AGL8_HALVD
ID AGL8_HALVD Reviewed; 156 AA.
AC D4GU73;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 03-AUG-2022, entry version 53.
DE RecName: Full=Low-salt glycan biosynthesis protein Agl8;
DE EC=3.6.1.-;
GN Name=agl8; OrderedLocusNames=HVO_2060; ORFNames=C498_05588;
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: Nudix hydrolase involved in N-glycan biosynthetic pathway
CC that takes place under low-salt conditions (1.75 M instead of 3.4 M).
CC Participates in the formation of the tetrasaccharide present at 'Asn-
CC 532' of S-layer glycoprotein Csg, consisting of a sulfated hexose, 2
CC hexoses and rhamnose. Mediates attachment of sugar 3 in the
CC tetrasaccharide. {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 Nudix hydrolase family. {ECO:0000305}.
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DR EMBL; CP001956; ADE04487.1; -; Genomic_DNA.
DR EMBL; AOHU01000040; ELY33654.1; -; Genomic_DNA.
DR RefSeq; WP_004041945.1; NZ_AOHU01000040.1.
DR AlphaFoldDB; D4GU73; -.
DR SMR; D4GU73; -.
DR STRING; 309800.C498_05588; -.
DR EnsemblBacteria; ADE04487; ADE04487; HVO_2060.
DR EnsemblBacteria; ELY33654; ELY33654; C498_05588.
DR GeneID; 8925149; -.
DR KEGG; hvo:HVO_2060; -.
DR PATRIC; fig|309800.29.peg.1084; -.
DR eggNOG; arCOG01075; Archaea.
DR HOGENOM; CLU_037162_12_0_2; -.
DR OMA; HDNSRAY; -.
DR OrthoDB; 116493at2157; -.
DR UniPathway; UPA00378; -.
DR UniPathway; UPA00977; -.
DR Proteomes; UP000008243; Chromosome.
DR Proteomes; UP000011532; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; 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 InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR InterPro; IPR000086; NUDIX_hydrolase_dom.
DR Pfam; PF00293; NUDIX; 1.
DR SUPFAM; SSF55811; SSF55811; 1.
DR PROSITE; PS51462; NUDIX; 1.
PE 3: Inferred from homology;
KW Hydrolase; Magnesium; Metal-binding; Reference proteome.
FT CHAIN 1..156
FT /note="Low-salt glycan biosynthesis protein Agl8"
FT /id="PRO_0000428773"
FT DOMAIN 25..156
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT MOTIF 61..82
FT /note="Nudix box"
FT BINDING 14..15
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 47
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 60
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 80
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 130
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 156 AA; 17700 MW; FD48F40239418B09 CRC64;
MADQRNQADK PTTRIPDDEW EAIVANVPLV SVDLVIRHEG GVLLGFRENE PARGEWFVPG
GTVFKNETLT DALYRVADEE LGVDVTIESR LGTFEHFYDT SDVEGIDSKH YLATAFEVTL
DDDNLEMDTQ HSQLKVFEPP YEGLHPYVER YLDALD
