AGL7_HALVD
ID AGL7_HALVD Reviewed; 405 AA.
AC D4GU60;
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 sulfotransferase Agl7 {ECO:0000305|PubMed:24194539};
DE EC=2.8.2.- {ECO:0000305|PubMed:24194539};
GN Name=agl7 {ECO:0000303|PubMed:24194539}; OrderedLocusNames=HVO_2046;
GN ORFNames=C498_05521;
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: Involved in N-glycan biosynthetic pathway that takes place
CC under low-salt conditions (1.75 M instead of 3.4 M). Participates in
CC the formation of the tetrasaccharide present at 'Asn-532' of S-layer
CC glycoprotein Csg, consisting of a sulfated hexose, 2 hexoses and
CC rhamnose. Mediates sulfation of sugar 1 in the tetrasaccharide.
CC {ECO:0000269|PubMed:24194539}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC Note=Binds 1 Ca(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 with formation of a
CC tetrasaccharide that is not sulfated. No effect on 'Asn-47' and 'Asn-
CC 117' glycosylation of S-layer glycoprotein Csg.
CC {ECO:0000269|PubMed:24194539}.
CC -!- SIMILARITY: Belongs to the sulfatase family. {ECO:0000305}.
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DR EMBL; CP001956; ADE02348.1; -; Genomic_DNA.
DR EMBL; AOHU01000038; ELY34562.1; -; Genomic_DNA.
DR RefSeq; WP_004041932.1; NZ_AOHU01000038.1.
DR AlphaFoldDB; D4GU60; -.
DR SMR; D4GU60; -.
DR STRING; 309800.C498_05521; -.
DR EnsemblBacteria; ADE02348; ADE02348; HVO_2046.
DR EnsemblBacteria; ELY34562; ELY34562; C498_05521.
DR GeneID; 8926286; -.
DR KEGG; hvo:HVO_2046; -.
DR eggNOG; arCOG02785; Archaea.
DR HOGENOM; CLU_691886_0_0_2; -.
DR OMA; TGGFERT; -.
DR OrthoDB; 37407at2157; -.
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:0008484; F:sulfuric ester hydrolase activity; IEA:InterPro.
DR GO; GO:0016740; F:transferase 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 Gene3D; 3.40.720.10; -; 2.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR000917; Sulfatase_N.
DR Pfam; PF00884; Sulfatase; 1.
DR SUPFAM; SSF53649; SSF53649; 1.
PE 3: Inferred from homology;
KW Calcium; Metal-binding; Reference proteome; Transferase.
FT CHAIN 1..405
FT /note="Low-salt glycan biosynthesis sulfotransferase Agl7"
FT /id="PRO_0000428772"
FT BINDING 24
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 201
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 202
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
SQ SEQUENCE 405 AA; 45557 MW; 01A9041364C0B83E CRC64;
MITGPISNLS GESGFENVFI FISDSLRYDA LPERIRSKGL TIKTIAAAPW TASSIPSLMS
GKYPSSHNVW MFEDRLPQRP PLLSEQEDWD AGFDSEKHWL KFESSEKPPV KMLRLDGEQK
LADIEPPFVH VVHDLGPHAP YGFENDEYET GPYFRDYNDP KDLQQKYQND AEKSANYFLE
ILDKLENLGL REDTLCVFTS DHGELLGEGG RLGGKWGHST PLCPELLEVP MTFIGKGIPK
GETLSGVASG VDLAPTCLSA VGREIGHVDG IDLWAETPDE DRRVRSDVWQ RYNAFGRELP
VYVASGLWDN DGGWVKHRRS KLLRMAYYGY DVFLGDYAPP ARSTTGISEL VSGLKFWGRD
WEKFGNTTIS LQEAQKELSD ELVRSEDSVE LSEEQTEHLE ALGYV
