AGL5_HALVD
ID AGL5_HALVD Reviewed; 372 AA.
AC D4GU66;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 25-MAY-2022, entry version 55.
DE RecName: Full=Low-salt glycan biosynthesis hexosyltransferase Agl5;
DE EC=2.4.1.-;
DE AltName: Full=Archaeal glycosylation protein 5;
GN Name=agl5; OrderedLocusNames=HVO_2053; ORFNames=C498_05553;
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: Hexosyltransferase 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. Together with Agl6, mediates the addition of
CC sugars 1 and 2 to dolichol phosphate in the tetrasaccharide.
CC {ECO:0000269|PubMed:24194539}.
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: Abolishes formation of the tetrasaccharide
CC present at 'Asn-532' of S-layer glycoprotein Csg. No effect on 'Asn-47'
CC and 'Asn-117' glycosylation of S-layer glycoprotein Csg.
CC {ECO:0000269|PubMed:24194539}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase group 1 family.
CC {ECO:0000305}.
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DR EMBL; CP001956; ADE03016.1; -; Genomic_DNA.
DR EMBL; AOHU01000039; ELY34304.1; -; Genomic_DNA.
DR AlphaFoldDB; D4GU66; -.
DR SMR; D4GU66; -.
DR STRING; 309800.C498_05553; -.
DR CAZy; GT4; Glycosyltransferase Family 4.
DR EnsemblBacteria; ADE03016; ADE03016; HVO_2053.
DR EnsemblBacteria; ELY34304; ELY34304; C498_05553.
DR KEGG; hvo:HVO_2053; -.
DR eggNOG; arCOG01415; Archaea.
DR HOGENOM; CLU_009583_6_2_2; -.
DR UniPathway; UPA00378; -.
DR UniPathway; UPA00977; -.
DR Proteomes; UP000008243; Chromosome.
DR Proteomes; UP000011532; Unassembled WGS sequence.
DR GO; GO:0016757; F:glycosyltransferase 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.
PE 3: Inferred from homology;
KW Glycosyltransferase; Reference proteome; Transferase.
FT CHAIN 1..372
FT /note="Low-salt glycan biosynthesis hexosyltransferase
FT Agl5"
FT /id="PRO_0000428768"
SQ SEQUENCE 372 AA; 41199 MW; CBCD8613CF3F0818 CRC64;
MGQDSGGLPH YTAELANSMS EYARVTVLKP NETSADEVLR DEITVINAFK PTDISMQNLF
DLKLDVLDSI RGLFSFWNIK LINQIDPDIV HDPTDEFPQV NLFSWVHSVY EDRPYVVTSH
ETKHGGAGGV LRVVNPLLSL VPDFEKSAAI VHSADQRELL LNNHKAVDEV HVIPHGVYSF
FRELDYDEQK EEDKHALFFG SLIPPKGIEY LIDAVPKVSE EVPGFSLTIA GSGSIPDECA
DVVEQYSDVI NIRNEFIPNE EVGTLFSRAQ VVVLPYRRGW QTGHSGTLSI AFAFGKPIIT
SEVGDFPELV GESGAGIVVE PESPEAIADG LIEVFSSDSA LDQMSNASSR VADRLSWEKI
AEQHFEVYQN LL