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Glycosyltransferase AglD (EC 2.4.1.-) (Archaeal glycosylation protein D)

 AGLD_HALVD              Reviewed;         624 AA.
D4GUA0; A4VB68;
25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
18-MAY-2010, sequence version 1.
30-AUG-2017, entry version 36.
RecName: Full=Glycosyltransferase AglD;
EC=2.4.1.-;
AltName: Full=Archaeal glycosylation protein D;
Name=aglD; OrderedLocusNames=HVO_0798;
Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC
14742 / NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii).
Archaea; Euryarchaeota; Halobacteria; Haloferacales; Haloferacaceae;
Haloferax.
NCBI_TaxID=309800;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, PATHWAY, AND GENE NAME.
STRAIN=DS2 / DS70;
PubMed=17996897; DOI=10.1016/j.jmb.2007.10.042;
Abu-Qarn M., Yurist-Doutsch S., Giordana A., Trauner A., Morris H.R.,
Hitchen P., Medalia O., Dell A., Eichler J.;
"Haloferax volcanii AglB and AglD are involved in N-glycosylation of
the S-layer glycoprotein and proper assembly of the surface layer.";
J. Mol. Biol. 374:1224-1236(2007).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 /
VKM B-1768 / DS2;
PubMed=20333302; DOI=10.1371/journal.pone.0009605;
Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S.,
Madupu R., Robinson J., Khouri H., Ren Q., Lowe T.M.,
Maupin-Furlow J., Pohlschroder M., Daniels C., Pfeiffer F., Allers T.,
Eisen J.A.;
"The complete genome sequence of Haloferax volcanii DS2, a model
archaeon.";
PLoS ONE 5:E9605-E9605(2010).
[3]
MUTAGENESIS OF ASP-110; ASP-112; ASP-133; GLY-137; SER-138; ARG-139;
ASP-173; GLN-175; CYS-176; GLY-177; PHE-178; LYS-179; ASP-195 AND
ASP-201.
STRAIN=DS2 / DS70;
PubMed=20585355; DOI=10.1155/2010/315108;
Kaminski L., Eichler J.;
"Identification of residues important for the activity of Haloferax
volcanii AglD, a component of the archaeal N-glycosylation pathway.";
Archaea 2010:315108-315108(2010).
[4]
FUNCTION.
STRAIN=H53;
PubMed=21091511; DOI=10.1111/j.1365-2958.2010.07405.x;
Guan Z., Naparstek S., Kaminski L., Konrad Z., Eichler J.;
"Distinct glycan-charged phosphodolichol carriers are required for the
assembly of the pentasaccharide N-linked to the Haloferax volcanii S-
layer glycoprotein.";
Mol. Microbiol. 78:1294-1303(2010).
[5]
FUNCTION IN GLYCOSYLATION OF FLAGELLINS, AND DISRUPTION PHENOTYPE.
STRAIN=H53;
PubMed=22730124; DOI=10.1128/JB.00731-12;
Tripepi M., You J., Temel S., Onder O., Brisson D., Pohlschroder M.;
"N-glycosylation of Haloferax volcanii flagellins requires known Agl
proteins and is essential for biosynthesis of stable flagella.";
J. Bacteriol. 194:4876-4887(2012).
-!- FUNCTION: Involved in the assembly of a N-linked pentasaccharide
that decorates the S-layer glycoprotein and flagellins. Catalyzes
the addition of the mannose found at position 5 of the
pentasaccharide to its own distinct dolichol phosphate carrier.
{ECO:0000269|PubMed:17996897, ECO:0000269|PubMed:21091511,
ECO:0000269|PubMed:22730124}.
-!- PATHWAY: Cell surface structure biogenesis; S-layer biogenesis.
{ECO:0000269|PubMed:17996897}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass
membrane protein {ECO:0000305}.
-!- DISRUPTION PHENOTYPE: Mutants exhibit defective or limited
motility. {ECO:0000269|PubMed:22730124}.
-!- SIMILARITY: Belongs to the glycosyltransferase 2 family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AM698042; CAM91696.1; -; Genomic_DNA.
EMBL; CP001956; ADE04998.1; -; Genomic_DNA.
RefSeq; WP_004044138.1; NZ_AOHU01000097.1.
ProteinModelPortal; D4GUA0; -.
STRING; 309800.HVO_0798; -.
CAZy; GT2; Glycosyltransferase Family 2.
EnsemblBacteria; ADE04998; ADE04998; HVO_0798.
GeneID; 8924085; -.
KEGG; hvo:HVO_0798; -.
eggNOG; arCOG00895; Archaea.
eggNOG; arCOG00897; Archaea.
eggNOG; COG0392; LUCA.
eggNOG; COG0463; LUCA.
HOGENOM; HOG000267144; -.
KO; K07027; -.
OMA; LRDHQCG; -.
OrthoDB; POG093Z0EVE; -.
BioCyc; MetaCyc:MONOMER-19290; -.
UniPathway; UPA00977; -.
Proteomes; UP000008243; Chromosome.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0016757; F:transferase activity, transferring glycosyl groups; IEA:UniProtKB-KW.
GO; GO:0045232; P:S-layer organization; IEA:UniProtKB-UniPathway.
CDD; cd04188; DPG_synthase; 1.
Gene3D; 3.90.550.10; -; 1.
InterPro; IPR035518; DPG_synthase.
InterPro; IPR001173; Glyco_trans_2-like.
InterPro; IPR022791; L-PG_synthase/AglD.
InterPro; IPR029044; Nucleotide-diphossugar_trans.
Pfam; PF00535; Glycos_transf_2; 1.
Pfam; PF03706; LPG_synthase_TM; 1.
SUPFAM; SSF53448; SSF53448; 1.
TIGRFAMs; TIGR00374; TIGR00374; 2.
1: Evidence at protein level;
Cell membrane; Complete proteome; Glycosyltransferase; Membrane;
Reference proteome; Transferase; Transmembrane; Transmembrane helix.
CHAIN 1 624 Glycosyltransferase AglD.
/FTId=PRO_0000415388.
TRANSMEM 260 280 Helical. {ECO:0000255}.
TRANSMEM 285 305 Helical. {ECO:0000255}.
TRANSMEM 381 401 Helical. {ECO:0000255}.
TRANSMEM 427 447 Helical. {ECO:0000255}.
TRANSMEM 496 518 Helical. {ECO:0000255}.
TRANSMEM 532 552 Helical. {ECO:0000255}.
TRANSMEM 556 576 Helical. {ECO:0000255}.
TRANSMEM 587 607 Helical. {ECO:0000255}.
ACT_SITE 201 201 {ECO:0000305}.
MUTAGEN 110 110 D->A,E: Loss of activity.
{ECO:0000269|PubMed:20585355}.
MUTAGEN 112 112 D->E: Change in activity.
{ECO:0000269|PubMed:20585355}.
MUTAGEN 112 112 D->N: Loss of activity.
{ECO:0000269|PubMed:20585355}.
MUTAGEN 133 133 D->A: No change in activity.
{ECO:0000269|PubMed:20585355}.
MUTAGEN 137 137 G->A: No change in activity.
{ECO:0000269|PubMed:20585355}.
MUTAGEN 138 138 S->A: No change in activity.
{ECO:0000269|PubMed:20585355}.
MUTAGEN 139 139 R->A,E,K,M: Loss of activity.
{ECO:0000269|PubMed:20585355}.
MUTAGEN 173 173 D->E: Loss of activity.
{ECO:0000269|PubMed:20585355}.
MUTAGEN 173 173 D->N: No change in activity.
{ECO:0000269|PubMed:20585355}.
MUTAGEN 175 175 Q->A: No change in activity.
{ECO:0000269|PubMed:20585355}.
MUTAGEN 176 176 C->A: No change in activity.
{ECO:0000269|PubMed:20585355}.
MUTAGEN 177 177 G->A: No change in activity.
{ECO:0000269|PubMed:20585355}.
MUTAGEN 178 178 F->A: No change in activity.
{ECO:0000269|PubMed:20585355}.
MUTAGEN 179 179 K->A: No change in activity.
{ECO:0000269|PubMed:20585355}.
MUTAGEN 195 195 D->A: No change in activity.
{ECO:0000269|PubMed:20585355}.
MUTAGEN 201 201 D->A,N: Loss of activity.
{ECO:0000269|PubMed:20585355}.
MUTAGEN 201 201 D->E: No change in activity.
{ECO:0000269|PubMed:20585355}.
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


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