AGL11_HALVD
ID AGL11_HALVD Reviewed; 357 AA.
AC D4GU70;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Low-salt glycan biosynthesis nucleotidyltransferase Agl11;
DE EC=2.7.7.-;
GN Name=agl11; OrderedLocusNames=HVO_2057; ORFNames=C498_05568;
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 [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 [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=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
RN [3]
RP FUNCTION, PATHWAY, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC B-1768 / DS2;
RX PubMed=24194539; DOI=10.1128/mbio.00716-13;
RA Kaminski L., Guan Z., Yurist-Doutsch S., Eichler J.;
RT "Two distinct N-glycosylation pathways process the Haloferax volcanii S-
RT layer glycoprotein upon changes in environmental salinity.";
RL MBio 4:E00716-E00716(2013).
CC -!- FUNCTION: Nucleotidyltransferase involved in N-glycan biosynthetic
CC pathway that takes place under low-salt conditions (1.75 M instead of
CC 3.4 M). Participates in the formation of the tetrasaccharide present at
CC 'Asn-532' of S-layer glycoprotein Csg, consisting of a sulfated hexose,
CC 2 hexoses and rhamnose. Involved in the addition of final rhamnose
CC (sugar 4) of the tetrasaccharide on the dolichol phosphate carrier.
CC {ECO:0000269|PubMed:24194539}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000269|PubMed:24194539}.
CC -!- PATHWAY: Cell surface structure biogenesis; S-layer biogenesis.
CC {ECO:0000269|PubMed:24194539}.
CC -!- DISRUPTION PHENOTYPE: Impaired formation of the tetrasaccharide present
CC at 'Asn-532' of S-layer glycoprotein Csg. No effect on 'Asn-47' and
CC 'Asn-117' glycosylation of S-layer glycoprotein Csg.
CC {ECO:0000269|PubMed:24194539}.
CC -!- SIMILARITY: Belongs to the glucose-1-phosphate thymidylyltransferase
CC family. {ECO:0000305}.
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DR EMBL; CP001956; ADE02576.1; -; Genomic_DNA.
DR EMBL; AOHU01000040; ELY33650.1; -; Genomic_DNA.
DR RefSeq; WP_004041941.1; NZ_AOHU01000040.1.
DR AlphaFoldDB; D4GU70; -.
DR SMR; D4GU70; -.
DR STRING; 309800.C498_05568; -.
DR EnsemblBacteria; ADE02576; ADE02576; HVO_2057.
DR EnsemblBacteria; ELY33650; ELY33650; C498_05568.
DR GeneID; 8924305; -.
DR KEGG; hvo:HVO_2057; -.
DR PATRIC; fig|309800.29.peg.1080; -.
DR eggNOG; arCOG00667; Archaea.
DR HOGENOM; CLU_029499_0_1_2; -.
DR OMA; FTWLDTG; -.
DR OrthoDB; 61185at2157; -.
DR BioCyc; MetaCyc:MON-18751; -.
DR UniPathway; UPA00378; -.
DR UniPathway; UPA00977; -.
DR Proteomes; UP000008243; Chromosome.
DR Proteomes; UP000011532; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR GO; GO:0045232; P:S-layer organization; IEA:UniProtKB-UniPathway.
DR CDD; cd04189; G1P_TT_long; 1.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR005908; G1P_thy_trans_l.
DR InterPro; IPR001451; Hexapep.
DR InterPro; IPR005835; NTP_transferase_dom.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR Pfam; PF00132; Hexapep; 1.
DR Pfam; PF00483; NTP_transferase; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
DR TIGRFAMs; TIGR01208; rmlA_long; 1.
PE 3: Inferred from homology;
KW Magnesium; Metal-binding; Nucleotidyltransferase; Reference proteome;
KW Transferase.
FT CHAIN 1..357
FT /note="Low-salt glycan biosynthesis nucleotidyltransferase
FT Agl11"
FT /id="PRO_0000428774"
FT BINDING 108
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 221
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 357 AA; 37865 MW; 0CD7B5E8BA4C2985 CRC64;
MKGVLLSGGT GSRLRPITHT GPKQLVPVAN KPVLEYAVED LKEAGITEIG VILGHKGREE
IQNLLGDGSD YGVEITYIVQ GNPLGLAHAA GCAKDFVGDD DFVMYLGDNI LKEGVVDLVE
SFESGDFGAG IALQEVENPQ QFGIADVDDQ GNVTQLIEKP DEPPTNLALI GMYVFSPAVF
DAIEQLEPSW RGELEITDAI QSLLEDGYAI DSHVVEGWWK DTGKPEDILE ANQLVLEDKS
LKKRGTVSDD ATVDGRIELA ESATIEDGAV VRGPVSIADG AVIKSGTYVG PYTSVGPNST
LEGVHIENSV VIGESSINTS GRIVDSLLGK GANIGSADDF LPEGRRLVVG ENSQLKL
