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AGL13_HALVD
ID   AGL13_HALVD             Reviewed;         156 AA.
AC   D4GU69;
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=Probable low-salt glycan biosynthesis epimerase Agl13;
DE            EC=5.1.3.-;
GN   Name=agl13; OrderedLocusNames=HVO_2056; ORFNames=C498_05563;
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: Epimerase involved in N-glycan biosynthetic pathway that
CC       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. Involved in the addition of final rhamnose (sugar
CC       4) of the tetrasaccharide on the dolichol phosphate carrier.
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: 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 dTDP-4-dehydrorhamnose 3,5-epimerase family.
CC       {ECO:0000305}.
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DR   EMBL; CP001956; ADE02686.1; -; Genomic_DNA.
DR   EMBL; AOHU01000040; ELY33649.1; -; Genomic_DNA.
DR   RefSeq; WP_004041940.1; NZ_AOHU01000040.1.
DR   AlphaFoldDB; D4GU69; -.
DR   SMR; D4GU69; -.
DR   STRING; 309800.C498_05563; -.
DR   EnsemblBacteria; ADE02686; ADE02686; HVO_2056.
DR   EnsemblBacteria; ELY33649; ELY33649; C498_05563.
DR   GeneID; 8926740; -.
DR   KEGG; hvo:HVO_2056; -.
DR   PATRIC; fig|309800.29.peg.1079; -.
DR   eggNOG; arCOG04188; Archaea.
DR   HOGENOM; CLU_090940_3_0_2; -.
DR   OMA; KAWHYHK; -.
DR   OrthoDB; 96034at2157; -.
DR   BioCyc; MetaCyc:MON-18753; -.
DR   BRENDA; 5.1.3.13; 2561.
DR   UniPathway; UPA00378; -.
DR   UniPathway; UPA00977; -.
DR   Proteomes; UP000008243; Chromosome.
DR   Proteomes; UP000011532; Unassembled WGS sequence.
DR   GO; GO:0008830; F:dTDP-4-dehydrorhamnose 3,5-epimerase activity; IEA:InterPro.
DR   GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR   GO; GO:0045232; P:S-layer organization; IEA:UniProtKB-UniPathway.
DR   Gene3D; 2.60.120.10; -; 1.
DR   InterPro; IPR000888; dTDP_sugar_isom.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   InterPro; IPR011051; RmlC_Cupin_sf.
DR   PANTHER; PTHR21047; PTHR21047; 1.
DR   Pfam; PF00908; dTDP_sugar_isom; 1.
DR   SUPFAM; SSF51182; SSF51182; 1.
PE   3: Inferred from homology;
KW   Isomerase; Reference proteome.
FT   CHAIN           1..156
FT                   /note="Probable low-salt glycan biosynthesis epimerase
FT                   Agl13"
FT                   /id="PRO_0000428776"
FT   BINDING         19
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         24
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         39..41
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         51
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         54
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         109
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   156 AA;  18336 MW;  568276715EAC6D8B CRC64;
     MPNIHDVEVR DLQVNADQRG HLVEVFRSDW DEYEIDPEMS YYSMTYPGVV RAWHRHLEGQ
     IDHFVCPKGR ITVGIYDDRE DSPTQGELDT FVIGEHNQQV IRIPGDCWHG FKAIGDEPSL
     LINYPTNLYD YEDPDEERIP YDDDRIPYDW NAEIHG
 
 
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