeq; WP_004044138.1; NC_013967.1.
DR AlphaFoldDB; D4GUA0; -.
DR SMR; D4GUA0; -.
DR STRING; 309800.C498_14743; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR PRIDE; D4GUA0; -.
DR EnsemblBacteria; ADE04998; ADE04998; HVO_0798.
DR GeneID; 8924085; -.
DR KEGG; hvo:HVO_0798; -.
DR eggNOG; arCOG00897; Archaea.
DR HOGENOM; CLU_474611_0_0_2; -.
DR OMA; LRDHQCG; -.
DR OrthoDB; 9352at2157; -.
DR BioCyc; MetaCyc:MON-19290; -.
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 CDD; cd04188; DPG_synthase; 1.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR035518; DPG_synthase.
DR InterPro; IPR001173; Glyco_trans_2-like.
DR InterPro; IPR022791; L-PG_synthase/AglD.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR Pfam; PF00535; Glycos_transf_2; 1.
DR Pfam; PF03706; LPG_synthase_TM; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
DR TIGRFAMs; TIGR00374; TIGR00374; 2.
PE 1: Evidence at protein level;
KW Cell membrane; Glycosyltransferase; Membrane; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..624
FT /note="Glycosyltransferase AglD"
FT /id="PRO_0000415388"
FT TRANSMEM 260..280
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 285..305
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 381..401
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 427..447
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 496..518
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 532..552
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 556..576
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 587..607
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 201
FT /evidence="ECO:0000305"
FT MUTAGEN 110
FT /note="D->A,E: Loss of activity."
FT /evidence="ECO:0000269|PubMed:20585355"
FT MUTAGEN 112
FT /note="D->E: Change in activity."
FT /evidence="ECO:0000269|PubMed:20585355"
FT MUTAGEN 112
FT /note="D->N: Loss of activity."
FT /evidence="ECO:0000269|PubMed:20585355"
FT MUTAGEN 133
FT /note="D->A: No change in activity."
FT /evidence="ECO:0000269|PubMed:20585355"
FT MUTAGEN 137
FT /note="G->A: No change in activity."
FT /evidence="ECO:0000269|PubMed:20585355"
FT MUTAGEN 138
FT /note="S->A: No change in activity."
FT /evidence="ECO:0000269|PubMed:20585355"
FT MUTAGEN 139
FT /note="R->A,E,K,M: Loss of activity."
FT /evidence="ECO:0000269|PubMed:20585355"
FT MUTAGEN 173
FT /note="D->E: Loss of activity."
FT /evidence="ECO:0000269|PubMed:20585355"
FT MUTAGEN 173
FT /note="D->N: No change in activity."
FT /evidence="ECO:0000269|PubMed:20585355"
FT MUTAGEN 175
FT /note="Q->A: No change in activity."
FT /evidence="ECO:0000269|PubMed:20585355"
FT MUTAGEN 176
FT /note="C->A: No change in activity."
FT /evidence="ECO:0000269|PubMed:20585355"
FT MUTAGEN 177
FT /note="G->A: No change in activity."
FT /evidence="ECO:0000269|PubMed:20585355"
FT MUTAGEN 178
FT /note="F->A: No change in activity."
FT /evidence="ECO:0000269|PubMed:20585355"
FT MUTAGEN 179
FT /note="K->A: No change in activity."
FT /evidence="ECO:0000269|PubMed:20585355"
FT MUTAGEN 195
FT /note="D->A: No change in activity."
FT /evidence="ECO:0000269|PubMed:20585355"
FT MUTAGEN 201
FT /note="D->A,N: Loss of activity."
FT /evidence="ECO:0000269|PubMed:20585355"
FT MUTAGEN 201
FT /note="D->E: No change in activity."
FT /evidence="ECO:0000269|PubMed:20585355"
SQ SEQUENCE 624 AA; 66990 MW; EEAF1CCBB682D8C0 CRC64;
MGRPTERRPA AATAAGVEVS VVLPAYNEAR TIENTVRVTV ETLESFLPAD AFEVIVAEDG
CDDETPEIAD RLAAEDDRIR HYHSDDRLGR GGALERAFEA ARGDTLVYFD TDLATDMRHL
EELVERVRSG EYDAATGSRW MPDRVADRPR KRGVPSRAYN GLVRLFLRSD LRDHQCGFKA
FSREAFEALR DDVEDNHWFW DTEMLVRAQR AGFRVAEFPV DWEPKGDTKV DLVRDILGMG
SQILRTWWQL TVRPRITRRV TIVAGLLLTV LALALMTLYI DPSEVISVLG DADPALVAAA
AVIYVVSWPL RGIRYREILR ELGYREKAGF LTGAIFISQT GNLVFPARAG DAVRAYVVKA
RRNIPYPSGF ASLAVERVFD LLTIAGLAGV VLVGLAATGG LDDIATVLAT GVSGGSVDVS
ADDVRTAAYV ATGVGVVAIL GVLGIALSAR ADRNVVRAFV GRFSSDSYVE LVAGVIEQFV
SDLQAVAGNR AAFGRVGLTS LAIWTVDVVT AVVVLLALGV DIDPVVLVGV SFFAVSVGNL
AKVLPLSPGG VGLYEIAFTV FMAALAPVTP AAALAAAVLD HAVKNAVTIV GGVGSMLSLN
VSLTTAVEES AEVRDREHEL ADSK
