ID AGL5_HALVD Reviewed; 378 AA.
AC D4GU66;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 22-FEB-2023, sequence version 2.
DT 24-JAN-2024, entry version 60.
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 SEQUENCE REVISION TO N-TERMINUS, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC B-1768 / DS2;
RX PubMed=32561711; DOI=10.1038/s41467-020-16784-7;
RA Schulze S., Adams Z., Cerletti M., De Castro R., Ferreira-Cerca S.,
RA Fufezan C., Gimenez M.I., Hippler M., Jevtic Z., Knueppel R., Legerme G.,
RA Lenz C., Marchfelder A., Maupin-Furlow J., Paggi R.A., Pfeiffer F.,
RA Poetsch A., Urlaub H., Pohlschroder M.;
RT "The Archaeal Proteome Project advances knowledge about archaeal cell
RT biology through comprehensive proteomics.";
RL Nat. Commun. 11:3145-3145(2020).
RN [4]
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ELY34304.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000269|PubMed:32561711};
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DR EMBL; CP001956; ADE03016.2; -; Genomic_DNA.
DR EMBL; AOHU01000039; ELY34304.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; D4GU66; -.
DR SMR; D4GU66; -.
DR STRING; 309800.HVO_2053; -.
DR CAZy; GT4; Glycosyltransferase Family 4.
DR PaxDb; 309800-C498_05553; -.
DR EnsemblBacteria; ADE03016; ADE03016; HVO_2053.
DR KEGG; hvo:HVO_2053; -.
DR eggNOG; arCOG01415; Archaea.
DR HOGENOM; CLU_009583_6_2_2; -.
DR OrthoDB; 132546at2157; -.
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.
DR CDD; cd03801; GT4_PimA-like; 1.
DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR PANTHER; PTHR46401; GLYCOSYLTRANSFERASE WBBK-RELATED; 1.
DR PANTHER; PTHR46401:SF2; GLYCOSYLTRANSFERASE WBBK-RELATED; 1.
DR Pfam; PF13692; Glyco_trans_1_4; 1.
DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE 1: Evidence at protein level;
KW Glycosyltransferase; Reference proteome; Transferase.
FT CHAIN 1..378
FT /note="Low-salt glycan biosynthesis hexosyltransferase
FT Agl5"
FT /id="PRO_0000428768"
SQ SEQUENCE 378 AA; 41956 MW; 9F66A2C8DB62F8B0 CRC64;
MHVLYIMGQD SGGLPHYTAE LANSMSEYAR VTVLKPNETS ADEVLRDEIT VINAFKPTDI
SMQNLFDLKL DVLDSIRGLF SFWNIKLINQ IDPDIVHDPT DEFPQVNLFS WVHSVYEDRP
YVVTSHETKH GGAGGVLRVV NPLLSLVPDF EKSAAIVHSA DQRELLLNNH KAVDEVHVIP
HGVYSFFREL DYDEQKEEDK HALFFGSLIP PKGIEYLIDA VPKVSEEVPG FSLTIAGSGS
IPDECADVVE QYSDVINIRN EFIPNEEVGT LFSRAQVVVL PYRRGWQTGH SGTLSIAFAF
GKPIITSEVG DFPELVGESG AGIVVEPESP EAIADGLIEV FSSDSALDQM SNASSRVADR
LSWEKIAEQH FEVYQNLL
//
